FABI_BRANA
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 03-AUG-2022, entry version 139.
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 (1.90 ANGSTROMS) OF 74-383 IN COMPLEX WITH NAD, AND
RP 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 (2.50 ANGSTROMS) OF 85-380 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 (1.90 ANGSTROMS) OF 84-380 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 H(+) + NADH; 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}.
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DR EMBL; S60064; AAB20114.2; -; mRNA.
DR PIR; S17761; S17761.
DR RefSeq; XP_013685121.1; XM_013829667.1.
DR RefSeq; XP_013685122.1; XM_013829668.1.
DR RefSeq; XP_013714468.1; XM_013859014.1.
DR RefSeq; XP_013714469.1; XM_013859015.1.
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=74-383.
DR PDB; 1ENP; X-ray; 2.60 A; A=74-383.
DR PDBsum; 1CWU; -.
DR PDBsum; 1D7O; -.
DR PDBsum; 1ENO; -.
DR PDBsum; 1ENP; -.
DR AlphaFoldDB; P80030; -.
DR SMR; P80030; -.
DR PRIDE; P80030; -.
DR GeneID; 106389421; -.
DR GeneID; 106418332; -.
DR KEGG; bna:106389421; -.
DR KEGG; bna:106418332; -.
DR BRENDA; 1.3.1.9; 944.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; P80030; -.
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:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05372; ENR_SDR; 1.
DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43159; PTHR43159; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
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..235
FT /evidence="ECO:0007829|PDB:1D7O"
FT HELIX 237..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
