ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P34916

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name G3P1_ANAVT
Primary accession number P34916
Secondary accession number Q3MFW7
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    July 22, 2008 (Entry version 64)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase 1
Synonym EC 1.2.1.12
Gene name
Name: gap1
OrderedLocusNames: Ava_0495
From
Anabaena variabilis (strain ATCC 29413 / PCC 7937) [TaxID: 240292] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8378350 [NCBI, ExPASy, EBI, Israel, Japan]
Martin W., Brinkmann H., Savona C., Cerff R.;
"Evidence for a chimeric nature of nuclear genomes: eubacterial origin of eukaryotic glyceraldehyde-3-phosphate dehydrogenase genes.";
Proc. Natl. Acad. Sci. U.S.A. 90:8692-8696(1993).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
"Complete sequence of Anabaena variabilis ATCC 29413.";
Submitted (SEP-2005) 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
L07497; AAA21995.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000117; ABA20119.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I39602; I39602.
RefSeq YP_321014.1; -.
3D structure databases
HSSP P06977; 1DC5. [HSSP ENTRY / PDB]
ModBase P34916.
Enzyme and pathway databases
BioCyc AVAR240292:AVA_0495-MON; -.
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 P34916.
Genome annotation databases
GeneID 3682402; -.
GenomeReviews CP000117_GR; Ava_0495.
KEGG ava:Ava_0495; -.
NMPDR fig|240292.3.peg.1853; -.
Phylogenomic databases
HOGENOM P34916; -.
Genome annotation databases
CMR P34916; Ava_0495.
Other
ProtoNet P34916.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   343  342     Glyceraldehyde-3-phosphate dehydrogenase 1. PRO_0000145624
NP_BIND   13    14  2     NAD (By similarity). 
REGION   154   156  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   214   215  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   155   155        Nucleophile (By similarity). 
BINDING   35    35        NAD (By similarity). 
BINDING   79    79        NAD; via carbonyl oxygen (By similarity). 
BINDING   185   185        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   237   237        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   319   319        NAD (By similarity). 
SITE   182   182  1     Activates thiol group during catalysis (By similarity). 
CONFLICT   240   240        T -> I (in Ref. 1; AAA21995). 
Sequence information
Length: 343 AA [This is the length of the unprocessed precursor] Molecular weight: 36666 Da [This is the MW of the unprocessed precursor] CRC64: 307D0703DF8D279C [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAKLKVGING FGRIGRLVLR AGINNPNIEF VGINDLVPPD NLAYLLKYDS THGKLRSQVE 

        70         80         90        100        110        120 
AKDDGIVIDG HFIPCVSVRN PAELPWGKLG ADYVVESTGL FTDSEGASKH LQAGAKRVII 

       130        140        150        160        170        180 
SAPTKDPDRV RTLLVGVNHD LFDPSKDVIV SNASCTTNCL APIAKVINDN FGLTEGLMTT 

       190        200        210        220        230        240 
VHAMTATQPT VDGPSKKDWR GGRGAAQNII PSSTGAAKAV ALVLPELKGK LTGMAFRVPT 

       250        260        270        280        290        300 
PDVSVVDLTF KTAKATSYKE ICAAMKQASE GSLAGILGYT DEEVVSTDFQ GDTHSSIFDA 

       310        320        330        340 
GAGIELNSNF FKVVAWYDNE WGYSNRVVDL MLSMIQKEQL AAV
P34916 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!