CAZyme Information: MGYG000001514_04162

Basic Information

• Species: Paenibacillus_A ihumii
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A ihumii
• CAZyme ID: MGYG000001514_04162
• CAZy Family: GT2
• CAZyme Description: Plipastatin synthase subunit C

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2517	MGYG000001514_12|CGC49	283954.91	5.1243

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001514	5923787	Isolate	not provided	not provided

• Gene Location: Start: 2923119; End: 2930672 Strand: -

Full Sequence      

MDKSNVLDIYELTPMQKGMLFHAIRDGRDNFYFVQGSAILEGTVDRCVLESSFQAMIDKY
DVLRTAFVHENLQQPVQIVLKKREVSLQYEDITHLSAEEQTHFLAEYKEADREKPFQLAK
DPLIRLHLIKLSSDRYELIWNFHHIVMDGWCWGLVFEDLLETYGRLLNRQQPAPGQPPKY
SSYMKWLQRQDAKESAAFWSDYLSGYEEAAVIPRQQKRQGSEYLHREHIFRLSKETTFRL
AQLAKELQTTLNNVIQTAWAILLYKYNRADDVVFGSVVSGRPPELERVQDIVGLFINTIP
VRVKKEPGQTFSSLVASVHRSSLAAKPYEYSSLADIQANSECGGQLVNHIVVFENYVSSL
DSVRELSSRLGFTFRQGDSVERNNYDFSLIIQPGEELEFNMTYNQEAYTPDFIERLSGHL
RNIVEAVAADRDIEVDRIDIVDDAERRELLAFNPPAADYPRQQTINGLFGEQARRTPDRI
AVVHGAESLTYQQLDEAANRLAREILAQGAKRESIVGILLDRSADMIIAILAALKAGTTY
LPIDPAYPAERIQYMLEDSGAELLLAASGQTAPNSYRGAVISLDGDFWKSGDSSSLEELN
RPDSRAYIIYTSGSTGKPKGVMVEHKNVVRLLFNSDNLFDFNENDVWTMFHSMCFDFSVW
EMYGALLYGGKLVIVPADTARDAREFRALLRSEGVTILNQTPSAFNMLASEEAAHEDHLN
IRKVIFGGEALSPIQLKAWHEKYPSTALINMYGITETTVHVTYKEITKREIDSNVSNIGR
AIPTLQAYVLDERQQLLPIGVPGELYVSGDGVALGYLNRAELTAERFIENPFAPGERMYR
SGDLVKWLPGGEMEYLGRIDHQVKIRGHRIELEEVSAQLLLHEHIRDGIVLARSDGDGIP
YLCAYFVASQTIHTDSLREYMSERLPQYMVPSFFIELDRLPMTPNGKIRRDALPSPADIR
KSATEYAAPQSELELALLGIYQDVLGMADLGVTDHFLRLGGHSLKATMLVSKIRKALGAN
VPVSEVFSNPTVRDLARYIRSEEGLPEMKIIHPAPELPQYPVTSQQKRLYSIQELDPSGV
SYNIPVALEITGALDIPKLEQSLQRLADRHESLRTLLRAEDGRLVQYVADRVETRLALLA
AAPDPAELERIMMEFIRPFELDKAPLFRAGLVQAGPERHILLLDVHHIISDGLSMNILLH
DLFHFYQDKALPVIQVQYKDYAVWQERWAGSPEYAKQEQFWVSRFAGELPILDFPTDYAR
PPVQTFAGDQLGFEVDKASTEELKSLAVQQQATLFMALLAVYHILLAKYSGQRDVIVGTP
LSGRPSEQLDYTTGMFANVVPLRNPLSFDQTFSEYLQNVRNELLKVYQHGDYPLEELVKR
LSLQRDPSRNPLFDTLFTLQDIEEVDIDAGGLKLRELRLGEPAAKFDMTWEIVTGEKLFI
HLCYNTSLFQRATMERLAGHFKSIVAQVLRNPQIAIKDILLATPEEEQILQSFNAARGTT
EHRHSTIVGLFENQARLNPDDTALFWREQSLSYRELNSKANQIANILRRKGVGRNQIVGI
MLPPSPEMIIVMLGILKAGGAYLPIDPTYPAERIHHFLSDSGAGLLFTREGMEDRVVAGQ
QELLLVEDLAFEEEECPNPEHAAAPDDLAYVIYTSGSTGKPKGVMIRHHSVCNLSLVSDT
LGIQRGSRVLQFSSFSFDASVWEIFMTLLRGATLYIEDRNVLLEQGLGSWLKAKRINVAT
LLPSVLRSIPYEELPDLHTLVTGGEACTMDLIEKWAEGRTLINAYGPTEATVCSTLTPVS
RSTKRITIGKPIKNTEAYILNSYRQLQPVGVPGELCIGGAGLAKGYLNRPELTAEKFIDN
PFQPGTQLYRTGDLARWLPNGEIEYLGRMDHQVKIRGYRIELEEISDCLLRHESVREAVV
VPVQQGGTTALAAYYVAVGPIGASELRRHLSEELPEYMIPAYFTPLEQMPLTANGKVDAK
RLPKPQLGSREKIAPRNAQEEQLLKVWQEVLAVDEIGVEDNFFELGGDSIKAIEISAKLN
RSSLRFRIKDIFESPTIAGLSAKLVKQSSGASTAAVEGRVPLTPVQQWVFQLAGHPEHWN
QAIMLEREDSWNVDAVTAAFQSITEHHDALRMIYYPDDHGMIQENQSASGRHFDLECFDF
QGRADAESLIEREADRLQRSIRLEQGPLTKLGVFRTDAGSYLLIIIHHLVVDAVSWRIIM
EDFEYLYGCYEHGETPQLPAKTTSFQAWSEALARYANTADVLEEAEYWSSVISKEVPGLP
AGQNAGTSHTFGDMEEIEVDLTAEETGILVRRAPAAWGTEMNDLLIAAYLRTLNEWCGHT
RFAIDLEGHGRSEFSPDQDLTRTVGWFTSLYPAVYEIPEGNLLSVLKTVRENHRSIPRKG
FGYSILKFLTDPERKEGIDFGFAPEICFNYLGEFQDGLKQEGVRSASIPFGDLIDHSMIW
PYQMELNAHIVNGQLRCALRFNRRRIARGSMDMLASRFRHHLVLLSEHCSEEDLLRI

Enzyme Prediction     

No EC number prediction in MGYG000001514_04162.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd17655	A_NRPS_Bac	0.0	1510	1985	2	489	bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. 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.
PRK05691	PRK05691	0.0	472	2281	18	1937	peptide synthase; Validated
cd17655	A_NRPS_Bac	0.0	468	957	2	490	bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. 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	1060	2086	2647	3686	peptide synthase; Provisional
cd12117	A_NRPS_Srf_like	0.0	1510	1982	2	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
QND46664.1	0.0	4	2067	555	2665
BAY90071.1	2.25e-223	180	2064	299	3283
BAY30132.1	1.32e-219	180	2064	300	3294
BAZ00088.1	1.06e-213	180	2064	300	3292
BAZ75991.1	1.06e-213	180	2064	300	3292

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	0.0	447	2057	184	1790	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	6.42e-318	447	1985	184	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]
2VSQ_A	8.57e-240	3	1056	6	1058	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6MFW_A	1.05e-192	447	1491	184	1210	Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis]
6MFX_A	5.16e-192	447	1491	184	1210	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	0.0	4	2513	5	2531	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
P94459	0.0	40	2513	1086	3574	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P45745	0.0	10	2082	9	2122	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
P39847	0.0	6	2513	7	2526	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
Q04747	0.0	10	2513	1058	3552	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3

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
1.000057	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001514_04162.