ID K7WNE4_9NOST Unreviewed; 273 AA.
AC K7WNE4;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:AFW97063.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:AFW97063.1};
GN ORFNames=ANA_C20639 {ECO:0000313|EMBL:AFW97063.1};
OS Anabaena sp. 90.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=46234 {ECO:0000313|EMBL:AFW97063.1, ECO:0000313|Proteomes:UP000010101};
RN [1] {ECO:0000313|EMBL:AFW97063.1, ECO:0000313|Proteomes:UP000010101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90 {ECO:0000313|EMBL:AFW97063.1};
RX PubMed=23148582; DOI=10.1186/1471-2164-13-613;
RA Wang H., Sivonen K., Rouhiainen L., Fewer D.P., Lyra C., Rantala-Ylinen A.,
RA Vestola J., Jokela J., Rantasarkka K., Li Z., Liu B.;
RT "Genome-derived insights into the biology of the hepatotoxic bloom-forming
RT cyanobacterium Anabaena sp. strain 90.";
RL BMC Genomics 13:613-613(2012).
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.
CC {ECO:0000256|ARBA:ARBA00004948}.
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DR EMBL; CP003285; AFW97063.1; -; Genomic_DNA.
DR AlphaFoldDB; K7WNE4; -.
DR STRING; 46234.ANA_C20639; -.
DR KEGG; anb:ANA_C20639; -.
DR PATRIC; fig|46234.3.peg.5069; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_0_3; -.
DR Proteomes; UP000010101; Chromosome chANA02.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:RHEA.
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:InterPro.
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:AFW97063.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010101};
KW Transferase {ECO:0000313|EMBL:AFW97063.1}.
FT DOMAIN 19..264
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 273 AA; 28640 MW; E9063F897F196542 CRC64;
MMTTNKTFVP VALTIAGSDS GGGAGIQTDL RTFAFHCVHG TSAITCITAQ NTVGVSRVDA
IASDAVVAQI QAVVEDIGVQ SAKTGMLLNQ EIILAVAQQI AAYKINNLVV DPVMVSRTGA
QLIDDDAVQT LRNTLIPLAS IITPNRYEAQ ILSGLEITSL ADMQAAAAIM HRELGVKAVL
VKGGGMSGNL RGVDVWFNGE KLQILRTKQV ETKNTHGTGC TLSAAIAANL ALGKDLWTAV
QAAKEYVTNA LTYSLDIGKG QGPVGHFFPL LIK
//
