ID L8LSG4_9CHRO Unreviewed; 268 AA.
AC L8LSG4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ELR98956.1};
GN ORFNames=GLO73106DRAFT_00027990 {ECO:0000313|EMBL:ELR98956.1};
OS Gloeocapsa sp. PCC 73106.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Chroococcaceae; Gloeocapsa.
OX NCBI_TaxID=102232 {ECO:0000313|EMBL:ELR98956.1, ECO:0000313|Proteomes:UP000011180};
RN [1] {ECO:0000313|EMBL:ELR98956.1, ECO:0000313|Proteomes:UP000011180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 73106 {ECO:0000313|EMBL:ELR98956.1,
RC ECO:0000313|Proteomes:UP000011180};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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}.
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:ELR98956.1}.
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DR EMBL; ALVY01000162; ELR98956.1; -; Genomic_DNA.
DR RefSeq; WP_006528234.1; NZ_ALVY01000162.1.
DR AlphaFoldDB; L8LSG4; -.
DR STRING; 102232.GLO73106DRAFT_00027990; -.
DR PATRIC; fig|102232.3.peg.1260; -.
DR eggNOG; COG0351; Bacteria.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000011180; Unassembled WGS sequence.
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:ELR98956.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011180};
KW Transferase {ECO:0000313|EMBL:ELR98956.1}.
FT DOMAIN 14..258
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 268 AA; 28584 MW; EFCD038DFB48147E CRC64;
MNDYPVALTI AGSDSGGGAG IQADLRTFAF HRVHGASAIT CITAQNTLGV TAVEGVRPSL
VGLQITSVAR DLKPKAVKLG MLYNQEIMQT VISQVREWNF SALVVDPVMV SRTGAKLIDE
AAITTLAREI IPLALIVTPN RYEAQILSGL EIQTWADMEK AAEKIYNLGA KAVLVKGGAM
AGELQGVDLW FDGQTFYTLK TTRVLTKHNH GTGCTLSAAI AANLALGKTI FQSVVQAKEY
LTEALKHSLK VGQGHGPVGH FFPLDVVT
//