OXSM_SCHPO
ID OXSM_SCHPO Reviewed; 426 AA.
AC O94297;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Putative 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 AltName: Full=mtKAS;
DE Flags: Precursor;
GN ORFNames=SPBC887.13c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 -!- 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; CU329671; CAA21898.1; -; Genomic_DNA.
DR PIR; T40738; T40738.
DR RefSeq; NP_596487.1; NM_001022407.2.
DR AlphaFoldDB; O94297; -.
DR SMR; O94297; -.
DR STRING; 4896.SPBC887.13c.1; -.
DR MaxQB; O94297; -.
DR PaxDb; O94297; -.
DR EnsemblFungi; SPBC887.13c.1; SPBC887.13c.1:pep; SPBC887.13c.
DR GeneID; 2541226; -.
DR KEGG; spo:SPBC887.13c; -.
DR PomBase; SPBC887.13c; -.
DR VEuPathDB; FungiDB:SPBC887.13c; -.
DR eggNOG; KOG1394; Eukaryota.
DR HOGENOM; CLU_000022_69_2_1; -.
DR InParanoid; O94297; -.
DR OMA; QIGHCLG; -.
DR PhylomeDB; O94297; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:O94297; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; ISS:PomBase.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISS:PomBase.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
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; 1.
DR TIGRFAMs; TIGR03150; fabF; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Mitochondrion; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..426
FT /note="Putative 3-oxoacyl-[acyl-carrier-protein] synthase,
FT mitochondrial"
FT /id="PRO_0000310303"
SQ SEQUENCE 426 AA; 45489 MW; A7C6EA9264C7DE48 CRC64;
MKRVVITGLG AVTPLGNGVK TNWRNLIQGK SGIVSLKGFP EYEQIPSKVA GVIPRGKEKE
EWNVLDYVDQ GKLREVATFT QLALTSAAEA LKDARWIDID EQEKLATGVC FGTGIGNLDD
ALNENGVLNK AGIRKVSPRV ISKILINMPA GYISQRYGFT ALNHTTTTAC AAGCHAIGDA
FNFIKLGHAD VIIAGGSESC INPLTVAGFS KARSLSTKFN DNPKAASRPF DANRDGFVIG
EGSAALVLEE LEHAKNRNAH IYAEIVGYGL ASDSYHITAP NPNGDAAYYA MKRSLKQAGL
SASQLDYINA HATSTKLGDV AESIAITRLL CDVNRNPEAF PVSSSKGSIG HLLGAAGAIE
SVYTVLTVQK GVLPPTLNFE YSDIPQQFQC DYVPNVAKES RINVALSNSF GFGGTNASLC
FKKFLQ
