ID   POK_METHJ               Reviewed;         289 AA.
AC   Q2FUB2;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Pantoate kinase {ECO:0000255|HAMAP-Rule:MF_02223, ECO:0000303|PubMed:23200110};
DE            Short=PoK {ECO:0000255|HAMAP-Rule:MF_02223, ECO:0000303|PubMed:23200110};
DE            EC=2.7.1.169 {ECO:0000255|HAMAP-Rule:MF_02223};
GN   OrderedLocusNames=Mhun_0831 {ECO:0000312|EMBL:ABD40583.1};
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX   PubMed=23200110; DOI=10.1016/j.jbiosc.2012.10.019;
RA   Katoh H., Tamaki H., Tokutake Y., Hanada S., Chohnan S.;
RT   "Identification of pantoate kinase and phosphopantothenate synthetase from
RT   Methanospirillum hungatei.";
RL   J. Biosci. Bioeng. 115:372-376(2013).
CC   -!- FUNCTION: Phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in
CC       the CoA biosynthesis pathway (PubMed:23200110). ATP is the best
CC       phosphate donor. Can be replaced with UTP, with lower efficiency
CC       (PubMed:23200110). {ECO:0000269|PubMed:23200110}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + ATP = (R)-4-phosphopantoate + ADP + H(+);
CC         Xref=Rhea:RHEA:28246, ChEBI:CHEBI:15378, ChEBI:CHEBI:15980,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61294, ChEBI:CHEBI:456216;
CC         EC=2.7.1.169; Evidence={ECO:0000255|HAMAP-Rule:MF_02223,
CC         ECO:0000269|PubMed:23200110};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:23200110};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:23200110};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02223, ECO:0000305|PubMed:23200110}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. PoK subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02223}.
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DR   EMBL; CP000254; ABD40583.1; -; Genomic_DNA.
DR   RefSeq; WP_011447862.1; NC_007796.1.
DR   AlphaFoldDB; Q2FUB2; -.
DR   SMR; Q2FUB2; -.
DR   STRING; 323259.Mhun_0831; -.
DR   EnsemblBacteria; ABD40583; ABD40583; Mhun_0831.
DR   GeneID; 3922282; -.
DR   KEGG; mhu:Mhun_0831; -.
DR   eggNOG; arCOG04263; Archaea.
DR   HOGENOM; CLU_081191_0_0_2; -.
DR   OMA; MLGETVF; -.
DR   OrthoDB; 104702at2157; -.
DR   BRENDA; 2.7.1.169; 3282.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000001941; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_02223; Pantoate_kinase; 1.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR012043; PoK.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR42282; PTHR42282; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF016896; GHMP_arc_MJ0969; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coenzyme A biosynthesis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..289
FT                   /note="Pantoate kinase"
FT                   /id="PRO_0000448240"
SQ   SEQUENCE   289 AA;  31027 MW;  67243687E089DE0B CRC64;
     MELTRVTAFC PGHISGYFLP VIHDDPDLSG SIGAGIVISE GVRVIAEKSA DSTVKIFQTD
     RYGLPEEIAE SSPVLMDLLA YMQVNASIET FCHLPIGSGY GMSAAALLGT VHALNALYNF
     HLSPRECARI AHRIEVQHQS GLGDISACQG GGFVIRKTPG PDGDIMRVID TRPIYALTIS
     PIKTSSVLSS HDMIAQITQS FPSRIPQNLD DIMSLSREFA EKSGLISKEI RTVLTACDKE
     NLPASMTMLG CGVFALGKRA ETVLKKFGEV FKLTISPGGP AILFGERSS