ID A0A0P1GQQ2_9RHOB Unreviewed; 266 AA.
AC A0A0P1GQQ2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:CUH77560.1};
DE EC=2.7.1.49 {ECO:0000313|EMBL:CUH77560.1};
GN Name=thiD {ECO:0000313|EMBL:CUH77560.1};
GN ORFNames=TRM7557_01435 {ECO:0000313|EMBL:CUH77560.1};
OS Tritonibacter multivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=928856 {ECO:0000313|EMBL:CUH77560.1, ECO:0000313|Proteomes:UP000052022};
RN [1] {ECO:0000313|EMBL:CUH77560.1, ECO:0000313|Proteomes:UP000052022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7557 {ECO:0000313|EMBL:CUH77560.1,
RC ECO:0000313|Proteomes:UP000052022};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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}.
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DR EMBL; CYSD01000020; CUH77560.1; -; Genomic_DNA.
DR RefSeq; WP_058289530.1; NZ_JAQIPA010000011.1.
DR AlphaFoldDB; A0A0P1GQQ2; -.
DR STRING; 928856.SAMN04488049_11195; -.
DR OrthoDB; 9810880at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000052022; Unassembled WGS sequence.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC.
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:CUH77560.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052022};
KW Transferase {ECO:0000313|EMBL:CUH77560.1}.
FT DOMAIN 12..259
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 266 AA; 27400 MW; B65D106F80F6C59F CRC64;
MIANVLSIAG SDPSGGAGIQ ADLKSISANG AFAMAAITAL TAQNTQGVTG IQLVPGDFVE
NQIKTVFDDV RVDGVKIGMI ATAEIAQAVA NALQPHKNVP IVLDPVMIAK GGAPLLADDA
IETLRSALLP LAHVLTPNLP EAAHLLGLEP ATTRDEMVSQ GRALCALGPR AVLMKGGHLE
QDDSPDALVT ADDVHWFEAA RTQTKNTHGT GCTLSSALAA QIAQGQPLPE AVQAAKSYVA
QAIAQADQLT VGSGHGPTHH FCKFYS
//
