FABI_PSEAE
ID FABI_PSEAE Reviewed; 265 AA.
AC Q9ZFE4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 140.
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=PA1806;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10464225; DOI=10.1128/jb.181.17.5489-5497.1999;
RA Hoang T.T., Schweizer H.P.;
RT "Characterization of Pseudomonas aeruginosa enoyl-acyl carrier protein
RT reductase (FabI): a target for the antimicrobial triclosan and its role in
RT acylated homoserine lactone synthesis.";
RL J. Bacteriol. 181:5489-5497(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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:0000250}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. FabI subfamily. {ECO:0000305}.
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DR EMBL; AF104262; AAC95362.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG05195.1; -; Genomic_DNA.
DR PIR; C83419; C83419.
DR RefSeq; NP_250497.1; NC_002516.2.
DR RefSeq; WP_003087936.1; NZ_QZGE01000003.1.
DR PDB; 4NQZ; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-265.
DR PDB; 4NR0; X-ray; 1.80 A; A/B/C/D=1-265.
DR PDBsum; 4NQZ; -.
DR PDBsum; 4NR0; -.
DR AlphaFoldDB; Q9ZFE4; -.
DR SMR; Q9ZFE4; -.
DR STRING; 287.DR97_73; -.
DR ChEMBL; CHEMBL3308935; -.
DR PaxDb; Q9ZFE4; -.
DR PRIDE; Q9ZFE4; -.
DR DNASU; 878311; -.
DR EnsemblBacteria; AAG05195; AAG05195; PA1806.
DR GeneID; 878311; -.
DR KEGG; pae:PA1806; -.
DR PATRIC; fig|208964.12.peg.1876; -.
DR PseudoCAP; PA1806; -.
DR HOGENOM; CLU_010194_10_1_6; -.
DR InParanoid; Q9ZFE4; -.
DR OMA; GILDMIH; -.
DR PhylomeDB; Q9ZFE4; -.
DR BioCyc; PAER208964:G1FZ6-1844-MON; -.
DR BRENDA; 1.3.1.9; 5087.
DR SABIO-RK; Q9ZFE4; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; ISS:UniProtKB.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IDA:PseudoCAP.
DR GO; GO:0042802; F:identical protein binding; ISS: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; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..265
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI"
FT /id="PRO_0000054904"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 19..20
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 66..67
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 195..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 204
FT /note="Involved in acyl-ACP binding"
FT /evidence="ECO:0000250"
FT SITE 207
FT /note="Involved in acyl-ACP binding"
FT /evidence="ECO:0000250"
FT SITE 208
FT /note="Involved in acyl-ACP binding"
FT /evidence="ECO:0000250"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:4NR0"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:4NR0"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:4NQZ"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:4NR0"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:4NR0"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:4NR0"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4NR0"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:4NR0"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:4NR0"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:4NR0"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:4NR0"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:4NR0"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:4NR0"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:4NR0"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:4NR0"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:4NR0"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:4NQZ"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:4NR0"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:4NR0"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:4NR0"
FT HELIX 161..180
FT /evidence="ECO:0007829|PDB:4NR0"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:4NR0"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:4NR0"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:4NR0"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:4NR0"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:4NR0"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:4NR0"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:4NR0"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:4NR0"
SQ SEQUENCE 265 AA; 28006 MW; 3E7A946886DFB293 CRC64;
MGFLTGKRAL IVGVASKLSI ASGIAAAMHR EGAELAFTYQ NDKLRGRVEE FASGWGSRPE
LCFPCDVADD SQIEAVFAAL GKHWDGLDII VHSVGFAPGD QLDGDFTAVT TREGFRIAHD
ISAYSFIALA KAGREMMKGR NGSLLTLSYL GAERTMPNYN VMGMAKASLE AGVRYLAGSL
GAEGTRVNAV SAGPIRTLAA SGIKSFRKML AANERQTPLR RNVTIEEVGN AGAFLCSDLA
SGISGEILYV DGGFNTTAMG PLDDD
