ID A0A076NEV7_9CORY Unreviewed; 502 AA.
AC A0A076NEV7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=4-amino-5-aminomethyl-2-methylpyrimidine hydrolase {ECO:0000313|EMBL:AIJ32964.1};
GN ORFNames=CIMIT_02735 {ECO:0000313|EMBL:AIJ32964.1};
OS Corynebacterium imitans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=156978 {ECO:0000313|EMBL:AIJ32964.1, ECO:0000313|Proteomes:UP000028780};
RN [1] {ECO:0000313|EMBL:AIJ32964.1, ECO:0000313|Proteomes:UP000028780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44264 {ECO:0000313|EMBL:AIJ32964.1,
RC ECO:0000313|Proteomes:UP000028780};
RA Mollmann S., Albersmeier A., Ruckert C., Tauch A.;
RT "Complete genome sequence of Corynebacterium imitans DSM 44264, isolated
RT from a five-month-old boy with suspected pharyngeal diphtheria.";
RL Submitted (AUG-2014) 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; CP009211; AIJ32964.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A076NEV7; -.
DR STRING; 156978.CIMIT_02735; -.
DR KEGG; cii:CIMIT_02735; -.
DR eggNOG; COG0351; Bacteria.
DR eggNOG; COG0819; Bacteria.
DR HOGENOM; CLU_020520_2_0_11; -.
DR OrthoDB; 34166at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000028780; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; 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 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; 2.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AIJ32964.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028780}.
FT DOMAIN 16..263
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 318..365
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
FT DOMAIN 384..493
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
SQ SEQUENCE 502 AA; 53757 MW; 519D3B9980B6E09C CRC64;
MNTPALPRIL TIAGTDPTGG AGVQADIKSI QAAGGFSYSV VTSLVAQNTT GVQEIFTPPI
DFLRTQLRSI TDDVAIDAIK IGMLGTTEII EVVREFLTTH ARDCKVVLDP VMVASSSDRL
LTREAEEALR ELASLADVIT PNLPELAVLA GVDPAENFDA AIAQAQGLAH TLGTTVIVKG
GHLTGERADN AVVTADSVHH VPVTRVETKN THGTGCSFSS ALATRLGAGF DTPAATEWAS
RWLHEAIAHA DALAVGHGRG PVDHGHVGRR MQRAADCNPE HFLLIDAGPT PPLAKPAGPH
TQALWDASAP YLTAIMELPF IRTLGDGTLD HADFMFYLEQ DAYYLTKYAR SLRALGGAWA
SDADAAIADE QEMQRTWLAD LGRETLPSPV TRAYTDFLLA STLGESAAIG QAAVLPCYWL
YYEVGARLAE RNHDAHPYRD WLATYAGDGF HEAVRGAIER CEATLAANPD ALDAAVRACA
VASRYELDFF DQADRAWVVR DA
//
