FABH3_STRCO
ID FABH3_STRCO Reviewed; 335 AA.
AC O54151;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 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 protein 3 {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=Beta-ketoacyl-ACP synthase III 3 {ECO:0000255|HAMAP-Rule:MF_01815};
DE Short=KAS III 3 {ECO:0000255|HAMAP-Rule:MF_01815};
GN Name=fabH3 {ECO:0000255|HAMAP-Rule:MF_01815}; OrderedLocusNames=SCO5888;
GN ORFNames=SC3F7.08;
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; AL939125; CAA16179.1; -; Genomic_DNA.
DR PIR; T34914; T34914.
DR RefSeq; NP_630009.1; NC_003888.3.
DR RefSeq; WP_011030514.1; NZ_VNID01000007.1.
DR AlphaFoldDB; O54151; -.
DR SMR; O54151; -.
DR STRING; 100226.SCO5888; -.
DR PRIDE; O54151; -.
DR GeneID; 1101330; -.
DR KEGG; sco:SCO5888; -.
DR PATRIC; fig|100226.15.peg.5987; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_4_0_11; -.
DR InParanoid; O54151; -.
DR OMA; LFGCPGW; -.
DR PhylomeDB; O54151; -.
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..335
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3 protein
FT 3"
FT /id="PRO_0000110485"
FT REGION 257..261
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 256
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 286
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
SQ SEQUENCE 335 AA; 34697 MW; 1629F0EE6FBC6860 CRC64;
MTRASVLTGL GSCLPSRCVT NAELERTMDT SDEWIRARTG IAQRYVAEEG TLTSDLAVGA
AERALKSARL TPDEIDAVIV ATTTPDRPCP ATAPTVAARL GTGPVPAFDV SAVCSGFLYG
LATGSGLIAS GAAERVLVIG AETFSRILNP QDRSTSVIFG DGAGAVVLRA GEPGETGALG
PLRLGSDGTG VDLITVPAGG PPRPGAAAPD DLADRYFTME GKRVFWLAVQ RMGECAESVL
DRAGWRVADV DWLVSHQANH RITARLADEI GIPRERSVSN IAEVGNTAAA SIPLALDHAH
ARGTLRPGDR VLLTAFGGGL TWGAAALTWP AVDPV
