ID K9UYH2_9CYAN Unreviewed; 274 AA.
AC K9UYH2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:AFZ00626.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:AFZ00626.1};
GN ORFNames=Cal6303_1583 {ECO:0000313|EMBL:AFZ00626.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ00626.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFZ00626.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ00626.1,
RC ECO:0000313|Proteomes:UP000010477};
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003610; AFZ00626.1; -; Genomic_DNA.
DR RefSeq; WP_015197274.1; NC_019751.1.
DR AlphaFoldDB; K9UYH2; -.
DR STRING; 1170562.Cal6303_1583; -.
DR KEGG; calt:Cal6303_1583; -.
DR PATRIC; fig|1170562.3.peg.1720; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_0_3; -.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000010477; Chromosome.
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:AFZ00626.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010477};
KW Transferase {ECO:0000313|EMBL:AFZ00626.1}.
FT DOMAIN 19..264
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 274 AA; 29205 MW; B6CDD3E8BDF63C94 CRC64;
MKTDSASQVP VAMTIAGSDS GGGAGIQADL RTFAFHCVHG TSAVTCITAQ NTLGVRRVDA
MSPEAVTAQI EAVVEDIGVD AAKTGMLLNR EIILCVAEQV QKLQIRNLVV DPVMVSRTGA
QLIDDAAIQT LREVLIPLAV LVTPNRYEAQ ILSGLEINSL DEMKLSAEMI QQKLSAKTVL
VKGGGMSGEL RGVDVWFDGE RLEVLTTKQI ETKNTHGTGC TLSAAIASNL ARHENLLTSV
KNAKEYLTYA LTYGLDIGKG QGPVGHFYPL QKLS
//
