ID A0A133ZIN5_9CORY Unreviewed; 527 AA.
AC A0A133ZIN5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:KXB55312.1};
GN ORFNames=HMPREF0307_00957 {ECO:0000313|EMBL:KXB55312.1};
OS Corynebacterium sp. DNF00584.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1384076 {ECO:0000313|EMBL:KXB55312.1, ECO:0000313|Proteomes:UP000070591};
RN [1] {ECO:0000313|EMBL:KXB55312.1, ECO:0000313|Proteomes:UP000070591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00584 {ECO:0000313|EMBL:KXB55312.1,
RC ECO:0000313|Proteomes:UP000070591};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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:KXB55312.1}.
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DR EMBL; LSCZ01000014; KXB55312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133ZIN5; -.
DR PATRIC; fig|1384076.3.peg.936; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000070591; 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:KXB55312.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070591};
KW Transferase {ECO:0000313|EMBL:KXB55312.1}.
FT DOMAIN 27..274
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 325..523
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
SQ SEQUENCE 527 AA; 55329 MW; 65ECB1CB9644ED98 CRC64;
MNDAVIGAPA SARIPAVPRV LSIAGTDPTG GAGIQADLKS IAAAGGYGMS AVTALVAQNT
QGVREVHTPP VEFLRAQLTA VASDVTIDAV KIGMLGSAAI VAEVSRFLAQ LSDVPVVLDP
VMVATSGDRL LDRDAEAAVR ELCARATVVT PNLKELAVLT QTAEATTLEE AIAHATAWSA
DTRTTVIVKG GHLRGDLADN AVVTPDGAVH RVSCPRVDTP HTHGTGCSLS SALATRLGAG
ASLSDALSWS TRWLHEAISH AAALEVGQGH GPVDHGHRAR RLAAAASTVP ARFYSDVTST
AAAPAPHVSA AGPETARLWE LTGDAWQSIT QLPFIQALGT GTLREEDFAF YLAQDAQYLN
QYSKALARLA ALAPDAGAQL HWASGAAECL AVEMSLHKDW IAHHTTTVPS TALTAPSRVT
SAYTDFLVST THTDDYVVAA AAVLPCYWLY AEVGLHLAAQ NSPEHPYNAW ITQYGGEEFL
TGVRAAIALV EEALTAADPA TRSRATRAYL AACWHEVDFF DQADRRW
//
