FABH_AQUAE
ID FABH_AQUAE Reviewed; 309 AA.
AC O67185;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
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}; OrderedLocusNames=aq_1099;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RC STRAIN=VF5;
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase III from
RT Aquifex aeolicus VF5.";
RL Submitted (AUG-2007) to the PDB data bank.
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:0000305}.
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; AE000657; AAC07144.1; -; Genomic_DNA.
DR PIR; F70394; F70394.
DR RefSeq; NP_213748.1; NC_000918.1.
DR RefSeq; WP_010880686.1; NC_000918.1.
DR PDB; 2EBD; X-ray; 2.10 A; A/B=1-309.
DR PDBsum; 2EBD; -.
DR AlphaFoldDB; O67185; -.
DR SMR; O67185; -.
DR STRING; 224324.aq_1099; -.
DR PRIDE; O67185; -.
DR EnsemblBacteria; AAC07144; AAC07144; aq_1099.
DR KEGG; aae:aq_1099; -.
DR PATRIC; fig|224324.8.peg.857; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_3_1_0; -.
DR InParanoid; O67185; -.
DR OMA; YAKHKGK; -.
DR OrthoDB; 872193at2; -.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; O67185; -.
DR Proteomes; UP000000798; 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..309
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT /id="PRO_0000110392"
FT REGION 237..241
FT /note="ACP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 111
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 236
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 266
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:2EBD"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:2EBD"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 50..65
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:2EBD"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:2EBD"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:2EBD"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:2EBD"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2EBD"
FT TURN 150..155
FT /evidence="ECO:0007829|PDB:2EBD"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:2EBD"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:2EBD"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:2EBD"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2EBD"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 201..223
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2EBD"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:2EBD"
FT HELIX 271..281
FT /evidence="ECO:0007829|PDB:2EBD"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:2EBD"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:2EBD"
FT STRAND 301..308
FT /evidence="ECO:0007829|PDB:2EBD"
SQ SEQUENCE 309 AA; 33825 MW; EB97518DB168140D CRC64;
MGTKIIGTGV YLPKNVLTNF DLEKIVDTSD EWITTRTGIK ERRIAKEETI TYMATQAAKE
ALREANLSPE ELDLIILATL TPQKRFPSTA CLVQAQLKAK GVYAFDISAA CSGFIYALDI
ADSFIKSGKA KNVLVIGAEK LSEAVDWEDR STCVLFGDGA GAVVVTRSED KSDILATRMY
AEGSLEELLH ADNCGYIRMK GRELFKVAVR SMEEVCREVL EKAGVKPEEV SLVIPHQANV
RIINALAEKL NIPKEKVFVN IQKYGNTSAA SIPIALHEAI KEGKVKRGDL ILMTAMGGGL
TWGAVLLRY
