ID A0A1Z2TPI0_9EURY Unreviewed; 300 AA.
AC A0A1Z2TPI0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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 ORFNames=CDI07_08450 {ECO:0000313|EMBL:ASA78323.1};
OS Thermococcus sp. 5-4.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=2008440 {ECO:0000313|EMBL:ASA78323.1, ECO:0000313|Proteomes:UP000196843};
RN [1] {ECO:0000313|EMBL:ASA78323.1, ECO:0000313|Proteomes:UP000196843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-4 {ECO:0000313|EMBL:ASA78323.1,
RC ECO:0000313|Proteomes:UP000196843};
RX PubMed=28628615; DOI=10.1371/journal.pgen.1006847;
RA Cossu M., Badel C., Catchpole R., Daniele G., Marguet E., Barbe V.,
RA Forterre P., Oberto J.;
RT "Flipping chromosomes in deep-sea archaea.";
RL PLoS Genet. 13:e1006847-e1006847(2017).
RN [2] {ECO:0000313|Proteomes:UP000196843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-4 {ECO:0000313|Proteomes:UP000196843};
RA Cossu M., Badel C., Catchpole R., Daniele G., Marguet E., Barbe V.,
RA Forterre P., Oberto J.;
RT "Flipping Chromosomes in Deep-Sea Archaea.";
RL PLoS Genet. 0:0-0(2017).
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}.
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DR EMBL; CP021848; ASA78323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z2TPI0; -.
DR KEGG; thh:CDI07_08450; -.
DR OrthoDB; 85822at2157; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000196843; 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 HAMAP; MF_02223; Pantoate_kinase; 1.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR012043; PoK.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR NCBIfam; NF041122; panto_kin_Thplsm; 1.
DR PANTHER; PTHR42282:SF1; PANTOATE KINASE; 1.
DR PANTHER; PTHR42282; PANTOATE KINASE-RELATED; 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, ECO:0000313|EMBL:ASA78323.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02223};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02223}.
FT DOMAIN 89..151
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
SQ SEQUENCE 300 AA; 32531 MW; 64860F9481E210BB CRC64;
MLVRTFVPAH ITAFFVPRFH DDPLRAGSLG AGVNLDKGVN VFASIETGTL ERHIHVAFNG
EPVERKRAII SYSVADELVP DNFVGEVEIW QYFDFPNGHG FGNSAGGALG TALALSYSFG
GTWLKAAQIA HKHEVLNRGG LGDVVGQLAG GIEVRVKAGG PGVGVVDNLF FEDYRVLVVP
LGRLSTREVL DGDVVEAIER EGKEALEKLL LEPRPERMMA LAREFAEKTG LLSGELLELA
RELDKVISTP SSMIMLGRGL FALLHENEVE NAISLLSDLN LPYDVTGIHE GRPKVGRWVG
//
