ID A0A1I4UTX7_9EURY Unreviewed; 297 AA.
AC A0A1I4UTX7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=SAMN04488696_2884 {ECO:0000313|EMBL:SFM92422.1};
OS Methanolobus profundi.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX NCBI_TaxID=487685 {ECO:0000313|EMBL:SFM92422.1, ECO:0000313|Proteomes:UP000198535};
RN [1] {ECO:0000313|EMBL:SFM92422.1, ECO:0000313|Proteomes:UP000198535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mob M {ECO:0000313|EMBL:SFM92422.1,
RC ECO:0000313|Proteomes:UP000198535};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOUJ01000008; SFM92422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4UTX7; -.
DR STRING; 487685.SAMN04488696_2884; -.
DR OrthoDB; 85822at2157; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000198535; Unassembled WGS sequence.
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_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; 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:SFM92422.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02223};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02223}.
FT DOMAIN 89..153
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
SQ SEQUENCE 297 AA; 31261 MW; D77E3606BEB6B584 CRC64;
MQCGSCKDKF TARAFAPAHI TGFFQIHDHK EPMKKGSTGC GVVLDRGVHT TVTIGDDIES
TDIYLNGEKV AGDTSRAVVS SMTEIPVTVE STSEIPIGCG FGASGAGALG TAYALDHALS
LGHTASQLND IAHVAEVSNG SGLGDVTGQA HGGILIRKTP GAPSVASVDQ IPSKENDVYC
VVLGELSTSS VLSDQEMVND INNAGKEAMK KLMQKPSVEN FMHCSRDFTI QSMLASEKVM
DAIEAADTIG VTASQAMLGN AVFSMPSQKD SNELENIFSE FGTVLRFKVR TGTIRIN
//
