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UniProtKB/Swiss-Prot entry Q32FD7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PDXY_SHIDS
Primary accession number Q32FD7
Secondary accession numbers None
Integrated into Swiss-Prot on January 9, 2007
Sequence was last modified on January 15, 2008 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 24)
Name and origin of the protein
Protein name Pyridoxamine kinase
Synonyms PM kinase
EC 2.7.1.35
Gene name
Name: pdxY
OrderedLocusNames: SDY_1859
From
Shigella dysenteriae serotype 1 (strain Sd197) [TaxID: 300267] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Shigella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gki954; PubMed=16275786 [NCBI, ExPASy, EBI, Israel, Japan]
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.;
"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery.";
Nucleic Acids Res. 33:6445-6458(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000034; ABB61968.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_403459.1; -.
3D structure databases
SMR Q32FD7; 1-286.
ModBase Q32FD7.
Enzyme and pathway databases
BioCyc SDYS300267:SDY_1859-MON; -.
Ontologies
GO
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0004340; Molecular function: glucokinase activity (inferred from electronic annotation from HAMAP).
GO:0008478; Molecular function: pyridoxal kinase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from HAMAP).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from HAMAP).
GO:0008615; Biological process: pyridoxine biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
HAMAP MF_01639; -; 1.
PBIL [Tree]
InterPro IPR011611; Carb/pur_kinase.
IPR004625; PyrdxlP_synth_PyrdxlKinase.
Graphical view of domain structure.
Pfam PF00294; PfkB; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00687; pyridox_kin; 1.
ProtoNet Q32FD7.
Genome annotation databases
GeneID 3795770; -.
GenomeReviews CP000034_GR; SDY_1859.
KEGG sdy:SDY_1859; -.
NMPDR fig|216598.1.peg.3613; -.
Phylogenomic databases
HOGENOM Q32FD7; -.
Genome annotation databases
CMR Q32FD7; SDY_1859.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; Kinase; Metal-binding; Nucleotide-binding; Transferase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   287  287     Pyridoxamine kinase. PRO_0000269831
NP_BIND   182   183  2     ATP (By similarity). 
NP_BIND   208   223  16     ATP (By similarity). 
BINDING   10    10        Substrate (By similarity). 
BINDING   45    45        Substrate (By similarity). 
BINDING   224   224        Substrate (By similarity). 
Sequence information
Length: 287 AA [This is the length of the unprocessed precursor] Molecular weight: 31348 Da [This is the MW of the unprocessed precursor] CRC64: 4BCDDF7BADC69618 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MMKNILAIQS HVVYGHAGNS AVEFPMRRLG ANVWPLNTVQ FSNHTQYGKW TGCVMPPSHL 

        70         80         90        100        110        120 
TEIVQGIAAI DKLHTCDAVL SGYLGSAEQG EHILGIVRQV KAANPQAKYF CDPVMGHPEK 

       130        140        150        160        170        180 
GCIVAPGVAE FHVRHGLPAS DIIAPNLVEL EILCEHPVNN VEEAVLAARE LIAQGPQIVL 

       190        200        210        220        230        240 
VKHLAQAGYS RDRFEMLLVT ADEAWHISRP LVDFGMRQPV GVGDVTSGLL LVKLLQGATL 

       250        260        270        280 
QEALEHVTAA VYEIMVTTKA MQEYELQVVA AQDRIAKPEH YFSATKL 

Q32FD7 in FASTA format

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