FABA_PSEAE
ID FABA_PSEAE Reviewed; 171 AA.
AC O33877;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase;
DE EC=4.2.1.59;
DE AltName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA;
DE AltName: Full=Beta-hydroxydecanoyl thioester dehydrase;
DE AltName: Full=Trans-2-decenoyl-[acyl-carrier-protein] isomerase;
DE EC=5.3.3.14;
GN Name=fabA; OrderedLocusNames=PA1610;
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=9286984; DOI=10.1128/jb.179.17.5326-5332.1997;
RA Hoang T.T., Schweizer H.P.;
RT "Fatty acid biosynthesis in Pseudomonas aeruginosa: cloning and
RT characterization of the fabAB operon encoding beta-hydroxyacyl-acyl carrier
RT protein dehydratase (FabA) and beta-ketoacyl-acyl carrier protein synthase
RT I (FabB).";
RL J. Bacteriol. 179:5326-5332(1997).
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: Necessary for the introduction of cis unsaturation into fatty
CC acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-
CC (2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can
CC catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with
CC saturated chain lengths up to 16:0, being most active on intermediate
CC chain length (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP];
CC Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927,
CC ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14;
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioester dehydratase family. FabA
CC subfamily. {ECO:0000305}.
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DR EMBL; U70470; AAC45619.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04999.1; -; Genomic_DNA.
DR PIR; D83443; D83443.
DR RefSeq; NP_250301.1; NC_002516.2.
DR RefSeq; WP_003087475.1; NZ_QZGE01000003.1.
DR PDB; 4B0B; X-ray; 1.90 A; A/B=1-171.
DR PDB; 4B0C; X-ray; 2.70 A; A/B/C/D/E=1-171.
DR PDB; 4B0I; X-ray; 2.03 A; A/B/C/D/E=1-171.
DR PDB; 4B0J; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-171.
DR PDB; 4B8U; X-ray; 2.76 A; A/B/C/D/E=1-171.
DR PDB; 4CL6; X-ray; 2.41 A; A/B/C/D/E=1-171.
DR PDB; 4FQ9; X-ray; 2.02 A; A/B/C/D/E/F/G/H/I/J=1-171.
DR PDB; 7BHJ; X-ray; 2.11 A; A/B/C/D/E=1-171.
DR PDB; 7BIS; X-ray; 1.96 A; A/B/C/D/E=1-171.
DR PDB; 7BK9; X-ray; 1.94 A; A/B/C/D/E=1-171.
DR PDB; 7BKA; X-ray; 1.88 A; A/B/C/D/E=1-171.
DR PDBsum; 4B0B; -.
DR PDBsum; 4B0C; -.
DR PDBsum; 4B0I; -.
DR PDBsum; 4B0J; -.
DR PDBsum; 4B8U; -.
DR PDBsum; 4CL6; -.
DR PDBsum; 4FQ9; -.
DR PDBsum; 7BHJ; -.
DR PDBsum; 7BIS; -.
DR PDBsum; 7BK9; -.
DR PDBsum; 7BKA; -.
DR AlphaFoldDB; O33877; -.
DR SMR; O33877; -.
DR STRING; 287.DR97_279; -.
DR PaxDb; O33877; -.
DR PRIDE; O33877; -.
DR DNASU; 881984; -.
DR EnsemblBacteria; AAG04999; AAG04999; PA1610.
DR GeneID; 881984; -.
DR KEGG; pae:PA1610; -.
DR PATRIC; fig|208964.12.peg.1670; -.
DR PseudoCAP; PA1610; -.
DR HOGENOM; CLU_097925_0_0_6; -.
DR InParanoid; O33877; -.
DR OMA; FDCHFKG; -.
DR PhylomeDB; O33877; -.
DR BioCyc; PAER208964:G1FZ6-1640-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:O33877; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0034017; F:trans-2-decenoyl-acyl-carrier-protein isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IMP:PseudoCAP.
DR CDD; cd01287; FabA; 1.
DR HAMAP; MF_00405; FabA; 1.
DR InterPro; IPR010083; FabA.
DR InterPro; IPR013114; FabA_FabZ.
DR InterPro; IPR029069; HotDog_dom_sf.
DR PANTHER; PTHR30272; PTHR30272; 1.
DR PANTHER; PTHR30272:SF8; PTHR30272:SF8; 1.
DR Pfam; PF07977; FabA; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR01749; fabA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Isomerase; Lipid biosynthesis; Lipid metabolism; Lyase; Reference proteome.
FT CHAIN 1..171
FT /note="3-hydroxydecanoyl-[acyl-carrier-protein]
FT dehydratase"
FT /id="PRO_0000091606"
FT ACT_SITE 70
FT /evidence="ECO:0000250"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:4B0B"
FT TURN 17..21
FT /evidence="ECO:0007829|PDB:4B0I"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:4B0B"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:4B0B"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:4B0B"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:4B0B"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:4B0I"
FT HELIX 79..96
FT /evidence="ECO:0007829|PDB:4B0B"
FT STRAND 101..113
FT /evidence="ECO:0007829|PDB:4B0B"
FT STRAND 123..149
FT /evidence="ECO:0007829|PDB:4B0B"
FT STRAND 152..166
FT /evidence="ECO:0007829|PDB:4B0B"
SQ SEQUENCE 171 AA; 18748 MW; 801E2B9C741A28FC CRC64;
MTKQHAFTRE DLLRCSRGEL FGPGNAQLPA PNMLMIDRIV HISDVGGKYG KGELVAELDI
NPDLWFFACH FEGDPVMPGC LGLDAMWQLV GFYLGWQGNP GRGRALGSGE VKFFGQVLPT
AKKVTYNIHI KRTINRSLVL AIADGTVSVD GREIYSAEGL RVGLFTSTDS F
