CAZyme Information: MGYG000002350_02182

Basic Information

• Species: Serratia marcescens_I
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Serratia; Serratia marcescens_I
• CAZyme ID: MGYG000002350_02182
• CAZy Family: GT2
• CAZyme Description: Tyrocidine synthase 3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1241		135815.59	6.1761

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002350	5255807	Isolate	United States	North America

• Gene Location: Start: 861; End: 4586 Strand: -

Full Sequence      

MQVVWRKAELSLRELRLNPAEGEIGSRLTAVFDPRRVRPDLTRAPLLSFVAAQGEEGSWC
VLQQWHHLIGDHSTLAVMQEEINLILAGRGDELAKAPPFRNAVAQARLGVSKAEHEQFFR
TMLADIDEPSLPFGLSDVHGEGRDISTAHLALPHALNQQLRRQARRLGVSLASLCHLAWA
QVLARATGRDEVVFGTVLLGRMQAGDGAERALGLFINTLPLRLDVNEVGAESAVLQAHIR
LSGLLAHEHAPLALAQRCSGVAAGTPLFSALLNYRHNSGEDTALPTGVTLLDSQERTNYP
FVLSVEDGGDSLGLTAQVRQPIEAQRVCGYMAQALSALAQALEQAPQTPVCELEVMPDEE
YALQLCRWNHTAEAYPADTCVHELFEQQARQTPQAIALIQDAQRLSYAQLNARANRLAHR
LIERGVQPGDRVAVRLARSIELVCAQLAVIKAGAAYVPIDPQLPAVRQAWIADDSGACLM
LTDAVGDEGIPQLTVEDREAEGHDGNPALRVSSGATAYIMYTSGSTGTPKGVMTPHQGIT
RLVRNNRYAAFDADDRIAFAANPAFDASTMEVWAALLNGGALVVIAPEVMMEAERLAAEL
QRHRITTLFLTTALFNQYVHSISGALAQLKYLISGGEKEDPGAYARLLQERGPVHLIHAY
GPTETTTFATTARIERAEGEARLPIGKPIGNTRAYLLDARGRPVPMGAVGELHIGGVGVA
LGYLNRPELTAQRFLSDPFNPVGGGRMYRTGDLARYLPDGSLEYQGRCDQQIKLRGFRIE
PGEIEVQLAASPWVREAVVQVCSTEHHPRLVAWIVPTADVDRSALQGQLRAYLSERLPEY
MVPSAYVWLDALPLTANGKLDRRALPEPERAAVGIREYAAPQGETETTLARVWCELLEIG
QIGRHDNFFELGGHSLLAVRLSSQLRQQGITLPVQAIFNHPILAELAERIDRRTAEAPLR
KAVPARSSGSRPPLFFVPTGFGDHSYVFELAKEIDETFPVYAVPWPAVEEKPATMSDMAA
SAVALIREVQPQGPYHLAGYSSGGVLAYAIAEQLQSAGEAVAFLGLIDTLRPVAAMHSPV
QLLLNWVESTQERPDPQFCQQLAELPLPEAIAAVQRAGIKTQREEVADEAALWQQRHHYA
KLVEATLVQPASLKIHLFKAKQEQVSVNSQNAQFQAYWQKIKQAGYCREDASALGWDRLL
PPATVRVSQVNGDHVSMMEHPVHRRELGQHFNLALRELGQA

Enzyme Prediction     

No EC number prediction in MGYG000002350_02182.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd05930	A_NRPS	0.0	393	865	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.
PRK10252	entF	0.0	59	1139	133	1233	enterobactin non-ribosomal peptide synthetase EntF.
PRK12467	PRK12467	0.0	40	1144	2752	3866	peptide synthase; Provisional
PRK12316	PRK12316	0.0	1	955	4169	5144	peptide synthase; Provisional
cd12117	A_NRPS_Srf_like	0.0	383	865	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QND46664.1	2.42e-254	1	965	627	1605
AFZ04852.1	7.40e-133	168	1072	374	1312
BAY90071.1	8.09e-131	146	1072	2457	3408
BAY30132.1	1.72e-120	136	958	340	1189
BAZ75991.1	6.03e-119	169	958	370	1187

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VSQ_A	8.47e-145	1	1085	79	1171	Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6P1J_A	1.40e-135	40	865	108	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]
5U89_A	1.18e-121	358	1004	4	646	Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
5JA1_A	9.12e-114	45	1122	118	1210	EntF,a Terminal Nonribosomal Peptide Synthetase Module Bound to the MbtH-Like Protein YbdZ [Escherichia coli K-12],5JA2_A EntF, a Terminal Nonribosomal Peptide Synthetase Module Bound to the non-Native MbtH-Like Protein PA2412 [Escherichia coli K-12],5T3D_A Crystal structure of holo-EntF a nonribosomal peptide synthetase in the thioester-forming conformation [Escherichia coli K-12]
5ES5_A	1.28e-112	376	955	200	769	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
P0DUV3	0.0	2	1069	4321	5404	Malpicyclin synthetase OS=Mortierella alpina OX=64518 GN=mpcA PE=1 SV=1
P0DUV4	0.0	2	1069	4331	5414	Malpibaldin synthetase OS=Mortierella alpina OX=64518 GN=mpbA PE=1 SV=1
Q70LM5	1.85e-160	1	949	76	1047	Linear gramicidin synthase subunit C OS=Brevibacillus parabrevis OX=54914 GN=lgrC PE=3 SV=1
P45745	2.81e-159	20	1068	1135	2228	Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
O30409	4.12e-155	40	950	3229	4146	Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC 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
1.000032	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002350_02182.