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Database: UniProt
Entry: A0A066WSM6_9FLAO
LinkDB: A0A066WSM6_9FLAO
Original site: A0A066WSM6_9FLAO 
ID   A0A066WSM6_9FLAO        Unreviewed;       251 AA.
AC   A0A066WSM6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Pyridoxamine kinase/Phosphomethylpyrimidine kinase domain-containing protein {ECO:0000259|Pfam:PF08543};
GN   ORFNames=FEM21_02940 {ECO:0000313|EMBL:KDN56791.1};
OS   Flavobacterium seoulense.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1492738 {ECO:0000313|EMBL:KDN56791.1, ECO:0000313|Proteomes:UP000027064};
RN   [1] {ECO:0000313|EMBL:KDN56791.1, ECO:0000313|Proteomes:UP000027064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EM1321 {ECO:0000313|EMBL:KDN56791.1,
RC   ECO:0000313|Proteomes:UP000027064};
RA   Shin S.-K., Yi H.;
RT   "Genome Sequence of Flavobacterium sp. EM1321.";
RL   Submitted (MAY-2014) 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}.
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:KDN56791.1}.
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DR   EMBL; JNCA01000001; KDN56791.1; -; Genomic_DNA.
DR   RefSeq; WP_035656918.1; NZ_JNCA01000001.1.
DR   AlphaFoldDB; A0A066WSM6; -.
DR   STRING; 1492738.FEM21_02940; -.
DR   PATRIC; fig|1492738.3.peg.288; -.
DR   eggNOG; COG0351; Bacteria.
DR   OrthoDB; 9810880at2; -.
DR   Proteomes; UP000027064; Unassembled WGS sequence.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
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   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;
FT   DOMAIN          15..248
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   251 AA;  28093 MW;  2BF594F4661061DA CRC64;
     MSTNRPFVLS IAGFDPSAGA GVLADIKTFE QHQVYGFAIN TANTIQTEDE FIAIQWTALD
     FVLQSVETLF DSYEIKAVKI GIVPSLDYLK EIVFLIKKLS PTIKIVWDTV LKSTTEFDFL
     TIENQNNLIT ILQKTELITP NYTEISKLIP AQKKTEISLE ILSKYCAVLL KGGHHPTEIG
     TDYLHTQNQF FRLLPKNTDI YQKHGSGCVL SAAITSNLAL DQDLLNACKN AKNYTETFLL
     SNPTQLGNHY V
//
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