ID   FABH_MYCBO              Reviewed;         335 AA.
AC   P0A575; A0A1R3XWN5; O06399; X2BF69;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3;
DE            EC=2.3.1.180;
DE   AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III;
DE   AltName: Full=Beta-ketoacyl-ACP synthase III;
DE            Short=KAS III;
GN   Name=fabH; OrderedLocusNames=BQ2027_MB0547C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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. Has some substrate specificity for long
CC       chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer.
CC       Its substrate specificity determines the biosynthesis of mycolic acid
CC       fatty acid chain, which is characteristic of mycobacterial cell wall
CC       (By similarity). {ECO:0000250}.
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;
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The last Arg residue of the ACP-binding site is essential for
CC       the weak association between ACP/AcpP and FabH. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC       {ECO:0000305}.
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DR   EMBL; LT708304; SIT99143.1; -; Genomic_DNA.
DR   RefSeq; NP_854208.1; NC_002945.3.
DR   RefSeq; WP_003402861.1; NC_002945.4.
DR   AlphaFoldDB; P0A575; -.
DR   SMR; P0A575; -.
DR   GeneID; 45424497; -.
DR   PATRIC; fig|233413.5.peg.595; -.
DR   OMA; WGSEGDK; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001419; 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; Transferase.
FT   CHAIN           1..335
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT                   /id="PRO_0000110444"
FT   REGION          259..263
FT                   /note="ACP-binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        122
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        258
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   335 AA;  34873 MW;  6573BE1FAE5BCFB6 CRC64;
     MTEIATTSGA RSVGLLSVGA YRPERVVTND EICQHIDSSD EWIYTRTGIK TRRFAADDES
     AASMATEACR RALSNAGLSA ADIDGVIVTT NTHFLQTPPA APMVAASLGA KGILGFDLSA
     GCAGFGYALG AAADMIRGGG AATMLVVGTE KLSPTIDMYD RGNCFIFADG AAAVVVGETP
     FQGIGPTVAG SDGEQADAIR QDIDWITFAQ NPSGPRPFVR LEGPAVFRWA AFKMGDVGRR
     AMDAAGVRPD QIDVFVPHQA NSRINELLVK NLQLRPDAVV ANDIEHTGNT SAASIPLAMA
     ELLTTGAAKP GDLALLIGYG AGLSYAAQVV RMPKG