FAT2_YEAST
ID FAT2_YEAST Reviewed; 543 AA.
AC P38137; D6VQL9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Oxalate--CoA ligase {ECO:0000305};
DE EC=6.2.1.8 {ECO:0000269|PubMed:24291261};
DE AltName: Full=Acyl-activating enzyme 3 {ECO:0000303|PubMed:24291261};
DE AltName: Full=Oxalyl-CoA synthetase {ECO:0000303|PubMed:24291261};
DE AltName: Full=Peroxisomal-coenzyme A synthetase {ECO:0000303|PubMed:8841414};
GN Name=PCS60 {ECO:0000303|PubMed:8841414};
GN Synonyms=AAE3 {ECO:0000303|PubMed:24291261}, FAT2;
GN OrderedLocusNames=YBR222C; ORFNames=YBR1512;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8841414; DOI=10.1111/j.1432-1033.1996.0468h.x;
RA Blobel F., Erdmann R.;
RT "Identification of a yeast peroxisomal member of the family of AMP-binding
RT proteins.";
RL Eur. J. Biochem. 240:468-476(1996).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24291261; DOI=10.1016/j.febslet.2013.11.026;
RA Foster J., Nakata P.A.;
RT "An oxalyl-CoA synthetase is important for oxalate metabolism in
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 588:160-166(2014).
RN [6]
RP INTERACTION WITH PEX5.
RX PubMed=26359497; DOI=10.1074/jbc.m115.657973;
RA Hagen S., Drepper F., Fischer S., Fodor K., Passon D., Platta H.W.,
RA Zenn M., Schliebs W., Girzalsky W., Wilmanns M., Warscheid B., Erdmann R.;
RT "Structural insights into cargo recognition by the yeast PTS1 receptor.";
RL J. Biol. Chem. 290:26610-26626(2015).
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:0000269|PubMed:24291261}.
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:0000269|PubMed:24291261};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for oxalate {ECO:0000269|PubMed:24291261};
CC Vmax=12 umol/min/mg enzyme {ECO:0000269|PubMed:24291261};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:24291261};
CC -!- SUBUNIT: Interacts with PEX5. {ECO:0000269|PubMed:26359497}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:8841414}.
CC Peroxisome membrane {ECO:0000269|PubMed:8841414}; Peripheral membrane
CC protein {ECO:0000269|PubMed:8841414}. Note=Imported in peroxisome via
CC recognition by the peroxisomal targeting signal receptor PEX5.
CC {ECO:0000269|PubMed:26359497}.
CC -!- INDUCTION: By oleic acid. {ECO:0000269|PubMed:8841414}.
CC -!- DOMAIN: The FACS motif is required for catalytic activity and substrate
CC specificity. {ECO:0000250|UniProtKB:P30624}.
CC -!- DISRUPTION PHENOTYPE: Decreases recovery from exposure to oxalate, to
CC oxalate-secreting microbes, and to oxidative stress.
CC {ECO:0000269|PubMed:24291261}.
CC -!- MISCELLANEOUS: Present with 8770 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; Z36091; CAA85185.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07339.1; -; Genomic_DNA.
DR PIR; S46098; S46098.
DR RefSeq; NP_009781.3; NM_001178570.3.
DR AlphaFoldDB; P38137; -.
DR SMR; P38137; -.
DR BioGRID; 32919; 57.
DR DIP; DIP-2796N; -.
DR IntAct; P38137; 10.
DR MINT; P38137; -.
DR STRING; 4932.YBR222C; -.
DR iPTMnet; P38137; -.
DR MaxQB; P38137; -.
DR PaxDb; P38137; -.
DR PRIDE; P38137; -.
DR EnsemblFungi; YBR222C_mRNA; YBR222C; YBR222C.
DR GeneID; 852523; -.
DR KEGG; sce:YBR222C; -.
DR SGD; S000000426; PCS60.
DR VEuPathDB; FungiDB:YBR222C; -.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_0_1; -.
DR InParanoid; P38137; -.
DR OMA; PNIRFIR; -.
DR BioCyc; MetaCyc:G3O-29157-MON; -.
DR BioCyc; YEAST:G3O-29157-MON; -.
DR BRENDA; 6.2.1.3; 984.
DR BRENDA; 6.2.1.8; 984.
DR PRO; PR:P38137; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38137; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:SGD.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:SGD.
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:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0050203; F:oxalate-CoA ligase activity; IDA:SGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0033611; P:oxalate catabolic process; IDA:SGD.
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; Direct protein sequencing; Ligase; Membrane;
KW Nucleotide-binding; Peroxisome; Reference proteome.
FT CHAIN 1..543
FT /note="Oxalate--CoA ligase"
FT /id="PRO_0000193182"
FT MOTIF 410..458
FT /note="FACS"
FT /evidence="ECO:0000250|UniProtKB:P30624"
FT MOTIF 541..543
FT /note="C-terminal peroxisome targeting signal (PTS1)"
FT /evidence="ECO:0000269|PubMed:26359497"
FT BINDING 196..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69451"
SQ SEQUENCE 543 AA; 60489 MW; 2BA18B77D10D62F2 CRC64;
MTSAATVTAS FNDTFSVSDN VAVIVPETDT QVTYRDLSHM VGHFQTMFTN PNSPLYGAVF
RQDTVAISMR NGLEFIVAFL GATMDAKIGA PLNPNYKEKE FNFYLNDLKS KAICVPKGTT
KLQSSEILKS ASTFGCFIVE LAFDATRFRV EYDIYSPEDN YKRVIYRSLN NAKFVNTNPV
KFPGFARSSD VALILHTSGT TSTPKTVPLL HLNIVRSTLN IANTYKLTPL DRSYVVMPLF
HVHGLIGVLL STFRTQGSVV VPDGFHPKLF WDQFVKYNCN WFSCVPTISM IMLNMPKPNP
FPHIRFIRSC SSALAPATFH KLEKEFNAPV LEAYAMTEAS HQMTSNNLPP GKRKPGTVGQ
PQGVTVVILD DNDNVLPPGK VGEVSIRGEN VTLGYANNPK ANKENFTKRE NYFRTGDQGY
FDPEGFLVLT GRIKELINRG GEKISPIELD GIMLSHPKID EAVAFGVPDD MYGQVVQAAI
VLKKGEKMTY EELVNFLKKH LASFKIPTKV YFVDKLPKTA TGKIQRRVIA ETFAKSSRNK
SKL
