CAZyme Information: MGYG000001279_00011

Basic Information

• Species: Pseudomonas_E fulva
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_E; Pseudomonas_E fulva
• CAZyme ID: MGYG000001279_00011
• CAZy Family: GT2
• CAZyme Description: Linear gramicidin synthase subunit B

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
4316	MGYG000001279_1|CGC1	475319.5	5.684

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001279	4682858	MAG	Italy	Europe

• Gene Location: Start: 12643; End: 25593 Strand: -

Full Sequence      

MTHAFELPTSLVQALMQRAAQSPDKIALRFLADAPGEQAVLTYQALDQRARAIAAALQAR
AAFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARQHHQERLLSIIDDAEPRLL
LTVAALQKSLQGLEALQAAQAPELLAVDPLDPAQAAAWREPALQPHDIAFLQYTSGSTAL
PKGVQVTHGNLVANEQLIRHGFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVL
MSPGYFLARPLRWLQAISEYGGTISGGPDFAYRLCSERISKASLAGLDLSRWRVAYSGSE
PIRQDSLATFADTFQVCGFNPQSFFASYGLAEATLFVSGSRRGEGIGALALDAQAFAENR
AEPGEGSVVMSCGWPQPGHAVRIVEPRQRQVLADNEVGEIWAAGPSIAHGYWRNVQASAQ
TFVEMDGQRWLRTGDLGFMRGGEVFVTGRLKDMLIVRGQNLYPQDLEKTLEREVPTLRKG
RVAVFAVEHEGEQAIGVAVEISRNVQKTTAPDALIKTLRHVVADACRQAPAVVLLLNPGA
LPKTSSGKLQRSACRLRMDDGTLDCYARFPQPALPATETVTGEGLQAQIARLWCDILKVE
AVAADDHFMLLGGNSIAATQVTAALADALGIELSLRTLFEAPVLADYTQAVAASLAQGQQ
AGAIDLLPRDRPLPQSLAQNRLWLLWQLQPQSAAYNIPAGLQLRGALDEPALEAALQALV
ERHEALRTVFSEADGQPWQRVLAHLPVNLQRLDLQGQAPEQVDSQREAEACLPFDLQRGP
LLRLTLVHLDEEHHQLWVTLHHVVADGWSLTLLMDELARLYAAYCQGLEPKLAPLGLGYA
DYGNWQRTWLAEGAAERQLAYWRDQLGDAAPVLDLCTDHPRASQRGNHAARLNVKVPAHL
SQPLNALAHQHQCSLFMVLLAGWQALLHRYTGQADIRVGVPNANRSRLQSQGLVGFFINT
QVLRAQVHGRLPFAELLCQVRQATLDAQANQDLPFEQLVEALPQAREQGLFQVMFNHQQR
DLSALRRLPGLLAEELPWHSREAKFDLQLHSEQDHQGRVRLAFDYASELFEQDTVARLAQ
HLLSLFEHVCETPQLPIGEVPLLDEASRARLLDWGQAPAAQPPQLLVEQLNEQARLHPQR
TALAWEGGSLGYAELHQQANRLAHYLRDKGVGPDTCVAIAIERSPQLLVGLLAILKAGGA
YVPLDVDYPAERLAFMLGDCNAGLLLSHSSQLATLPHVQGVGVIALDQLHLDNWPSQPPR
LHLDADNLAYVIYTSGSTGQPKGVGNTHGALAERLQWMQATYALGADDVLMQKAPISFDV
SVWECFWPLITGCKLVLAGAGEHRDPQRIAALVQAHGVTTLHFVPPLLQVFVQEPQAAGC
SSLRRLFSGGEALSAALRDRVLQVLPQVQLHNRYGPTETAINVTHWHCTASDGGHSPMGR
PLGNVLCQVLDDELHLSAPGVPGELYLGGTGLARGYLGRPGLTAERFVPQPGGNGQRLYR
SGDRVRWLVQYPALEYLGRLDHQVKVRGFRVEPEEVQACLLAQAGVEQAVVRVYQDTVGA
QLVGYYSGTAESGPLLAALAEQLPAYMVPAQLMWLAQMPLGPSGKVDRKALPAPVWQQRE
HIEPHSPLQRQVAAIWCEVLGLPQVGLQDDFFALGGHSLLATQIVSRTRQACDVELPLKA
LFDASELGAFCAEVARIQASGERNAQGDIPRVDRRQAVPLSYSQQRMWFLWQMEPNSPAY
NVGGMARLRGTLHVDAFERALHALVVRHETLRTTFPSIEGVPYQCVADDSNLQLAWQDFS
ALPDAARQQRLQQLADQQAHQAFDLESGPLLRACLVKLQEREHVFVLTLHHIVTEGWAMD
IFARELGELYEAFVDDRESPLTPLPVQYLDYSVWQRQWLDSGEGARQLAYWKQRLGQEHP
VLALPTDRPRPAVQSHKGELYRFELDPALVQRVHTFNSQRGLTLFMTMTATLAVLLHRYS
GQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCELDGQMTAAEVLEQVRQAAIEGQSHQ
DLPFEQLVEALHPPRSSAYNPLFQVMCNVQRWAFQQSRTLAGMQVDYLVNDAAATKFDLY
LEVTDLDGRLGCCLTYSQDLFDAPRIARMAAHWQQLLIGLLDQPQQRLCELPMLSSAEQQ
GLVAQLRGEPVSTARHTLHGLFAAQAAEDPQARALTFAGQHLSYAELDQQANRLARALRE
RGVGPQVRVGVALERSLEMVVGLLAVLKAGGAYVPLDPEYPLDRLRYMIEDSQVAVLLSQ
RRLLQDLGPLPEHLACWSLEDDQPTLGAYSEAPLDDVSLAQHPAYLIYTSGSTGKPKGVV
VSHGEFAMHCQAVIQAFGMRSDDCELHFYSINFDAASERLWVPLLCGARVVIRAQGQWGA
DEICQLVREQHVSVLGFTPSYGSQLAQHLAVQGECLPMRLVITGGEALTGEHLQRIRQAF
TPDQLFNAYGPTETVVMPLAALAPQSLAADLGSVPIGRVIGQRTAYILDDDLALLPQGGI
GELYVGGAGLAQGYHDRPGLTAERFVADPFSHTGGRLYRTGDLVRLGQDGLVEYIGRADQ
QVKIRGFRIELGEIESRLQAHADVDEAVVIAVDMQGVRQLVGYLVSQHAAGDPHAQQQLR
EAVKAHAHQHLPDYMVPAHLVLLDSLPLMGNGKLDRRALPLPDLDQARQHYQAPTNDVQA
QLAQVWGEVLNVDQVGVQDNFFELGGDSILSIQVVSRARQVGLQFSPRDLFQHQTIQALA
AIVQPVQVTDSIEQGLRQGSAQLTPIQHWFFDSALAQPQHWNQAVLLQCRVPLDQTRLHT
ALAALVEHHDSLRLRFSDAAGHWQAEYAQPDDQQLLWSATVADLDDCQALYTDLQRSLDL
QRGPLLRALLVSDGEGEQRLALTIHHLVVDGVSWRILLEDLQALYRGQALPAKTHAPGDW
AARLAAYASSDSLRDELGQWQAQVGEVRHELPCDHPQGGNVQRHARTVTIGLDAQQTRQL
LQQAPAAYHTQVNALLLTALARTLCQWTGQPQALVQLEGHGRDGLFEDMDLTRSVGWFTN
AYPLSLSPLAGDDDQARAASIKRIKEQLRQVPHKGLGYGVLRYLADPAAREQMAALAQAR
ITFNYLGQFDQQFDDGALFTPVDAPVGLAHDPDAALPNWLSVDGQVYGGALQLRWTFSRE
RYEPHTIATLANAYRQELVALIDHCLADGQGSYTPSDFPLAHLTQAQIDALPVPANLIED
VYPLTPMQEGMLLHTLLEPGTGLYYMQDRYRISSALDPQRFAQAWQQVVARHEALRASFS
WNSGEAMLQIIHKPGQLAMDYQDWRDLDDADQEARLQALHKQEREAGFDVLHTPPFHLRL
VRVADARYWFMMSNHHILIDAWCRSLLMNDFFEIYQALGEDRQAQLPVPPRYRDYIGWLQ
RQGLDDARAWWQANLAGFERATALPSDRPLRHEHAGSGMVVGDCYTRLAVSEGTRLRELA
QAHQLTVNTFAQAAWALVLARYSGERDVAFGVTVAGRPVSMPQMQRTVGLFINSVVLRVQ
LPAVGQGCTVRQWLQGLLERNMELREYEYLPLVDIQACSELPKGQPLFDSLFVFENAPVE
TAVLDHAKHLDATSDSGRTHTNFPLTAVCYPGDDLGLHLSFDQRYFDYPTVERLLAEFKR
LLLALVQGFDEQVQALPLVGAEEQRFLLQACNDTQRAYPLEQSYVAQFEARVAAHPQRTV
ARCLDAEYDYARLNLAANRLGHALIGAGVRLDQPVALLADRGLPLLGMIVGSFKAGAGYL
PLDPGLPPARLQSILELSRAPVLVCSAACAEQGQALLQALNPGVRPQLLVWETVQTCTMD
SHNPGVHSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALTEHDVIAQTAS
QSFDISVWQFLAAPLFGAQVEIVPNAIAHDPQGLLTHVQATGITVLESVPSLIQGMLASE
HQALDGLRWMLPTGEAMPPELAAQWLQRYPRIGLVNAYGPAECSDDVAFFRVDADSTQGS
YLPIGTPTDNNRLYLLGDEQQLVPLGAVGELCVAGTGVGRGYVGDPARTALAFIPHPYGA
AGERLYRTGDLARQRPDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQPQVRDAAVAVQ
EGVNGKHLVGYLVPHHGVTGDDTVLAQLKARLRAELPEYMVPLHWAWLEALPHNANGKLD
RKALPAIDIGSQHSQAYQAPRSDLEGLLAGIWAEVLKADRVGVHDNFFELGGHSLLATQI
ASRVQKQLQLNVPLRAMFECSTVAELAVYVEGLQGSALNEDKVDRLSDLMAELEGL

Enzyme Prediction     

No EC number prediction in MGYG000001279_00011.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17646	A_NRPS_AB3403-like	0.0	1127	1611	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.
cd17649	A_NRPS_PvdJ-like	0.0	2190	2680	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.
cd19531	LCL_NRPS-like	0.0	672	1093	1	427	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	1717	2144	1	427	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.
PRK12467	PRK12467	0.0	667	4294	40	3676	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	168	2781	75	2680
ACX49739.1	8.97e-215	673	2455	10	1846
BAY30132.1	1.16e-214	17	2763	587	3294
BAY90071.1	2.51e-214	17	2763	586	3283
BAZ00088.1	3.17e-213	17	2763	587	3292

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	1.64e-255	1132	2768	213	1802	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
6P1J_A	3.80e-236	674	1611	7	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]
6MFY_A	3.29e-234	1132	2683	213	1716	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]
6OYF_A	1.74e-220	674	1528	4	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]
6P3I_A	1.29e-214	674	1528	4	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
P45745	0.0	667	2760	1	2104	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
Q0VZ70	0.0	1703	4291	3	3061	Chondramide synthase cmdD OS=Chondromyces crocatus OX=52 GN=cmdD PE=1 SV=1
Q04747	0.0	6	3218	460	3561	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
P94459	0.0	388	3238	792	3600	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
Q70LM4	0.0	672	4291	12	3616	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD 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
1.000039	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001279_00011.