FABV_XANOM
ID FABV_XANOM Reviewed; 402 AA.
AC Q2P9J6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000303|PubMed:22039545};
DE Short=ENR {ECO:0000303|PubMed:22039545};
DE EC=1.3.1.9 {ECO:0000269|PubMed:22039545};
DE AltName: Full=Trans-2-enoyl-CoA reductase [NADH] {ECO:0000303|PubMed:22039545};
DE Short=TER {ECO:0000303|PubMed:22039545};
DE EC=1.3.1.44 {ECO:0000269|PubMed:22039545};
GN Name=fabV {ECO:0000303|PubMed:22039545}; OrderedLocusNames=XOO0026;
OS Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=342109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 311018;
RA Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT large numbers of effector genes and insertion sequences to its race
RT diversity.";
RL Jpn. Agric. Res. Q. 39:275-287(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-50; TYR-53; ASP-111;
RP PHE-113; TYR-226; TYR-236; LYS-245; VAL-246 AND THR-276, AND SUBUNIT.
RX PubMed=22039545; DOI=10.1371/journal.pone.0026743;
RA Li H., Zhang X., Bi L., He J., Jiang T.;
RT "Determination of the crystal structure and active residues of FabV, the
RT enoyl-ACP reductase from Xanthomonas oryzae.";
RL PLoS ONE 6:E26743-E26743(2011).
CC -!- FUNCTION: Involved in the final reduction of the elongation cycle of
CC fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-
CC carbon double bond in an enoyl moiety that is covalently linked to an
CC acyl carrier protein (ACP). It can also use crotonyl-CoA.
CC {ECO:0000269|PubMed:22039545}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC Evidence={ECO:0000269|PubMed:22039545};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-CoA + NAD(+) = a (2E)-enoyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:18177, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.1.44;
CC Evidence={ECO:0000269|PubMed:22039545};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.7 uM for NADH {ECO:0000269|PubMed:22039545};
CC KM=293 uM for crotonyl-CoA {ECO:0000269|PubMed:22039545};
CC Note=kcat is 1335 sec(-1) for reductase activity.
CC {ECO:0000269|PubMed:22039545};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22039545}.
CC -!- SIMILARITY: Belongs to the TER reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_01838}.
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DR EMBL; AP008229; BAE66781.1; -; Genomic_DNA.
DR RefSeq; WP_011407173.1; NC_007705.1.
DR PDB; 3S8M; X-ray; 1.60 A; A=1-402.
DR PDBsum; 3S8M; -.
DR AlphaFoldDB; Q2P9J6; -.
DR SMR; Q2P9J6; -.
DR KEGG; xom:XOO0026; -.
DR HOGENOM; CLU_057698_1_0_6; -.
DR OMA; EGCIEQI; -.
DR BRENDA; 1.3.1.9; 6717.
DR UniPathway; UPA00094; -.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IDA:UniProtKB.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050343; F:trans-2-enoyl-CoA reductase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
DR HAMAP; MF_01838; FabV_reductase; 1.
DR InterPro; IPR024906; Eno_Rdtase_FAD-bd_dom.
DR InterPro; IPR024910; Enoyl-CoA_Rdtase_cat_dom.
DR InterPro; IPR010758; Trans-2-enoyl-CoA_reductase.
DR PANTHER; PTHR37480; PTHR37480; 1.
DR Pfam; PF07055; Eno-Rase_FAD_bd; 1.
DR Pfam; PF12242; Eno-Rase_NADH_b; 1.
DR Pfam; PF12241; Enoyl_reductase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase.
FT CHAIN 1..402
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH]"
FT /id="PRO_1000070506"
FT ACT_SITE 236
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 48..53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 74..75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 111..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 140..141
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 245
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 274..276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT SITE 75
FT /note="Plays an important role in discriminating NADH
FT against NADPH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT MUTAGEN 50
FT /note="S->A: Same reductase activity as the wild-type.
FT Restores fatty acid synthesis in the E.coli fabI mutant."
FT /evidence="ECO:0000269|PubMed:22039545"
FT MUTAGEN 53
FT /note="Y->A: Loss of reductase activity. Partially restores
FT fatty acid synthesis in the E.coli fabI mutant."
FT /evidence="ECO:0000269|PubMed:22039545"
FT MUTAGEN 53
FT /note="Y->F: 50-fold decrease of catalytic efficiency.
FT Restores fatty acid synthesis in the E.coli fabI mutant."
FT /evidence="ECO:0000269|PubMed:22039545"
FT MUTAGEN 111
FT /note="D->A: Loss of reductase activity. It is not able to
FT restore fatty acid synthesis in the E.coli fabI mutant."
FT /evidence="ECO:0000269|PubMed:22039545"
FT MUTAGEN 113
FT /note="F->A: Slight decrease of catalytic efficiency.
FT Restores fatty acid synthesis in the E.coli fabI mutant."
FT /evidence="ECO:0000269|PubMed:22039545"
FT MUTAGEN 226
FT /note="Y->F: 50-fold decrease of catalytic efficiency.
FT Restores fatty acid synthesis in the E.coli fabI mutant."
FT /evidence="ECO:0000269|PubMed:22039545"
FT MUTAGEN 236
FT /note="Y->A: Loss of reductase activity. It is not able to
FT restore fatty acid synthesis in the E.coli fabI mutant."
FT /evidence="ECO:0000269|PubMed:22039545"
FT MUTAGEN 236
FT /note="Y->F: Loss of reductase activity. It is not able to
FT restore fatty acid synthesis in the E.coli fabI mutant."
FT /evidence="ECO:0000269|PubMed:22039545"
FT MUTAGEN 245
FT /note="K->A: Loss of reductase activity. It is not able to
FT restore fatty acid synthesis in the E.coli fabI mutant."
FT /evidence="ECO:0000269|PubMed:22039545"
FT MUTAGEN 245
FT /note="K->R: Loss of reductase activity. It is not able to
FT restore fatty acid synthesis in the E.coli fabI mutant."
FT /evidence="ECO:0000269|PubMed:22039545"
FT MUTAGEN 246
FT /note="V->A: Same reductase activity as the wild-type.
FT Restores fatty acid synthesis in the E.coli fabI mutant."
FT /evidence="ECO:0000269|PubMed:22039545"
FT MUTAGEN 276
FT /note="T->A: Loss of reductase activity. Restores fatty
FT acid synthesis in the E.coli fabI mutant."
FT /evidence="ECO:0000269|PubMed:22039545"
FT HELIX 17..33
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:3S8M"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:3S8M"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 215..226
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 239..260
FT /evidence="ECO:0007829|PDB:3S8M"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 284..298
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 305..315
FT /evidence="ECO:0007829|PDB:3S8M"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:3S8M"
FT TURN 337..340
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 342..351
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 360..363
FT /evidence="ECO:0007829|PDB:3S8M"
FT HELIX 366..376
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:3S8M"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:3S8M"
SQ SEQUENCE 402 AA; 43711 MW; FCEEFEA4EED3C351 CRC64;
MIIHPKVRGF ICTTTHPLGC ERNVLEQIAA TRARGVRNDG PKKVLVIGAS SGYGLASRIT
AAFGFGADTL GVFFEKPGTA SKAGTAGWYN SAAFDKHAKA AGLYSKSING DAFSDAARAQ
VIELIKTEMG GQVDLVVYSL ASPVRKLPGS GEVKRSALKP IGQTYTATAI DTNKDTIIQA
SIEPASAQEI EETITVMGGQ DWELWIDALE GAGVLADGAR SVAFSYIGTE ITWPIYWHGA
LGKAKVDLDR TAQRLNARLA KHGGGANVAV LKSVVTQASA AIPVMPLYIS MVYKIMKEKG
LHEGTIEQLD RLFRERLYRQ DGQPAEVDEQ NRLRLDDWEL RDDVQDACKA LWPQVTTENL
FELTDYAGYK HEFLKLFGFG RTDVDYDADV ATDVAFDCIE LA
