FABI2_ORYSJ
ID FABI2_ORYSJ Reviewed; 371 AA.
AC Q6H5J0; A0A0P0XJW8;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] 2, chloroplastic;
DE Short=ENR;
DE EC=1.3.1.9;
DE AltName: Full=NADH-dependent enoyl-ACP reductase;
DE Flags: Precursor;
GN OrderedLocusNames=Os09g0277800, LOC_Os09g10600; ORFNames=P0701E06.10;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Catalyzes the NAD-dependent reduction of a carbon-carbon
CC double bond in an enoyl moiety that is covalently linked to an acyl
CC carrier protein (ACP). Catalyzes the last reduction step in the de novo
CC synthesis cycle of fatty acids. Involved in the elongation cycle of
CC fatty acids which are used in lipid metabolism. Required for normal
CC plant growth (By similarity). {ECO:0000250}.
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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. FabI subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP005594; BAD26009.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF24666.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT07201.1; -; Genomic_DNA.
DR EMBL; AK103141; BAG95916.1; -; mRNA.
DR RefSeq; XP_015610600.1; XM_015755114.1.
DR AlphaFoldDB; Q6H5J0; -.
DR SMR; Q6H5J0; -.
DR STRING; 4530.OS09T0277800-01; -.
DR PaxDb; Q6H5J0; -.
DR PRIDE; Q6H5J0; -.
DR EnsemblPlants; Os09t0277800-01; Os09t0277800-01; Os09g0277800.
DR GeneID; 4346596; -.
DR Gramene; Os09t0277800-01; Os09t0277800-01; Os09g0277800.
DR KEGG; osa:4346596; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_10_0_1; -.
DR InParanoid; Q6H5J0; -.
DR OMA; WMGPAKA; -.
DR OrthoDB; 913128at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR Genevisible; Q6H5J0; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05372; ENR_SDR; 1.
DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43159; PTHR43159; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..371
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH] 2,
FT chloroplastic"
FT /id="PRO_0000420280"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 260
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 151..152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 198..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 298..302
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 371 AA; 39021 MW; 7AEE27D8CBC35E68 CRC64;
MGASVTTGLQ MAAARPCIPA CQRLLGSRAA LPSFGRALST QTGFASCRKT ASAGPFVSLN
HKRFAVRAMS AQGLPIDLRG KRAFIAGVAD DNGYGWAIAK ALAAAGAEIL VGTWVPALNI
FETSLRRGKF DESRKLPDGS LMEITKVYPL DAVFDSPEDV PDDVKANKRY AGSSNWTVKE
VAETVKNDFG TIDILVHSLA NGPEVKNSLL ETSRKGYLAA VSASSYSFIS LLQHFLPIMN
PGGATISLTY IASERTIPGY GGGMSSAKAA LESDTRVLAY EAGRKGKIRV NTISAGPLGS
RAAKAIGFIE KMIEYSYVNA PLQKELLADE VGNTAAFLAS PLASAITGST IYVDNGLNTM
GLALDSPTLS T
