ID FABI_BRANA Reviewed; 385 AA. AC P80030; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 2. DT 04-NOV-2026, entry version 152. DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic; DE EC=1.3.1.9; DE AltName: Full=NADH-dependent enoyl-ACP reductase; DE Flags: Precursor; 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 [MRNA], AND PROTEIN SEQUENCE OF 74-86. RC STRAIN=cv. Rafal; RX PubMed=1912503; DOI=10.1007/bf00037070; RA Kater M.M., Koningstein G.M., Nijkamp H.J., Stuitje A.R.; RT "cDNA cloning and expression of Brassica napus enoyl-acyl carrier protein RT reductase in Escherichia coli."; RL Plant Mol. Biol. 17:895-909(1991). RN [2] RP PROTEIN SEQUENCE OF 74-122; 146-174; 181-193; 250-295; 301-311; 316-346 AND RP 371-385. RC TISSUE=Seed; RX PubMed=1912504; DOI=10.1007/bf00037071; RA Slabas A.R., Cottingham I., Austin A., Fawcett T., Sidebottom C.M.; RT "Amino acid sequence analysis of rape seed (Brassica napus) NADH-enoyl ACP RT reductase."; RL Plant Mol. Biol. 17:911-914(1991). RN [3] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH NAD, AND SUBUNIT. RX PubMed=8535786; DOI=10.1016/s0969-2126(01)00227-1; RA Rafferty J.B., Simon J.W., Baldock C., Artymiuk P.J., Baker P.J., RA Stuitje A.R., Slabas A.R., Rice D.W.; RT "Common themes in redox chemistry emerge from the X-ray structure of RT oilseed rape (Brassica napus) enoyl acyl carrier protein reductase."; RL Structure 3:927-938(1995). RN [4] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH NAD. RX PubMed=10521472; DOI=10.1074/jbc.274.43.30811; RA Roujeinikova A., Sedelnikova S., de Boer G.J., Stuitje A.R., Slabas A.R., RA Rafferty J.B., Rice D.W.; RT "Inhibitor binding studies on enoyl reductase reveal conformational changes RT related to substrate recognition."; RL J. Biol. Chem. 274:30811-30817(1999). RN [5] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH NAD. RX PubMed=10610777; DOI=10.1006/jmbi.1999.3240; RA Roujeinikova A., Levy C.W., Rowsell S., Sedelnikova S., Baker P.J., RA Minshull C.A., Mistry A., Colls J.G., Camble R., Stuitje A.R., Slabas A.R., RA Rafferty J.B., Pauptit R.A., Viner R., Rice D.W.; RT "Crystallographic analysis of triclosan bound to enoyl reductase."; RL J. Mol. Biol. 294:527-535(1999). 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 NADH + H(+); 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 -!- ACTIVITY REGULATION: Inactivated by phenylglyoxal by binding covalently CC to two arginine residues. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10521472, CC ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Seeds and leaves. 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; S60064; AAB20114.2; -; mRNA. DR PIR; S17761; S17761. DR PDB; 1CWU; X-ray; 2.50 A; A/B=85-380. DR PDB; 1D7O; X-ray; 1.90 A; A=84-380. DR PDB; 1ENO; X-ray; 1.90 A; A=74-385. DR PDB; 1ENP; X-ray; 2.60 A; A=74-385. DR SMR; P80030; -. DR OMA; AATRQCV; -. DR BRENDA; 1.3.1.9; 944. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; P80030; -. DR CDD; cd05372; ENR_SDR; 1. DR FunFam; 1.10.8.400:FF:000001; Enoyl-[acyl-carrier-protein] reductase [NADH]; 1. DR FunFam; 3.40.50.720:FF:000192; Enoyl-[acyl-carrier-protein] reductase [NADH]; 1. DR Gene3D; 1.10.8.400; Enoyl acyl carrier protein reductase; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR43159; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE; 1. DR PANTHER; PTHR43159:SF2; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH], CHLOROPLASTIC; 1. DR Pfam; PF13561; adh_short_C2; 1. DR PRINTS; PR00081; GDHRDH. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR NCBIfam; NF004957; PRK06300.1; 1. 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:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR AlphaFoldDB; P80030; -. PE 1: Evidence at protein level; KW 3D-structure; Chloroplast; Direct protein sequencing; KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; NAD; Oxidoreductase; Plastid; Transit peptide. FT TRANSIT 1..73 FT /note="Chloroplast" FT /evidence="ECO:0000269|PubMed:1912503, FT ECO:0000269|PubMed:1912504" FT CHAIN 74..385 FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH], FT chloroplastic" FT /id="PRO_0000031984" FT ACT_SITE 261 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 271 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 98 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10521472, FT ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786" FT BINDING 105 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10521472, FT ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786" FT BINDING 162..163 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10521472, FT ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786" FT BINDING 209..210 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10521472, FT ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786" FT BINDING 259 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10521472, FT ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786" FT BINDING 279 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10521472, FT ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786" FT BINDING 309..313 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10521472, FT ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786" FT VARIANT 333 FT /note="I -> V" FT CONFLICT 104 FT /note="G -> A (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 109 FT /note="V -> I (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 280..281 FT /note="AA -> N (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 93..97 FT /evidence="ECO:0007829|PDB:1D7O" FT STRAND 100..104 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 105..115 FT /evidence="ECO:0007829|PDB:1D7O" FT STRAND 119..125 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 126..137 FT /evidence="ECO:0007829|PDB:1D7O" FT TURN 138..142 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 143..145 FT /evidence="ECO:0007829|PDB:1D7O" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:1D7O" FT STRAND 155..161 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 173..176 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 179..183 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 189..200 FT /evidence="ECO:0007829|PDB:1D7O" FT STRAND 203..208 FT /evidence="ECO:0007829|PDB:1D7O" FT TURN 214..217 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 220..222 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 225..232 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 233..237 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 238..246 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 247..249 FT /evidence="ECO:0007829|PDB:1D7O" FT STRAND 250..260 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 262..264 FT /evidence="ECO:0007829|PDB:1D7O" FT TURN 272..274 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 275..297 FT /evidence="ECO:0007829|PDB:1D7O" FT STRAND 300..306 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 312..317 FT /evidence="ECO:0007829|PDB:1CWU" FT HELIX 319..330 FT /evidence="ECO:0007829|PDB:1D7O" FT STRAND 331..333 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 339..349 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 352..354 FT /evidence="ECO:0007829|PDB:1D7O" FT STRAND 361..365 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 368..370 FT /evidence="ECO:0007829|PDB:1D7O" FT HELIX 378..380 FT /evidence="ECO:0007829|PDB:1ENO" SQ SEQUENCE 385 AA; 40479 MW; C435BCE32A8D059B CRC64; MAATAAASSL QMATTRPSIS AASSKARTYV VGANPRNAYK IACTPHLSNL GCLRNDSALP ASKKSFSFST KAMSESSESK ASSGLPIDLR GKRAFIAGIA DDNGYGWAVA KSLAAAGAEI LVGTWVPALN IFETSLRRGK FDQSRVLPDG SLMEIKKVYP LDAVFDNPED VPEDVKANKR YAGSSNWTVQ EAAECVRQDF GSIDILVHSL ANGPEVSKPL LETSRKGYLA AISASSYSFV SLLSHFLPIM NPGGASISLT YIASERIIPG YGGGMSSAKA ALESDTRVLA FEAGRKQNIR VNTISAGPLG SRAAKAIGFI DTMIEYSYNN APIQKTLTAD EVGNAAAFLV SPLASAITGA TIYVDNGLNS MGVALDSPVF KDLNK //