CAZyme Information: MGYG000003208_00233

Basic Information

• Species: Pseudomonas_E extremaustralis
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_E; Pseudomonas_E extremaustralis
• CAZyme ID: MGYG000003208_00233
• CAZy Family: GT2
• CAZyme Description: D-alanine--poly(phosphoribitol) ligase subunit 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
4676	MGYG000003208_5|CGC1	514677.89	5.6011

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003208	6254364	MAG	United States	North America

• Gene Location: Start: 1709; End: 15739 Strand: -

Full Sequence      

MNAEDSLKLARRFIGLPLEKRQLFLQALQKEGVDFSRFPIPAGVDAEDRDALSYAQQRMW
FLWQLDPSSGAYNLPGAVRLKGALNLGAMQQAFASLVARHETLRTVFQRQADERLAQVAA
PPALAVEQRDLSDLAPAEREQAVNDAATRQSLLPFDLEHGPLLRVQLLKLDAQEHVLLLT
LHHIVSDGWSMNVLIDEFIRFYDAHDRNETPQLPALPIQYSDYALWQRRWLEAGEQARQL
EYWQARLGDEHPLLELPTDRPRPATPSYRGTRHTFAIDPDLAAQLRSCAQAHNVTLFMLL
LGAFNVLLHRYTGQGDIRVGVPIANRNRTEVEGLIGFFVNTQVLRTELNGQTRVSELLRA
IKEHALGAQAHQDLPFERLVEALNVERSLSHTPLFQVMYNHQPVVADIASIRTASGLELA
AVEWQGRTTQFDLTLDTYEQSGTLQAALTYANDLFDAPSIARMARHWISLLQAMVADGEQ
RIGELPMLAADEQQVLVSAWNQTAQAYPTERGIHQLIEDQVRATPDAPALVFGATSLTYA
QLDARANQLAHALREQGVGPDALVGLCLERSIEMVVGLLGILKAGGAYVPLDPEYPQDRL
AYMIEDSGIQLLLSQQSLLPSLPAAGIRVIALDPPARWLDGYSREAPAVAIHGLNLAYVI
YTSGSTGQPKGAGNSHRALVNRLCWMQQAYTLEARDAVLQKTPFSFDVSVWEFFWPLMTG
ARLVVAAPGAHREPARLIETIERHGITTVHFVPSMLQAFIHEPGVQACTSLKRIVCSGEA
LPLDAQVQVFTKLPQAGLFNLYGPTEAAIDVTHWTCIDEGADSVPIGRPIANLHTYVLDA
QLNPVPAGVAGELYLGGSGLARSYHRRAALTAERFVPSPFADGVRLYRTGDRVRQRADGV
IEYLGRLDHQVKLRGLRIELGEIETRLLQHPGVREAVVLVQGGKQLVAYLVPQDEAPTDL
KAWLLGSLPEYMVPTHMLYLDRLPVTANGKLDRKALPVPDAAAQQAYSAPQTPAQQALAA
IWSDVLGIPQVGLDDNFFELGGDSIISIQVVSRARQAGLRLSPRDLFQYQSVRSLALVAT
FEQAAAIDQGPVSGEVLLTPVQRGFFAQAIPARAHWNQSLLLTPREALEPARLEAALTQV
INHHDALRLRFVEQAEGWQQTHAAPITAPGLWQAHAADDTELTALCDKAQRSLDLEQGPL
LRAALVNMADGTQRLLLVVHHLVVDGVSWRILLEDLQQAYGAAPLPAKTCAYQVWARQLQ
AHAQTLDAQLPYWQAQTVDADLPCDNPQGGLQTRLGAKLETRLDAELTRQLLQDAPAAYR
TQVNDLLLTALARVICRWSGQPAALIQLEGHGREELFDGVDLSRTVGWFTSLFPLRLRAD
GELADGIKAVKEQLRDVPDKGIGYGLLRYLGTPDAREALSRLAAPRIPFNSLGQFDRQFN
ESALFVPATGGSGQAQDREAPLANWLTLEGQVYGGELTLQWGFSREMFEAATIQRLADDY
GAELEALIEHCCATPAGQVTPSDFPLARVTQRQLDGLPVAGPAIADLYPLSPMQQGMLFH
SLYEPEAQAYINQLRLDIDGLDRLAFARAWQAALDRHDILRSSFHWLGLDSAHQLIERQV
DLPLHVIETLDVDVEALATAERDKGFALDAAPLFRLLLVRGAGATWHLIFTSHHILMDGW
SNAQLLGEVIAHYAGHQMPAPLGQFRDYLGWLQRQGSGEAFWKAALAPLQAPTLLAQALR
VPAHGAGMAEHHVVLDSDFTQALGEFARRQKITLNTLLQGAWSLLLQRYTGQDCVAFGAT
VAGRSAPLPGIEQQLGLFINTLPIVSVAAPAQSAARWLSDLQALNLSLRDHEHVPLYDIQ
GWAGQQGALFDTLLVFENFPVAEALKQGAPAGLTFGRLHNHERTHYPLTLGIELGASLRL
EWSYDRARFSADQVARLSANLQHLLVQLLADAQAPLGNLRLLDPTAQRNMLALGQSPAAA
PHELHVHQRIAAQAAATPDALAVQAGEVRLSYAQLNDHANRLAHRLLALGVGAGQRVGLA
CRRGPQLIVSLLAVLKSGAAYVPLDPKYPNERLAYLLADSRVDLLLSETGLLADLPLPRG
LVRVDFSAAGAELAAYPSANPPSHVSAADLAYVIYTSGSTGQPKGVAIDHAALGQFCDSA
EVYSRLDAADRVLQFATFSFDGFVEQCYPPLCVGAALIMRGDELWDAGQLAREIVEQGVT
LADLPAAYWYLLAQECVIDRRTLGHLRQVHVGGEAMSVEGLRAWHAAGLGHVRLVNTYGP
TEATVVSSVHDCQLADASDAFGVPIGQAIEGRSLYVLDSGFELLATEGVGELCIGAEYGL
AQGYFERPALTAERFLPDPFCAVPGARLYRSGDLARYNQAGALEYVGRIDHQVKIRGFRI
EIGEIEASLQGVPQVREAAVIAQPGASGAQLVAYVVPADGQCLDTQALAATLQRTLPDYM
VPAQWVVLDALPLNNNGKLDRRALPAPDLNQPPQAYRAPHSALAMELAAIWQAVLQVERV
GLDDHFFERGGHSLLATQVISRVRHDLKLEVPLRALFEQPTLEAFAAACAGMQADTAPAL
RAVGRDRPLALSFAQERQWFLWQLDPTSAAYHVPVALHLRGQLDIAALEQAFHALVQRHE
PLRTSFVEEGEQAWQVIHSQLAIVIDRQCVDTSAIESTVAQEIQRPFDLVNGPLMRVQLL
EIAAEHHVLVITQHHIISDGGSMQVMVDELLALYQGRAPLPVLPLQYADYAVWQREWMAA
GEKRRQLDYWCARLGSEHTLLELPLDHPRPAVQSHRGARRQLHLDAALVAELKALAQRQD
VTLFMLLLAVFQTLLFRYSGQSEIRVGVPIANRNRLETEGLIGFFVNTQVLQAELRGQMG
FDRLLAQVKQRAVEAQAHQDLPFEQLVEALQPERSLSHNPLFQVMFNHQDNLRAGPLQLP
GLDLQPVDWAGHSTQFDLNLETEESPDGLWAGLTYATDLFEPLTIERLAEHWQNLLRAVV
RDASLPVDELALLSAPQSRQMLEAWNHTAFDYPRERCVHQLFEAQALAHPDAIAVQFNDD
ALSYAELNRRANRLAHRLLAAGVGPDVLVAVHVERSLDMAVALLATLKAGGAYVPLDPQF
PAQRLAFMLEDSRARVLLTQPALSGRLAQPQGLQVLLVDDASGDERNPQVNVTAEHLAYV
IYTSGSTGQPKGVMVRHRGLCSFTCGMAASLDIGGEARVLSLTTFSFDIFALELYVPLTV
GATVLLSDQSLALDPEAIIDLAQRQCANVLQATPSTWRMLLDSPRAERLHGIKALCGGEA
LPADLAQRLLDLQGPVWNLYGPTETTIWSAAHRLLAPQPFVGRPIANTALFILNAGLSPC
PLGAAGELLIGGVGLARGYHARPALTAERFVPNPYGAPGERLYRSGDLARYRDHGVVEYI
GRVDHQVKVRGFRIELGEIEACLRQQPGVREAVVLADNDRLIAYLVTSTPHTPQVYQAAL
RQRLPDYMVPAHLMCLDSLPLTPNGKLDRKALPAVDASLSRKGHVAPVTLRQQQVAAIWA
EVLDVAQVGLEDHFFELGGHSLLATRVVSRVRQSLALEVPLKTLFEHPALGDFVAALGEE
GVVAPTLLKADRTRPLPLSYAQERQWFLWQLDPHSAGYHIPSALRLKGRLDLAALQRSFD
TLLARHESLRTHLRQDAGGTWQVIEESGLIDVEQLDNDVAGLKAQVAAEVARPFDLLRGP
LLRVTLLRLADDDHVLVLVQHHIVSDGWSMQLMVEELVQLYAAFSQGRTPQLPALPIQYA
DYALWQRGWMEAGEKERQLAYWRAQLGGVQPVLELPLDYQRPALPSHRGARLGIELPAPL
LADLRRLAQRAGVTLPMVLLASYQALLHRYSGQEDVRVGVPIANRNRLETEGLIGFFVNT
QVLKADIHGQMSVEHLLHQARQRCLEAQAHQDLPFEQLVEALQPERSMSLSPLFQVLFNH
RVTSAERHWQHLAELDVEVLNWDEGVAQFDLALDIEESQTLLRASLSYATDLFAPSTIAR
MAGHWQNLLQAMVVDQQQTIGQLNLLDEDEQRHILQLWNQADAGFPSQRLVHELVADRAR
ENPQAIAVKFDAQTLTYGELDRRANQLAHALIARGIGPEVRVAIAMPRSAESLVAFLAVM
KAGGVYVPLDVEYPRDRLLYMMQDSRAQLLLTHSSALPQLPIPEGLDTLAIDHTETWSRF
SDTAPSVDLDGDNLAYVIYTSGSTGLPKGVAVAHGPLVAHIIATGERYETSPADCELHFM
SFAFDGSHEGWMHPLINGASVLIRDDSLWLPEYTYEQMHRHNVTMAVFPPVYLQQLAEHA
ERDGNPPKVRVYCFGGDAVAQASYDLAWRALKPTYLFNGYGPTETVVTPLLWKARKGDPC
GAVYAPIGTLLGNRSGYILDAQLNLQPIGVAGELYLGGEGVARGYLERPALTAERFVPDP
FGQPGRRVYRSGDLTRGRPDGVVDYLGRVDHQVKIRGFRIELGEIEARLREQDNVGESVV
VAQDGPTGKQLVAYVVPASSAINETEWRDSLRRALKAHLPDYMVPAHFMFLAQMPLTPNG
KLDRKGLPEPDASLMQQAYVAAETELEQQIAAIWAEVLRLPRVGLNDNFFEVGGHSLLAI
QITSRVQAELGLDVPLVEVFQTETLRAYVQAAATFRAGSAEDFDDLRDFLSELEAI

Enzyme Prediction     

No EC number prediction in MGYG000003208_00233.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17649	A_NRPS_PvdJ-like	0.0	4083	4568	1	450	non-ribosomal peptide synthetase. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
cd17646	A_NRPS_AB3403-like	0.0	514	996	1	488	Peptide Synthetase. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
cd19531	LCL_NRPS-like	0.0	52	477	4	426	LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
cd19531	LCL_NRPS-like	0.0	3615	4035	1	426	LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
cd19531	LCL_NRPS-like	0.0	2588	3002	1	426	LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	2062	4631	1	2641
BAY90071.1	0.0	240	3615	315	3305
BAY30132.1	0.0	240	3615	316	3316
BAZ00088.1	0.0	240	3615	316	3314
BAZ75991.1	0.0	240	3615	316	3314

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6P1J_A	3.52e-278	48	996	4	964	Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae],6P1J_B The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae]
6MFZ_A	2.53e-269	3033	4627	202	1773	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
6OYF_A	4.91e-255	52	915	5	873	Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module [Eleftheria terrae],6OZV_A The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with AMP [Eleftheria terrae],6P4U_A The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with Mg and AMP [Eleftheria terrae]
6MFY_A	7.46e-252	3033	4574	202	1719	Crystalstructure of a 5-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis],6MG0_A Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis],6MG0_B Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis]
6P3I_A	2.77e-247	52	915	5	873	Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with Mg [Eleftheria terrae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39847	0.0	1542	3818	5	2294	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
Q04747	0.0	1543	4650	5	3102	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
P94459	0.0	1543	4664	6	3119	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P45745	0.0	2585	4662	5	2117	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
Q0VZ70	0.0	52	2566	25	3057	Chondramide synthase cmdD OS=Chondromyces crocatus OX=52 GN=cmdD PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000069	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003208_00233.