FABH_YERPE
ID FABH_YERPE Reviewed; 316 AA.
AC Q8ZFT7; Q0WGI0;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000255|HAMAP-Rule:MF_01815};
DE EC=2.3.1.180 {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=Beta-ketoacyl-ACP synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
DE Short=KAS III {ECO:0000255|HAMAP-Rule:MF_01815};
GN Name=fabH {ECO:0000255|HAMAP-Rule:MF_01815};
GN OrderedLocusNames=YPO1597, y1756, YP_2257;
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: Catalyzes the condensation reaction of fatty acid synthesis
CC by the addition to an acyl acceptor of two carbons from malonyl-ACP.
CC Catalyzes the first condensation reaction which initiates fatty acid
CC synthesis and may therefore play a role in governing the total rate of
CC fatty acid production. Possesses both acetoacetyl-ACP synthase and
CC acetyl transacylase activities. Its substrate specificity determines
CC the biosynthesis of branched-chain and/or straight-chain of fatty
CC acids. {ECO:0000255|HAMAP-Rule:MF_01815}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2
CC + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-
CC COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450;
CC EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_01815}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01815}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01815}.
CC -!- DOMAIN: The last Arg residue of the ACP-binding site is essential for
CC the weak association between ACP/AcpP and FabH. {ECO:0000255|HAMAP-
CC Rule:MF_01815}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC {ECO:0000255|HAMAP-Rule:MF_01815}.
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DR EMBL; AL590842; CAL20242.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM85324.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62463.1; -; Genomic_DNA.
DR PIR; AH0194; AH0194.
DR RefSeq; WP_002210933.1; NZ_WUCM01000105.1.
DR RefSeq; YP_002346608.1; NC_003143.1.
DR PDB; 4YLT; X-ray; 2.20 A; A=1-316.
DR PDB; 4Z19; X-ray; 1.80 A; A=1-316.
DR PDBsum; 4YLT; -.
DR PDBsum; 4Z19; -.
DR AlphaFoldDB; Q8ZFT7; -.
DR SMR; Q8ZFT7; -.
DR STRING; 214092.YPO1597; -.
DR PaxDb; Q8ZFT7; -.
DR PRIDE; Q8ZFT7; -.
DR DNASU; 1146703; -.
DR EnsemblBacteria; AAM85324; AAM85324; y1756.
DR EnsemblBacteria; AAS62463; AAS62463; YP_2257.
DR GeneID; 66845102; -.
DR KEGG; ype:YPO1597; -.
DR KEGG; ypk:y1756; -.
DR KEGG; ypm:YP_2257; -.
DR PATRIC; fig|214092.21.peg.1940; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_3_1_6; -.
DR OMA; WGSEGDK; -.
DR BRENDA; 2.3.1.180; 4559.
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:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0033818; F:beta-ketoacyl-acyl-carrier-protein synthase III activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.47.10; -; 1.
DR HAMAP; MF_01815; FabH; 1.
DR InterPro; IPR013751; ACP_syn_III.
DR InterPro; IPR013747; ACP_syn_III_C.
DR InterPro; IPR004655; FabH_synth.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF08545; ACP_syn_III; 1.
DR Pfam; PF08541; ACP_syn_III_C; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR TIGRFAMs; TIGR00747; fabH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Multifunctional enzyme; Reference proteome; Transferase.
FT CHAIN 1..316
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT /id="PRO_0000110515"
FT REGION 244..248
FT /note="ACP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 112
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 243
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 273
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:4Z19"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:4Z19"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4Z19"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:4Z19"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:4Z19"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:4Z19"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:4Z19"
FT STRAND 160..171
FT /evidence="ECO:0007829|PDB:4Z19"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 208..229
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:4Z19"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 247..257
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:4Z19"
FT HELIX 278..288
FT /evidence="ECO:0007829|PDB:4Z19"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:4Z19"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:4Z19"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:4Z19"
SQ SEQUENCE 316 AA; 33738 MW; 1BC70E25F7EFA3C8 CRC64;
MYTKILGTGS YLPVQVRSNA DLEKMVDTSD EWIVTRTGIR ERRIAGLDET VATMGFQAAE
KALEMAGIDK DDIGLIIVAT TSSSHAFPSS ACQVQRMLGI KDAASFDLAA ACAGFTYALS
VADQYVKSGA VKHAIVIGSD VLSRALDPED RGTIILFGDG AGAVVLGASE QPGIMSTHLH
ADGRYGELLA LPYPDRQQDQ PAYVTMAGNE VFKVAVTELA HIVDETLQAN NLDRTALDWL
VPHQANLRII SATAKKLGMG MDKVVITLDR HGNTSAASVP SAFDEAVRDG RIQRGQLVLL
EAFGGGFTWG SALVRF
