ID   PPS_METJA               Reviewed;         266 AA.
AC   Q57662;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=4-phosphopantoate--beta-alanine ligase {ECO:0000255|HAMAP-Rule:MF_02224};
DE            EC=6.3.2.36 {ECO:0000255|HAMAP-Rule:MF_02224};
DE   AltName: Full=Phosphopantothenate synthetase {ECO:0000255|HAMAP-Rule:MF_02224};
DE            Short=PPS {ECO:0000255|HAMAP-Rule:MF_02224};
GN   OrderedLocusNames=MJ0209;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Catalyzes the condensation of (R)-4-phosphopantoate and beta-
CC       alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway.
CC       {ECO:0000255|HAMAP-Rule:MF_02224}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-4-phosphopantoate + ATP + beta-alanine = (R)-4'-
CC         phosphopantothenate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:27930,
CC         ChEBI:CHEBI:10986, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:61294,
CC         ChEBI:CHEBI:456215; EC=6.3.2.36; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02224};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02224}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02224}.
CC   -!- SIMILARITY: Belongs to the archaeal phosphopantothenate synthetase
CC       family. {ECO:0000255|HAMAP-Rule:MF_02224}.
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DR   EMBL; L77117; AAB98192.1; -; Genomic_DNA.
DR   PIR; B64326; B64326.
DR   AlphaFoldDB; Q57662; -.
DR   SMR; Q57662; -.
DR   STRING; 243232.MJ_0209; -.
DR   PRIDE; Q57662; -.
DR   EnsemblBacteria; AAB98192; AAB98192; MJ_0209.
DR   KEGG; mja:MJ_0209; -.
DR   eggNOG; arCOG04262; Archaea.
DR   HOGENOM; CLU_078701_0_0_2; -.
DR   InParanoid; Q57662; -.
DR   OMA; PKSHPRY; -.
DR   PhylomeDB; Q57662; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.12640; -; 1.
DR   HAMAP; MF_02224; PPS; 1.
DR   InterPro; IPR002855; PPS/PS.
DR   InterPro; IPR038138; PPS/PS_sf.
DR   PANTHER; PTHR40695; PTHR40695; 1.
DR   Pfam; PF02006; PPS_PS; 1.
DR   PIRSF; PIRSF004853; UCP004853; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coenzyme A biosynthesis; Ligase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..266
FT                   /note="4-phosphopantoate--beta-alanine ligase"
FT                   /id="PRO_0000106742"
FT   BINDING         22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02224"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02224"
FT   BINDING         193..195
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02224"
FT   BINDING         199..200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02224"
SQ   SEQUENCE   266 AA;  29853 MW;  D3B064215551E6C5 CRC64;
     MLSVMRMQIP KTHPRYESLM KREKIIEALD KGILAKAGLI AHGRGETFDY LIGEKTAPIA
     LEAIKAAAAL LILAENPVIS VNGNTVALAI DEVVELAKEL NGKIEVNLFY RTKERELAIK
     RAFEEKFKDD IETGKIKILG IDDANKQIPN LDSLRGKVSE EGIFTADVVL VPLEDGDRAE
     ALVNMGKKVI AIDLNPLSRT ARKSTITIVD ELTRAMPLLI KYVKEFKNKD REELLKIVED
     FDNKKNLKDM IDYIAERLKN LSLDEL