JLP1_YEAST
ID JLP1_YEAST Reviewed; 412 AA.
AC Q12358; D6VXV1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Alpha-ketoglutarate-dependent sulfonate dioxygenase;
DE EC=1.14.11.-;
GN Name=JLP1; OrderedLocusNames=YLL057C; ORFNames=L0572;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RA Wedler H., Wambutt R.;
RT "Sequence of a 37 kb DNA fragment from chromosome XII of Saccharomyces
RT cerevisiae including the subtelomeric region of the left arm.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, AND COFACTOR.
RX PubMed=10482536; DOI=10.1128/jb.181.18.5876-5879.1999;
RA Hogan D.A., Auchtung T.A., Hausinger R.P.;
RT "Cloning and characterization of a sulfonate/alpha-ketoglutarate
RT dioxygenase from Saccharomyces cerevisiae.";
RL J. Bacteriol. 181:5876-5879(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Acts as an alpha-ketoglutarate-dependent dioxygenase active
CC on sulfonates. Although taurine is a poor substrate, a variety of other
CC sulfonates are utilized, with the best natural substrates being
CC isethionate and taurocholate. {ECO:0000269|PubMed:10482536}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Organosulfur degradation; alkanesulfonate degradation.
CC -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR EMBL; Z47973; CAA88000.1; -; Genomic_DNA.
DR EMBL; Z73162; CAA97510.1; -; Genomic_DNA.
DR EMBL; AY692737; AAT92756.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09267.1; -; Genomic_DNA.
DR PIR; S50963; S50963.
DR RefSeq; NP_013043.1; NM_001181877.1.
DR AlphaFoldDB; Q12358; -.
DR SMR; Q12358; -.
DR BioGRID; 31258; 49.
DR DIP; DIP-1933N; -.
DR IntAct; Q12358; 1.
DR MINT; Q12358; -.
DR STRING; 4932.YLL057C; -.
DR iPTMnet; Q12358; -.
DR PaxDb; Q12358; -.
DR PRIDE; Q12358; -.
DR EnsemblFungi; YLL057C_mRNA; YLL057C; YLL057C.
DR GeneID; 850669; -.
DR KEGG; sce:YLL057C; -.
DR SGD; S000003980; JLP1.
DR VEuPathDB; FungiDB:YLL057C; -.
DR eggNOG; ENOG502QT05; Eukaryota.
DR HOGENOM; CLU_036005_0_0_1; -.
DR InParanoid; Q12358; -.
DR OMA; GFADVWH; -.
DR BioCyc; YEAST:G3O-32156-MON; -.
DR UniPathway; UPA00338; -.
DR PRO; PR:Q12358; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12358; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000907; F:sulfonate dioxygenase activity; IDA:SGD.
DR GO; GO:0046306; P:alkanesulfonate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0044273; P:sulfur compound catabolic process; IMP:SGD.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..412
FT /note="Alpha-ketoglutarate-dependent sulfonate dioxygenase"
FT /id="PRO_0000194022"
FT BINDING 218
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 412 AA; 46983 MW; F1BB8588B56CEEBD CRC64;
MSPAAAQTAI PLPSTDLPVK IITNGLKNLN YTSKQGYGNF DTHFYDGQDE VSPSGLLKIR
KSYREKSKYP DYLPTWDPTE KYGPLEFHEY HDPALRADGN FSNLFAKENV GQLKVKKITP
KLGLEINGIQ LTDLSDAAKD ELALLVAQKG VVVFRNQNFA DEGPDYVTEY GRHFGKLHIH
QTSGHPQNNP ELHITFRRPD AEEFARVFDD STSSGGWHTD VSYELQPPSY TFFSVVEGPD
GGGDTLFADT IEAFDRLSKP LQDFLSTLHV IHSSKEQAEN SQRQGGIKRR APVTHIHPLV
RVHPVLKKKC LYVNRAFSRK IVELKRQESE SLLNFLYNLV ESSHDLQLRA KWEPHSVVIW
DNRRVQHSAV IDWEEPIHRH AFRITPQAER PVEDLKFLND ENYYPSSLTL DI
