FABH1_STRCO
ID FABH1_STRCO Reviewed; 343 AA.
AC P72392;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 121.
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=SCO2388;
GN ORFNames=SC4A7.16;
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 [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=7608065; DOI=10.1128/jb.177.14.3946-3952.1995;
RA Revill W.P., Bibb M.J., Hopwood D.A.;
RT "Purification of a malonyltransferase from Streptomyces coelicolor A3(2)
RT and analysis of its genetic determinant.";
RL J. Bacteriol. 177:3946-3952(1995).
RN [2]
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).
RN [3]
RP FUNCTION.
RX PubMed=11344162; DOI=10.1128/jb.183.11.3526-3530.2001;
RA Revill W.P., Bibb M.J., Scheu A.-K., Kieser H.J., Hopwood D.A.;
RT "Beta-ketoacyl acyl carrier protein synthase III (FabH) is essential for
RT fatty acid biosynthesis in Streptomyces coelicolor A3(2).";
RL J. Bacteriol. 183:3526-3530(2001).
CC -!- FUNCTION: Essential enzyme that catalyzes the condensation reaction of
CC fatty acid synthesis by the addition to an acyl acceptor of two carbons
CC from malonyl-ACP. Catalyzes the first condensation reaction which
CC initiates fatty acid synthesis and may therefore play a role in
CC governing the total rate of fatty acid production. Possesses both
CC acetoacetyl-ACP synthase and acetyl transacylase activities. Its
CC substrate specificity determines the biosynthesis of branched-chain of
CC fatty acids. {ECO:0000269|PubMed:11344162}.
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; X86475; CAA60200.1; -; Genomic_DNA.
DR EMBL; AL939112; CAB62720.1; -; Genomic_DNA.
DR RefSeq; NP_626634.1; NC_003888.3.
DR RefSeq; WP_003976418.1; NZ_VNID01000001.1.
DR AlphaFoldDB; P72392; -.
DR SMR; P72392; -.
DR STRING; 100226.SCO2388; -.
DR GeneID; 1097822; -.
DR KEGG; sco:SCO2388; -.
DR PATRIC; fig|100226.15.peg.2429; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_4_0_11; -.
DR InParanoid; P72392; -.
DR OMA; WGSEGDK; -.
DR PhylomeDB; P72392; -.
DR BRENDA; 2.3.1.180; 5998.
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; -; 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 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..343
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3 protein
FT 1"
FT /id="PRO_0000110483"
FT REGION 269..273
FT /note="ACP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 122
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 268
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 299
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
SQ SEQUENCE 343 AA; 35982 MW; 7838429F06A1AF21 CRC64;
MSKIKPSKGA PYARILGVGG YRPTRVVPNE VILEKIDSSD EWIRSRSGIE TRHWAGPEET
VAAMSVEASG KALADAGIDA SRIGAVVVST VSHFSQTPAI ATEIADRLGT DKAAAFDISA
GCAGFGYGLT LAKGMVVEGS AEYVLVIGVE RLSDLTDLED RATAFLFGDG AGAVVVGPSQ
EPAIGPTVWG SEGDKAETIK QTVSWDRFRI GDVSELPLDS EGNVKFPAIT QEGQAVFRWA
VFEMAKVAQQ ALDAAGISPD DLDVFIPHQA NVRIIDSMVK TLKLPEHVTV ARDIRTTGNT
SAASIPLAME RLLATGDARS GDTALVIGFG AGLVYAATVV TLP
