FAT2_SCHPO
ID FAT2_SCHPO Reviewed; 512 AA.
AC O74976; P78757;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Oxalate--CoA ligase {ECO:0000305};
DE EC=6.2.1.8 {ECO:0000250|UniProtKB:P38137};
DE AltName: Full=Oxalyl-CoA synthetase;
DE AltName: Full=Peroxisomal-coenzyme A synthetase;
GN Name=pcs60; ORFNames=SPCC1827.03c;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-319.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-284, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Catalyzes the first step in a degradation pathway of oxalate
CC to CO(2) to protect the cell against the harmful effects of oxalate
CC derived from endogenous processes or an environmental sources.
CC {ECO:0000250|UniProtKB:P38137}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + oxalate = AMP + diphosphate + oxalyl-CoA;
CC Xref=Rhea:RHEA:18293, ChEBI:CHEBI:30616, ChEBI:CHEBI:30623,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57388,
CC ChEBI:CHEBI:456215; EC=6.2.1.8;
CC Evidence={ECO:0000250|UniProtKB:P38137};
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:P38137}.
CC Peroxisome membrane {ECO:0000250|UniProtKB:P38137}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P38137}.
CC -!- DOMAIN: The FACS motif is required for catalytic activity and substrate
CC specificity. {ECO:0000250|UniProtKB:P30624}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAA19311.1; -; Genomic_DNA.
DR EMBL; D89105; BAA13768.1; -; mRNA.
DR PIR; T41164; T41164.
DR RefSeq; NP_588549.1; NM_001023536.2.
DR AlphaFoldDB; O74976; -.
DR SMR; O74976; -.
DR BioGRID; 275823; 27.
DR STRING; 4896.SPCC1827.03c.1; -.
DR iPTMnet; O74976; -.
DR MaxQB; O74976; -.
DR PaxDb; O74976; -.
DR PRIDE; O74976; -.
DR EnsemblFungi; SPCC1827.03c.1; SPCC1827.03c.1:pep; SPCC1827.03c.
DR PomBase; SPCC1827.03c; pcs60.
DR VEuPathDB; FungiDB:SPCC1827.03c; -.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_0_1; -.
DR InParanoid; O74976; -.
DR OMA; PNIRFIR; -.
DR PhylomeDB; O74976; -.
DR PRO; PR:O74976; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0050203; F:oxalate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; ISM:PomBase.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR CDD; cd05926; FACL_fum10p_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR045310; Pcs60-like.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Membrane; Nucleotide-binding; Peroxisome;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..512
FT /note="Oxalate--CoA ligase"
FT /id="PRO_0000193183"
FT MOTIF 381..429
FT /note="FACS"
FT /evidence="ECO:0000250|UniProtKB:P30624"
FT MOTIF 510..512
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 168..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69451"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 218
FT /note="Missing (in Ref. 2; BAA13768)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="P -> T (in Ref. 2; BAA13768)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="A -> G (in Ref. 2; BAA13768)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 56274 MW; 7D7D851734277808 CRC64;
MSFTTLYSAI QGDASARALV APSLNAELSF SELRIAIMDL QRQIASLGIK VGDPVNIAIP
NGLEFVVAFY AVSWQRAICG PLNSNYKQSE FEFYIDDLKS KLVIVPEGSV AANTPAVRAA
KKLSVAVAEL AWCPKSRLVR IVHFEGAKIN APQPLGLPQP DDVMLVLHTS GTTGRPKVVP
LTHKNLCRSI HNITTSYRLD PRDTSYVVMP LFHVHGLLCG LLSTLASGGC AVVPPKFSAH
SFWKEFIQYG ATWYTAVPTI HQILLRTPPP KPLPRIRFIR SCSSPLAPPV LSKLEATFRA
PVLEAYAMTE ASHQMTTNPL PPLVHKPHSV GKPFGVELKI LDQKGNEMPQ GKEGEICVRG
INVTKGYLNN PAANKSSFTK DRFFRTGDEG KLDKDGYVFI TGRIKELVNR GGEKISPAEI
DAVLMQHPDV SEAVCFAVPD EKYGQDIQAA INPVAGKTVT PKQLHDYLEQ KVAAFKIPKK
FYFTDRIPKT ATGKVQRRLV CDAFFNHSKA KL
