PPCS_YEAST
ID PPCS_YEAST Reviewed; 365 AA.
AC P40506; D6VVK3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Phosphopantothenate--cysteine ligase CAB2;
DE EC=6.3.2.5;
DE AltName: Full=Coenzyme A biosynthesis protein 2;
DE AltName: Full=Phosphopantothenoylcysteine synthetase;
DE Short=PPC synthetase;
GN Name=CAB2; OrderedLocusNames=YIL083C;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 338.
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 FUNCTION.
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 first step in the biosynthesis of coenzyme A
CC from vitamin B5, where cysteine is conjugated to 4'-phosphopantothenate
CC to form 4-phosphopantothenoylcysteine. {ECO:0000269|PubMed:19266201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantothenate + CTP + L-cysteine = CMP +
CC diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine;
CC Xref=Rhea:RHEA:19397, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:35235, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:59458, ChEBI:CHEBI:60377; EC=6.3.2.5;
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 2/5.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P40506; P36076: CAB3; NbExp=6; IntAct=EBI-25089, EBI-26778;
CC P40506; P53332: CAB4; NbExp=6; IntAct=EBI-25089, EBI-23648;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PPC synthetase family. {ECO:0000305}.
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DR EMBL; Z46728; CAA86711.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08469.2; -; Genomic_DNA.
DR PIR; S49797; S49797.
DR RefSeq; NP_012183.2; NM_001179431.2.
DR PDB; 6AI8; X-ray; 2.30 A; A/B=1-365.
DR PDB; 6AI9; X-ray; 2.09 A; A/B=1-365.
DR PDB; 6AIK; X-ray; 1.83 A; A/B=1-365.
DR PDB; 6AIM; X-ray; 2.04 A; A/B=1-365.
DR PDB; 6AIP; X-ray; 1.99 A; A/B=1-365.
DR PDBsum; 6AI8; -.
DR PDBsum; 6AI9; -.
DR PDBsum; 6AIK; -.
DR PDBsum; 6AIM; -.
DR PDBsum; 6AIP; -.
DR AlphaFoldDB; P40506; -.
DR SMR; P40506; -.
DR BioGRID; 34909; 70.
DR ComplexPortal; CPX-396; Coenzyme A-synthesizing protein complex.
DR IntAct; P40506; 3.
DR STRING; 4932.YIL083C; -.
DR iPTMnet; P40506; -.
DR MaxQB; P40506; -.
DR PaxDb; P40506; -.
DR PRIDE; P40506; -.
DR EnsemblFungi; YIL083C_mRNA; YIL083C; YIL083C.
DR GeneID; 854726; -.
DR KEGG; sce:YIL083C; -.
DR SGD; S000001345; CAB2.
DR VEuPathDB; FungiDB:YIL083C; -.
DR eggNOG; KOG2728; Eukaryota.
DR GeneTree; ENSGT00950000182834; -.
DR HOGENOM; CLU_042326_1_0_1; -.
DR InParanoid; P40506; -.
DR OMA; WEVVFVT; -.
DR BioCyc; MetaCyc:MON3O-285; -.
DR BioCyc; YEAST:MON3O-285; -.
DR Reactome; R-SCE-196783; Coenzyme A biosynthesis.
DR UniPathway; UPA00241; UER00353.
DR PRO; PR:P40506; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40506; protein.
DR GO; GO:1990143; C:CoA-synthesizing protein complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IDA:SGD.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IGI:SGD.
DR Gene3D; 3.40.50.10300; -; 1.
DR InterPro; IPR035929; CoaB-like_sf.
DR InterPro; IPR007085; DNA/pantothenate-metab_flavo_C.
DR Pfam; PF04127; DFP; 2.
DR SUPFAM; SSF102645; SSF102645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coenzyme A biosynthesis; Cytoplasm; Ligase; Nucleus;
KW Reference proteome.
FT CHAIN 1..365
FT /note="Phosphopantothenate--cysteine ligase CAB2"
FT /id="PRO_0000182042"
FT REGION 228..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 338
FT /note="S -> I (in Ref. 1; CAA86711)"
FT /evidence="ECO:0000305"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:6AIK"
FT HELIX 53..69
FT /evidence="ECO:0007829|PDB:6AIK"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:6AIK"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:6AIK"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:6AIK"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:6AIK"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:6AIK"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:6AIK"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:6AIK"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:6AIK"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:6AIK"
FT HELIX 154..171
FT /evidence="ECO:0007829|PDB:6AIK"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:6AIK"
FT HELIX 185..196
FT /evidence="ECO:0007829|PDB:6AIK"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:6AIK"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:6AIK"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:6AIK"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:6AIK"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:6AIM"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:6AIK"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:6AIK"
FT TURN 270..274
FT /evidence="ECO:0007829|PDB:6AIK"
FT STRAND 275..284
FT /evidence="ECO:0007829|PDB:6AIK"
FT HELIX 286..300
FT /evidence="ECO:0007829|PDB:6AIK"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:6AIK"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:6AIK"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:6AIK"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:6AIK"
FT STRAND 324..331
FT /evidence="ECO:0007829|PDB:6AIK"
FT HELIX 340..359
FT /evidence="ECO:0007829|PDB:6AIK"
SQ SEQUENCE 365 AA; 41867 MW; D67655BC0267DDAB CRC64;
MPPLPVLNRP QIHTSVTEIS HAIDRTIKEE LFPVAYTTEE EQYFKTNPKP AYIDELIKDA
KEFIDLQYSL KRNKIVLITS GGTTVPLENN TVRFIDNFSA GTRGASSAEQ FLANGYSVIF
LHREFSLTPY NRSFSHSINT LFLDYIDSEG KIKPEFAENV LKNKKLYDKY MEKEEKLLLL
PFTTVNQYLW SLKSIAKLLN NSGCLFYLAA AVSDFFVPYS RLPQHKIQSG DNGKMGANND
TEGTTRTTPD GKLIVNLDPV PKFLRRLVES WATQAMIVSF KLETDESMLL YKCTQALDRY
NHQLVIGNLL QTRNKQVIFV SPENRKGDWV RLDEKHHSIE EMIIPEVIAR HDKWVAHSKT
KLATK
