FABH1_VIBCH
ID FABH1_VIBCH Reviewed; 316 AA.
AC Q9KQH5;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=VC_2023;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF95171.1; -; Genomic_DNA.
DR PIR; H82128; H82128.
DR RefSeq; NP_231657.1; NC_002505.1.
DR RefSeq; WP_000287010.1; NZ_LT906614.1.
DR PDB; 4NHD; X-ray; 1.78 A; A/B/C/D=1-316.
DR PDBsum; 4NHD; -.
DR AlphaFoldDB; Q9KQH5; -.
DR SMR; Q9KQH5; -.
DR STRING; 243277.VC_2023; -.
DR DNASU; 2613402; -.
DR EnsemblBacteria; AAF95171; AAF95171; VC_2023.
DR GeneID; 57740644; -.
DR KEGG; vch:VC_2023; -.
DR PATRIC; fig|243277.26.peg.1933; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_4_1_6; -.
DR OMA; WGSEGDK; -.
DR BioCyc; VCHO:VC2023-MON; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000584; Chromosome 1.
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; -; 2.
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 protein
FT 1"
FT /id="PRO_0000110502"
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:4NHD"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:4NHD"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4NHD"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:4NHD"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:4NHD"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:4NHD"
FT STRAND 132..141
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:4NHD"
FT STRAND 159..171
FT /evidence="ECO:0007829|PDB:4NHD"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:4NHD"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 208..229
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:4NHD"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:4NHD"
FT HELIX 278..288
FT /evidence="ECO:0007829|PDB:4NHD"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:4NHD"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:4NHD"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:4NHD"
SQ SEQUENCE 316 AA; 33749 MW; 041CF820D7C35173 CRC64;
MYSKILGTGS YLPSQVRTNA DLEKMVETSD EWIVARTGIR ERRIAADNET VADMAFFAAQ
NAINMAGIDK HDIDMIIVAT TSASHTFPSA ACQVQGKLGI KGCPAFDLAA ACSGFMYALS
IADQHVKSGM CKHVLVIGAD ALSKTCDPTD RSTIILFGDG AGAVVVGASN EPGILSTHIH
ADGEFGDLLS LEVPVRGGDS DKWLHMAGNE VFKVAVTQLS KLVVDTLKAN NMHKSELDWL
VPHQANYRII SATAKKLSMS LDQVVITLDR HGNTSAATVP TALDEAVRDG RIQRGQMLLL
EAFGGGFTWG SALVKF
