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 Q2FNA2

[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 G3P_METHJ
Primary accession number Q2FNA2
Secondary accession numbers None
Integrated into Swiss-Prot on September 11, 2007
Sequence was last modified on March 21, 2006 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 22)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase
Synonyms GAPDH
EC 1.2.1.59
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
Gene name
Name: gap
OrderedLocusNames: Mhun_2462
From
Methanospirillum hungatei (strain JF-1 / DSM 864) [TaxID: 323259] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales; Methanospirillaceae; Methanospirillum.
Protein existence 3: Inferred from homology;
References
[1]
 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., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D., Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J., Stams A.J.M., Boone D.R., Richardson P.;
"Complete sequence of Methanospirillum hungatei JF-1.";
Submitted (JAN-2006) 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
CP000254; ABD42162.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_503881.1; -.
3D structure databases
ModBase Q2FNA2.
Enzyme and pathway databases
BioCyc MHUN323259:MHUN_2462-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004365; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from electronic annotation from HAMAP).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00559; -; 1.
PBIL [Tree]
InterPro IPR000173; GlycerAld_3-P_DHase.
IPR006436; Glyceraldehyde-3-P_DHase_2_arc.
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.
ProDom PD004105; DapB; 1.
PD007761; GAPDH_like; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01546; GAPDH-II_archae; 1.
PROSITE PS00071; GAPDH; 1.
BLOCKS Q2FNA2.
Genome annotation databases
GeneID 3923967; -.
GenomeReviews CP000254_GR; Mhun_2462.
KEGG mhu:Mhun_2462; -.
NMPDR fig|323259.5.peg.2588; -.
Phylogenomic databases
HOGENOM Q2FNA2; -.
Genome annotation databases
CMR Q2FNA2; Mhun_2462.
Other
ProtoNet Q2FNA2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   339  339     Glyceraldehyde-3-phosphate dehydrogenase. PRO_0000300974
NP_BIND   11    12  2     NAD (By similarity). 
REGION   139   141  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   194   195  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   140   140        Nucleophile (By similarity). 
BINDING   110   110        NAD; via amide nitrogen (By similarity). 
BINDING   168   168        NAD (By similarity). 
BINDING   301   301        NAD; via carbonyl oxygen (By similarity). 
Sequence information
Length: 339 AA [This is the length of the unprocessed precursor] Molecular weight: 36818 Da [This is the MW of the unprocessed precursor] CRC64: 3C149595098A350B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIKVAINGYG TIGKRVADAV SAQKDMEIIG VSKTKPSAEA LIAVQRGYPI YIADMSKKDA 

        70         80         90        100        110        120 
FAKAGIPVAG SVEDMLKKAD IVVDGTPGGV GESNKALYEK AGVKAIWQGG EDHEVAGFSF 

       130        140        150        160        170        180 
NAHANYKDAI GRQFVRVVSC NTTGLCRVIK AVDDAFGVVK VRAVMVRRGA DPHVVKKGPI 

       190        200        210        220        230        240 
DAVVLDPPTI PSHHGPDVNT VLPHIDIVTM AMIVPTTQMH MHAITIELKK EVSRDDVLAV 

       250        260        270        280        290        300 
MRSHNRIGLV QPKTAIKSTA ELKEYVMDMG RPRSDLWENG IFEASVNMVG KELFFFQAIH 

       310        320        330 
QEADVVIENV DAIRAMMGEV RDPETSIRMT NEAMQFTAL
Q2FNA2 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!