ID A0A3P5XPM4_9MICC Unreviewed; 515 AA.
AC A0A3P5XPM4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 08-OCT-2025, entry version 29.
DE SubName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:VDC32350.1};
DE EC=2.7.1.49 {ECO:0000313|EMBL:VDC32350.1};
GN Name=thiD {ECO:0000313|EMBL:VDC32350.1};
GN ORFNames=PSET11_03081 {ECO:0000313|EMBL:VDC32350.1};
OS Arthrobacter ulcerisalmonis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=2483813 {ECO:0000313|EMBL:VDC32350.1, ECO:0000313|Proteomes:UP000280861};
RN [1] {ECO:0000313|EMBL:VDC32350.1, ECO:0000313|Proteomes:UP000280861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT11b {ECO:0000313|EMBL:VDC32350.1};
RA Criscuolo A.;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine
CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
CC {ECO:0000256|ARBA:ARBA00003848}.
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; 4-
CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole: step 3/3. {ECO:0000256|ARBA:ARBA00004769}.
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DR EMBL; UXAU01000040; VDC32350.1; -; Genomic_DNA.
DR RefSeq; WP_377947625.1; NZ_CBCRYA010000011.1.
DR AlphaFoldDB; A0A3P5XPM4; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000280861; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01169; HMPP_kinase; 1.
DR CDD; cd19365; TenA_C-like; 1.
DR FunFam; 3.40.1190.20:FF:000003; Phosphomethylpyrimidine kinase ThiD; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR004305; Thiaminase-2/PQQC.
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 Pfam; PF03070; TENA_THI-4; 1.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:VDC32350.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000280861};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:VDC32350.1}.
FT DOMAIN 39..290
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 322..510
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
SQ SEQUENCE 515 AA; 53756 MW; 04B79FA885AC59C0 CRC64;
MSSTLIDSAA PAHSTHAASL AAPPSIRAIP RVLSIAGSDP SGGAGIQADL KSIAAHGGYG
MAAITALTVQ NTLGVQAVHV PPAEFLAQQL AAVSADITID AVKIGMLADA AVIRAVRVWL
EEVRPAVVVL DPVMVSTSGD RLLADDAEAE LLALLPLAHL ITPNLAELAV LVGGAEQQTW
AGALAQGRQL ASITGATVLV KGGHLPGDSC PDALVNTTGL LATEVVEFAG ERISTSNSHG
TGCTLSSAMA TVQAQVGDWE AALRAVKPWL AGALTASDQL DVGAGNGPVH HFHHLTQGVP
GSFAAQLWAG AAKDLEAIYT LPFIRALVDG SLPEHEFADY LSQDAIYLNG YARVLARTSA
LAPTEAEQVF WAGSAQQCLE VESDLHRTWL ASRPAPRQTG PVTKAYVDHL TAVSASGSYG
TLAAAVLPCF WLYAEVGQTL HAQFIEAGEP AGHPYAAWLR TYADEDFAAA TRRAIKIVDQ
AGRDASERER AAMVEAFNHA CRLEVEFFDA PRVHA
//
