CAZyme Information: MGYG000002963_00940

Basic Information

• Species: Anaerosporobacter mobilis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerosporobacter; Anaerosporobacter mobilis
• CAZyme ID: MGYG000002963_00940
• CAZy Family: GT2
• CAZyme Description: Plipastatin synthase subunit B

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
604		69018.22	5.661

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002963	5077023	MAG	United States	North America

• Gene Location: Start: 222802; End: 224616 Strand: -

Full Sequence      

MRNQENPQKEDLNSLNSIFEKVAERFPDRIAVTDSNIELTYKELSHKSSTLAKYLIHKGV
KSGELLCIYTTRNVNMIIGILGILKAGATYIPIDPKYPSQRIKDIFDVSGAKFCVSDSKM
DLRYISCINILLDCIPESEVNGDKPADLNNEKSLAYVIFTSGSTGKPKGVMVEHKSVIRL
FTKTEEIFHFNEHTVWSLFHSIAFDYSVWEIWGALLFGGKLVIVPRKVALNPESFYNLMQ
KEKISVLSLTPTAFRNFCLAALRKEQRKLEQLEYIVFGGEKLDFEILNPWIKEYGDSKPV
LVNMYGITEVTVHSTWKIISHADVCNNTKSLIGKPISDLQIEIVDSEGQKVSRGKAGRMF
ISGDGVARGYLNREELTAERFFNRTGQDGEPIRWFDTGDIAVEISENEFEYIGRNDRQVK
ISGYRVELEEIEYYLKQFKGVTDCVIVENDQGENGVRLRAFIILDNKENKESILKELRKY
AAEKLPKYMCPSTYTVVDKFPMNINGKFSISELQTIQEPKKDNDISGLKTKEIIYNIWSD
ILGEKEIDEKDSFFYLGGTSFMMIRMMKKIMGIFNIDIGLDDIDEITINSLEAVIERSSD
RKKQ

Enzyme Prediction     

No EC number prediction in MGYG000002963_00940.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17643	A_NRPS_Cytc1-like	0.0	27	507	1	444	similar to adenylation domain of cytotrienin synthetase CytC1. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. 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.
cd05930	A_NRPS	3.96e-160	27	507	1	438	The adenylation domain of nonribosomal peptide synthetases (NRPS). 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.
cd17655	A_NRPS_Bac	1.40e-136	19	507	3	480	bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. 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.
cd12117	A_NRPS_Srf_like	2.58e-134	18	507	2	477	The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C). 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 adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
TIGR01733	AA-adenyl-dom	1.34e-132	40	445	1	408	amino acid adenylation domain. This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAZ75991.1	6.04e-131	19	598	585	1182
BAZ00088.1	6.04e-131	19	598	585	1182
BAY90071.1	2.06e-130	19	598	584	1181
BAY30132.1	9.58e-130	19	598	585	1184
AFY93865.1	2.92e-113	15	578	333	911

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VNQ_A	1.27e-97	13	507	35	527	Co-crystalstructure of NRPS adenylation protein CytC1 with ATP from streptomyces [Streptomyces sp.],3VNR_A Co-crystal structure of NRPS adenylation protein CytC1 with aminobutyric acid and AMP from streptomyces [Streptomyces sp.],3VNS_A Co-crystal structure of NRPS adenylation protein CytC1 with D-valine and AMP from streptomyces [Streptomyces sp.]
6N8E_A	1.39e-97	7	570	473	1046	Crystalstructure of holo-ObiF1, a five domain nonribosomal peptide synthetase from Burkholderia diffusa [Burkholderia diffusa]
5N9W_A	1.63e-93	14	507	19	515	Structureof adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, apo structure [Streptomyces sp.],5N9W_B Structure of adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, apo structure [Streptomyces sp.],5N9X_A Structure of adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, ligand bound structure [Streptomyces sp.],5N9X_B Structure of adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, ligand bound structure [Streptomyces sp.]
1AMU_A	3.80e-84	14	543	40	556	PhenylalanineActivating Domain Of Gramicidin Synthetase 1 In A Complex With Amp And Phenylalanine [Brevibacillus brevis],1AMU_B Phenylalanine Activating Domain Of Gramicidin Synthetase 1 In A Complex With Amp And Phenylalanine [Brevibacillus brevis]
5U89_A	6.94e-83	18	602	29	609	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q52400	2.48e-122	15	570	23	580	Syringomycin synthase SyrB1 OS=Pseudomonas syringae pv. syringae OX=321 GN=syrB1 PE=1 SV=2
P39846	8.05e-118	17	570	1504	2051	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
P45745	1.43e-113	19	599	1520	2111	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
P0C064	7.83e-91	14	580	469	1026	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P0C063	7.83e-91	14	580	469	1026	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2

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
1.000080	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002963_00940.