FABI1_ORYSJ
ID FABI1_ORYSJ Reviewed; 375 AA.
AC Q6Z0I4; A0A0P0XEL9;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] 1, chloroplastic;
DE Short=ENR;
DE EC=1.3.1.9;
DE AltName: Full=NADH-dependent enoyl-ACP reductase;
DE Flags: Precursor;
GN OrderedLocusNames=Os08g0327400, LOC_Os08g23810;
GN ORFNames=OSJNBa0049I01.2, P0670E08.13;
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; AP004759; BAD03449.1; -; Genomic_DNA.
DR EMBL; AP005490; BAD03622.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF23471.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT04915.1; -; Genomic_DNA.
DR EMBL; AK070992; BAG92250.1; -; mRNA.
DR RefSeq; XP_015648059.1; XM_015792573.1.
DR RefSeq; XP_015648060.1; XM_015792574.1.
DR AlphaFoldDB; Q6Z0I4; -.
DR SMR; Q6Z0I4; -.
DR STRING; 4530.OS08T0327400-01; -.
DR PaxDb; Q6Z0I4; -.
DR PRIDE; Q6Z0I4; -.
DR EnsemblPlants; Os08t0327400-01; Os08t0327400-01; Os08g0327400.
DR GeneID; 4345286; -.
DR Gramene; Os08t0327400-01; Os08t0327400-01; Os08g0327400.
DR KEGG; osa:4345286; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_10_0_1; -.
DR InParanoid; Q6Z0I4; -.
DR OMA; GILDMIH; -.
DR OrthoDB; 913128at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q6Z0I4; 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..375
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH] 1,
FT chloroplastic"
FT /id="PRO_0000420279"
FT ACT_SITE 254
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 155..156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 202..203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 302..306
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 375 AA; 39131 MW; 9D3F6A953D1AAFB1 CRC64;
MGASAATGMQ MVAARPCISA SQGMLTSRAA VSRIGRALST TTGFATCPRI CYSSPLGSSK
RSGVAIRAMS SESGPQGLPI DLRGKRAFIA GVADDNGYGW AIAKALAAAG AEILVGTWVP
ALNIFETSLR RGKFDESRKL PDGSLMEIVK VYPLDAVYDS PEDVPEDVKG NKRYAGSSNW
TVKEVAESVK NDFGSIDILV HSLANGPEVT KPLLETSRRG YLAALSASSY SFVSLLQHFL
PIMNPGGASI SLTYIASERA IPGYGGGMSS AKAALESDTK VLAFEAGRKG KIRVNTISAG
PLGSRAAKAI GFIEKMIEYS YVNAPLQKEL LADEVGNTAA FLVSPLASAI TGSTVYVDNG
LNTMGLAVDS PTISS
