CAZyme Information: MGYG000003214_00747

Basic Information

• Species: NSJ-32 sp014384895
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; UBA1390; NSJ-32; NSJ-32 sp014384895
• CAZyme ID: MGYG000003214_00747
• CAZy Family: GT2
• CAZyme Description: D-alanine--poly(phosphoribitol) ligase subunit 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2494		285587.89	5.292

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003214	5745180	MAG	United States	North America

• Gene Location: Start: 20946; End: 28430 Strand: -

Full Sequence      

MNKTKNVVRRAFPPDNRRIDTETDALQEILKFSFDDETSSRILQVTQRNTEACYVLFVSV
IQLLLWQYHGMEDVLLGVYRGDSPSILQACVEMQPEQRFKDYLYAVRDVMRMPKRMPPDV
EESIGVCVAFDDLHAANSQIPLDAWMIRLRVEENRFEAAVQYPGDLYFQNTIWLICHQIQ
ALLIQCLQHPDSPIWELSAQTEWQKNRILSWNRTTVSYDARGGLLSRFLSQVGRNPQNRA
VIDCDGTMSSYEEMDHRSTIVARHLLRCGCRSGDVVAVAMDRQSDLIAVLLGILKAGAVY
LPLDKQNPLQRLQYILCDTDARILVTDVPGIFKSIQEELFVIDTDALKENSNCPELPVIT
TKESDAAYIIYTSGSTGTPKGVIVDHGAIVNRLNWMMHKYQFDTSDCLLQKTNIAFDVSI
WELYLWFFAGASVYMLPPGDEKDAQRIGDAICKHGVTTVHFVPTMFSSFLSYCQQAHVPL
PSLRRVFTSGEALETIHVERFFSLFKNKEVGLYNLYGPTEATVDVSYYDCSPQFFSTDVP
IGGPIENIRLYILDEHYRLAPIGMPGTLYIAGDGLARGYLNRPELTAKQFMTVCSERVYN
TNDRARQTLDGHIHFLGRKDFQVKLNGFRIELDEIQHVLNRSAFVEQSVVIKYEDASPDS
ARLVAYYVPKKENDLPELTDSQADSSRVSEWRLVFNKTYSSHESEDTQDQLFNISGWKSS
YTGEAFSREEMSDWLDNGIRHVRRLPNRHVLEIGCGTGLVLYRLAPSTDSYRASDISETA
VAMLNDTISQDQNLQHVKVDVQAADNPLLYQSLYDMVILNSVIQYFPNHAYLEKVLRLIG
DTIAENGHALIGDIRSEPLLKAFHTSVELSRMPGDTSAPLLKAAVDRGIFMDYELCVNPA
FFMNLRDVHPRMAGVEILYKQSRYDNEMRRYRYDVVIYFDHIPDSWPCDKKLVWGQQSPA
ELEKMVSSQMYNSIRLSHVPNTDVSPELYQYQQLLYDSDEKRIVCDIHAAAARMRQQEAW
SKEQWRKMAEHYGYHMECLWSGPDMDSYYDLVFIRSCEIPNLSHYICRQAKREIVSDFSD
YFNLRYGQADEMWKTNAAIREYLAAYLPSYMIPSILIPLDAMPAKPNGKIDYAALPQPYI
LQNTAEMESPKTQWQRQLLEVWQTVLRLQAIGINDDFFMCGGDSIKAISLVNRINQSLHI
NMHVNDIYMYSTIKKLSQVIDKRLKETSDDTLRKGMEILQNLKERVLSDRYLVSLLPVDW
EDLYPVSPIQMGMFLYTRMYPDVPMYLDQFIYQVKLDSFSYVFFCQCMETMVQKHAIMRT
TFDFTRFPQPLQIVRQGLSLSRLISMEDLRALPDPQTQIRAYLEDDLSNHFELEKDFLWR
IKIFWLGEGAYCIVLSFHHAILDGWSVATFMSELVKLYEIGVKRNFHWEPEPAASTFRDY
IAYTMGRTQSDQDMAYWHEVLDGFHYNALPYNPEKTPLSQMRRTHIVIRDLPNFYQHKLQ
SYAYKNKVSLKELCIAAYVFLLRITSYEHDVLTGIVSHDRPELADAEKIVGCFLNTVPLR
VQINGNNKKDLLYAVRDYLRRSKQHEMFLSDIAKTVQEVGRHVNPLFETIFNYVDFHVLD
SIRLAESVQEIVSPLSLEPNEMTNTPFDFEVSRTMDKFSVRIKYDSRYFHKSEMQECLDM
YLEILDQMMDEHHAEFSCESLKGRARIQADYNSLNNTSSDFPLGGLHTLFERWAAGNPER
IAASDAQHRISYGELNAWANRLARKLVKHGIRPGDIVAIQMQRCIPLIAALLAILKAGAA
YVPLDRKYPLERRAYMIRHAGAVCLLTDKVTGDMTVPVVDMEGLENYESGNLDIPVSENQ
LAYIIYTSGSTGRPKGVMIEHRSAVNIVHWVNEKFAVGPGDKLLFVTSVCFDLSVYDIFG
TLAAGAQVVMAQEEDVLDIGQLFKIMQREKITIWNSVPSTMQGLVHKVKGYGEHSDSLRL
ALLSGDWIPVDLPSKAETIFPHAKFISLGGATEAAIWSIYYEIDPQQVYSPSIPYGRPVA
NSSFYVLNDNRELLAPGYVGELYIGGAGVARGYVNDPQKNMAFMVDPFVNRDAKMYRTGD
LGRLKRDGTIEFLGRKDSQVKIRGFRVELGEIESILCRFPTVKDCVVALQSSPQGDQVLS
AYLVTDSPIDKKRIQDHLANYLPSYMIPVFYMAIDSIPLNVNGKVDRSQLKPVAAAAEKM
PSSSRPLTRTQDKIHDIWKQTLGVDAVDITDSFFEIGGNSLSLLQVQTMLEELYGDKCVT
ITDLFTYHTIEALSKYLDEWLLKENADKVSTSMTLVQEYRMSATDKPQETDLEYVFQLDD
KTQQGLENFASGLESLYSMQIILMGNFIQLMYEICKETHVTLLDGNDLSSCYRWDMAQIQ
TYEDLFDAFQNRSSYRIAAMNLQVDEAVSRQDGCLVSCFVLAENSCEDSQLQGNFELVVG
CGGELRFLFDHRIFCPHNAERIVQDYFKLLSNCL

Enzyme Prediction     

No EC number prediction in MGYG000003214_00747.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK12316	PRK12316	0.0	11	2298	2804	5140	peptide synthase; Provisional
cd05930	A_NRPS	0.0	1738	2210	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	1095	2294	972	2160	peptide synthase; Provisional
cd12114	A_NRPS_TlmIV_like	2.30e-176	1738	2210	1	477	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	8.47e-163	1090	2294	2453	3619	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	1.51e-169	174	2303	960	2668
AXG46165.1	9.01e-126	152	1648	467	1952
AXG41638.1	9.01e-126	152	1648	467	1952
AWK40831.1	9.01e-126	152	1648	467	1952
AFZ04852.1	1.54e-96	1454	2299	321	1185

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	5.54e-161	228	2297	211	1797	Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
6MFY_A	2.16e-147	228	2220	211	1725	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]
7LY7_A	1.65e-137	1290	2270	39	991	ChainA, BmdB, Bacillamide NRPS [Thermoactinomyces vulgaris]
7LY4_E	1.69e-137	1290	2270	39	991	ChainE, BmdB, bacillamide NRPS [Thermoactinomyces vulgaris]
5WMM_A	1.56e-117	189	1137	20	924	Crystalstructure of an adenylation domain interrupted by a methylation domain (AMA4) from nonribosomal peptide synthetase TioS [Micromonospora sp. ML1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9R9I9	3.13e-213	52	2277	66	2334	Mycosubtilin synthase subunit C OS=Bacillus subtilis OX=1423 GN=mycC PE=3 SV=1
Q70LM5	1.07e-201	37	2316	3882	6230	Linear gramicidin synthase subunit C OS=Brevibacillus parabrevis OX=54914 GN=lgrC PE=3 SV=1
Q9R9J0	3.77e-196	33	2324	48	2374	Mycosubtilin synthase subunit B OS=Bacillus subtilis OX=1423 GN=mycB PE=3 SV=1
Q70LM6	1.14e-190	116	2297	1414	3612	Linear gramicidin synthase subunit B OS=Brevibacillus parabrevis OX=54914 GN=lgrB PE=1 SV=1
P94459	2.99e-190	14	2297	1242	3104	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD 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
0.999940	0.000067	0.000000	0.000000	0.000000	0.000002

TMHMM  Annotations     

start	end
53	70