ID   FABG_ARATH              Reviewed;         319 AA.
AC   P33207; O04463; Q9FPJ6;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 2.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic;
DE            EC=1.1.1.100;
DE   AltName: Full=3-ketoacyl-acyl carrier protein reductase;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g24360; ORFNames=F21J9.2, F3I6.30;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=1575676; DOI=10.1042/bj2830321;
RA   Slabas A.R., Chase D., Nishida I., Murata N., Sidebottom C.M., Safford R.,
RA   Sheldon P.S., Kekwick R.G.O., Hardie D.G., Mackintosh R.W.;
RT   "Molecular cloning of higher-plant 3-oxoacyl-(acyl carrier protein)
RT   reductase. Sequence identities with the nodG-gene product of the nitrogen-
RT   fixing soil bacterium Rhizobium meliloti.";
RL   Biochem. J. 283:321-326(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-58, CLEAVAGE OF TRANSIT PEPTIDE
RP   [LARGE SCALE ANALYSIS] AFTER LYS-57, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC         + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC         COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid. Note=And non-
CC       photosynthetic plastids.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC00590.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAF97951.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X64464; CAA45794.1; -; mRNA.
DR   EMBL; AC000103; AAF97951.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC002396; AAC00590.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE30522.1; -; Genomic_DNA.
DR   EMBL; AF324985; AAG40337.1; -; mRNA.
DR   EMBL; AY059816; AAL24298.1; -; mRNA.
DR   EMBL; AY081491; AAM10053.1; -; mRNA.
DR   PIR; A86378; A86378.
DR   PIR; S22416; S22416.
DR   PIR; T00667; T00667.
DR   RefSeq; NP_564216.1; NM_102282.4.
DR   AlphaFoldDB; P33207; -.
DR   SMR; P33207; -.
DR   BioGRID; 24291; 16.
DR   STRING; 3702.P33207; -.
DR   iPTMnet; P33207; -.
DR   MetOSite; P33207; -.
DR   PaxDb; 3702-AT1G24360-1; -.
DR   ProteomicsDB; 222314; -.
DR   EnsemblPlants; AT1G24360.1; AT1G24360.1; AT1G24360.
DR   GeneID; 839053; -.
DR   Gramene; AT1G24360.1; AT1G24360.1; AT1G24360.
DR   KEGG; ath:AT1G24360; -.
DR   Araport; AT1G24360; -.
DR   TAIR; AT1G24360; -.
DR   eggNOG; KOG1200; Eukaryota.
DR   HOGENOM; CLU_010194_1_3_1; -.
DR   InParanoid; P33207; -.
DR   OMA; CQKHMVD; -.
DR   OrthoDB; 2263846at2759; -.
DR   PhylomeDB; P33207; -.
DR   BioCyc; ARA:AT1G24360-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G24360-MONOMER; -.
DR   UniPathway; UPA00094; -.
DR   PRO; PR:P33207; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P33207; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IGI:TAIR.
DR   GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IGI:TAIR.
DR   CDD; cd05333; BKR_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR011284; 3oxo_ACP_reduc.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   NCBIfam; TIGR01830; 3oxo_ACP_reduc; 1.
DR   PANTHER; PTHR42879; 3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE; 1.
DR   PANTHER; PTHR42879:SF2; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE FABG; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
DR   Genevisible; P33207; AT.
PE   1: Evidence at protein level;
KW   Acetylation; Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..57
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255, ECO:0007744|PubMed:22223895"
FT   CHAIN           58..319
FT                   /note="3-oxoacyl-[acyl-carrier-protein] reductase,
FT                   chloroplastic"
FT                   /id="PRO_0000031976"
FT   ACT_SITE        226
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         81..105
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         58
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CONFLICT        17
FT                   /note="A -> G (in Ref. 1; CAA45794)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        227..229
FT                   /note="AAA -> TAT (in Ref. 1; CAA45794)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        238..240
FT                   /note="KTA -> ETP (in Ref. 1; CAA45794)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   319 AA;  33548 MW;  755ADDD16F3F69DE CRC64;
     MAAAVAAPRL ISLKAVAKLG FREISQIRQL APLHSAIPHF GMLRCRSRQP FSTSVVKAQA
     TATEQSPGEV VQKVESPVVV ITGASRGIGK AIALALGKAG CKVLVNYARS AKEAEEVAKQ
     IEEYGGQAIT FGGDVSKATD VDAMMKTALD KWGTIDVVVN NAGITRDTLL IRMKQSQWDE
     VIALNLTGVF LCTQAAVKIM MKKKRGRIIN ISSVVGLIGN IGQANYAAAK GGVISFSKTA
     AREGASRNIN VNVVCPGFIA SDMTAELGED MEKKILGTIP LGRYGKAEEV AGLVEFLALS
     PAASYITGQA FTIDGGIAI
//