ID FABG1_BRANA Reviewed; 320 AA. AC Q93X62; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 110. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase 1, chloroplastic; DE EC=1.1.1.100; DE AltName: Full=3-ketoacyl-acyl carrier protein reductase 1; DE AltName: Full=Beta-keto acyl-carrier protein reductase 1; DE Flags: Precursor; GN Name=gbkr1; OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica. OX NCBI_TaxID=3708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Jet neuf; TISSUE=Leaf; RA McDonald F.S., White A.J., Elborough K.M., Slabas A.R.; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP CRYSTALLIZATION. RX PubMed=10666637; DOI=10.1107/s0907444999013918; RA Fisher M., Sedelnikova S.E., Martindale W., Thomas N.C., Simon J.W., RA Slabas A.R., Rafferty J.B.; RT "Crystallization of the NADP-dependent beta-keto acyl-carrier protein RT reductase from Brassica napus."; RL Acta Crystallogr. D 56:86-88(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 77-320. RX PubMed=10801480; DOI=10.1016/s0969-2126(00)00115-5; RA Fisher M., Kroon J.T.M., Martindale W., Stuitje A.R., Slabas A.R., RA Rafferty J.B.; RT "The X-ray structure of Brassica napus beta-keto acyl carrier protein RT reductase and its implications for substrate binding and catalysis."; RL Structure 8:339-347(2000). 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. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}. Note=And non- CC photosynthetic plastids. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. {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; AJ243091; CAC41370.1; -; Genomic_DNA. DR RefSeq; XP_013662543.1; XM_013807089.1. DR PDB; 1EDO; X-ray; 2.30 A; A=77-320. DR PDB; 2CDH; X-ray; 4.20 A; G/H/I/J/K/L=77-320. DR PDBsum; 1EDO; -. DR PDBsum; 2CDH; -. DR AlphaFoldDB; Q93X62; -. DR SMR; Q93X62; -. DR EnsemblPlants; CDY27597; CDY27597; GSBRNA2T00038341001. DR GeneID; 106367337; -. DR Gramene; CDY27597; CDY27597; GSBRNA2T00038341001. DR KEGG; bna:106367337; -. DR OMA; KELLYCH; -. DR OrthoDB; 2263846at2759; -. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; Q93X62; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. 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. PE 1: Evidence at protein level; KW 3D-structure; Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase; Plastid; KW Transit peptide. FT TRANSIT 1..60 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 61..320 FT /note="3-oxoacyl-[acyl-carrier-protein] reductase 1, FT chloroplastic" FT /id="PRO_0000031977" FT ACT_SITE 227 FT /note="Proton acceptor" FT BINDING 82..106 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 214 FT /ligand="substrate" FT STRAND 79..82 FT /evidence="ECO:0007829|PDB:1EDO" FT HELIX 88..99 FT /evidence="ECO:0007829|PDB:1EDO" FT STRAND 103..110 FT /evidence="ECO:0007829|PDB:1EDO" FT HELIX 112..125 FT /evidence="ECO:0007829|PDB:1EDO" FT STRAND 128..133 FT /evidence="ECO:0007829|PDB:1EDO" FT HELIX 139..152 FT /evidence="ECO:0007829|PDB:1EDO" FT STRAND 157..161 FT /evidence="ECO:0007829|PDB:1EDO" FT HELIX 171..173 FT /evidence="ECO:0007829|PDB:1EDO" FT HELIX 176..186 FT /evidence="ECO:0007829|PDB:1EDO" FT HELIX 188..204 FT /evidence="ECO:0007829|PDB:1EDO" FT STRAND 207..212 FT /evidence="ECO:0007829|PDB:1EDO" FT HELIX 216..219 FT /evidence="ECO:0007829|PDB:1EDO" FT HELIX 225..246 FT /evidence="ECO:0007829|PDB:1EDO" FT TURN 247..249 FT /evidence="ECO:0007829|PDB:1EDO" FT STRAND 250..257 FT /evidence="ECO:0007829|PDB:1EDO" FT HELIX 263..266 FT /evidence="ECO:0007829|PDB:1EDO" FT HELIX 270..277 FT /evidence="ECO:0007829|PDB:1EDO" FT HELIX 288..300 FT /evidence="ECO:0007829|PDB:1EDO" FT HELIX 303..306 FT /evidence="ECO:0007829|PDB:1EDO" FT STRAND 311..315 FT /evidence="ECO:0007829|PDB:1EDO" FT TURN 316..319 FT /evidence="ECO:0007829|PDB:1EDO" SQ SEQUENCE 320 AA; 33671 MW; 3D79CEA41AFFBC49 CRC64; MATTVAATKL TSLKAVKKLG FREIRQVRQW SPLQSAMPHF GMLRCGSRQS FATSTVVKAQ ATAVEQSTGE AVPKVESPVV VVTGASRGIG KAIALSLGKA GCKVLVNYAR SAKEAEEVSK QIEAYGGQAI TFGGDVSKEA DVEAMMKTAI DAWGTIDVVV NNAGITRDTL LIRMKKSQWD EVIDLNLTGV FLCTQAATKI MMKKRKGRII NIASVVGLIG NIGQANYAAA KAGVIGFSKT AAREGASRNI NVNVVCPGFI ASDMTAKLGE DMEKKILGTI PLGRYGQPED VAGLVEFLAL SPAASYITGQ AFTIDGGIAI //