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Database: UniProt
Entry: A0A2T6AD53_9RHOB
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ID   A0A2T6AD53_9RHOB        Unreviewed;       270 AA.
AC   A0A2T6AD53;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Hydroxymethylpyrimidine kinase /phosphomethylpyrimidine kinase {ECO:0000313|EMBL:PTX41749.1};
GN   ORFNames=C8N44_12715 {ECO:0000313|EMBL:PTX41749.1};
OS   Allosediminivita pacifica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Allosediminivita.
OX   NCBI_TaxID=1267769 {ECO:0000313|EMBL:PTX41749.1, ECO:0000313|Proteomes:UP000244069};
RN   [1] {ECO:0000313|EMBL:PTX41749.1, ECO:0000313|Proteomes:UP000244069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29329 {ECO:0000313|EMBL:PTX41749.1,
RC   ECO:0000313|Proteomes:UP000244069};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-
CC         amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP;
CC         Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841,
CC         ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00000565};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-
CC         methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+);
CC         Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216;
CC         EC=2.7.1.49; Evidence={ECO:0000256|ARBA:ARBA00000151};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
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:PTX41749.1}.
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DR   EMBL; QBKN01000027; PTX41749.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T6AD53; -.
DR   OrthoDB; 9810880at2; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000244069; Unassembled WGS sequence.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01169; HMPP_kinase; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR029056; Ribokinase-like.
DR   NCBIfam; TIGR00097; HMP-P_kinase; 1.
DR   PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR   PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:PTX41749.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244069};
KW   Transferase {ECO:0000313|EMBL:PTX41749.1}.
FT   DOMAIN          12..258
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   270 AA;  27497 MW;  95D4EBA7974C225E CRC64;
     MIPNILSIAG SDPSGGAGIQ ADIKTISAEG GYAMAAITAL TAQNTQGVTG FEVTAPGLVR
     DQIAAIREDI RIDAVKIGML GSAEVVEVVA RALEGIEAPI VLDPVMVAKG GDRLLATDAV
     LALRDALLPI ATVITPNLPE AGDLLGETAP TTRDEMQAQA AALLALGPAA VLLKGGHLPG
     DGCPDLLARR EGAVWIEGTR HATRNTHGTG CTLSSALATA LGHRLPLEDA ARRTKAYVAA
     SIAGAGRLTV GSGHGPVHHF HAITRGNHND
//
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