FABH4_STRCO
ID FABH4_STRCO Reviewed; 316 AA.
AC Q9ZBV4;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 4 {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 4 {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=Beta-ketoacyl-ACP synthase III 4 {ECO:0000255|HAMAP-Rule:MF_01815};
DE Short=KAS III 4 {ECO:0000255|HAMAP-Rule:MF_01815};
GN Name=fabH4 {ECO:0000255|HAMAP-Rule:MF_01815}; OrderedLocusNames=SCO6564;
GN ORFNames=SC4B5.14;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; AL939128; CAA22368.1; -; Genomic_DNA.
DR PIR; T35006; T35006.
DR RefSeq; NP_630645.1; NC_003888.3.
DR RefSeq; WP_011031009.1; NZ_VNID01000002.1.
DR AlphaFoldDB; Q9ZBV4; -.
DR SMR; Q9ZBV4; -.
DR STRING; 100226.SCO6564; -.
DR PRIDE; Q9ZBV4; -.
DR GeneID; 1102003; -.
DR KEGG; sco:SCO6564; -.
DR PATRIC; fig|100226.15.peg.6669; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_4_0_11; -.
DR InParanoid; Q9ZBV4; -.
DR OMA; QFVFKNA; -.
DR PhylomeDB; Q9ZBV4; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001973; 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 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..316
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3 protein
FT 4"
FT /id="PRO_0000110486"
FT REGION 243..247
FT /note="ACP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 114
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 242
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 272
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
SQ SEQUENCE 316 AA; 32479 MW; 4CBD505F0E581392 CRC64;
MHQGSRITAV GHYQPARILT NEDLAGMVDT SDEWIRSRVG IRTRRIAGPD EPVDELAGHA
AAKALASAGL TPADVDLVVV ATSTAIDRSP NTAARVAARL GIPGPAALDL NVVCAGFTHA
LATADHAVRA GSASRALVVG ADKMSEVVDW TDRTTCVLVG DGAGAAVVEA CAPGEEPGIG
PVLWGSVPEM GNAVRIEGTP PRFAQEGQSV YRWATTRLPA IARQACERSG LEPADLAAVV
LHQANLRIVE PLAAKIGAVN AVVARDVVES GNTSAASIPL ALSKLAERGE ITTGDPALLF
GFGGNLSYAG QVVRCP
