FABH5_STRCO
ID FABH5_STRCO Reviewed; 332 AA.
AC Q9JN82;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 5 {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 5 {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=Beta-ketoacyl-ACP synthase III 5 {ECO:0000255|HAMAP-Rule:MF_01815};
DE Short=KAS III 5 {ECO:0000255|HAMAP-Rule:MF_01815};
GN Name=fabH5 {ECO:0000255|HAMAP-Rule:MF_01815}; Synonyms=mmyC;
GN OrderedLocusNames=SCP1.233.2; ORFNames=SCP1.233B;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OG Plasmid SCP1.
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; PLASMID=SCP1;
RA Bruton C.J., Wietzorrek A., Hartley N., Woodburn L., Chater K.F.;
RT "Genes involved in methylenomycin biosynthesis from plasmid SCP1 of
RT Streptomyces coelicolor A3(2).";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
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).
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; AJ276673; CAB82875.1; -; Genomic_DNA.
DR EMBL; AL589148; CAC36759.1; -; Genomic_DNA.
DR RefSeq; NP_639843.1; NC_003903.1.
DR RefSeq; WP_011039535.1; NC_003903.1.
DR AlphaFoldDB; Q9JN82; -.
DR SMR; Q9JN82; -.
DR GeneID; 1095316; -.
DR KEGG; sco:SCP1.233B; -.
DR PATRIC; fig|100226.15.peg.8180; -.
DR HOGENOM; CLU_039592_4_0_11; -.
DR InParanoid; Q9JN82; -.
DR OMA; DIRQQCT; -.
DR PhylomeDB; Q9JN82; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001973; Plasmid SCP1.
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; Plasmid;
KW Reference proteome; Transferase.
FT CHAIN 1..332
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3 protein
FT 5"
FT /id="PRO_0000110487"
FT REGION 254..258
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 253
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 283
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
SQ SEQUENCE 332 AA; 34016 MW; CE2787DA1BDC03EC CRC64;
MSGAGVLAGL GTALPARLVT NEELSRHLDT DDEWIRSRTG IGQRYWSDGA STGDLAVEAG
QRALKAAGTD TVDLVVLATT TPDHPCPATA PDVADRLGLS GVAAYDIAAV CSGFIYGLAS
AVAHITAGLV GSALVIGAET YSTILDPLDR TTSVIFGDGA GAVVLRSGSV DERGAFLGFD
LGSDGALKDL IVIPGGGSRE RAAAERPQPA GAYFTMQGKP VFRHAVTRMT SSAGALLDRT
GWSPASVDRF VGHQANARIL HAVADQLRID GARTVIDLDR VGNTSAASIP LALSRACGEG
LLSPGDRVLL SAFGGGLTWG STALLWPDIT AL
