FABH1_VIBVY
ID FABH1_VIBVY Reviewed; 316 AA.
AC Q7M7J9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 1 {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 protein 1 {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=Beta-ketoacyl-ACP synthase III 1 {ECO:0000255|HAMAP-Rule:MF_01815};
DE Short=KAS III 1 {ECO:0000255|HAMAP-Rule:MF_01815};
GN Name=fabH1 {ECO:0000255|HAMAP-Rule:MF_01815}; OrderedLocusNames=VV1273;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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; BA000037; BAC94037.1; -; Genomic_DNA.
DR RefSeq; WP_011149967.1; NC_005139.1.
DR AlphaFoldDB; Q7M7J9; -.
DR SMR; Q7M7J9; -.
DR STRING; 672.VV93_v1c11900; -.
DR EnsemblBacteria; BAC94037; BAC94037; BAC94037.
DR KEGG; vvy:VV1273; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_4_1_6; -.
DR OMA; WGSEGDK; -.
DR OrthoDB; 872193at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002675; Chromosome I.
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 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Multifunctional enzyme;
KW Reference proteome; Transferase.
FT CHAIN 1..316
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3 protein
FT 1"
FT /id="PRO_0000110508"
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"
SQ SEQUENCE 316 AA; 33857 MW; ADFAF13AEAEDF098 CRC64;
MYSKILGTGS YLPSQIRTNA DLEKMVETSD EWIVARTGIK ERRIAAENET VADMGFYAAQ
NAIEMAGIDK NDIDLIIVAT TSGSHTFPSS ACQVQAKLGI KGCPAFDLAA ACSGFVYALS
IADQHIKTGM CKNVLVIGSD TLSKTCDPTD RSTIILFGDG AGAVVVGASE EPGILSTHIY
ADGEFGDLLS LEVPERGKDA DKWLHMAGNE VFKVAVTQLS KLVKDTLEAN GMHKSELDWL
VPHQANYRII SATAKKLSMS LDQVVITLDR HGNTSAATVP TALDEAVRDG RIQRGQTLLL
EAFGGGFTWG SALVRF
