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Database: UniProt/TrEMBL
Entry: G0AMK4_BORBD
LinkDB: G0AMK4_BORBD
Original site: G0AMK4_BORBD 
ID   G0AMK4_BORBD            Unreviewed;       264 AA.
AC   G0AMK4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   01-OCT-2014, entry version 17.
DE   SubName: Full=Phosphomethylpyrimidine kinase family protein {ECO:0000313|EMBL:AEL18930.1};
GN   OrderedLocusNames=BbiDN127_0782 {ECO:0000313|EMBL:AEL18930.1};
OS   Borrelia bissettii (strain DN127).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=521010 {ECO:0000313|EMBL:AEL18930.1, ECO:0000313|Proteomes:UP000001634};
RN   [1] {ECO:0000313|Proteomes:UP000001634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DN127 {ECO:0000313|Proteomes:UP000001634};
RA   Mongodin E.F., Casjens S.R., Fraser-Liggett C.M., Qiu W.-G.,
RA   Dunn J.J., Luft B.J., Schutzer S.E.;
RT   "Complete genome sequence of Borrelia bissettii strain DN127.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DN127;
RA   Mongodin E.F., Casjens S.R., Fraser-Liggett C.M., Qiu W.-G.,
RA   Dunn J.J., Luft B.J., Schutzer S.E.;
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + pyridoxal = ADP + pyridoxal 5'-
CC       phosphate. {ECO:0000256|SAAS:SAAS00088584}.
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DR   EMBL; CP002746; AEL18930.1; -; Genomic_DNA.
DR   RefSeq; WP_014023975.1; NC_015921.1.
DR   RefSeq; YP_004777995.1; NC_015921.1.
DR   EnsemblBacteria; AEL18930; AEL18930; BbiDN127_0782.
DR   GeneID; 11039836; -.
DR   KEGG; bbs:BbiDN127_0782; -.
DR   KO; K00868; -.
DR   BioCyc; BBIS521010:GKCM-779-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008478; F:pyridoxal kinase activity; IEA:InterPro.
DR   GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR004625; PyrdxlP_synth_PyrdxlKinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   PANTHER; PTHR10534; PTHR10534; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|SAAS:SAAS00088594};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001634};
KW   Kinase {ECO:0000256|SAAS:SAAS00088614, ECO:0000313|EMBL:AEL18930.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00088617};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00088603};
KW   Transferase {ECO:0000256|SAAS:SAAS00088629}.
SQ   SEQUENCE   264 AA;  30169 MW;  6724505BAF450C2B CRC64;
     MKRILAMHDI SSMGRTSLTI CIPIISSFNM QVCPFVTAVL SASTAYKKFE IVDLTDHLEK
     FINIWKEQKE HFDILYTGFL GSEKQQLTIE KIIKLIKFEK IVIDPVFADD GIIYPTFDNK
     IISGFRKIIK YANIITPNIT ELEMLSKSPQ LKNKDDIIKA ILNLDTKGIV VVTSVKKGDL
     LGNICYNPKN KEYSEFFLEK LEQNFSGTGD LFTSLLIGYL EKFEIEKALE KTTKAIHLII
     KDSIKENALK KEGVQIEKFL KNTF
//
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