FABA_YERPE
ID FABA_YERPE Reviewed; 172 AA.
AC Q8ZG80; Q0WGY6;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 145.
DE RecName: Full=3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase {ECO:0000255|HAMAP-Rule:MF_00405};
DE EC=4.2.1.59 {ECO:0000255|HAMAP-Rule:MF_00405};
DE AltName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA {ECO:0000255|HAMAP-Rule:MF_00405};
DE AltName: Full=Beta-hydroxydecanoyl thioester dehydrase {ECO:0000255|HAMAP-Rule:MF_00405};
DE AltName: Full=Trans-2-decenoyl-[acyl-carrier-protein] isomerase {ECO:0000255|HAMAP-Rule:MF_00405};
DE EC=5.3.3.14 {ECO:0000255|HAMAP-Rule:MF_00405};
GN Name=fabA {ECO:0000255|HAMAP-Rule:MF_00405};
GN OrderedLocusNames=YPO1430, y2740, YP_0875;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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. {ECO:0000255|HAMAP-Rule:MF_00405}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00405};
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00405};
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00405};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_00405}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00405}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00405}.
CC -!- SIMILARITY: Belongs to the thioester dehydratase family. FabA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00405}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM86292.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS61132.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL20082.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM86292.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS61132.1; ALT_INIT; Genomic_DNA.
DR PIR; AH0174; AH0174.
DR RefSeq; WP_002220006.1; NZ_WUCM01000140.1.
DR RefSeq; YP_002346452.1; NC_003143.1.
DR PDB; 5F6R; X-ray; 1.18 A; A/B=1-172.
DR PDB; 5HD6; X-ray; 1.35 A; A/B/C/D/E/F/G/H=1-172.
DR PDBsum; 5F6R; -.
DR PDBsum; 5HD6; -.
DR AlphaFoldDB; Q8ZG80; -.
DR SMR; Q8ZG80; -.
DR STRING; 214092.YPO1430; -.
DR PaxDb; Q8ZG80; -.
DR EnsemblBacteria; AAM86292; AAM86292; y2740.
DR EnsemblBacteria; AAS61132; AAS61132; YP_0875.
DR GeneID; 66842115; -.
DR KEGG; ype:YPO1430; -.
DR KEGG; ypk:y2740; -.
DR KEGG; ypm:YP_0875; -.
DR PATRIC; fig|214092.21.peg.1757; -.
DR eggNOG; COG0764; Bacteria.
DR HOGENOM; CLU_097925_0_0_6; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
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..172
FT /note="3-hydroxydecanoyl-[acyl-carrier-protein]
FT dehydratase"
FT /id="PRO_0000091626"
FT ACT_SITE 71
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00405"
FT HELIX 10..17
FT /evidence="ECO:0007829|PDB:5F6R"
FT TURN 18..22
FT /evidence="ECO:0007829|PDB:5F6R"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:5F6R"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:5F6R"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:5F6R"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:5F6R"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:5F6R"
FT HELIX 80..97
FT /evidence="ECO:0007829|PDB:5F6R"
FT STRAND 102..114
FT /evidence="ECO:0007829|PDB:5F6R"
FT STRAND 124..135
FT /evidence="ECO:0007829|PDB:5F6R"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:5F6R"
FT STRAND 141..150
FT /evidence="ECO:0007829|PDB:5F6R"
FT STRAND 153..167
FT /evidence="ECO:0007829|PDB:5F6R"
SQ SEQUENCE 172 AA; 18810 MW; 19037054D0A721EC CRC64;
MVDKRESYTK EDLEASGRGE LFGAGGPPLP AGNMLMMDRI VKMIEDGGSH NKGYVEAELD
INPDLWFFGC HFIGDPVMPG CLGLDAMWQL VGFYLGWLGG EGKGRALGVG EVKFTGQVLP
DAKKVTYRIN FKRVIMRKLI MGVADGEVLV DGKVIYTATD LKVGLFKDTN AF
