CAB5_YEAST
ID CAB5_YEAST Reviewed; 241 AA.
AC Q03941; D6VSH9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Dephospho-CoA kinase CAB5;
DE Short=DPCK;
DE EC=2.7.1.24;
DE AltName: Full=Dephosphocoenzyme A kinase;
GN Name=CAB5; OrderedLocusNames=YDR196C; ORFNames=YD9346.07C;
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 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [5]
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 [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [7]
RP GENE NAME, FUNCTION, AND DISRUPTION PHENOTYPE.
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: Catalyzes the phosphorylation of the 3'-hydroxyl group of
CC dephosphocoenzyme A to form coenzyme A. {ECO:0000269|PubMed:19266201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+);
CC Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216;
CC EC=2.7.1.24;
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 5/5.
CC -!- INTERACTION:
CC Q03941; P36076: CAB3; NbExp=7; IntAct=EBI-22174, EBI-26778;
CC Q03941; P53332: CAB4; NbExp=6; IntAct=EBI-22174, EBI-23648;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:14690591}. Mitochondrion
CC {ECO:0000269|PubMed:14690591, ECO:0000269|PubMed:16823961}. Nucleus
CC {ECO:0000269|PubMed:14690591}. Note=Nuclear envelope.
CC {ECO:0000269|PubMed:14690591}.
CC -!- DISRUPTION PHENOTYPE: Lethal. {ECO:0000269|PubMed:19266201}.
CC -!- MISCELLANEOUS: Present with 1660 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000305}.
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DR EMBL; Z48784; CAA88709.1; -; Genomic_DNA.
DR EMBL; AY557679; AAS56005.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12039.1; -; Genomic_DNA.
DR PIR; S52703; S52703.
DR RefSeq; NP_010482.3; NM_001180504.3.
DR AlphaFoldDB; Q03941; -.
DR SMR; Q03941; -.
DR BioGRID; 32248; 306.
DR ComplexPortal; CPX-396; Coenzyme A-synthesizing protein complex.
DR DIP; DIP-5705N; -.
DR IntAct; Q03941; 19.
DR STRING; 4932.YDR196C; -.
DR iPTMnet; Q03941; -.
DR MaxQB; Q03941; -.
DR PaxDb; Q03941; -.
DR PRIDE; Q03941; -.
DR EnsemblFungi; YDR196C_mRNA; YDR196C; YDR196C.
DR GeneID; 851777; -.
DR KEGG; sce:YDR196C; -.
DR SGD; S000002604; CAB5.
DR VEuPathDB; FungiDB:YDR196C; -.
DR eggNOG; KOG3220; Eukaryota.
DR GeneTree; ENSGT00550000075038; -.
DR HOGENOM; CLU_057180_0_1_1; -.
DR InParanoid; Q03941; -.
DR OMA; QMDIEQK; -.
DR BioCyc; MetaCyc:MON3O-504; -.
DR BioCyc; YEAST:MON3O-504; -.
DR UniPathway; UPA00241; UER00356.
DR PRO; PR:Q03941; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03941; protein.
DR GO; GO:1990143; C:CoA-synthesizing protein complex; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004140; F:dephospho-CoA kinase activity; ISS:SGD.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IGI:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR InterPro; IPR001977; Depp_CoAkinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01121; CoaE; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00152; TIGR00152; 1.
DR PROSITE; PS51219; DPCK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coenzyme A biosynthesis; Endoplasmic reticulum; Kinase;
KW Mitochondrion; Nucleotide-binding; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..241
FT /note="Dephospho-CoA kinase CAB5"
FT /id="PRO_0000173043"
FT DOMAIN 3..211
FT /note="DPCK"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 241 AA; 27340 MW; 1E71FDB8A107CB6D CRC64;
MLVVGLTGGI ACGKSTVSRR LRDKYKLPIV DADKIARQVV EPGQNAYDQI VLYFKDKIPN
LLLEDGHLNR EALGKWVFSH KEDLQALNGI THPAIRYAMF KEIGYYYLKG YRMCVLDVPL
LFEGNLDSIC GVTVSVICTQ ELQLERLMTR NPELSEEDAK NRLNSQMSTE ERMARSDYIL
QNNSTLVDLY EQIESVVKKI QPSKLRTVLE YFPPFGAVSA SSIVMSRLLM KKLQNKKSSA
V
