OXSM_BOVIN
ID OXSM_BOVIN Reviewed; 460 AA.
AC Q0VCA7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial {ECO:0000305};
DE EC=2.3.1.41 {ECO:0000250|UniProtKB:Q9NWU1};
DE AltName: Full=Beta-ketoacyl-ACP synthase;
DE Flags: Precursor;
GN Name=OXSM;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in the biosynthesis of lipoic acid as well as
CC longer chain fatty acids required for optimal mitochondrial function.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC EC=2.3.1.41; Evidence={ECO:0000250|UniProtKB:Q9NWU1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC Evidence={ECO:0000250|UniProtKB:Q9NWU1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] +
CC CO2 + holo-[ACP]; Xref=Rhea:RHEA:41820, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9628, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78454, ChEBI:CHEBI:78456;
CC Evidence={ECO:0000250|UniProtKB:Q9NWU1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821;
CC Evidence={ECO:0000250|UniProtKB:Q9NWU1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] +
CC CO2 + holo-[ACP]; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460;
CC Evidence={ECO:0000250|UniProtKB:Q9NWU1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837;
CC Evidence={ECO:0000250|UniProtKB:Q9NWU1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] +
CC CO2 + holo-[ACP]; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464;
CC Evidence={ECO:0000250|UniProtKB:Q9NWU1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853;
CC Evidence={ECO:0000250|UniProtKB:Q9NWU1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469;
CC Evidence={ECO:0000250|UniProtKB:Q9NWU1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869;
CC Evidence={ECO:0000250|UniProtKB:Q9NWU1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl-
CC [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473;
CC Evidence={ECO:0000250|UniProtKB:Q9NWU1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885;
CC Evidence={ECO:0000250|UniProtKB:Q9NWU1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-[ACP] = 3-
CC oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41900,
CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649,
CC Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477,
CC ChEBI:CHEBI:78478; Evidence={ECO:0000250|UniProtKB:Q9NWU1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901;
CC Evidence={ECO:0000250|UniProtKB:Q9NWU1};
CC -!- ACTIVITY REGULATION: Inhibited by cerulenin. {ECO:0000250}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000305}.
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DR EMBL; BC120268; AAI20269.1; -; mRNA.
DR RefSeq; NP_001069092.1; NM_001075624.2.
DR AlphaFoldDB; Q0VCA7; -.
DR SMR; Q0VCA7; -.
DR STRING; 9913.ENSBTAP00000009250; -.
DR PaxDb; Q0VCA7; -.
DR GeneID; 513530; -.
DR KEGG; bta:513530; -.
DR CTD; 54995; -.
DR eggNOG; KOG1394; Eukaryota.
DR InParanoid; Q0VCA7; -.
DR OrthoDB; 1014523at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11712; PTHR11712; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR PIRSF; PIRSF000447; KAS_II; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR03150; fabF; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Acyltransferase; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..460
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase,
FT mitochondrial"
FT /id="PRO_0000310304"
FT MOD_RES 110
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D404"
FT MOD_RES 110
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D404"
FT MOD_RES 114
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D404"
FT MOD_RES 175
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWU1"
FT MOD_RES 175
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D404"
SQ SEQUENCE 460 AA; 48617 MW; 34D49F1E15BD27B3 CRC64;
MLSDGLQIFL RITKCHLIHA RSCQRLVNER RFLATAPAPG LRRRVVITGI GLVTPLGVGT
QLVWDRLVRG ESGIVSLVGD EYQSIPCSVA AYVPRGCDEG QFNEQNFVPK SDTKSMSPPT
VMAIAAAELA LKDAGWHPQS EADQAATGVA IGMGMVPLEV ISETALTFQT KGYSKVSPFF
VPKILVNMAS GQVSIRHKLK GPNHAVSTAC TTGAHAVGDS FRFVAHGDAD VMVAGGTDSC
ISPLSLAGFA RARALSTNTD PKSACRPFHP QRDGFVMGEG AAVLVLEEHR HALRRGARVY
AEIVGYGLSG DAGHITAPDP GGEGAFRCMA AAVKDAGIQP EEVSYINAHA TSTPLGDAAE
NKAIKQLFKD HAHVLAVSST KGATGHLLGT AGAAEAAFTA LACYHRKLPP TLNLDCTEPH
FDLNYVPLKA QEWKAENRRI ALTNSFGFGG TNATLCIAGM
