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UniProtKB/Swiss-Prot entry Q9USN5

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

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Entry information
Entry name DHE2_SCHPO
Primary accession number Q9USN5
Secondary accession numbers None
Integrated into Swiss-Prot on November 13, 2007
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 38)
Name and origin of the protein
Protein name Putative NAD-specific glutamate dehydrogenase
Synonyms NAD-GDH
EC 1.4.1.2
Gene name
ORFNames: SPCC132.04c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nbt1222; PubMed=16823372 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
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
CU329672; CAB58131.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T40931; T40931.
RefSeq NP_588149.1; -.
3D structure databases
ModBase Q9USN5.
Organism-specific databases
GeneDB_Spombe SPCC132.04c; -.
Gene expression databases
ArrayExpress Q9USN5; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004352; Molecular function: glutamate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0019551; Biological process: glutamate catabolic process to 2-oxoglutarate (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR006096; Glu/Leu/Phe/Val_DHase_C.
IPR016210; Glu_DHase_NAD-dep.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00208; ELFV_dehydrog; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000184; GDH_NAD; 1.
BLOCKS Q9USN5.
ProtoNet Q9USN5.
Genome annotation databases
GeneID 2539148; -.
KEGG spo:SPCC132.04c; -.
NMPDR fig|4896.1.peg.487; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   1106  1106     Putative NAD-specific glutamate dehydrogenase. PRO_0000310353
ACT_SITE   654    654        By similarity. 
Sequence information
Length: 1106 AA [This is the length of the unprocessed precursor] Molecular weight: 125712 Da [This is the MW of the unprocessed precursor] CRC64: 5AFFEAB84F1295CA [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MYLTKQIPHY SRIHTTQLLT VVNHRTIPFK IRGSFSNCRR YSNFATVPLL ERPFKNKSKH 

        70         80         90        100        110        120 
NTARASRPFS TQKMLLTKSH PPNMYKDSVF FGYRPIVFSG KQDQKSKVIQ CLRTERKTIP 

       130        140        150        160        170        180 
DDLVEDEVDR FYNKLGLDDY YFQMEPVSII ADHIEIIYAA KIAAHASHAK EELNIHVKNE 

       190        200        210        220        230        240 
NEDLAIYLDS SPVTQPELDQ SSAVEESIST RYLDPFKLTD PTAYRVESFT SVTNIDRTST 

       250        260        270        280        290        300 
ENSNIYTYFV TKCDFVDNPK KDASPDVPTD IASVSDKTFL EKASDNTIEM YQDVMNSVLT 

       310        320        330        340        350        360 
RFGPVVRLFD YQGRSEIRLV VGYRRGSIFQ YFPSLSKLFR YYGLHSTRTY VEQFSNGVTI 

       370        380        390        400        410        420 
ISYNFKPELF KNAAVTSINE LFSQITREAS LLYCLPSTDF QPLFVSEKLS IQEVTYAHCV 

       430        440        450        460        470        480 
RIFCEHVMNK LGPEYSSLSA ILDHSNNIHA EILETIKRRL STLAFTRTKI HDTIMQYPGL 

       490        500        510        520        530        540 
VHTLFEQFYL EHAINHNSTP HLHRAKSATS LADEASTYSI TPMSATALMD LIQKTCTNEE 

       550        560        570        580        590        600 
DVSVMEMFVK FNTHLLKTNF FQTTKVALSF RFDPSFLDST QYKDPLYAMI MSIGNEFRGF 

       610        620        630        640        650        660 
HLRFRDVARG GIRLIKSANP EAFGLNARGL FDENYNLAKT QMLKNKDIPE GGAKGVILLG 

       670        680        690        700        710        720 
KDCQDKPELA FMKYIDSIID LLIVNKSQPL VDKLGKPEIL FMGPDENTAD LVNWATIHAH 

       730        740        750        760        770        780 
RRNAPWWKSF FTGKKPTMGG IPHDKYGMTS LSVRCYVEGI YKKLNITDPS KLTKVQTGGP 

       790        800        810        820        830        840 
DGDLGSNEIK LSNEKYIAVI DGSGVLYDPA GLDRTELLRL ADERKTIDHF DAGKLSPEGY 

       850        860        870        880        890        900 
RVLVKDTNLK LPNGEIVRNG TIFRNTAHLR YKADTFVPCG GRPNAININN VEQLIDDHGR 

       910        920        930        940        950        960 
PAFKYLVEGA NLFITQDAKS VLEKAGVIVI RDASANKGGV TSSSLEVLAS LSFDDASFKE 

       970        980        990       1000       1010       1020 
NMCVHDGKVP TFYADYVNEV KRIIQRNANL EFEAIWKGHS ENKIPYTSLS NHLSTEIVKL 

      1030       1040       1050       1060       1070       1080 
DHDIYNYEKL WADVGFRNAV LRASIPKTLQ AKIGLEKMLE RIPESYLRAI FSTYLASRFV 

      1090       1100 
YQHVVSSDPF AFFDYISTEM KMLKDA
Q9USN5 in FASTA format

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