CAZyme Information: MGYG000001453_04126

Basic Information

• Species: Aneurinibacillus aneurinilyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Aneurinibacillales; Aneurinibacillaceae; Aneurinibacillus; Aneurinibacillus aneurinilyticus
• CAZyme ID: MGYG000001453_04126
• CAZy Family: GT2
• CAZyme Description: D-alanine--poly(phosphoribitol) ligase subunit 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
3032	MGYG000001453_225|CGC1	343810.76	5.2889

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001453	5302959	Isolate	not provided	not provided

• Gene Location: Start: 24210; End: 33308 Strand: -

Full Sequence      

MKRTLNGTQSSTYISSLSYEEVRAQIKAVLPSPVEFDDDQNLIELGLDSLQMMRLVNKWR
RDGSTVTFAELITAPRLSEWWPLLNKDNTANSGADECTKGIERYENVQGPFPLTDVQYAY
WIGRRDDQPLGGVGCHAYLEIDGKDVEPERLRAAWEQLLMHHSMLRASFLADGQQEVLDF
PFTKAVPVHDLRLYMEDELTLELDRIRNRLSHRRLAVEAGEVAGLELSLLPGGRTRLHFD
IDLLVADVQSLHIILRDLAAAYARGCRPAAPLNWSFAEYVEQEARRRISDKKRAAQYWSE
RLSTMPAAPGLPLKEKPETIKTPIFNRRNYFIKRADWILLQKRAAAYRVTPAMVLLTAYA
EVLDRWSTNSQFLINMPLFDRQTGKAGIEDVVADFTNLLLLAVDCSSQQSFLERVRSVQA
QFHQDVAHAAYSGVQLQRDLARVRQGERDFAPVVFACNLGTLLINDECRNTLGKLSYMIS
QTPQVWLDFQTYEMDDGLLLAWDAIDQLFPDGMIDQMFTAYIQLMNWLVADNNDWQSSPN
ILLASKQKSRDMAAEWSPSQPAQCLHTSFFAVAAANPQATALIDSYSNTYFSYGELSSYA
LRVAAFLKEEGVKEGDPVAITLPRGIEQIAAVLGILAIGACYVPIGIEQPTARRERIHKK
ADIRYVLTDYERAQTLDWPANTVVLHIADAANIAPLAEPVEISAEHLAYIIFTSGSTGEP
KGVEISHSGAWNTISDINRRYKVGSADRILAVSSLDFDLSVYDIFGLLSAGGSLVLMTED
TRRDAVHWLKLLNKHEVTLWNSVPVLLDMLLTVAESGRHNMLPLRLTMLSGDWIGLDLPS
RLKRVAEHSHLVAMGGATEASIWSNFFDVALPLPVQWKSIPYGRPLANQVYRVVDRKGRD
CPDWVAGELWIGGAGVARGYRGDPELTADRFVSWNGSLWYRTGDLGRYWPDGNIEFLGRE
DFQVKIRGHRIELGEIETALRQHPGVRDAVVSVVGDPRGNKHLVGYVVPVRESELSLFDS
ENIDLERAKDFWAGLVSTGRKQVRQAMPQGINFEDFSVFWEYIERLSVCYICRTLKKAGA
ILPPGERYTLETLMHRCGIQHRYRELIKQWLGILEGEGLLRKEEIDTFVNISILPTELFE
MLKESRAYPAWEQYTQGLLRYLQQLDNVNMNLLTGDIEPLEFFFSDDLSLSPTDLMQTLP
GVDYRNSIARRIMETIAHGFPRSGPIRILEVGSRSGDLTESLLSLLTPDRAIYTYTDNST
FFTNAAKNKFKNYSFVQYQLLDIDQNPQAQGYDTHCYDVIIASDSLHRARNIETALAHTQ
SLLAPGGLLILLEMTRNSRLQQISTGFLEEGFTRFEDKRCAEHLPLLSTETWQNVLQSQK
FAEVASFPEHGDPTSIFGQHVIVAQAPYHIKRFKPEELSVFLNRKLPAYMLPSAFIPLNE
LPLTSNGKVDRQALPTPDNLIKAKSKKVFTAPRTPLESSLAAIWCQSFGMDQVGITDNYF
ELGGDSLLATKLSVMVRKNLGVELSLGSIFERPTIAELAEHVQMLMEKKVETTDSAVCLP
QIVPVPEQRHLSFPLTDIQQAYWVGRSGVYSLGNVATHCYFEIEGTDLNLERINRAWQRL
IDHHEMMRTVIMPDGQHQRILDQVPSYQIKIKDLRGKDPESVEAELKKIREEMSHQVLST
DEWPLFDVRASRFGEQYVRLHISFDNLLFDGWSMFHLLSEWTRLYHNPDISLSSLELSFR
DYVLALERLKESDVYRRDKEYWVNRLPDLPPAPELPLAQNPEAIFEQRFSRLDARLSCQT
WQQLKKRAAEMGLTPSGILLTAYAEVLGVWSKRPRFTINLTQFNRLPLHPQVHDIIGDFT
SLTLLAVDHSSGKTFLERGRNLQQQLWQDLDHPYVGGIQVQRELAKQNGEHHGVAMPVVF
TSALGVDQWSGEDSDEKWLGKLVYNITQTPQVWLDHQVVEQDGELLLIWDAVEGLFPEGL
LADMFEAYCHLLQRLADEEAAWRETVPNLVSVPWLETRIEANHTDAPVSSETLTRLFGKQ
AARQSEHSAIVSPDRTLTYGELSFLSANVAGCLREKGVQSNTLVAVVMEKGWEQAVASLG
ILESGAAYLPIDPAHPEERRWQLLRDGHVRIVLTQSWLDGRLNWPGNVERLFVDRMTLRD
KAMRPLPFAGQPEDLAYVIYTSGSTGLPKGVMIDHRGAVNTIQDVNKRFSVGPKDRILAL
SNLNFDLSVYDIFGILAAGGTIIMPEADKARDPSHWIELMQQEQVTVWNTVPALMQMLLE
YASDRDVVMPQSLRLVLLSGDWIPLDLPDKIKAHFRGVQVIGLGGATEASIWSNLYPIQE
VNPNWKSIPYGRPMVNQRYYVLNEFMGDCPVWVPGQLYIGGIGLAKGYWKDESKTRDKFI
HHPRTGERLYRTGDLGRYLPDGNIEFLGREDFQVKIRGHRIELGEIETTLKRHDGVKDAV
VTVSDESYGEKRLVGYVVLDHQKGSELFETEHVDPAICASRWQAISSTGQLQALRIPDFV
DVEAIRVFMDDAERLSFVYICRTLYNMGIFLYEGEQYSIDELMCRFQIHPRYRTLILHWL
NVLIEEGLLEKNEAGMYLNHHSLYEELPDFTQDGELLVSPRLSKKALALAAFFWRDHSSY
ISLLKGEIDPLELFLTEDSFLTPEGLSQFDLAREYYVNLAREVFSTIVNSHPSDKEIQVL
EIGTRAGSLTEALVSILPMDRGRYLYADESSFFADRARKIFGEMASLEYGLFDMNTTPLQ
QGYEPHYFDVIVADNTLHRTRNIETTLGYLKTMLAPGGFLLLIEATRNNRLMLTTVGFFE
DGFSHLEDERKLNHLPLITAEKWREVLNKQGFSNVVAFPESGQAADRFGRHVIVAQAPET
VRVFKPEILSDAMRRKLPDYMVPTTYVLLDKLPLSANGKVDRKALAELGKERENLPKKTH
VAPFTETQMKIASVWEEILDCNNVGIHDSFFALGGDSLRAIQCINLLRERYQIDLSLQNL
LESSTIHLLAQFIEAGDPETEQLAANYEEGTI

Enzyme Prediction     

No EC number prediction in MGYG000001453_04126.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd19535	Cyc_NRPS	0.0	110	532	1	423	Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family. Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. 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). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, 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 Cyc-domains. 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.
cd19535	Cyc_NRPS	0.0	1573	1999	2	423	Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family. Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. 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). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, 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 Cyc-domains. 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.
cd12114	A_NRPS_TlmIV_like	0.0	577	1012	1	432	The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes. 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 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. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
PRK12316	PRK12316	0.0	39	2478	2537	4998	peptide synthase; Provisional
cd12114	A_NRPS_TlmIV_like	0.0	2046	2482	2	432	The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes. 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 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. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	1.35e-115	1422	2482	1473	2532
BAY90071.1	6.47e-92	1467	2492	2128	3162
BAZ00088.1	5.59e-91	1467	2492	2137	3171
BAZ75991.1	5.59e-91	1467	2492	2137	3171
AXG41638.1	9.43e-90	1573	3013	80	1539

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7EMY_A	3.52e-257	38	1552	35	1431	ChainA, Dihydroaeruginoic acid synthetase [Pseudomonas aeruginosa PAO1],7EMY_B Chain B, Dihydroaeruginoic acid synthetase [Pseudomonas aeruginosa PAO1],7EN1_A Chain A, Dihydroaeruginoic acid synthetase [Pseudomonas aeruginosa PAO1],7EN1_B Chain B, Dihydroaeruginoic acid synthetase [Pseudomonas aeruginosa PAO1],7EN2_A Chain A, Dihydroaeruginoic acid synthetase [Pseudomonas aeruginosa PAO1],7EN2_B Chain B, Dihydroaeruginoic acid synthetase [Pseudomonas aeruginosa PAO1]
6LTA_A	2.27e-219	1559	2478	43	956	ChainA, Nonribosomal peptide synthetase [Streptomyces sp. Sp080513GE-23],6LTB_A Chain A, Nonribosomal peptide synthetase [Streptomyces sp. Sp080513GE-23],6LTC_A Chain A, Nonribosomal peptide synthetase [Streptomyces sp. Sp080513GE-23],6LTD_A Chain A, Nonribosomal peptide synthetase [Streptomyces sp. Sp080513GE-23],6LTD_B Chain B, Nonribosomal peptide synthetase [Streptomyces sp. Sp080513GE-23]
7LY7_A	6.43e-216	1573	2482	11	890	ChainA, BmdB, Bacillamide NRPS [Thermoactinomyces vulgaris]
7LY4_E	6.62e-216	1573	2482	11	890	ChainE, BmdB, bacillamide NRPS [Thermoactinomyces vulgaris]
6MFY_A	6.46e-123	577	2482	219	1670	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P48633	0.0	19	2010	21	1917	High-molecular-weight protein 2 OS=Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) OX=393305 GN=irp2 PE=3 SV=1
G3XCV2	1.19e-256	38	1552	35	1431	Pyochelin synthase PchE OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=pchE PE=1 SV=1
A0A0H2ZGB9	2.28e-256	38	1543	35	1422	Pyochelin synthase PchE OS=Pseudomonas aeruginosa (strain UCBPP-PA14) OX=208963 GN=pchE PE=1 SV=1
Q9HWG4	8.77e-245	1536	2992	35	1457	Pyochelin synthase PchF OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=pchF PE=2 SV=1
A0A0H2ZGJ4	4.31e-244	1536	2992	35	1457	Pyochelin synthase PchF OS=Pseudomonas aeruginosa (strain UCBPP-PA14) OX=208963 GN=pchF 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
1.000057	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001453_04126.