FABH2_DEIRA
ID FABH2_DEIRA Reviewed; 338 AA.
AC Q9RT22;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 123.
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=DR_1947;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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=AAF11499.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000513; AAF11499.1; ALT_INIT; Genomic_DNA.
DR PIR; C75334; C75334.
DR RefSeq; NP_295670.1; NC_001263.1.
DR RefSeq; WP_027479820.1; NC_001263.1.
DR AlphaFoldDB; Q9RT22; -.
DR SMR; Q9RT22; -.
DR STRING; 243230.DR_1947; -.
DR EnsemblBacteria; AAF11499; AAF11499; DR_1947.
DR KEGG; dra:DR_1947; -.
DR PATRIC; fig|243230.17.peg.2167; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_3_1_0; -.
DR InParanoid; Q9RT22; -.
DR OMA; QFVFKNA; -.
DR OrthoDB; 872193at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002524; 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..338
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3 protein
FT 2"
FT /id="PRO_0000110423"
FT REGION 256..260
FT /note="ACP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 119
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 255
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 285
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
SQ SEQUENCE 338 AA; 34926 MW; DF38A5DA32D12FF0 CRC64;
MTASLSAPAI GILAVGAYAP AAVITNAHYA TRLDTSDDWI TSRTGIRERR HAAPDESSSV
LGIRATQDLA GRFPGALDGV NLVICATSSP DAMFPSTAAL IAGGTGLRGA AAFDVSVACS
GFLYALSVGY GMIRAGLAKK ALIVGSEVMS GAVDQNDRNT AILFGDGAGC VVIGEVPQGY
GFQSFVLGAD SAGGPHLYLR GAALRLPEGT EMGPHLTQNG REVFKFAVRT LGDSAEQAMR
QAGKTTADID WLVPHQANIR IIEAACERFG LPIERAVTNL DRYGNTSAAS IPLALAEAQA
QGRFKDGDQL LLAGFGGGLS WGAAALKWWS GPTGKQSS
