ID D7DZI5_NOSA0 Unreviewed; 274 AA.
AC D7DZI5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ADI62937.1};
GN OrderedLocusNames=Aazo_0366 {ECO:0000313|EMBL:ADI62937.1};
OS Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC Trichormus.
OX NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI62937.1, ECO:0000313|Proteomes:UP000001511};
RN [1] {ECO:0000313|EMBL:ADI62937.1, ECO:0000313|Proteomes:UP000001511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0708 {ECO:0000313|EMBL:ADI62937.1,
RC ECO:0000313|Proteomes:UP000001511};
RX PubMed=20628610; DOI=10.1371/journal.pone.0011486;
RA Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K.,
RA Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.;
RT "Genome erosion in a nitrogen-fixing vertically transmitted endosymbiotic
RT multicellular cyanobacterium.";
RL PLoS ONE 5:E11486-E11486(2010).
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; CP002059; ADI62937.1; -; Genomic_DNA.
DR RefSeq; WP_013189957.1; NC_014248.1.
DR AlphaFoldDB; D7DZI5; -.
DR STRING; 551115.Aazo_0366; -.
DR KEGG; naz:Aazo_0366; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_0_3; -.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000001511; Chromosome.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
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:ADI62937.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001511};
KW Transferase {ECO:0000313|EMBL:ADI62937.1}.
FT DOMAIN 19..264
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 274 AA; 28925 MW; 9CB8C1BA1609BA77 CRC64;
MIKTNAKLIP VALTIAGSDS GGGAGIQTDL RTFAFHCVHG TSAITCVTAQ NTVGVVRVDA
MSKEAVIAQI RAVVEDIGVQ AAKTGMLLNE EIITAVAREV TALEIDHLVV DPVMVSRTGA
QLIDDDAVQT LCDELIPQAA IITPNRYEAQ ILSGLEIVSL EDMQTAAEII FKKLGIKAVL
VKGGVMSGSL RGVDVWFDGQ RLETLTTQQI ETKNTHGTGC TLSAAITANL ALGKDLWTAV
QQAKDYVTTA LTYSLEIGKG QGPVGHFFPL LVKG
//
