ID Q8TRA1_METAC Unreviewed; 322 AA.
AC Q8TRA1;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Pantoate kinase {ECO:0000256|HAMAP-Rule:MF_02223};
DE Short=PoK {ECO:0000256|HAMAP-Rule:MF_02223};
DE EC=2.7.1.169 {ECO:0000256|HAMAP-Rule:MF_02223};
GN OrderedLocusNames=MA_1279 {ECO:0000313|EMBL:AAM04698.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM04698.1, ECO:0000313|Proteomes:UP000002487};
RN [1] {ECO:0000313|EMBL:AAM04698.1, ECO:0000313|Proteomes:UP000002487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC {ECO:0000313|Proteomes:UP000002487};
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A., Hedderich R., Ingram-Smith C.,
RA Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B.,
RA Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H.,
RA de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L.,
RA Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H.,
RA Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
CC -!- FUNCTION: Phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in
CC the CoA biosynthesis pathway. {ECO:0000256|HAMAP-Rule:MF_02223}.
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:0000256|HAMAP-Rule:MF_02223};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02223}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. PoK subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02223}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE010299; AAM04698.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TRA1; -.
DR STRING; 188937.MA_1279; -.
DR EnsemblBacteria; AAM04698; AAM04698; MA_1279.
DR KEGG; mac:MA_1279; -.
DR HOGENOM; CLU_081191_0_0_2; -.
DR InParanoid; Q8TRA1; -.
DR PhylomeDB; Q8TRA1; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000002487; 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; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR012043; PoK.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR42282:SF1; PANTOATE KINASE; 1.
DR PANTHER; PTHR42282; PANTOATE KINASE-RELATED; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF016896; GHMP_arc_MJ0969; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02223};
KW Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_02223};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_02223};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02223};
KW Reference proteome {ECO:0000313|Proteomes:UP000002487};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02223}.
FT DOMAIN 104..168
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 226..295
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
SQ SEQUENCE 322 AA; 34291 MW; DAC4085FDD10DA18 CRC64;
MNFENSLNNK KAFYMYTYES EGADFIAKAY APGHITGFFQ IHEHNDPHRK GSTGCGIVLN
GGVTTEVKAG KSVEKTEIFL NGKKVEGRTT RTVVEMLTDV PVKVKSWAEI PVGCGFGASG
AGALGAAYAL NRVLSLNQTV KSLTEYAHVA EVVNRSGLGD IAAQSNGGVV IRLHPGGPEF
GRIDRIPAPE ARVFGIALGE ISTDSILTDE VTAGKINAAG KVAMSELLKK PTLENFMHQA
KDFASNTGLM SSTAKDVIEA AHANGGLASQ AMLGDTVFAI APYAQEFPLF EALQEFGQVA
LQEFGQVLEY GISTCVPRLL YD
//
