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UniProtKB/Swiss-Prot entry P58839

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

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Entry information
Entry name G3P_METKA
Primary accession number P58839
Secondary accession numbers None
Integrated into Swiss-Prot on May 27, 2002
Sequence was last modified on May 27, 2002 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 47)
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
Synonyms: gapA
OrderedLocusNames: MK0618
From
Methanopyrus kandleri [TaxID: 2320] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae; Methanopyrus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
DOI=10.1073/pnas.032671499; PubMed=11930014 [NCBI, ExPASy, EBI, Israel, Japan]
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.;
"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.";
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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
AE010355; AAM01833.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_613903.1; -.
3D structure databases
HSSP P10618; 1CF2. [HSSP ENTRY / PDB]
ModBase P58839.
Enzyme and pathway databases
BioCyc MKAN190192:MK0618-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0043891; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity (inferred from electronic annotation from EC).
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.
Pfam PF02800; Gp_dh_C; 1.
PF00044; Gp_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000149; GAP_DH; 1.
ProDom 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 P58839.
Genome annotation databases
GeneID 1476719; -.
GenomeReviews AE009439_GR; MK0618.
KEGG mka:MK0618; -.
NMPDR fig|190192.1.peg.616; -.
Phylogenomic databases
HOGENOM P58839; -.
Genome annotation databases
CMR P58839; MK0618.
Other
ProtoNet P58839.
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   350  350     Glyceraldehyde-3-phosphate dehydrogenase. PRO_0000145724
NP_BIND   13    14  2     NAD (By similarity). 
REGION   147   149  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   202   203  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   148   148        Nucleophile (By similarity). 
BINDING   118   118        NAD; via amide nitrogen (By similarity). 
BINDING   176   176        NAD (By similarity). 
BINDING   309   309        NAD; via carbonyl oxygen (By similarity). 
Sequence information
Length: 350 AA [This is the length of the unprocessed precursor] Molecular weight: 38367 Da [This is the MW of the unprocessed precursor] CRC64: F9BCB72702E22E02 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MADVSVLING YGTIGKRVAD AVDAQRDMEV LGVVKTSPDY LARLAVEEYG YPLFVPEDRV 

        70         80         90        100        110        120 
ERFEDAGIET EGTVEDVVLN AEDYGLDVVV DCTPEGIGAR NKETLYEKAG VKAIFQGGEE 

       130        140        150        160        170        180 
AEVAEVSFVA QCNYEEALGA DYVRCVSCNT TALCRTLGTL KEEFELGRVY VTIVRRAADP 

       190        200        210        220        230        240 
HQVKKGPINA IAPNPVTVPS HHGPDVKTVM PDIDITTAAV KVPTTLMHMH VVRVELKEEV 

       250        260        270        280        290        300 
TSDDVIDAFE EARRIWVVPH GEGLGSTAEL IELGRDLGRK RYDLYEILVW EESINVEDGV 

       310        320        330        340        350 
LYYMQAVHQE ADVVPENVDA IRAMTELEED PEASMDATDS ALGVLNSPPL
P58839 in FASTA format

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