ID A0A2I0PVV1_9EURY Unreviewed; 288 AA.
AC A0A2I0PVV1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=CVV30_03280 {ECO:0000313|EMBL:PKL70393.1};
OS Methanomicrobiales archaeon HGW-Methanomicrobiales-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales.
OX NCBI_TaxID=2013817 {ECO:0000313|EMBL:PKL70393.1, ECO:0000313|Proteomes:UP000233367};
RN [1] {ECO:0000313|EMBL:PKL70393.1, ECO:0000313|Proteomes:UP000233367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGW-Methanomicrobiales-1 {ECO:0000313|EMBL:PKL70393.1};
RX PubMed=28350393; DOI=10.1038/ismej.2017.39;
RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K.,
RA Probst A., Burstein D., Thomas B.C., Banfield J.F.;
RT "Potential for microbial H2 and metal transformations associated with novel
RT bacteria and archaea in deep terrestrial subsurface sediments.";
RL ISME J. 11:1915-1929(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}.
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:PKL70393.1}.
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DR EMBL; PGYM01000001; PKL70393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0PVV1; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000233367; 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 NCBIfam; NF040725; panto_kin_Meth; 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:PKL70393.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02223};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02223}.
FT DOMAIN 88..148
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
SQ SEQUENCE 288 AA; 30426 MW; FDF6BFD1C73154C5 CRC64;
MRPNSVSAFC PGHISGYFKK ISGSTSLTTG SIGAGIVITE GVTATVMPAD SPSVVIMHRA
VNGTTTIIAR ESPLMTSVME RLGVTASITT ECRLPIGAGF GLSAAALLAS ATALNRLFSL
GLTPWDIARH SHEIEVEHRT GLGDVAAAQG GGRVIRHGPG IDAKIERNFD LPESLYSISF
GPIHTPTVLG SPSQMEQVSS AFPSVVPHDT GEFFTASRQF AEQSGLITDQ VKKVFNICEH
ENIPVGMTML GNGVFAYGKK ARHVLSAFGE VYEFRVSPTG PEITGEEI
//
