PANK_YEAST
ID PANK_YEAST Reviewed; 367 AA.
AC Q04430; D6VTF2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Pantothenate kinase CAB1;
DE EC=2.7.1.33 {ECO:0000269|PubMed:19266201};
DE AltName: Full=Coenzyme A biosynthesis protein 1;
DE AltName: Full=Pantothenic acid kinase CAB1;
GN Name=CAB1; OrderedLocusNames=YDR531W;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP FUNCTION, MUTAGENESIS OF GLY-351, AND CATALYTIC ACTIVITY.
RX PubMed=19266201; DOI=10.1007/s00294-009-0234-1;
RA Olzhausen J., Schuebbe S., Schueller H.-J.;
RT "Genetic analysis of coenzyme A biosynthesis in the yeast Saccharomyces
RT cerevisiae: identification of a conditional mutation in the pantothenate
RT kinase gene CAB1.";
RL Curr. Genet. 55:163-173(2009).
CC -!- FUNCTION: Plays a role in the physiological regulation of the
CC intracellular CoA concentration. {ECO:0000269|PubMed:19266201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP +
CC H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC EC=2.7.1.33; Evidence={ECO:0000269|PubMed:19266201};
CC -!- ACTIVITY REGULATION: Regulated by feedback inhibition by malonyl-CoA.
CC {ECO:0000250}.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5. {ECO:0000305|PubMed:19266201}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 6190 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the type II pantothenate kinase family.
CC {ECO:0000305}.
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DR EMBL; U33057; AAB64970.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12362.1; -; Genomic_DNA.
DR PIR; S69586; S69586.
DR RefSeq; NP_010820.3; NM_001180839.3.
DR PDB; 6UJ5; X-ray; 1.80 A; A/B=1-367.
DR PDBsum; 6UJ5; -.
DR AlphaFoldDB; Q04430; -.
DR SMR; Q04430; -.
DR BioGRID; 32580; 263.
DR DIP; DIP-5375N; -.
DR IntAct; Q04430; 10.
DR STRING; 4932.YDR531W; -.
DR iPTMnet; Q04430; -.
DR MaxQB; Q04430; -.
DR PaxDb; Q04430; -.
DR PRIDE; Q04430; -.
DR EnsemblFungi; YDR531W_mRNA; YDR531W; YDR531W.
DR GeneID; 852144; -.
DR KEGG; sce:YDR531W; -.
DR SGD; S000002939; CAB1.
DR VEuPathDB; FungiDB:YDR531W; -.
DR eggNOG; KOG2201; Eukaryota.
DR GeneTree; ENSGT00940000158896; -.
DR HOGENOM; CLU_011154_3_0_1; -.
DR InParanoid; Q04430; -.
DR OMA; WAQEGDN; -.
DR BioCyc; MetaCyc:MON3O-268; -.
DR BioCyc; YEAST:MON3O-268; -.
DR BRENDA; 2.7.1.33; 984.
DR UniPathway; UPA00241; UER00352.
DR PRO; PR:Q04430; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04430; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004594; F:pantothenate kinase activity; IMP:SGD.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IGI:SGD.
DR GO; GO:0008204; P:ergosterol metabolic process; IMP:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:2001023; P:regulation of response to drug; IMP:SGD.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004567; Type_II_PanK.
DR PANTHER; PTHR12280; PTHR12280; 1.
DR Pfam; PF03630; Fumble; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00555; panK_eukar; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..367
FT /note="Pantothenate kinase CAB1"
FT /id="PRO_0000253828"
FT MUTAGEN 351
FT /note="G->S: Leads to thermo-sensitivity."
FT /evidence="ECO:0000269|PubMed:19266201"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:6UJ5"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:6UJ5"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:6UJ5"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:6UJ5"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:6UJ5"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:6UJ5"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:6UJ5"
FT TURN 81..86
FT /evidence="ECO:0007829|PDB:6UJ5"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:6UJ5"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:6UJ5"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:6UJ5"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:6UJ5"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:6UJ5"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:6UJ5"
FT STRAND 150..167
FT /evidence="ECO:0007829|PDB:6UJ5"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:6UJ5"
FT HELIX 181..192
FT /evidence="ECO:0007829|PDB:6UJ5"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:6UJ5"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6UJ5"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:6UJ5"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:6UJ5"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:6UJ5"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:6UJ5"
FT TURN 266..271
FT /evidence="ECO:0007829|PDB:6UJ5"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6UJ5"
FT HELIX 276..301
FT /evidence="ECO:0007829|PDB:6UJ5"
FT STRAND 306..314
FT /evidence="ECO:0007829|PDB:6UJ5"
FT HELIX 318..332
FT /evidence="ECO:0007829|PDB:6UJ5"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:6UJ5"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:6UJ5"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:6UJ5"
SQ SEQUENCE 367 AA; 40903 MW; E87F23FFAA08E2AA CRC64;
MPRITQEISY NCDYGDNTFN LAIDIGGTLA KVVFSPIHSN RLMFYTIETE KIDKFMELLH
SIIKEHNNGC YRMTHIIATG GGAFKFYDLL YENFPQIKGI SRFEEMEGLI HGLDFFIHEI
PDEVFTYNDQ DGERIIPTSS GTMDSKAIYP YLLVNIGSGV SILKVTEPNN FSRVGGSSLG
GGTLWGLLSL ITGAQTYDQM LDWAQEGDNS SVDMLVGDIY GTDYNKIGLK SSAIASSFGK
VFQNRMTSNK SLENNENKLY SSHESIEKNN GQMFKNPDIC KSLLFAISNN IGQIAYLQAK
INNIQNIYFG GSYTRGHLTT MNTLSYAINF WSQGSKQAFF LKHEGYLGAM GAFLSASRHS
STKKTST
