CAZyme Information: MGYG000002490_04136

Basic Information

• Species: Paenibacillus_B thiaminolyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B thiaminolyticus
• CAZyme ID: MGYG000002490_04136
• CAZy Family: GT2
• CAZyme Description: Tyrocidine synthase 3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2132	MGYG000002490_36|CGC10	241614.61	5.0307

Genome Property

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

• Gene Location: Start: 528039; End: 534437 Strand: -

Full Sequence      

MKRDAEIMSKQDSITALFEEQVELHPDAAALVYKDARLTYRELNTRANKLANYLKKSGVK
PDMRVGLYMDRSFEMIIGMLSILKAGGTYVPLDTAYPDRRLLYMLHDASITIVLTQESYF
SRLPDGVKPVCPDLDHAQINDESDANLGESASPEDVAYLMYTSGSTGNPKGVLIPHRGVI
RLTKNISYAELTPQDTMLQFASVSFDAATFEIWGSLLNGATLVIYPFNGLSLDELGQVLR
DYQISTLVLTSAVFHQMIDFRIEDFKGVRQLLVGGDSVSPKHAQLALDVLEDTLLINGYG
PTESTTFACCYTVKKKSAIQHSVPIGRPINDTEVYILNDKQKPVPIGLLGELYVGGKGLA
LGYLNRPEITQDKFIKHPFNTDPEARLYKTGDLMKYLPDGNIEFIGRKDNQVKIRGNRIE
LGEIEAVLSQHKDVREAVVIVHEYEPDDKRLIAYIVGTGDADQWKKHVSEQLPPFMVPSY
FVTMDSLPLTVNGKIDRKALPLPETRAIDDNYIAPRNRTEDLVASIWREILKAERISIHD
SFFDLGGHSLLATQVISRLQDAFHLSIPLRALFDCPTVASLHTRIMEIRQQGKRERTPAI
RPAHNREKLPLSFAQQRLWFLHQLEPNSTAYNIPYMWRLTGAWNANALEAGLNALIQRHE
ILRTVFPNENGQPIQTIEPYRFRTLPVIDLSDLTAAEKDEKINAYTEQEAGITFDLTRGP
LVQAKLLATGQEEYILLCTMHHIISDGWSEDIFLNEWLALYEEAHSGTRAELAALPIQYA
DYALWQREWLTDEVMGQQLEYWNTELSGELPVLQLPIDRPRPAVQSYAGSMHKIVLPPSL
LEKLKAVSRQVNTTLFMTMLAAYQGFLSRYTGQTDILVGSPAANRNIKEIEGLIGFFVNT
LVYRANVQDNPTFKQLLAQVKEKSLQAQENQDVPFEKMVEMLQPERNTSYSPIFQTMFTW
AEMKSAVYHTSSGMLETLDIDHSVSKFDMELSMCESEDGLVANMIYNTDLFNESTIRTMA
GHFENWLQELVNNPDVPIAMLELLSEEERRQIVVEWNHTEAPVPEDTCLHDLFMRQASKT
PEWIAAEMGNDKITYRELDKRSNQLAHYLVSLGVRPNTPVGICMNRSIDLVISLLGIIKA
GGAFLPLDTEMPQARMSKLLESSRTNICISQLEFMELFDQAAHVQCIYPEAEREKIASMP
EALPEQTVKPADLVSIYYTSGSTGNPKGVENHHLGWVNRMLWMQRQHRLEQGESVLQKTT
LTFDDAAVEFFWPLSVGGRISLLEPWLHRDPEAIIKAAIQYQAACIQFVPSMLNMFLDAL
SPEDIQQLHHVKNIVSSGEALLPETAGKFFRKLNCKLHNTWGATEVSIDSTIYTCTPDDA
LDKDCVSIGKPIDNNKIYILDRNLKPVPIGVIGDLYIGGIGLAKGYLYNSEKTKEVFIDS
PFVPGERIYRTGDKGYFQPSGNIKYAGRQDNQIKIRGIRVELGEIEATLSKHPSIREAAV
ISVQNDKSITELAAYIVGEGDIYDWRAFLKEQLPTYMIPTYFVQLDHIPKTTSGKIDRNA
LDLPEMKPISSSIIEPRTIPEELIHSIWCDILQLERVSIQDSFFDMGGHSLLATQVISRM
RTVFGLDIPLRTIFEYTTIEAIASRISEIKQGDETNTRVREISKVTHNTESIFEASHGQK
RQWFHAAFSNQKAVGGVYPIELEGPVDDIFMHKSMGIMIERHRIMRTTIIANEGHLQQQV
HSDLAVPNEYIDLSSLSETDSYQRIRQDLQAALDQPFDLARESFFRMTLYRITPTKHFLI
LSAHHIGFDGWSLDVFMKDLADIYQTMKSGISYDERSKPLDYIDYTLWQQTRLSNGELNR
QRDYWLTQLQQSVDAPLMPRDSHALTYENLGSNELSLNLEPQMAQALHELTRMAGGTLYT
TMLAAINIWLSLITEQDVITVGSTLSGRTQTDLEGIIGPLINPVAMRTDLSGNPTVLEMM
NRTRGTAYGAYENQDYPYNLVVEDQLAAKGRKMNLYSLVFIGQNASDIRIELDGLTYKHC
PLSRFLDEEMIKTYEGSHFVQDDQLDIMLFLFTRSEQLTLTARYNTDVLSANSMNAFMKQ
LEHIIAHMIEDPMQRLSQLNVVEEYDFNELFN

Enzyme Prediction     

No EC number prediction in MGYG000002490_04136.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK05691	PRK05691	0.0	26	2003	23	2060	peptide synthase; Validated
PRK12316	PRK12316	0.0	598	1907	41	1320	peptide synthase; Provisional
PRK10252	entF	0.0	602	1648	1	1047	enterobactin non-ribosomal peptide synthetase EntF.
cd19531	LCL_NRPS-like	0.0	609	1034	2	427	LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity. LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of 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). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, 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. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
PRK12316	PRK12316	0.0	14	1870	2005	3830	peptide synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	0.0	17	1648	1014	2664
BAZ00088.1	2.30e-235	503	1648	2134	3294
BAZ75991.1	2.30e-235	503	1648	2134	3294
BAY30132.1	2.33e-235	515	1648	2144	3296
BAY90071.1	1.32e-232	515	1648	2133	3285

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFZ_A	5.11e-301	17	1643	210	1794	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	7.66e-287	17	1565	210	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]
5U89_A	1.49e-235	11	1053	23	1071	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
6P1J_A	3.17e-234	605	1561	2	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]
6OYF_A	6.50e-209	610	1477	4	873	Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module [Eleftheria terrae],6OZV_A The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with AMP [Eleftheria terrae],6P4U_A The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with Mg and AMP [Eleftheria terrae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39847	0.0	3	1876	455	2292	Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
P94459	0.0	12	2132	463	2520	Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P45745	0.0	13	1646	459	2107	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
Q04747	0.0	13	2124	466	2520	Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
Q9R9J0	0.0	9	2131	3281	5361	Mycosubtilin synthase subunit B OS=Bacillus subtilis OX=1423 GN=mycB PE=3 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
1.000064	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002490_04136.