ID A0A1D8SV75_STROV Unreviewed; 264 AA.
AC A0A1D8SV75;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:MBF8170401.1};
DE EC=2.7.1.49 {ECO:0000313|EMBL:MBF8170401.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:MBF8170401.1};
GN Name=thiD {ECO:0000313|EMBL:MBF8170401.1};
GN ORFNames=IW294_06400 {ECO:0000313|EMBL:MBF8170401.1};
OS Streptomyces olivaceus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=47716 {ECO:0000313|EMBL:MBF8170401.1, ECO:0000313|Proteomes:UP000621371};
RN [1] {ECO:0000313|EMBL:MBF8170401.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL B-3009 {ECO:0000313|EMBL:MBF8170401.1};
RA Hu D.;
RT "Activation and comparative analysis of cryptic gene cluster from mangrove-
RT derived Streptomyces olivaceus.";
RL Submitted (NOV-2020) 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}.
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:MBF8170401.1}.
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DR EMBL; JADOEJ010000006; MBF8170401.1; -; Genomic_DNA.
DR RefSeq; WP_031034161.1; NZ_JOFH01000008.1.
DR AlphaFoldDB; A0A1D8SV75; -.
DR Proteomes; UP000621371; 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 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:MBF8170401.1};
KW Transferase {ECO:0000313|EMBL:MBF8170401.1}.
SQ SEQUENCE 264 AA; 26915 MW; B230F37389E0C950 CRC64;
MRPPLVLTVA GSDSGGGAGI QADLKTMLAL GTHGMSVLTA VTAQNSLGVQ GAWELPVAAV
RAQYRSVVDD IGVHAVKTGM LSSAELVEAV AELIDGTDAP AVVDPVGVSK HGDALLAASA
LDSVRTRLLP VATVATPNLD EVAQLTGVRV GSEADLRRAA SAVLEYGPRW VLVKGGHLPG
DAVDLLTDGS EEHWLRGPRL DNRHTHGTGC TLASAVACGL AKGQPVPDAV RAAKEYVTGA
IRSGFALGAG IGPVDHGWEL GRPS
//
