logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: EPrPVT00000016673-p1

You are here: Home > Sequence: EPrPVT00000016673-p1

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 Phytopythium vexans
Lineage Oomycota; NA; ; Pythiaceae; Phytopythium; Phytopythium vexans
CAZyme ID EPrPVT00000016673-p1
CAZy Family GH13
CAZyme Description Enoyl-[acyl-carrier-protein] reductase [NADH]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
681 73107.32 4.5498
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PvexansDAOMBR484 11991 1223560 34 11957
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC - -

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA17 454 662 4.5e-63 0.8163265306122449
AA17 282 434 4.1e-40 0.5918367346938775

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
187630 ENR_SDR 1.57e-93 9 272 1 250
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR. This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
223696 FabI 1.47e-89 6 272 3 254
Enoyl-[acyl-carrier-protein] reductase (NADH) [Lipid transport and metabolism].
404451 adh_short_C2 5.25e-88 16 269 1 236
Enoyl-(Acyl carrier protein) reductase.
181020 PRK07533 1.39e-83 1 272 2 258
enoyl-[acyl-carrier-protein] reductase FabI.
180949 PRK07370 4.84e-73 7 271 4 256
enoyl-[acyl-carrier-protein] reductase FabI.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.41e-77 445 653 5 219
5.42e-76 445 641 5 200
6.15e-76 445 641 5 200
4.47e-69 467 641 59 233
8.54e-67 472 641 2 163

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.51e-53 7 271 6 255
High resolution structure of Thermus thermophilus enoyl-acyl carrier protein reductase apo-form [Thermus thermophilus HB8],2WYU_B High resolution structure of Thermus thermophilus enoyl-acyl carrier protein reductase apo-form [Thermus thermophilus HB8],2WYU_C High resolution structure of Thermus thermophilus enoyl-acyl carrier protein reductase apo-form [Thermus thermophilus HB8],2WYU_D High resolution structure of Thermus thermophilus enoyl-acyl carrier protein reductase apo-form [Thermus thermophilus HB8],2WYV_A High resolution structure of Thermus thermophilus enoyl-acyl carrier protein reductase NAD-form [Thermus thermophilus HB8],2WYV_B High resolution structure of Thermus thermophilus enoyl-acyl carrier protein reductase NAD-form [Thermus thermophilus HB8],2WYV_C High resolution structure of Thermus thermophilus enoyl-acyl carrier protein reductase NAD-form [Thermus thermophilus HB8],2WYV_D High resolution structure of Thermus thermophilus enoyl-acyl carrier protein reductase NAD-form [Thermus thermophilus HB8],2WYW_A High resolution structure of Thermus thermophilus enoyl-acyl carrier protein reductase NAD and triclosan-form [Thermus thermophilus HB8],2WYW_B High resolution structure of Thermus thermophilus enoyl-acyl carrier protein reductase NAD and triclosan-form [Thermus thermophilus HB8],2WYW_C High resolution structure of Thermus thermophilus enoyl-acyl carrier protein reductase NAD and triclosan-form [Thermus thermophilus HB8],2WYW_D High resolution structure of Thermus thermophilus enoyl-acyl carrier protein reductase NAD and triclosan-form [Thermus thermophilus HB8],2YW9_A Crystal structure of TT0143 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2YW9_B Crystal structure of TT0143 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2YW9_C Crystal structure of TT0143 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2YW9_D Crystal structure of TT0143 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2YW9_E Crystal structure of TT0143 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2YW9_F Crystal structure of TT0143 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2YW9_G Crystal structure of TT0143 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2YW9_H Crystal structure of TT0143 from Thermus thermophilus HB8 [Thermus thermophilus HB8]
3.06e-50 7 267 6 251
Crystal structure of tt0143 from Thermus thermophilus HB8 [Thermus thermophilus],1ULU_B Crystal structure of tt0143 from Thermus thermophilus HB8 [Thermus thermophilus],1ULU_C Crystal structure of tt0143 from Thermus thermophilus HB8 [Thermus thermophilus],1ULU_D Crystal structure of tt0143 from Thermus thermophilus HB8 [Thermus thermophilus]
5.72e-49 7 269 4 253
Crystal Structure of Enoyl-Acyl Carrier Protein Reductase (FabI) from Neisseria meningitidis [Neisseria meningitidis FAM18],4M86_B Crystal Structure of Enoyl-Acyl Carrier Protein Reductase (FabI) from Neisseria meningitidis [Neisseria meningitidis FAM18],4M87_A Crystal Structure of Enoyl-Acyl Carrier Protein Reductase (FabI) from Neisseria meningitidis in complex with NAD+ [Neisseria meningitidis FAM18],4M87_B Crystal Structure of Enoyl-Acyl Carrier Protein Reductase (FabI) from Neisseria meningitidis in complex with NAD+ [Neisseria meningitidis FAM18],4M89_A Crystal Structure of Enoyl-Acyl Carrier Protein Reductase (FabI) from Neisseria meningitidis in complex with NAD+ and Triclosan [Neisseria meningitidis FAM18],4M89_B Crystal Structure of Enoyl-Acyl Carrier Protein Reductase (FabI) from Neisseria meningitidis in complex with NAD+ and Triclosan [Neisseria meningitidis FAM18]
1.13e-48 6 280 18 273
Crystal structure of Enoyl-[acyl-carrier-protein] reductase (NADH) from Aquifex aeolicus VF5 [Aquifex aeolicus VF5],2P91_B Crystal structure of Enoyl-[acyl-carrier-protein] reductase (NADH) from Aquifex aeolicus VF5 [Aquifex aeolicus VF5],2P91_C Crystal structure of Enoyl-[acyl-carrier-protein] reductase (NADH) from Aquifex aeolicus VF5 [Aquifex aeolicus VF5],2P91_D Crystal structure of Enoyl-[acyl-carrier-protein] reductase (NADH) from Aquifex aeolicus VF5 [Aquifex aeolicus VF5]
4.08e-48 7 274 4 262
Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NQZ_B Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NQZ_C Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NQZ_D Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NQZ_E Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NQZ_F Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NQZ_G Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NQZ_H Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NQZ_I Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NQZ_J Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NQZ_K Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NQZ_L Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NQZ_M Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NQZ_N Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NQZ_O Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NQZ_P Crystal Structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in apo form [Pseudomonas aeruginosa PAO1],4NR0_A Crystal structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in complex with NAD+ and triclosan [Pseudomonas aeruginosa PAO1],4NR0_B Crystal structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in complex with NAD+ and triclosan [Pseudomonas aeruginosa PAO1],4NR0_C Crystal structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in complex with NAD+ and triclosan [Pseudomonas aeruginosa PAO1],4NR0_D Crystal structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in complex with NAD+ and triclosan [Pseudomonas aeruginosa PAO1]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.94e-48 7 269 4 253
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI OS=Neisseria meningitidis serogroup B (strain MC58) OX=122586 GN=fabI PE=1 SV=1
3.80e-48 6 280 3 258
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI OS=Aquifex aeolicus (strain VF5) OX=224324 GN=fabI PE=1 SV=2
1.67e-47 7 274 4 262
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=fabI PE=1 SV=1
6.94e-47 7 271 4 256
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI OS=Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) OX=103690 GN=fabI PE=3 SV=2
6.69e-46 7 271 4 256
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=fabI PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000050 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in EPrPVT00000016673-p1.