CAZyme Information: MGYG000001031_01706

Basic Information

• Species: CAG-269 sp900556945
• Lineage: Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; CAG-269; CAG-269 sp900556945
• CAZyme ID: MGYG000001031_01706
• CAZy Family: GT2
• CAZyme Description: D-alanine--poly(phosphoribitol) ligase subunit 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1435	MGYG000001031_189|CGC1	166195.6	6.6324

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001031	1736770	MAG	Sweden	Europe

• Gene Location: Start: 7970; End: 12277 Strand: +

Full Sequence      

MKVKGEKMEKDVYELTNAQKSIWNTELFYNGSNINNICGTIHIFEPLDFNILKQTIDLII
AENDNFHANFVIKDGCIYQTFEEYVDYHIDLLEIDSKRDLRKIEKKMKSHIFDILHSDLF
DFKIFKYPDETGGVIVNIHHLISDSWTLGLIAKDIIKKYYHISHSIPMESNKTSYIDYIN
YEKKYLTSHKFEKDKEFWQTYLENRPDCITIPTFQTEKKQDFSFQAKRKIFHLPSSLVGK
MNDFCRSYNLSLFNLLIAVYSIYIGRINQSNDFILGTPILNRTSVAQKDTMGMFINTIPV
RIKIEDTSNFTNFASKIATNFTSIYRHQKYSYQNILENVRKEDSKVPNLYQILLSYQITK
IKTEDDMQYTSEWSFNGSISDDFDIHFFDLNDSGSINIAYDYKLSKYTETSVRQFHARVL
YILSQVLKKPEIALKDISITTPKELKEILSFSEKSDCSYPSNKTISQLFEEQVKLTPNHI
AIRYKNSFMTYEELNKKANQVAYFLRNLGVQPNDVIAIRLNKSLEMVVGILGILKAGGCY
LPIDLSYPQERVSFMLKDSSAKIFLTNHLHQKDLEIPIDCYLLDNVNSNPIYQNDTTDLP
CLNSPEDLIYIIYTSGSTGIPKGVMLCHRNVVRLIKNSQFQFNFDENDVWTMFHSVAFDF
SVWELYGSLLYGGKLILVPETTAKDPNQFLQLLRSEKVTVLNQTPTYFYNLLDRELLNKD
SSLCIRYLIFGGEALKPILVRPWKEKYPFTKIINMYGITETTVHVTFKELSDTDLLSSDS
NIGKPIPTLKVYVMDQYLHILPYGVEGEMCISGLGVCKGYLNRPELNKDRFVKNPYCPDE
ILYHSADDAILDSNGDLYYMGRIDNQVKIRGFRIEIGEIESKLLKHPHIHKCVVLPKKNG
DTDSYLVAYVVMDKKEAVDDLKTYISKLVPEYMVPNFFVFLDKLPLTSNGKVDRKALLAM
EVKVEKKKKYVAPRNDFERTFQAVLEDAMHINSIGIDDNILELGADSLTLMKITIELLEK
NYIVNIQDIYELKTIREISDNFYYPKKSNVYKRTISDNIFYPFQEDFSSDQLTVKNILLT
GATGYLGIHLLNELMKKTDSHVYCVVRYKNGKDSKERLLHKLSFYFGTSMLQYVDSRIHV
LVADITLPKLGLSDEDYNKLGEKIDLVIHSAAIVDHYGNKDLFELINVTGTNHIIDFCKD
FSIYMNHISTTSVSASLPDGEKPTIFDEHALYVGQNYSDNIYIKTKFEAEYNILQAILHS
DLKASIYRIGNICARYSDAKFQENDDKNAFLNRIITLSKLDKIAKSFSDFEIDLSPVDTC
ASIISSFVMFTNSYPKIFHIYHNHALKLIDLINQLRPEKNKIEVVPDDEFYSYIKNKSDI
LGIINDLTSKSSYHTNIIMKNDFTINYMKNMNLSWPTIDQNYINKFFKKYINKGD

Enzyme Prediction     

No EC number prediction in MGYG000001031_01706.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd05930	A_NRPS	0.0	477	957	1	444	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.
cd17643	A_NRPS_Cytc1-like	0.0	477	957	1	450	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.
PRK12467	PRK12467	0.0	15	1039	1119	2160	peptide synthase; Provisional
PRK12467	PRK12467	9.82e-180	36	1013	73	1067	peptide synthase; Provisional
cd12117	A_NRPS_Srf_like	1.06e-175	467	957	1	483	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAZ00088.1	3.31e-165	172	1039	287	1175
BAZ75991.1	3.31e-165	172	1039	287	1175
BAY30132.1	1.48e-164	172	1039	287	1177
BAY90071.1	1.20e-163	192	1039	312	1174
QND46664.1	1.41e-127	12	1029	1614	2649

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	1.02e-134	36	1039	809	1794	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
2VSQ_A	3.92e-131	40	1011	40	1007	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
1AMU_A	2.20e-124	444	989	20	555	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]
6N8E_A	9.61e-122	11	1040	28	1064	Crystalstructure of holo-ObiF1, a five domain nonribosomal peptide synthetase from Burkholderia diffusa [Burkholderia diffusa]
6P1J_A	3.62e-120	11	957	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39846	1.46e-181	9	1039	1052	2073	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
P0C064	7.19e-163	11	1049	3140	4167	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P45745	1.15e-155	15	1040	1053	2105	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
P0C063	1.06e-154	9	1011	1058	2045	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
Q70LM4	4.93e-154	5	1434	3631	5075	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
1.000069	0.000004	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001031_01706.