ID FABI_BACCR Reviewed; 256 AA. AC Q81GI3; DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 129. DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] FabI; DE Short=ENR; DE EC=1.3.1.9; DE AltName: Full=NADH-dependent enoyl-ACP reductase; GN Name=fabI; OrderedLocusNames=BC_1216; OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=226900; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB RC 9373 / NCTC 2599 / NRRL B-3711; RX PubMed=12721630; DOI=10.1038/nature01582; RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G., RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.; RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus RT anthracis."; RL Nature 423:87-91(2003). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, RP AND SUBUNIT. RX PubMed=20800575; DOI=10.1016/j.bbrc.2010.08.083; RA Kim S.J., Ha B.H., Kim K.H., Hong S.K., Shin K.J., Suh S.W., Kim E.E.; RT "Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from RT Bacillus cereus."; RL Biochem. Biophys. Res. Commun. 400:517-522(2010). CC -!- FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an CC enoyl moiety that is covalently linked to an acyl carrier protein CC (ACP). Involved in the elongation cycle of fatty acid which are used in CC the lipid metabolism (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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20800575}. 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; AE016877; AAP08201.1; -; Genomic_DNA. DR RefSeq; NP_831000.1; NC_004722.1. DR RefSeq; WP_000421886.1; NZ_CP034551.1. DR PDB; 3OJE; X-ray; 3.02 A; A=1-256. DR PDB; 3OJF; X-ray; 2.20 A; A/B/C/D=1-256. DR PDB; 5YCR; X-ray; 1.96 A; A/B/C/D=1-256. DR PDB; 5YCS; X-ray; 1.95 A; A/B/C/D=1-256. DR PDB; 5YCV; X-ray; 1.85 A; A/B/C/D=1-256. DR PDB; 5YCX; X-ray; 1.70 A; A=1-256. DR PDBsum; 3OJE; -. DR PDBsum; 3OJF; -. DR PDBsum; 5YCR; -. DR PDBsum; 5YCS; -. DR PDBsum; 5YCV; -. DR PDBsum; 5YCX; -. DR AlphaFoldDB; Q81GI3; -. DR SMR; Q81GI3; -. DR STRING; 226900.BC_1216; -. DR MetOSite; Q81GI3; -. DR GeneID; 75084525; -. DR KEGG; bce:BC1216; -. DR PATRIC; fig|226900.8.peg.1186; -. DR HOGENOM; CLU_010194_10_1_9; -. DR OrthoDB; 9803628at2; -. DR BRENDA; 1.3.1.10; 648. DR BRENDA; 1.3.1.9; 648. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; Q81GI3; -. DR Proteomes; UP000001417; Chromosome. DR GO; GO:1902494; C:catalytic complex; IDA:UniProtKB. DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IDA:UniProtKB. DR GO; GO:0047117; F:enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0070401; F:NADP+ binding; IDA:UniProtKB. DR GO; GO:0036094; F:small molecule binding; EXP:DisProt. DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB. DR CDD; cd05372; ENR_SDR; 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] FABI; 1. DR Pfam; PF13561; adh_short_C2; 1. DR PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1. DR PRINTS; PR00081; GDHRDH. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 1: Evidence at protein level; KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; NAD; NADP; Nucleotide-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1..256 FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI" FT /id="PRO_0000407976" FT ACT_SITE 147 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 157 FT /note="Proton acceptor" FT BINDING 13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:20800575" FT BINDING 19..20 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:20800575" FT BINDING 66..67 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:20800575" FT BINDING 94 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:20800575" FT BINDING 97 FT /ligand="substrate" FT BINDING 164 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:20800575" FT BINDING 193..197 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:20800575" FT SITE 205 FT /note="Involved in acyl-ACP binding" FT /evidence="ECO:0000250" FT TURN 3..6 FT /evidence="ECO:0007829|PDB:5YCX" FT STRAND 8..12 FT /evidence="ECO:0007829|PDB:5YCX" FT HELIX 20..30 FT /evidence="ECO:0007829|PDB:5YCX" FT STRAND 34..41 FT /evidence="ECO:0007829|PDB:5YCX" FT HELIX 42..53 FT /evidence="ECO:0007829|PDB:5YCX" FT STRAND 55..58 FT /evidence="ECO:0007829|PDB:3OJF" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:5YCX" FT HELIX 70..83 FT /evidence="ECO:0007829|PDB:5YCX" FT STRAND 88..92 FT /evidence="ECO:0007829|PDB:5YCX" FT HELIX 99..101 FT /evidence="ECO:0007829|PDB:5YCV" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:3OJF" FT HELIX 106..108 FT /evidence="ECO:0007829|PDB:5YCV" FT HELIX 113..132 FT /evidence="ECO:0007829|PDB:5YCX" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:5YCX" FT STRAND 140..147 FT /evidence="ECO:0007829|PDB:5YCX" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:5YCV" FT TURN 155..157 FT /evidence="ECO:0007829|PDB:5YCV" FT HELIX 162..178 FT /evidence="ECO:0007829|PDB:5YCX" FT HELIX 179..181 FT /evidence="ECO:0007829|PDB:5YCX" FT STRAND 183..190 FT /evidence="ECO:0007829|PDB:5YCX" FT HELIX 196..198 FT /evidence="ECO:0007829|PDB:3OJF" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:5YCV" FT HELIX 205..214 FT /evidence="ECO:0007829|PDB:5YCX" FT HELIX 223..234 FT /evidence="ECO:0007829|PDB:5YCX" FT HELIX 236..238 FT /evidence="ECO:0007829|PDB:5YCX" FT STRAND 245..249 FT /evidence="ECO:0007829|PDB:5YCX" FT HELIX 252..255 FT /evidence="ECO:0007829|PDB:5YCX" SQ SEQUENCE 256 AA; 27740 MW; 66780350F497CA31 CRC64; MELLQGKTFV VMGVANQRSI AWGIARSLHN AGAKLIFTYA GERLERNVRE LADTLEGQES LVLPCDVTND EELTACFETI KQEVGTIHGV AHCIAFANRD DLKGEFVDTS RDGFLLAQNI SAFSLTAVAR EAKKVMTEGG NILTLTYLGG ERVVKNYNVM GVAKASLEAS VKYLANDLGQ HGIRVNAISA GPIRTLSAKG VGDFNSILRE IEERAPLRRT TTQEEVGDTA VFLFSDLARG VTGENIHVDS GYHILG //