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UniProtKB/Swiss-Prot entry A7MTQ2

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

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Entry information
Entry name E4PD_VIBHB
Primary accession number A7MTQ2
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on October 2, 2007 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 12)
Name and origin of the protein
Protein name D-erythrose-4-phosphate dehydrogenase
Synonyms E4PDH
EC 1.2.1.72
Gene name
Name: epd
OrderedLocusNames: VIBHAR_03566
From
Vibrio harveyi (strain ATCC BAA-1116 / BB120) [TaxID: 338187] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; Vibrio.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C., Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K., Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J., Wilson R.K.;
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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
CP000789; ABU72501.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001446728.1; -.
3D structure databases
ModBase A7MTQ2.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0048001; Molecular function: erythrose-4-phosphate dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0042823; Biological process: pyridoxal phosphate biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0008615; Biological process: pyridoxine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01640; -; 1.
PBIL [Tree]
InterPro IPR006422; E4P_DHase_bac.
IPR000173; GlycerAld_3-P_DHase.
Graphical view of domain structure.
PANTHER PTHR10836; GAP_DH; 1.
Pfam PF02800; Gp_dh_C; 1.
PF00044; Gp_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000149; GAP_DH; 1.
PRINTS PR00078; G3PDHDRGNASE.
TIGRFAMs TIGR01532; E4PD_g-proteo; 1.
PROSITE PS00071; GAPDH; FALSE_NEG.
BLOCKS A7MTQ2.
Genome annotation databases
GeneID 5554116; -.
GenomeReviews CP000789_GR; VIBHAR_03566.
KEGG vha:VIBHAR_03566; -.
NMPDR fig|338187.4.peg.2622; -.
CMR A7MTQ2; VIBHAR_03566.
Other
ProtoNet A7MTQ2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   345  345     D-erythrose-4-phosphate dehydrogenase. PRO_1000069898
NP_BIND   11    12  2     NAD (By similarity). 
REGION   158   160  3     Substrate binding (Potential). 
REGION   217   218  2     Substrate binding (Potential). 
ACT_SITE   159   159        Nucleophile (By similarity). 
BINDING   204   204        Substrate (Potential). 
BINDING   240   240        Substrate (Potential). 
BINDING   322   322        NAD (By similarity). 
SITE   186   186  1     Activates thiol group during catalysis (By similarity). 
Sequence information
Length: 345 AA [This is the length of the unprocessed precursor] Molecular weight: 38285 Da [This is the MW of the unprocessed precursor] CRC64: ADBD0B2DE56070B0 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLKVAINGFG RIGRNVLRAV YESGKHQQIK VVAVNELAQP EAMAHLLQYD TSHGRFGKKI 

        70         80         90        100        110        120 
SHDQEHLYVH HDSSEYDPIR ILHLAEIELL PWRDLEVDIV LDCTGVFGSQ ADGQAHIEAG 

       130        140        150        160        170        180 
AQKVLFSHPG ASDLDNTIIY GVNHETLKDE HRVVSNGSCT TNCIVPIIKV LDEAFGIESG 

       190        200        210        220        230        240 
TITTIHSSMN DQQVIDAYHN DLRRTRAASQ SIIPVDTKLH KGIERIFPKF SNKFEAISVR 

       250        260        270        280        290        300 
VPTVNVTAMD LSVTISTNVK VNDVNQTIVN ASQCTLRDIV DYTESPLVSI DFNHDPHSAI 

       310        320        330        340 
VDGTQTRVSN GQLVKMLVWC DNEWGFANRM LDTALAMQAS SQVEQ
A7MTQ2 in FASTA format

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