KAPS_YEAST
ID KAPS_YEAST Reviewed; 202 AA.
AC Q02196; D6VXT6;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Adenylyl-sulfate kinase;
DE EC=2.7.1.25;
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
DE AltName: Full=Adenosine-5'-phosphosulfate kinase;
DE Short=APS kinase;
GN Name=MET14; OrderedLocusNames=YKL001C;
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 204510 / AB320;
RX PubMed=1654509; DOI=10.1007/bf00264218;
RA Korch C., Mountain H.A., Bystroem A.S.;
RT "Cloning, nucleotide sequence, and regulation of MET14, the gene encoding
RT the APS kinase of Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 229:96-108(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1441752; DOI=10.1002/yea.320080908;
RA Duesterhoeft A., Philippsen P.;
RT "DNA sequencing and analysis of a 24.7 kb segment encompassing centromere
RT CEN11 of Saccharomyces cerevisiae reveals nine previously unknown open
RT reading frames.";
RL Yeast 8:749-759(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
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 [5]
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 [6]
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).
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:456216; EC=2.7.1.25;
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3.
CC -!- INTERACTION:
CC Q02196; Q00684: CDC14; NbExp=2; IntAct=EBI-9485, EBI-4192;
CC -!- MISCELLANEOUS: Present with 2170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000305}.
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DR EMBL; X57990; CAA41055.1; -; Genomic_DNA.
DR EMBL; S55315; AAB19854.1; -; Genomic_DNA.
DR EMBL; X65124; CAA46252.1; -; Genomic_DNA.
DR EMBL; Z28001; CAA81833.1; -; Genomic_DNA.
DR EMBL; AY558261; AAS56587.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09156.1; -; Genomic_DNA.
DR PIR; S17244; S17244.
DR RefSeq; NP_012925.3; NM_001179567.3.
DR AlphaFoldDB; Q02196; -.
DR SMR; Q02196; -.
DR BioGRID; 34132; 68.
DR DIP; DIP-1972N; -.
DR IntAct; Q02196; 4.
DR MINT; Q02196; -.
DR STRING; 4932.YKL001C; -.
DR MaxQB; Q02196; -.
DR PaxDb; Q02196; -.
DR PRIDE; Q02196; -.
DR EnsemblFungi; YKL001C_mRNA; YKL001C; YKL001C.
DR GeneID; 853869; -.
DR KEGG; sce:YKL001C; -.
DR SGD; S000001484; MET14.
DR VEuPathDB; FungiDB:YKL001C; -.
DR eggNOG; KOG0635; Eukaryota.
DR GeneTree; ENSGT00390000009613; -.
DR HOGENOM; CLU_046932_1_0_1; -.
DR InParanoid; Q02196; -.
DR OMA; GVTIWFT; -.
DR BioCyc; MetaCyc:YKL001C-MON; -.
DR BioCyc; YEAST:YKL001C-MON; -.
DR Reactome; R-SCE-174362; Transport and synthesis of PAPS.
DR UniPathway; UPA00140; UER00205.
DR PRO; PR:Q02196; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; Q02196; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IMP:SGD.
DR GO; GO:0000096; P:sulfur amino acid metabolic process; IMP:SGD.
DR CDD; cd02027; APSK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00455; apsK; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Cysteine biosynthesis; Kinase;
KW Methionine biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..202
FT /note="Adenylyl-sulfate kinase"
FT /id="PRO_0000105936"
FT ACT_SITE 105
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 202 AA; 23060 MW; 32F301FB6B2F41D3 CRC64;
MATNITWHPN LTYDERKALR KQDGCTIWLT GLSASGKSTI ACALEQLLLQ KNLSAYRLDG
DNIRFGLNKD LGFSEKDRNE NIRRISEVSK LFADSCAISI TSFISPYRVD RDRARELHKE
AGLKFIEIFV DVPLEVAEQR DPKGLYKKAR EGVIKEFTGI SAPYEAPKAP ELHLRTDQKT
VEECATIIYE YLISEKIIRK HL
