FABH2_VIBCH
ID FABH2_VIBCH Reviewed; 362 AA.
AC Q9KLJ3;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
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=VC_A0751;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF96649.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003853; AAF96649.1; ALT_INIT; Genomic_DNA.
DR PIR; A82423; A82423.
DR RefSeq; NP_233137.2; NC_002506.1.
DR RefSeq; WP_000189735.1; NZ_LT906615.1.
DR PDB; 4WZU; X-ray; 1.88 A; A=1-362.
DR PDB; 4X0O; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-362.
DR PDB; 4X9K; X-ray; 1.61 A; A=1-362.
DR PDB; 4X9O; X-ray; 2.30 A; A/B=1-362.
DR PDB; 5KP2; X-ray; 2.00 A; A/B=1-359.
DR PDB; 5V0P; X-ray; 2.16 A; A/B=1-362.
DR PDBsum; 4WZU; -.
DR PDBsum; 4X0O; -.
DR PDBsum; 4X9K; -.
DR PDBsum; 4X9O; -.
DR PDBsum; 5KP2; -.
DR PDBsum; 5V0P; -.
DR AlphaFoldDB; Q9KLJ3; -.
DR SMR; Q9KLJ3; -.
DR STRING; 243277.VC_A0751; -.
DR DNASU; 2611892; -.
DR EnsemblBacteria; AAF96649; AAF96649; VC_A0751.
DR KEGG; vch:VC_A0751; -.
DR PATRIC; fig|243277.26.peg.3377; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_3_0_6; -.
DR OMA; QFVFKNA; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000584; Chromosome 2.
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..362
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3 protein
FT 2"
FT /id="PRO_0000110503"
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"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:4X9K"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:4X9K"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 52..67
FT /evidence="ECO:0007829|PDB:4X9K"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:4X9K"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:4X9K"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:4X9K"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:4X9K"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:4X9K"
FT STRAND 160..173
FT /evidence="ECO:0007829|PDB:4X9K"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:4X9K"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:4X9K"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 216..238
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:4X9K"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 255..265
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 286..296
FT /evidence="ECO:0007829|PDB:4X9K"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:4X9K"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:4X9K"
FT HELIX 345..359
FT /evidence="ECO:0007829|PDB:4X9K"
SQ SEQUENCE 362 AA; 39025 MW; E0CC78C504B76213 CRC64;
MTQCYAEITG WGKCLPPATL SNHDLSTFLD TSDEWIQSRT GIEQRRISHV NTSDLATVAA
QHAIACAGVS VEEIDLIIVA TCSPDSLIPN IASRVQQNLG IPSAAAFDLN AACTGFLYGL
ETATRLMQAS HYRHALVIGA ERLSFYLDWT KRDTAVLFGD GAGAVVLSKT EQKVGLQDAQ
IGCDAQGRDI LAVPKFGTAM DRFDADNGYW AFDFVGKEIF KRAVRGMGAA AQQVLARSGL
STEEIDVVIP HQANIRIIQT LCDLAGIAQD KAFVNIHRYG NTSAATVPIA LCEALEQGKI
KPHDDLLVAA FGAGLTWGAG HIRWGERITP LGKSDAQLPS CDHTALDLLS KAIEHCKRHQ
SE
