ID   C9RDS2_METVM            Unreviewed;       258 AA.
AC   C9RDS2;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   04-NOV-2026, entry version 62.
DE   RecName: Full=4-phosphopantoate--beta-alanine ligase {ECO:0000256|HAMAP-Rule:MF_02224};
DE            EC=6.3.2.36 {ECO:0000256|HAMAP-Rule:MF_02224};
DE   AltName: Full=Phosphopantothenate synthetase {ECO:0000256|HAMAP-Rule:MF_02224};
DE            Short=PPS {ECO:0000256|HAMAP-Rule:MF_02224};
GN   OrderedLocusNames=Metvu_1598 {ECO:0000313|EMBL:ACX73451.1};
OS   Methanocaldococcus vulcanius (strain ATCC 700851 / DSM 12094 / M7)
OS   (Methanococcus vulcanius).
OC   Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC   Methanococci; Methanococcales; Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=579137 {ECO:0000313|EMBL:ACX73451.1, ECO:0000313|Proteomes:UP000002063};
RN   [1] {ECO:0000313|EMBL:ACX73451.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M7 {ECO:0000313|EMBL:ACX73451.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Lcollab F.I., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ovchinikova G., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT   "Complete sequence of chromosome of Methanocaldococcus vulcanius M7.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of (R)-4-phosphopantoate and beta-
CC       alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway.
CC       {ECO:0000256|HAMAP-Rule:MF_02224}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-4-phosphopantoate + beta-alanine + ATP = (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:0000256|HAMAP-
CC         Rule:MF_02224};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02224}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02224}.
CC   -!- SIMILARITY: Belongs to the archaeal phosphopantothenate synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_02224}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_02224}.
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DR   EMBL; CP001787; ACX73451.1; -; Genomic_DNA.
DR   RefSeq; WP_015733670.1; NC_013407.1.
DR   AlphaFoldDB; C9RDS2; -.
DR   STRING; 579137.Metvu_1598; -.
DR   GeneID; 8513955; -.
DR   KEGG; mvu:Metvu_1598; -.
DR   eggNOG; arCOG04262; Archaea.
DR   HOGENOM; CLU_078701_0_0_2; -.
DR   OMA; ACIREMT; -.
DR   OrthoDB; 10078at2157; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000002063; Chromosome.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.12640; Phosphopantoate/pantothenate synthetase; 1.
DR   HAMAP; MF_02224; PPS; 1.
DR   InterPro; IPR002855; PPS/PS.
DR   InterPro; IPR038138; PPS/PS_sf.
DR   NCBIfam; NF041123; phpantohe_syn_Arch; 1.
DR   NCBIfam; NF010324; PRK13761.1; 1.
DR   PANTHER; PTHR40695; 4-PHOSPHOPANTOATE--BETA-ALANINE LIGASE; 1.
DR   PANTHER; PTHR40695:SF1; 4-PHOSPHOPANTOATE--BETA-ALANINE LIGASE; 1.
DR   Pfam; PF02006; PPS_PS; 1.
DR   PIRSF; PIRSF004853; UCP004853; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02224};
KW   Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993, ECO:0000256|HAMAP-
KW   Rule:MF_02224};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02224};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02224}; Reference proteome {ECO:0000313|Proteomes:UP000002063}.
FT   BINDING         16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02224"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02224"
FT   BINDING         187..189
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02224"
FT   BINDING         193..194
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02224"
SQ   SEQUENCE   258 AA;  28967 MW;  B7B8E0849E0759DA CRC64;
     MQVPKTHPRY ESLMKREKII EALDKGILAK AGLIAHGRGE MFDYLIGERT IPPALKAIEA
     AAATLILSKN PVISVNGNTV ALAIEDTVEL AKELNGKIEV NLFYRTKERE LAIKNVFEEK
     FGNDIKEGKI TILGIDDATE QIPNLDSLRG KVSKEGIFSA DVVLVPLEDG DRAEALVNMG
     KKVIAIDLNP LSRTSKKSTI TIVDELTRAL PLLIKYVREF KRKNREDLLK IVEDFNNKKN
     LKETVEYIAE RLKKLEFE
//