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UniProtKB/Swiss-Prot entry P29272

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

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Entry information
Entry name G3P2_RHOSH
Primary accession number P29272
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 52)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase B
Synonyms GAPDH
EC 1.2.1.12
Gene name
Name: gapB
From
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides) [TaxID: 1063] 
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; Rhodobacteraceae; Rhodobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1939098 [NCBI, ExPASy, EBI, Israel, Japan]
Chen J.-H., Gibson J.L., McCue L.A., Tabita F.R.;
"Identification, expression, and deduced primary structure of transketolase and other enzymes encoded within the form II CO2 fixation operon of Rhodobacter sphaeroides.";
J. Biol. Chem. 266:20447-20452(1991).
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
M68914; AAA26156.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C41080; C41080.
3D structure databases
HSSP P00362; 1NQO. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase P29272.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004365; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from electronic annotation from InterPro).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000173; GlycerAld_3-P_DHase.
IPR006424; Glyceraldehyde-3-P_DHase_1.
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 TIGR01534; GAPDH-I; 1.
PROSITE PS00071; GAPDH; 1.
BLOCKS P29272.
ProtoNet P29272.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Glycolysis; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   333  333     Glyceraldehyde-3-phosphate dehydrogenase B. PRO_0000145675
NP_BIND   12    13  2     NAD (By similarity). 
REGION   150   152  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   209   210  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   151   151        Nucleophile (By similarity). 
BINDING   36    36        NAD (By similarity). 
BINDING   80    80        NAD; via carbonyl oxygen (By similarity). 
BINDING   181   181        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   196   196        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   232   232        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   314   314        NAD (By similarity). 
SITE   178   178  1     Activates thiol group during catalysis (By similarity). 
Sequence information
Length: 333 AA [This is the length of the unprocessed precursor] Molecular weight: 35679 Da [This is the MW of the unprocessed precursor] CRC64: B072F443A20C3AFD [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTIRVAINGF GRIGRNVLRA IVESGRTDIE VVAINDLGQV ETNAHLLRFD SVHGRFPAKV 

        70         80         90        100        110        120 
TSGDDWIDVG RGPIKVTAIR NPAELPWAGV DMAMECTGIF TTKEKAAAHL QNGAKRVLVS 

       130        140        150        160        170        180 
APCDGADRTI VYGVNHATLT ADDLVVSNAS CTTNCLSPVA KVLHDAIGIA KGFMTTIHSY 

       190        200        210        220        230        240 
TGDQPTLDTM HKDLYRARAA ALSMIPTSTG AAKAVGLVLP ELKGRLDGVS IRVPTPNVSV 

       250        260        270        280        290        300 
VDLVFEAARD TTVEEVNAAI EAAACGPLKG VLGFTTEPNV SSDFNHDPHS SVFHMDQTKV 

       310        320        330 
MEGRMVRILS WYDNEWGFSN RMADTAVAMG RLL
P29272 in FASTA format

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