ID   PANC_YEAST              Reviewed;         309 AA.
AC   P40459; D6VVE2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Pantoate--beta-alanine ligase;
DE            EC=6.3.2.1;
DE   AltName: Full=Pantoate-activating enzyme;
DE   AltName: Full=Pantothenate synthetase;
GN   Name=PAN6; OrderedLocusNames=YIL145C;
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.
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   FUNCTION.
RX   PubMed=11154694; DOI=10.1074/jbc.m009804200;
RA   White W.H., Gunyuzlu P.L., Toyn J.H.;
RT   "Saccharomyces cerevisiae is capable of de novo pantothenic acid
RT   biosynthesis involving a novel pathway of beta-alanine production from
RT   spermine.";
RL   J. Biol. Chem. 276:10794-10800(2001).
RN   [4]
RP   IDENTIFICATION OF PROBABLE INITIATION SITE.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(2003).
RN   [5]
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   [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: Required for pantothenic acid biosynthesis.
CC       {ECO:0000269|PubMed:11154694}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP +
CC         diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1;
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 2400 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA86133.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z38059; CAA86133.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006942; DAA08408.1; -; Genomic_DNA.
DR   PIR; S48389; S48389.
DR   RefSeq; NP_012121.2; NM_001179493.1.
DR   AlphaFoldDB; P40459; -.
DR   SMR; P40459; -.
DR   BioGRID; 34847; 106.
DR   DIP; DIP-4613N; -.
DR   IntAct; P40459; 3.
DR   STRING; 4932.YIL145C; -.
DR   MaxQB; P40459; -.
DR   PaxDb; 4932-YIL145C; -.
DR   PeptideAtlas; P40459; -.
DR   EnsemblFungi; YIL145C_mRNA; YIL145C; YIL145C.
DR   GeneID; 854661; -.
DR   KEGG; sce:YIL145C; -.
DR   AGR; SGD:S000001407; -.
DR   SGD; S000001407; PAN6.
DR   VEuPathDB; FungiDB:YIL145C; -.
DR   eggNOG; KOG3042; Eukaryota.
DR   HOGENOM; CLU_047148_1_0_1; -.
DR   InParanoid; P40459; -.
DR   OMA; CNHKLEP; -.
DR   OrthoDB; 5475139at2759; -.
DR   BioCyc; MetaCyc:YIL145C-MONOMER; -.
DR   BioCyc; YEAST:YIL145C-MONOMER; -.
DR   UniPathway; UPA00028; UER00005.
DR   BioGRID-ORCS; 854661; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P40459; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40459; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IDA:SGD.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IMP:SGD.
DR   CDD; cd00560; PanC; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.30.1300.10; Pantoate-beta-alanine ligase, C-terminal domain; 1.
DR   HAMAP; MF_00158; PanC; 1.
DR   InterPro; IPR003721; Pantoate_ligase.
DR   InterPro; IPR042176; Pantoate_ligase_C.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00018; panC; 1.
DR   PANTHER; PTHR21299; CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE; 1.
DR   PANTHER; PTHR21299:SF1; PANTOATE--BETA-ALANINE LIGASE; 1.
DR   Pfam; PF02569; Pantoate_ligase; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Nucleus;
KW   Pantothenate biosynthesis; Reference proteome.
FT   CHAIN           1..309
FT                   /note="Pantoate--beta-alanine ligase"
FT                   /id="PRO_0000128298"
SQ   SEQUENCE   309 AA;  35032 MW;  9787B366795B5D81 CRC64;
     MKIFHTVEEV VQWRTQELRE TRFRETIGFV PTMGCLHSGH ASLISQSVKE NTYTVVSIFV
     NPSQFAPTED LDNYPRTLPD DIKLLESLKV DVLFAPNAHV MYPQGIPLDI EEQKGPFVSV
     LGLSEKLEGK TRPNFFRGVA TVVTKLFNIV MADVAYFGQK DIQQFIVLQC MVDELFVNTR
     LQMMPIVRNN NGLALSSRNK YLCPESLKIS ENLYRGLKAA ENAIRRLAPG GRLSRSEIID
     TVTQIWAPYV DSHDFKIDYV SLADFKTLDE LSDVENTSEQ QPIVISCAVY VTDREKPDTV
     VRLIDNIVI
//