ID K6YZA8_9ALTE Unreviewed; 277 AA.
AC K6YZA8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:GAC16545.1};
GN Name=thiD {ECO:0000313|EMBL:GAC16545.1};
GN ORFNames=GLIP_3934 {ECO:0000313|EMBL:GAC16545.1};
OS Aliiglaciecola lipolytica E3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Aliiglaciecola.
OX NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC16545.1, ECO:0000313|Proteomes:UP000006334};
RN [1] {ECO:0000313|EMBL:GAC16545.1, ECO:0000313|Proteomes:UP000006334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:GAC16545.1,
RC ECO:0000313|Proteomes:UP000006334};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC16545.1}.
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DR EMBL; BAEN01000076; GAC16545.1; -; Genomic_DNA.
DR AlphaFoldDB; K6YZA8; -.
DR STRING; 1127673.GLIP_3934; -.
DR eggNOG; COG0351; Bacteria.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000006334; 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 GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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:GAC16545.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006334};
KW Transferase {ECO:0000313|EMBL:GAC16545.1}.
FT DOMAIN 19..269
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 277 AA; 29140 MW; 4F1585A2AD87E14C CRC64;
MMPNSSYKPS IALTIAGSDS GGGAGIQADL KAFSANGVYG ASVITAVTAQ NTQSLTHVHA
IPIDVVKAQI SAVLDDLDVH AIKIGMLFSS DLIAAVSDAL KGYRGQIVLD PVMISKTGNA
LLQEEAVDAL KELLIPQADL LTPNYPEAMV LLGLSPDTDL EECKLSAFAT ELLALGSKHV
LLKGGHGTGD TCTDVLVGNN SQLPTTLSAP RISTKNTHGT GCTYSSSIAA WLAKGATVKK
AVEESHAYLH QAIHFADNLR VGRGQGPVHH FHQWWEQ
//