CAZyme Information: MGYG000004490_00258

Basic Information

• Species: Muribaculum sp003150235
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Muribaculum; Muribaculum sp003150235
• CAZyme ID: MGYG000004490_00258
• CAZy Family: GT2
• CAZyme Description: Gramicidin S synthase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2427	MGYG000004490_2|CGC2	268657.61	4.7611

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004490	3323418	MAG	Israel	Asia

• Gene Location: Start: 127037; End: 134320 Strand: -

Full Sequence      

MDTTINRSPLSQTQLGIFLDCMRRDVDSYHIPNLFRMGKNIDAERLAEALNKVISKHPVI
YARIETDDDGNPVMYSDKNNFRRVEVEDISDAEFEALRRRLIEPFQIIGGNLSVIRVFRT
ESGVWLFTDYHHVISDGASQTGFLHSCDIAYRGEEPPEEGISGFEVAIREAEGRAGEEYN
AAKRWYEEMFGGTDTEGKVYADVKGDKESYDSRRIFLPLASDELKGGAPLCYAAMGVVLG
AFMHKNEVAYTTVTHGRKGRATDHTFCMMVKTQPVRCVMEKGMTIDGLVRKMKEHLIGCR
RNDLFSFAEVAALTGITSEILFAYQGHFLDIPQIGGEPVVREKLETVSTGIPLNLELLQD
DTHTWIDAEWRSDLYSTELVHTLCHTFAHVLKQMITLPGDTPLDNLSLIDDKDKEAIHEM
CIRKPLGYDMYRPIEECISSTAANQPDNTAIVFEGERISYRDLEKYVSRVAAYLQGIGIK
KGDTVGVMIRRSPLMAVYPLALMRLGVAYMPLDPEFPEERLSFMTGDAGVNVILTSNRLA
NDIMPGFAGRIIDITEIPDADASPAPVDGKLPDDPFVVLYTSGSTGKPKGVTLSRGNLLN
FCHDYIDLVNLTPADHIPAYANFGFDAHMMDIYPTLMAGGELHILNEETRHDLDALHSYI
EENAITVSFFTTQIAYQLATLYEFSTLRCMLTGGEKLPPLQSLPYPFYNVYGPTECSVLT
TYYRAEGDIDGTLIGKPLPGYGLRITDSAMRELPAGVPGELVILGKGVGLGYLNRPDMNR
EKFITLDGERAYRTGDLCRLTPEGDINFLGRMDGMVKLRGLRIELGEIEAVATRHEAVKQ
FAAAVKNISGNEQLVGYYSVKDGFTLAEDELREHMSHGLTEFMIPSILVKLDYLPLTPNG
KVDRKALKTPEITVSDELAAPENDNEREISQLVADIIGHSNFGVTTNLLTVGLTSLLAMR
LVATIAKKRNVKIAAKTVMTNPTVRGLAEEIVRLTGNVAEEIAKPEIRKRKYYPLSENQR
GVFIDWELNREALQYNVPQAITFSGDIDTERLADALRKVTAAHPALLARFVNHNGDIMQQ
RDDNREVNVGIVTLDKAPARDELQQMVKPFNLFEDALFRYTIMTHPEGTTLFLDFHHIVL
DGVSLMVFMNDLRNAYNGDSPLTESYTAFDRAVDEQSLMMSQEGEDAGEWFKTLLEGYES
TIYPHSAIPDSIVPGEMGRITLLIEGDKIDSFCTGNAITPSNYFLSAFMQLLHRLTRNER
IAITTVNNGRDDVRLIDDVGMFVKTLPVVSDISVAKAKVTSPMEAASTIQQQFLTTRGFD
FYPFTAIVEKYGIRPEIMYVYEGGISVDMENNTLAGTPIALGLDTAKVPLTMLVFTPEEG
KYELALEYDAGVYCRADMQRLISMMGTLSQNLADTPLLYGAGLTSAADVALLDMIRDGES
GDCGYESYHGAMEAWADATPEATALIASDRSMTYAEFDREANRIANGLIKRGVHHGDRVV
VLLPRDSRLITTIYGIMKAGAAYIPCDPDYPAERIRLITEDSDARYIVTTASRRDVFPDK
GIDVDELTASDISSRPGIKIAPDDLAYMIYTSGSTGRPKGVKIHHGAITNYLYAYRKDFY
TSQGENEPKVNMLLVTISFDASQVDLGTSLTSGHTLVLANEEECKDAVMLADLMTRTGVD
AFDATPSRLAAMLELPAFREAVSRCRLLNIGGEGFPQSLLKRLRVDAGFKGLIVNEYGPT
ETTVGSNHAILKLGEPVTAGRPFYNYREYIVDPWGAEVPVGVTGELYIAGKGVGKGYHNM
PEKNAESFVQFNGEPAYRTGDLARWTPEGDVEIAGRIDNQVKLRGLRIELGEIESVATTF
PGVKTAAADVRKINNVEHLCLWYETDGVDTDDLKTHLASRLTEYMVPDSYNPLKSMPVTP
NGKIDRRGLPQPIIEAGAEFVEPLPGKEADIAEAFRETLGLERVGALDDFFKIGGTSINA
IKLVAILSGKGIEVSYKEIFTAKTPRGLAGISPVEDTPNKTAATVAGATPRGEYADILEN
NSPESVTEGEPLPIGDVLLTGATGFMGVHMLHRLITSGNGKITCMVRGRGDITGESRLRS
LLFYYFGDTFDELWDTRLSVIDGDVTDKEAFRLLPDCEIDTVINCAANVKHFSAGDDIEK
VNVESVRNLVELCKQRNARLIHVSTVSIAGESVDGVPDPATKLTERDFDLGQNLSNQYVK
SKYDAEKIIFDAIKSDGLVAKIMRVGNLSARVSDGEFQINFRSNAFMGRLKAYLVLGCVP
YSHLDAPCEFSPIDEVCHAIIKLASTPSRMIVFHPCNNHRIPLGDVLDILGRICASPIKE
VEWHDFESRISKMMTEPNADITALQPLLAYQSSAGVTTSFIEYANEYTTQVLYRLGFKWN
YTSWDYVERFIKSIVALDYFSTGDASL

Enzyme Prediction     

No EC number prediction in MGYG000004490_00258.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK05691	PRK05691	0.0	373	2030	1075	2793	peptide synthase; Validated
PRK12316	PRK12316	0.0	9	2030	1558	3640	peptide synthase; Provisional
PRK12467	PRK12467	0.0	7	2030	49	2182	peptide synthase; Provisional
cd05930	A_NRPS	3.00e-153	1460	1929	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.
cd05930	A_NRPS	1.95e-150	446	907	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	3.14e-209	8	2011	564	2661
ACX49739.1	1.14e-127	5	1726	7	1850
AFZ04852.1	8.09e-87	299	1030	459	1221
BAY30132.1	1.38e-85	18	996	2258	3298
BAY90071.1	8.93e-83	18	988	2247	3280

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	2.33e-230	405	2023	177	1808	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	2.58e-217	405	1932	177	1715	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]
6MFW_A	1.22e-132	405	1403	177	1178	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFX_A	1.82e-131	424	1403	201	1178	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
5ES5_A	6.95e-109	405	987	175	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O68006	1.72e-237	9	2029	1673	3746	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
P0C064	1.54e-236	9	2017	1063	3127	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P0C063	2.55e-232	9	2017	1063	3128	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
Q70LM7	1.98e-225	405	2009	174	1791	Linear gramicidin synthase subunit A OS=Brevibacillus parabrevis OX=54914 GN=lgrA PE=1 SV=1
P94459	9.27e-222	9	2023	1058	3115	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
1.000046	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004490_00258.