CAZyme Information: MGYG000004453_00892

Basic Information

• Species: CAG-269 sp900760175
• Lineage: Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; CAG-269; CAG-269 sp900760175
• CAZyme ID: MGYG000004453_00892
• CAZy Family: GT2
• CAZyme Description: D-alanine--poly(phosphoribitol) ligase subunit 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1431	MGYG000004453_11|CGC1	164965.82	7.0911

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004453	1395523	MAG	Israel	Asia

• Gene Location: Start: 7220; End: 11515 Strand: +

Full Sequence      

MENTFYDLTNAQKSIWNTELFFNGSNINNICGTICLDEPLDFKDLQKALKLIIAENDNFR
TQFTIKDGSIYQSFLDKVDYDVEIVDINTKEDLKKLENTIISRIFDILNSNLFDIKIFRY
PDLTGGVIVNIHHLISDSWTLGLVAKDIVTKYTIVHNKLSNTPNTHSYINYINSEQKYIA
SSKFVKDKEFWLNYLKNRPDCISIPSFSDIPTNTKDLGFKGVRKVFNLDDKIVCKINDFC
KAYNVSMYNFLMAIYSVYIGRINKSEDFILGTPILNRTSSVQKNTMGMFINTVPVRVKPT
EHISFLAFVNNIALNFTSIYRHQKHSYQYILEELRKEDPTTPNLYQVLLSYQITKTTTND
SMKYSCDWNFTGAVADDIDIHFFDLNDSGSLNIAYDYKVCKYTEKDIENIHNRILYMIEQ
VLLNPGISLSEISIATPKELKEILNLAAKNDCAYPSNKTISQLFEDQVNLTPDNIAIKFK
DSFLTYKELNEKANQVAHFLRDLGVQPNDVVALRLNKSLEMVVGILGILKAGGCYLPIDL
SYPQERVSFMLKDSFAKLFLTNKSHEKDFEIPIDTYVLDINSRNEIYKNPTDNLDCVNSP
DDLIYIIYTSGSTGTPKGVMLKHRNVVRLIKNKNFQFDFNENDVWTMFHSVAFDFSVWEL
YGSLLYGSKLILVPELTAKDPNKFLQLLRDEKVSVLNQTPTYFYNLLDRELLNENNDLVV
RYIIYGGEALKPNLVKPWKDKYPFTKIINMYGITETTVHVTFKELSNEDLLSSNSNIGKP
IPTLKVFVMDKNLHILPYGVEGEMCVSGLGVCKGYLNRPELNKDRFVPNPYNPNEILYRS
ADDAYLTPDGDLHYLGRIDNQVKIRGFRVETGEIETKLLRHQNIQKCVVLPKKNGDFDSY
LVAYVVMNEKQPISELKDYISKLVPSYMVPNYFVFLDNLPLTSNGKVDRKKLLDMDVKIE
KKKKYESPRNEFEKTFQDILQHTLNIKQIGIDDNILELGADSLTLMRVTIELLEKNFIVN
IQDIYQFKTIREIADNFYYPKKSNLYKRTIANNVYFKFRDNFSSKKIKANNILLTGSTGY
LGIHILNELITNTNANVYCVIRNKNHKSPEERLSEKLSFYFGNKLLKHLHKRIFVLTADI
TVPQFGLSDEEYSKLGNTIDMVIHSAAYVSHYGDEHLFELINVTGTNNIIDFCSNFSIYL
NHISTTSVSASIPDSEKPVVFDEHCLYVGQNYSDNIYIKTKFEAEYNIWEALQNSNLKAS
VYRLGNISARYSDGKFQENDDKNAFLNRVLTVAKLDKIAKSFSNLKIDLSPVDYCAKIIV
RLCVLSSSYSKVFHIYHNKSLKFIDLINKIKPKNETISEVSDNEFYKYIKNKGDILGIIN
DLTSNSSTYNSNIEMKNKFTINYMKNVDLSWPEINTKYINNFFTKFLPKGD

Enzyme Prediction     

No EC number prediction in MGYG000004453_00892.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK12467	PRK12467	0.0	8	1034	1119	2160	peptide synthase; Provisional
cd17643	A_NRPS_Cytc1-like	0.0	472	952	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	29	1008	73	1067	peptide synthase; Provisional
cd05930	A_NRPS	0.0	472	952	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.
cd12117	A_NRPS_Srf_like	1.73e-179	462	952	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	1.10e-163	190	1034	318	1175
BAZ75991.1	1.10e-163	190	1034	318	1175
BAY30132.1	8.93e-163	190	1034	318	1177
BAY90071.1	5.36e-162	190	1034	317	1174
AFY93865.1	5.13e-125	453	1035	326	927

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	1.08e-135	29	1057	809	1814	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	8.97e-130	33	1006	40	1007	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
5ES5_A	1.38e-124	446	1057	185	776	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]
1AMU_A	5.56e-124	454	984	35	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	1.11e-120	8	1035	32	1064	Crystalstructure of holo-ObiF1, a five domain nonribosomal peptide synthetase from Burkholderia diffusa [Burkholderia diffusa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39846	5.83e-183	6	1034	1056	2073	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
P0C064	1.02e-157	2	1034	1058	2074	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P0C063	1.37e-157	2	1034	1058	2074	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
P45745	5.62e-152	8	1035	1053	2105	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
O30408	5.74e-149	5	1034	2097	3107	Tyrocidine synthase 2 OS=Brevibacillus parabrevis OX=54914 GN=tycB 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
1.000070	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004453_00892.