ID S2ZVF6_9CORY Unreviewed; 499 AA.
AC S2ZVF6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:EPD68034.1};
GN ORFNames=HMPREF1219_02458 {ECO:0000313|EMBL:EPD68034.1};
OS Corynebacterium pyruviciproducens ATCC BAA-1742.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1125779 {ECO:0000313|EMBL:EPD68034.1, ECO:0000313|Proteomes:UP000014408};
RN [1] {ECO:0000313|EMBL:EPD68034.1, ECO:0000313|Proteomes:UP000014408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1742 {ECO:0000313|EMBL:EPD68034.1,
RC ECO:0000313|Proteomes:UP000014408};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Tong J., Walker B., Young S.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Corynebacterium pyruviciproducens 1773O (ATCC BAA-
RT 1742).";
RL Submitted (MAY-2013) 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:EPD68034.1}.
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DR EMBL; ATBY01000017; EPD68034.1; -; Genomic_DNA.
DR AlphaFoldDB; S2ZVF6; -.
DR STRING; 1125779.HMPREF1219_02458; -.
DR PATRIC; fig|1125779.3.peg.2396; -.
DR eggNOG; COG0351; Bacteria.
DR eggNOG; COG0819; Bacteria.
DR HOGENOM; CLU_020520_2_0_11; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000014408; 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 CDD; cd19365; TenA_C-like; 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 Kinase {ECO:0000313|EMBL:EPD68034.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014408};
KW Transferase {ECO:0000313|EMBL:EPD68034.1}.
FT DOMAIN 12..259
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 315..470
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
SQ SEQUENCE 499 AA; 53751 MW; 78362E7A88109742 CRC64;
MLPRVLTIAG TDPTGGAGLQ ADIKSISEAG GFPLSVATAL VAQNTQGVRE IHTPPLEFLT
AQLDAVFDDV EVDAVKIGML GSAEITRLVI DYLDRHPVPF LVVDPVMVAT SGDRLLSVEA
EDAVRELCKR ATIVTPNLSE QAVLARAEEV HTHEEAIEQA TSLARDLGTA VLVKGGHLAG
NRADNAVVHP TGEVFRIRNV RVNTKNTHGT GCSLSSCLAT RLAVGQPLDK AAQWATLWLS
TAIRHADDLH VGKGNGPVDH TAWNRMYREA ASTAPWDLSP APSEEKPLVA PAGPRTQALW
SRCSSLLRAI LGDGFLTMLA DGTLPEHAFR FYLEQDALYL REYGKALAGV ASHSPNSQDM
IAWARDAQNT MTEEANLHRE ILGGETHAEP SYVTLGYTSL LGAAEGKDYV VAAATVLPCY
WLYAEVALRM AEKNTPNHPY HAWLTAYADE GFIEDTRQAI ERVERALEAA GEATPRRGDA
QLHVRRLLGA RVLQPGAAG
//
