FABG_ARATH
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 03-AUG-2022, entry version 172.
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.AT1G24360.1; -.
DR iPTMnet; P33207; -.
DR MetOSite; P33207; -.
DR PaxDb; P33207; -.
DR PRIDE; P33207; -.
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; locus:2024021; AT1G24360.
DR eggNOG; KOG1200; Eukaryota.
DR HOGENOM; CLU_010194_1_3_1; -.
DR InParanoid; P33207; -.
DR OMA; KHMVDAG; -.
DR OrthoDB; 1226147at2759; -.
DR PhylomeDB; P33207; -.
DR BioCyc; ARA:AT1G24360-MON; -.
DR BioCyc; MetaCyc:AT1G24360-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:P33207; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P33207; baseline and differential.
DR Genevisible; P33207; AT.
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:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IGI:TAIR.
DR GO; GO:0030497; P:fatty acid elongation; IBA:GO_Central.
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 PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01830; 3oxo_ACP_reduc; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
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
