FABG1_BRANA
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 03-AUG-2022, entry version 103.
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}.
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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; KMPERDY; -.
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 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 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
