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Database: UniProt
Entry: A0A285IVT1_9ACTN
LinkDB: A0A285IVT1_9ACTN
Original site: A0A285IVT1_9ACTN 
ID   A0A285IVT1_9ACTN        Unreviewed;       252 AA.
AC   A0A285IVT1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:SNY51933.1};
GN   ORFNames=SAMN05421748_112148 {ECO:0000313|EMBL:SNY51933.1};
OS   Actinoplanes atraurantiacus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1036182 {ECO:0000313|EMBL:SNY51933.1, ECO:0000313|Proteomes:UP000219612};
RN   [1] {ECO:0000313|EMBL:SNY51933.1, ECO:0000313|Proteomes:UP000219612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6857 {ECO:0000313|EMBL:SNY51933.1,
RC   ECO:0000313|Proteomes:UP000219612};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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; OBDY01000012; SNY51933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285IVT1; -.
DR   OrthoDB; 34166at2; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000219612; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   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:SNY51933.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219612};
KW   Transferase {ECO:0000313|EMBL:SNY51933.1}.
FT   DOMAIN          13..249
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   252 AA;  25144 MW;  FB3E3CA01FD8049D CRC64;
     MTPPVVLTIA GSDSGGGAGI QADLKTFAAL GAFGTSVITA VTAQNTLGVT AIHPIPIDIV
     AAQLDAVLAD FPVAAVKVGM IGDPAVAALI AGRATQLPNL VIDPVLVATS GARLADTAAV
     APLASYNCVL TPNRQEAAAL TGSPVETAEE MVFAAESLAK RGARAVVVTG SETAADVLWH
     DGTVETLHGE PVPTANNHGS GCTFSSAIAV RLAAGDPVPV AVRAAKRYVS AALAGGRDWR
     LGAGPGPLHH FI
//
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