CAZyme Information: MGYG000004255_00012

Basic Information

• Species: Amulumruptor sp900547825
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Amulumruptor; Amulumruptor sp900547825
• CAZyme ID: MGYG000004255_00012
• CAZy Family: GT2
• CAZyme Description: Gramicidin S synthase 2

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2422	MGYG000004255_1|CGC1	266372.45	4.7733

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004255	2427013	MAG	China	Asia

• Gene Location: Start: 11793; End: 19061 Strand: +

Full Sequence      

MTPLSQTQIGIYIESLRNEGQNIYHTPHLALMHGVDDPERLVKAVQAVVAAFPSISARVK
VDDNGTPVLIDASSTGPVEVQLTRTTEEKLMLTRNELIKPFELDGGTLAHINVIATEKHV
YLFTDFHHSIFDGHSHKLFLKAVDAAYVGKDLEKENVTIYEVARREKEARSSDALDRCRA
EYAEMLGGADTELEIMPDTAGVEEGYATLSVPVGIAGKDYKEFCRRMEMPSSVPAVAAMG
LVLSSFCNKEDVVFSTIWHGRKGHEFDRTFGMMVKTIPARVSVGAGESVSSLLRHTARRL
KIARDNGLYSFADVVSEFGINSDFLFAYQGDFLDLPQVGGVPVDDIMLESIATGARITVN
LSIKQGEMSVEVQYRRDLYSSRLINAFVSSLGEILRGMISGNRDTDVRTLRLVPAEDENE
IYTLGRGPEQGGDPQATIPDLFVKAAERYPDNIAVVFRDRRMTYAELDKVTDALAAELKG
RYGVRKESIVGVLIERSELMAVLPLAIMKAGGAYIPLDPHFPEERLMFMAQDAGVKLIIG
DDGLVAEKMPAFSGAVINASEIRDLPAPDFRPAIDTTPDSSMVVLYTSGSTGKPKGVTLE
QHNIVNFCHAYTELTGMSATDIAGAYAAFGFDAHMMDLYPALLSGATVHIFDSEIRLDLT
AMHGYMERERITVMFMTTQIAWQMATLFEFSTLRVLSGGGEKLPPLGPLPYVFFNVYGPT
ECSVLTTAFRLHDTTDGRLIGRPLAGYEVRILDRNLRLLPAGVTGELVIMGAGVGRGYLN
RPELTSEKFIEIDGVKAYRTGDQARWTADGDIEFLGRMDGMVKLRGLRIELGEIEAVAAS
HPDVASFTAAVKEIGGAGNLVGYFTVREGRELTADDLREYMAGELTEFMVPAVIMKLDSM
PLTPNGKVDRRALPVPEMAVEEHVEPATDIEIKVTGIVADILGHADFGVTTGLISVGLTS
LMVMRLAAAIMKNLGVKLTAKQIMSAPTVREIAVAIESAGTDTTARKESSRPRRRYYPLT
ENQRGVYIDWEMNRDALQYNIPQAFRFGPGTDTEALRKAVLKVADAHPGLKTRLSIRGGD
VVQERRDDDIVDVAVTDLAERPTPEFFQSLVKPFDLLSDALFRCGIFRYGSEVYMFMDTH
HIIFDGVSAMVFQQELAKAYAGATLEAEEYTALDYALDQKELVESEEMDKAAQWFDSLIG
ESEPTRYPQNRKPDSDIAGEMGRLRLRIPSEDIKKFCAAGGVTPSNYLLSSFLQLLHRIV
REETVQITTVTNGRSDLRLLNSTGMFVKTLPVVSRCKNPGVSPLEFVRDIQQQFITSTDY
DFYPFTSLVERNGVRPEIMYVFEGGINLGGDDAMKAEKIPLRLDTAKVPLTLLVFEPSEG
EYELVAEYDTSVYNKADMELLLRMMASLNLSLPEVAAVGHAKMVDDDQEHELSALRNGRR
CEVEYESFHGAMEMRADATPDAPALVACDRRMTYREFDEECNRVANALISRGVQRGDRIV
ILLPRRSYLITAIYGTMKAGAAYIPCDPDYPADRIRLITEDSGARYIVTTSDRLGIDPGR
TIDINDLLSGTDTARPAVSIDPEDVAYMIYTSGSTGRPKGVMIPHRAITNYLYGYRKLFF
EDNPDIRTQMLIVTISFDASLVNLGTALTSGHCLVLADEEECKDVVLLSKLMLENQVDSF
DITPSRLDAMLDLPEFRQAVSIAKHINIGGEGFQSSLVTKLYEAGFRGMTVNEYGPTETT
VGSNHAVLQPGGPIVAGRPFMNMSQRIVDAWGSELPVGAVGELYIFGRGVGLGYNKLPEK
TAEAYVTFHGERAYRTGDLARWTPDGEVVILGRIDHQVKIRGLRIELGEIENVARTFPGI
LAAAADVREINKIQHLCLYYTAAAAVDKEALREHLAASLTEYMVPDAYTQIEQMPLTPNG
KTNRKALPEPELAPLNPYVEPEGDLEKEIARVFGDILQRELIGANDDFFAIGGTSISAIK
VVAALVSAGHAITYKNVFACRTPRAIAAMLEGGDRAVSAVPEPASSSVVGESEFAAILNR
NTIDAFRGGERQPIGNVLLTGATGFMGIHMLHELLGNTDSNICCLLRSRQGLSAESRLRT
LLFYYFNDTFDDEFASGRLRVVEGDVTAAVPDAIAECGIDTVINCAANVKHFSAGDDIET
VNVESVRNLAAFCLGTGARLVHVSTVSIAGESVNGVPDPSILLTEKMFDFGQSLSNQYVH
SKYEAERVILENIRDHGLNAKIMRVGNLSARGSDGEFQINSRSNAFMGKLRAYAMLGCAP
YSDLDAPCEFSPIDEVCHAIVLLSTTPVDMTVFQPCNNHRFPLGDVLHILSETGIPVEPV
EAETFEAAKNEAMTETDTDRISALQPLLAYDSGTAGRTAFIRYDSSFTNQILYRLGFRWN
YTSSEYVRQFVKAISSLDYFSI

Enzyme Prediction     

No EC number prediction in MGYG000004255_00012.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK05691	PRK05691	0.0	100	2008	780	2773	peptide synthase; Validated
PRK12467	PRK12467	0.0	54	2019	102	2172	peptide synthase; Provisional
PRK12316	PRK12316	0.0	99	2013	1659	3625	peptide synthase; Provisional
cd05930	A_NRPS	3.80e-162	450	913	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	5.94e-157	1460	1927	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	3.89e-213	225	1997	792	2649
ACX49739.1	2.72e-146	3	1711	11	1837
BAZ00088.1	2.49e-95	4	1000	2247	3296
BAZ75991.1	2.49e-95	4	1000	2247	3296
BAY30132.1	4.27e-95	24	1000	2269	3298

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	8.20e-243	344	2022	113	1809	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	8.25e-232	344	1931	113	1716	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]
6MFX_A	1.30e-142	344	1406	113	1178	Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFW_A	1.09e-141	344	1406	113	1178	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
5ES5_A	5.68e-113	344	992	111	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	1.44e-253	3	1999	1673	3718	Bacitracin synthase 1 OS=Bacillus licheniformis OX=1402 GN=bacA PE=3 SV=1
P0C064	2.65e-245	3	1982	1063	3093	Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2
P0C063	2.25e-243	3	1982	1063	3094	Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2
Q70LM7	1.13e-237	344	2007	110	1791	Linear gramicidin synthase subunit A OS=Brevibacillus parabrevis OX=54914 GN=lgrA PE=1 SV=1
P39847	2.25e-228	237	1998	257	2061	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC 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
1.000031	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004255_00012.