FABI_BACCR
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 03-AUG-2022, entry version 121.
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; Firmicutes; 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 9373
RC / 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}.
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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 EnsemblBacteria; AAP08201; AAP08201; BC_1216.
DR GeneID; 64200095; -.
DR GeneID; 67505935; -.
DR KEGG; bce:BC1216; -.
DR PATRIC; fig|226900.8.peg.1186; -.
DR HOGENOM; CLU_010194_10_1_9; -.
DR OMA; GILDMIH; -.
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:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0070401; F:NADP+ binding; IDA:UniProtKB.
DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB.
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 PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 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
