CAZyme Information: MGYG000001110_01278

Basic Information

• Species: CAG-269 sp000431335
• Lineage: Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; CAG-269; CAG-269 sp000431335
• CAZyme ID: MGYG000001110_01278
• CAZy Family: GT2
• CAZyme Description: D-alanine--poly(phosphoribitol) ligase subunit 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1428	MGYG000001110_75|CGC1	164946.2	7.5171

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001110	1465150	MAG	China	Asia

• Gene Location: Start: 17490; End: 21776 Strand: +

Full Sequence      

MEKDVYELTNAQKSIWNTELFYNGSNINNICGTINIFEPLDINALKEALHLIVAENDNLH
AQFYIKDGCIYQSFKKDLDYNIDVLEISSKTDLRKLERKMRSHIFDILHSDLFDFKIFKY
PDSTGGVVVNIHHLISDSWTLGLIAKNIIKKYYSISHNIPMETNKASYIDYINYEQKYLS
SNKFQKDKEFWQNYLENRPDSITMPTFKKNIKQNFSYKAKRKILHLPSSLIKKMNAFCHT
HNVSLFNLFMAVYSIYIGRVNHSNDFILGTPILNRTSVSQKDTMGMFINTVPARIKIEDN
LDFSTFVSQIATNFTSIYRHQKYSYQNILEDIRKENSKVPNLYQVLLSYQITKIKTDDDI
KYSSEWSFNGSISDDFDIHLFDLNDSGSINIAYDYKISKYTDLDIRQIHSRILYIISQIL
KNPKINLKDILITTPKELKAILALSEKNDCSYPSNKTISQLFEEQVQLTPNNIAIKYNGS
YLTYDELNKKANQVAHFLRNIGIKPNDVVAIRLNKSLEMVVGILGILKAGGCYLPIDLSY
PQERVSFMLKDSSAKIFLTNKLHQKDLNIPIECYLLDNVDSNPIYKNDTINLPCLNSPED
LIYIIYTSGSTGTPKGVMLCHRNVVRLIKNSNFQFDFNQNDVWTMFHSVAFDFSVWELYG
SLLYGSKLILVPEPTAKDPKKFLQLLRDEKVTVLNQTPTYFYNLLDRELLNTDNSLSVRY
IIFGGEALKPNLVRPWKEKYSFTKIINMYGITETTVHVTFKELSDEDLLSSDSNIGKPIP
TLKVYVMDKYLNILPFGVEGEMCVSGLGVCKGYLNRPELNKNRFVKNPYYPDEILYHSAD
NAVLDSNGDLYYMGRIDNQVKIRGFRIEIGEIESKLLKHPHINKCVVLPKKNGDTDSYLV
AYVVMDEKESVDNLKTYISKLVPEYMVPNFFVFLDKLPLTSNGKVDRKALLSMEIKVEKK
KKYIAPRNDFEKTFQSILENSMHIKQIGIDDNILELGADSLTLMKITIELLEENYLVNIQ
DIYELKTIREISDNFYYPKKSNVYKRTISDNIFYNFKEDFSPEKLSVKNILLTGATGYLG
VHILNELMHKTNSTVYCVVRHKNGKDSKERLLNKLSFYFGNSMLQYVDSRIHVLVADISL
PQLGLSNEEYHKLGETIDLVIHSAAIVDHYGNKDLFELINVTGTNHIIDFCKDFSIYMNH
ISTTSISASLPENAKPSIFDEHVLYIGQNYSENIYIKTKFEAEYNILEAILHSDLKASIY
RLGNICARYSDAKFQENDDKNAFLNRVITLSKLDKLANSFSNFKIDLSPVDTCADIISSL
ILLNSSYQKVFHIYNNQEIKLVDLINQLKPENQKIKVVSDEKFYEYIKNKSDILGIINDL
TSKSSYNSNIIMKNDFTINYMKNSHLSWPTIDKNYINKFFKKYINKGD

Enzyme Prediction     

No EC number prediction in MGYG000001110_01278.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17643	A_NRPS_Cytc1-like	0.0	470	950	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.
cd05930	A_NRPS	0.0	470	950	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.
PRK12467	PRK12467	0.0	8	1032	1119	2160	peptide synthase; Provisional
PRK12467	PRK12467	0.0	29	1006	73	1067	peptide synthase; Provisional
cd12117	A_NRPS_Srf_like	3.99e-173	460	950	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	1.35e-160	165	1032	287	1175
BAZ75991.1	1.35e-160	165	1032	287	1175
BAY30132.1	6.56e-159	165	1032	287	1177
BAY90071.1	3.45e-156	190	1032	317	1174
QND46664.1	1.57e-122	5	1022	1614	2649

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VSQ_A	2.39e-130	33	1032	40	1036	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6MFZ_A	9.72e-129	29	1032	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]
1AMU_A	1.44e-124	452	980	35	553	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]
5ES5_A	3.33e-122	428	1031	174	760	Crystalstructure of the initiation module of LgrA in the 'open' and 'closed ' adenylation states [Brevibacillus parabrevis],5ES5_B Crystal structure of the initiation module of LgrA in the 'open' and 'closed ' adenylation states [Brevibacillus parabrevis],5ES8_A Crystal structure of the initiation module of LgrA in the thiolation state [Brevibacillus parabrevis],5ES8_B Crystal structure of the initiation module of LgrA in the thiolation state [Brevibacillus parabrevis],5ES9_A Crystal structure of the LgrA initiation module in the formylation state [Brevibacillus parabrevis],5ES9_B Crystal structure of the LgrA initiation module in the formylation state [Brevibacillus parabrevis]
6MFX_A	2.31e-118	428	1031	176	762	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39846	2.60e-182	2	1032	1052	2073	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
Q70LM4	3.23e-150	3	1427	3636	5075	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1
P45745	6.97e-150	8	1033	1053	2105	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
P27206	1.64e-149	1	1033	1	1040	Surfactin synthase subunit 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAA PE=1 SV=4
P0C064	3.31e-149	2	1199	1058	2261	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 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
1.000040	0.000007	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001110_01278.