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CAZyme Information: MGYG000002886_02575

You are here: Home > Sequence: MGYG000002886_02575

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Stenotrophomonas maltophilia
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia
CAZyme ID MGYG000002886_02575
CAZy Family GT2
CAZyme Description Enterobactin synthase component F
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1025 MGYG000002886_132|CGC1 110658.89 6.1797
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002886 4276654 MAG United States North America
Gene Location Start: 32;  End: 3109  Strand: +

Full Sequence      Download help

MGRLGNASAR  VPAMVMNVLP  LRVAAGEGSV  EAFTRGLGRK  LSQGRKHGRY  RGEQLRRDLG60
LVGAQQRLHG  PLVNVQPFYK  PLALAGVQAT  LEVLCTGPVD  DLTLGFRGDG  QSLLDLEIEA120
NPALYSREDV  EAHAARLLHF  VSAALQADDI  AAVPLATPEE  AQQVLQEFNA  TAHALPETTL180
VELLQQGMDR  DPHAPALVFG  DAALDYATLE  ARSFALAAQL  RAMDVGPGSV  VAVALPRSLE240
LVIALVAVLR  AGAAYLPLDL  AHPDERLARI  LASAQPVCVL  AAAEDSARMA  GVPMLAPEQW300
TALSFAAPWA  DPAPSDAAYV  IYTSGSTGEP  KGVVIEHRAI  VNRLLWMREH  YGIRADDRVL360
QKTPATFDVS  VWEFFLPLLC  GATLMVAGPD  AHRDPTELAR  LIRGHGITTA  HFVPSMLDAF420
LAAPASAGLQ  LRRVFTSGEA  LDASLRDRFH  GRVQAELHNL  YGPTEAAVDV  SYWPASAQDR480
SRPVPIGFPV  WNTRLYVLDA  RMQPVPIGVA  GDLYLGGVQL  ARGYLGRDDL  TTERFLADPF540
LPGERIYRTG  DVARWRRDGA  VEYLGRSDHQ  VKLRGLRIEL  GEIEAALREL  PGMERVEVLL600
RQDAPGDARL  VAYVPTALAD  AVMLRSHLAT  RVPDYMVPSA  FVGVDHWPVT  ANGKLDRNAL660
PKPPQLEVAG  LAPRTPLEQE  LALLFAQALG  REAPVAVDAD  FFSLGGDSLS  AVHLLLAIEQ720
RWRCDLGLGA  LFAQPTVAAL  AVRIAEPPAL  ADHALGPVIA  LAATDAAGPT  PLFVLHPAGG780
IAWNYRTLAR  ALQPARPVYG  LQSPALDARQ  PLPSSIEAMA  NDYVQRVVAL  QPKGPVHLLG840
WSVGGILAQA  MAVRLHEIGR  EVGELVLLDA  YPSECWRAEP  EPDAIAALRA  LLAIAGHDPD900
AHPELDSRER  ILAFLRRGGS  ALGSLPDVVL  DGVVRAVTGT  NRLIREHVHQ  PFDGTLVHVR960
AGRDHQARPQ  LQSALWRTHA  RKVQALELPF  LHAELTGRDA  VAQLAPWLSA  RLRQWDEQEE1020
IATCS1025

Enzyme Prediction      help

No EC number prediction in MGYG000002886_02575.

CDD Domains      download full data without filtering help

Created with Snap51102153205256307358410461512563615666717768820871922973181660A_NRPS_AB3403-like192660A_NRPS125872PRK1246711014entF189661A_NRPS_VisG_like
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd17646 A_NRPS_AB3403-like 0.0 181 660 1 488
Peptide Synthetase. 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 0.0 192 660 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.
PRK12467 PRK12467 0.0 125 872 3039 3795
peptide synthase; Provisional
PRK10252 entF 0.0 1 1014 279 1296
enterobactin non-ribosomal peptide synthetase EntF.
cd17651 A_NRPS_VisG_like 6.11e-170 189 661 6 491
similar to adenylation domain of virginiamycin S synthetase. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. 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      help

Created with Snap5110215320525630735841046151256361566671776882087192297316869QND46664.1|GT1114869BAY30132.1|GT2114869BAY90071.1|GT2114869BAZ75991.1|GT2114869BAZ00088.1|GT2
Hit ID E-Value Query Start Query End Hit Start Hit End
QND46664.1 7.47e-136 16 869 1903 2784
BAY30132.1 4.10e-128 114 869 2641 3415
BAY90071.1 7.49e-128 114 869 2630 3404
BAZ75991.1 6.18e-127 114 869 2639 3413
BAZ00088.1 6.18e-127 114 869 2639 3413

PDB Hits      download full data without filtering help

Created with Snap51102153205256307358410461512563615666717768820871922973110145JA1_A1016606P1J_A1567925U89_A1656636EA3_B19376N8E_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
5JA1_A 1.49e-206 1 1014 278 1295
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]
6P1J_A 1.98e-154 101 660 386 964
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 1.04e-143 156 792 2 664
Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1]
6EA3_B 1.13e-135 165 663 39 552
Thermobifidafusca FscH adenylation domain complexed with MbtH-like protein FscK and Ser-AMP [Thermobifida fusca YX]
6N8E_A 6.64e-125 1 937 301 1237
Crystalstructure of holo-ObiF1, a five domain nonribosomal peptide synthetase from Burkholderia diffusa [Burkholderia diffusa]

Swiss-Prot Hits      download full data without filtering help

Created with Snap5110215320525630735841046151256361566671776882087192297311014sp|Q8XBV9|ENTF_ECO5711014sp|P11454|ENTF_ECOLI11014sp|P29698|ENTF_SHIFL641014sp|P45745|DHBF_BACSU163874sp|Q0E7C4|VABF_VIBAN
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8XBV9 1.31e-207 1 1014 276 1293
Enterobactin synthase component F OS=Escherichia coli O157:H7 OX=83334 GN=entF PE=3 SV=1
P11454 7.76e-206 1 1014 276 1293
Enterobactin synthase component F OS=Escherichia coli (strain K12) OX=83333 GN=entF PE=1 SV=3
P29698 3.66e-194 1 1014 276 1281
Enterobactin synthase component F OS=Shigella flexneri OX=623 GN=entF PE=3 SV=2
P45745 4.46e-169 64 1014 1387 2375
Dimodular nonribosomal peptide synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=dhbF PE=1 SV=4
Q0E7C4 4.77e-162 163 874 1968 2704
Vanchrobactin synthase VabF OS=Vibrio anguillarum OX=55601 GN=vabF PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000066 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002886_02575.