ID A0A0N8PWI0_9ARCH Unreviewed; 302 AA.
AC A0A0N8PWI0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=AOA66_0498 {ECO:0000313|EMBL:KPV63981.1};
OS Candidatus Bathyarchaeota archaeon BA2.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1700836 {ECO:0000313|EMBL:KPV63981.1, ECO:0000313|Proteomes:UP000050284};
RN [1] {ECO:0000313|EMBL:KPV63981.1, ECO:0000313|Proteomes:UP000050284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA2 {ECO:0000313|EMBL:KPV63981.1};
RX PubMed=26494757; DOI=10.1126/science.aac7745;
RA Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J.,
RA Golding S.D., Tyson G.W.;
RT "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by
RT genome-centric metagenomics.";
RL Science 350:434-438(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPV63981.1}.
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DR EMBL; LIHK01000012; KPV63981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8PWI0; -.
DR STRING; 1700836.AOA66_0498; -.
DR KEGG; barb:AOA66_0498; -.
DR PATRIC; fig|1700836.3.peg.1273; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000050284; 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:KPV63981.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02223};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02223}.
FT DOMAIN 94..153
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
SQ SEQUENCE 302 AA; 32567 MW; 77445B0E60E300A7 CRC64;
MKEFTAFSPG HITGLFQICD EAEEPLLKGS RGAGVSITRG VITKIRIEKA PKTSFEIRIN
GHGVKSAKVS ECVINALLPV AEGNYRILVD HKVNVPIGSG FGSSGAGALS LALALNEAFR
CGLSHVEAAQ VVHIAEIKCK TGLGTVIAET FGGLEIREKP GAPGVGEVKH IPIDDDYVVA
CLKFGPMSTK EALTNERLRQ RINDLGGKLV DELIARPKPA NFMNFSRSFA EGVGLISKRM
RKALEEADGK GITCSMTMFG ECLFSLVRGD KAEELLEIFR RHTLSEDNII VAEIDHEGAR
LL
//
