CAZyme Information: MGYG000002490_02155

Basic Information

• Species: Paenibacillus_B thiaminolyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B thiaminolyticus
• CAZyme ID: MGYG000002490_02155
• CAZy Family: GT2
• CAZyme Description: D-alanine--poly(phosphoribitol) ligase subunit 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
4576	MGYG000002490_23|CGC1	508883.84	4.7812

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002490	6537383	Isolate	Japan	Asia

• Gene Location: Start: 52639; End: 66369 Strand: +

Full Sequence      

MRQRDTSRNPLFDAMLVLQNMDQAELELPGLQLTSYPFESNVAKFDLTLSVSEQENGMRC
SWEYAAMLFERSTIERWAGHFAELLRQSTMNPQVTLGSVGFLTAAEQEQLLTQFNESQQF
NHDNGTAAVLSRGMDMTLHAMFEDQAAKTPERLAVECGEDALTYRELNERANRLARVVRR
YGAGPESLVAVQLERSVNMAIALLAVLKAGAAYLPISPQDPADRVRFLLENSGATLLLSG
TAQEAASCPVLGLDDDRIELESPEALPSSANGDNLAYVIYTSGTSGQPKGVMVEHGSIVH
TLQWKTATYGFNGGRVLHASPFVFDASITHFFGPFVAGATVVMLRDEELSDPAAIISTLA
EQKITHAQFTTGLLAALLEMIGPEQLATVRSVVTGGEKISAALIRKMLTHRQIKFVSEYG
PTENSVVTAALPVSDPRQSHMLGTAIGQTKMYVLDANGQLQPIGVPGELCISGPGLARGY
LNQTELTAERFAASPFALGERIYRTGDLARWLPDGNLEYMGRMDAQVKIRGYRIEPGEIE
AELLRSAQVSEAVVAALPDAAGSMQLCAYVVGGELEPSELRSLLSTTLPAYMVPSFFVRL
EQLPLTANGKIDLKGLPKPDAAMAHAPYVSPRTPAEQALVTVWQQVLGVPRIGIHDSFFE
LGGDSIKAIQAMSRLMQAGYKLDMKDLFRYPAAAQLSDHIAPVSRIAEQGEIQGAVPLTP
IQHWFAERDLADAHHFNQAVMLYRESRFEVEALHLTMKGITEHHDALRMVFTPTADGSYA
AWNRAVDEGECYALEVFDFRQDQIRQNHDRQDPDLQEEREEQAWSRSVEAKARELQAGIS
LETGPLVKLGLFQCGDGDHLLIVIHHLVIDGISWRILLEDLAIAYEQAAEGQDIRLPLKT
DSFQLWSQQLTAYASSPAMEAEREYWSQMAGREQMPLPKDNDQGGDAVENSATLTLQWSR
RETQQLLTQANRAYGTEINDLLLTALGMAIQEWTGSEQVAVNLEGHGRESILPDVDVSRT
VGWFTSAYPVMLDMKADLDLPRRIKLVKETLRSIPHKGVGYGILHYLASPGEDNIRALAP
EISFNYLGQFDQDLQNSGLRISPLSSGDAASRRQKRAATLDFNGMIAGGTLTLNLSYSAE
QYRKKTMQRLAKRLKHHLQEVIRHCAAKESVELTPSDVLQQGMTIEELEALVRRNRPVGD
IENVYALTPMQQGMLFHSRLDPQSGAYVNQMLIALQGEPDPAALEHSWNTVIQRHAVLRT
SVDSGWRDQPLQVVYRSRTLKIAYADLSMKSAAEQERELALLKEEDRKRGFRAESDSLMR
VAVVRTGPESHQLLWSFHHILMDGWCLPLVVKEVLEIYTALCKEEEPQLPRVTEYSEYIR
WLSEQDGQAAAKYWADLLADFEQAGELPRRQRQAQGYEARRVTCSLGRKLTERISQAARE
QGVTVNTLLQTAWGLLLHKYSGTHDAVFGSVVSGRPADLPGVEGMIGLFINTIPVRVKCE
AGDTVARVLQQVQEQALASQAHDYYPLHEIQAQSWKNRELFNHILVFENYPVEEQAGSLG
DAAGLNITGVQAEEQTNYDLNVMILPREEITLHFDYNAQVYERDGIERLQRHLLHIVEQI
AAESSIPVQELELLTTAEREQLLVQFNDTQAAIAEEASIPSLFERQAAQTPDRPAVVCAD
QCLTYRELEEQANRIAQWLRAHGVSAEDRVGVLMNRSPRLIAGLLGIVKAGAAYVPIDPI
LPKERMEAMLRDSGMQVMLTDTAYAEALSIFQETSLRHALCVDDHELLAGYPSEPVGVEI
QPTGSAYVIYTSGTTGTPKGVVVEHGNVVNFISGMIRELPFGTHDSMLCITTVSFDIFAA
ESWVPLSCGMQVVLASEEAQQDAAVLAELLAQHPVQMMQMTPSRLMLLLGDARSAAHLRS
IETLLVGGEAFPYTLYEQLREHTDAAVYNMYGPTETTVWSTFDRLEGEERISIGRPMANT
QAYVLNEALQPQPIGVAGELCIGGAGVARGYWTRPELTAEKFVDSPFVSGERLYRTGDLA
RWLPDGRLEHLGRIDHQVKIRGYRIELGEIEARLLRIPGVNEAVVTAVEMINHAQELCAY
VTGGHPLEAAELRAALALSLPSYMMPAHFVQLEELPLTPNGKVDRRGLPKPAGSPGSGAA
VEYTAPRTDVEAKLAQLWQEVLGVERAGIHDNFFELGGHSLKAMTLVSKIHQALEIELPL
KQLFLSPTVEGLAAALNAADGSTAYHSLSPAGERAHYPMSSAQKRLYFLQQLEGAERSYN
MPVALRLEGELDRERLEEALQAFIARHESLHTSFAVVDGEPVQQVQDEWSFSVSYEEAEE
REVEDLIQAFLRPFVLNEAPLLRATVLRLEETQHLLLMDMHHIISDGTSMNILVAEFVKL
YAGEALVPLKLQYKDYAVWQQEYVLSDAYREQEKYWLDQLSGELPVLQLPTDFARPTLRN
FAGDRVDFKLGRTLSEAVQQLALDTGVTVYMVFLAAYSTLLSRLSGDEEVIVGSPVAGRP
HADLADIMGMFVNTLALRTFPSGQKAFAEYLEEIKQTALDAFEHGEYPFEELVDHVVTQR
DMSRNPLFDAVFVLQNAENSQLNLPDLTVESYPFADAQAKFDLTLMISEGAEGYYGSLEF
ATALFTRDTVERWAGHLTELLDHVTSEPDTTLAEARLVSGSAELNQLMTYSGLPVQDKPR
TTIHRRFEEIAGLYPERTAIVCGDRHLTYAELQLQARLVAARLRREGMRPRAAVAILAER
SIEFVVAVLGIVQAGGVYVPLDPDAPAERHLYILNDCGAEFLLAVPDSSVPASYPGTVIL
LDDGALVNGALEAFEELEALEELEALETLEALERGEANGCSCDDPAYILYTSGTTGRPKG
VLVTHGNVLNLVNNNGYVPFHADHRFAQTGAVSFDAATFEIFGALLHGSSLHPVEKDVLL
DARRMGAFMAEHGITVMFLTTSLFHQLADEDAGLFAGVEHLIMGGEVLSPKHAYAAKEAC
PGLTIWNGYGPTENTTFSTAFAVEETRNKHNIPIGRPIEGTTAYVLSARGQLLPVGVPGE
LCLGGAGVAAGYWNLPELTQENFVPDPWIEGGRMYRTGDLARWLPDGTLEYLGRIDQQVK
IRGYRIELGEIETRLLLHADIRQAAVMTWAERPGSEGLCAYYVSSKRLEPAELRHHLSIA
LPEYMVPAHFVHLSELPLTRNGKLDRKALPEPEETAVSCNEFLPPRSLTEIRLAMLWQDV
LGVQRVGLNDDFFELGGHSLRAMTLVSRIHQKLNAQIKLHDVFQSPTLERMSQVIESSAG
SPYEGLLPAPHQDCYPLSSAQKRMYVLQQLQGEEQTYNMPNIFRLEGPVNRDRINEALQG
LIRRHEVLRTSFEMMEGSPVQIIHDTVEFAVSYTEAKDEEDASKAIRAFYFPFDLTRAPL
LRVGLIRLQEERHLLLFDMHHIISDGVSMSILIKEFGKLYSGESMPSPRLQYKDYSTWQS
SYVTMDGYKKQEVYWLGKYAGELPVLELPLDFPRPPVRSYAGGRVHLELDSRLTGEITQL
AQHSGTTLYMLLLAAYSTLLSRLSGQDDIIVGSPTAGRPHADLADMLGMFVNTLALRTYP
AGEKEFVSYLQEVKESTLDAFVHQDYPFEDLVEKAVTRRDMSRSPLFDVMLVLQNTEQEP
MELEHVRLSAYPYEGLAAKFDLTLTVIEHEKGMSLTFAYAADLFARATIEQWASYFKVLL
EAVVSDPKQRLADLPLLNEEERQRMQAYSQGAWLDMSAGRTLDRWYAEQAARTPDRYAVI
SGERRLTYKELDEQAEHVAELLRDRGVGPDRIVGLVLPPSPEMIVGMLAIWKAGGAYLPI
DPDTNSDRVTYMLENSEAALLLTMSEWESRLHFPVECLSLDRIPARSPDTGTGRMEASRS
LDNLAYVIYTSGSTGKPKGVKVMHRNVAAYAEWFIEEAGIVEEDRTALVSSFAFDLGYTA
VFSALLSGAALHLPGKDTYMDPEKLLEYLIRERITYVKMTPSLFGLLVRSQRFAGHSVND
CIRLVVLGGESINCADVELFFAKYGRAQVMQHYGPTETTIGSIALRMDFEQFHFFRNRPV
LGRPIAGEQVYIVDSAARPVPMGVAGEIAIGGHGVSRGYVNLPNETEERFASQPCASNQR
LYLTRDRGRVLADGTIEYLGRSDHQVKIRGYRVELGEIESRLMQIEKIAEAAVLAIPDAQ
GVLDLCAFVAAEGQMDMTGLREQLRWQLPDYMIPSRFHQLAKLPLTANGKVDRATLAKQQ
ITMPVVQQASYAAPRNALEQALADLWQEVLGIERVGIEDDFFEIGGQSLKLIQVIGKIRR
NLKLDISLRDAFAYTTVSELAQYFEARGSKVEDNEVSVWNPDNGLSLFCFPPIVGYGQVF
MRMAEELQETAAIYAFDFIEAEDVIRHYTNKIQTLQPQGALHLLGYSAGGNLAFEVAKQL
ESEGREVAHLILLDSYPRKSALQAADQAAYAESLQDEISRFIAHVPEADVEEVLHNITQY
KSWVDSIATDGRIQARIHLIQSENVEESPEQYYWKPWTAGDQILYQGSGKHEQMLEGEEA
SKNGSVVRAILHEEVQ

Enzyme Prediction     

No EC number prediction in MGYG000002490_02155.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd12117	A_NRPS_Srf_like	0.0	2705	3209	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.
cd17655	A_NRPS_Bac	0.0	1662	2152	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.
cd19543	DCL_NRPS	0.0	1204	1624	1	423	DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
PRK12316	PRK12316	0.0	2	2244	2934	5147	peptide synthase; Provisional
PRK12316	PRK12316	0.0	3	3724	386	4063	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	1735	4454	1	2784
BAY90071.1	0.0	1358	4454	276	3404
BAY30132.1	0.0	1358	4454	277	3415
BAZ00088.1	8.93e-317	1358	4454	277	3413
BAZ75991.1	8.93e-317	1358	4454	277	3413

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	3.72e-293	2702	4352	206	1805	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	1.16e-271	2702	4256	206	1712	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	1.22e-229	1201	2236	9	1039	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
5U89_A	5.08e-205	1638	2674	6	1058	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
6P1J_A	8.36e-186	2257	3209	6	964	Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae],6P1J_B The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39846	0.0	1201	3495	7	2284	Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
Q04747	0.0	1201	4353	6	3113	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
P94459	0.0	1201	4361	7	3124	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P39847	0.0	1200	3616	6	2406	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
Q70LM4	0.0	3	3296	1393	4673	Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD 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
1.000071	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002490_02155.