FABH2_VIBVY
ID FABH2_VIBVY Reviewed; 362 AA.
AC Q7M7I3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=Beta-ketoacyl-ACP synthase III 2 {ECO:0000255|HAMAP-Rule:MF_01815};
DE Short=KAS III 2 {ECO:0000255|HAMAP-Rule:MF_01815};
GN Name=fabH2 {ECO:0000255|HAMAP-Rule:MF_01815}; OrderedLocusNames=VVA0906;
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; BA000038; BAC96932.1; -; Genomic_DNA.
DR RefSeq; WP_011152213.1; NC_005140.1.
DR AlphaFoldDB; Q7M7I3; -.
DR SMR; Q7M7I3; -.
DR STRING; 672.VV93_v1c38490; -.
DR EnsemblBacteria; BAC96932; BAC96932; BAC96932.
DR GeneID; 66967339; -.
DR KEGG; vvy:VVA0906; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_3_0_6; -.
DR OMA; QFVFKNA; -.
DR OrthoDB; 872193at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002675; Chromosome II.
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..362
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3 protein
FT 2"
FT /id="PRO_0000110509"
FT REGION 252..256
FT /note="ACP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 113
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 251
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 281
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
SQ SEQUENCE 362 AA; 38754 MW; B8781CEB5F62943C CRC64;
MTNYYAEITG WGKCLPPAVL SNDDLSTFLD TSDEWIRTRT GIENRRISHV NTSDLATVAA
KQALARAGIT AQDIDLIIVA TCSPDSLIPN IASMVQKNLE IEAAAAFDLN AACTGFVYGL
ETGTRLIQSG AYRHALIIGA ERLSFYIDWA MRDTAVLFGD GAGAVVLSRT EEAVGLQNAK
IGCDAQGRDI LSVPKFGTSM DRFAADNGYW DFNFVGKEIF KRAVKGMGSA AAHVLAHAGM
SKDDINVVIP HQANIRIIQT LCDLSGIDQS KAFVNIQKYG NTSAATVPIA LCEAVEQGHI
KAGDNILLAA FGAGLTWGAG LVKWGQRVEA ISESDAALPE CDKSALELLK NAIELCNARR
DK
