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 Q6FN96


[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 GPD1_CANGA
Primary accession number Q6FN96
Secondary accession numbers None
Integrated into Swiss-Prot on January 10, 2006
Sequence was last modified on July 19, 2004 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 31)
Name and origin of the protein
Protein name Glycerol-3-phosphate dehydrogenase [NAD+] 1
Synonym EC 1.1.1.8
Gene name
Name: GPD1
OrderedLocusNames: CAGL0K01683g
From
Candida glabrata (Yeast) (Torulopsis glabrata) [TaxID: 5478] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; Candida.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
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
CR380957; CAG61259.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_448298.1; -.
3D structure databases
ModBase Q6FN96.
Ontologies
GO
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013328; DHase_multihelical.
IPR016040; NAD(P)-bd.
IPR017751; NAD-dep_Gly3P_DH_euk.
IPR006168; NAD-dep_Gly3P_DHase.
IPR011128; NAD-dep_Gly3P_DHase_N.
IPR006109; NAD_Gly3P_DHase_C.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.
PANTHER PTHR11728; NAD_Gly3P_DH; 1.
Pfam PF07479; NAD_Gly3P_dh_C; 1.
PF01210; NAD_Gly3P_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000114; Glycerol-3-P_dh; 1.
PRINTS PR00077; GPDHDRGNASE.
ProDom PD001278; NAD_Gly3P_C; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00957; NAD_G3PDH; 1.
BLOCKS Q6FN96.
ProtoNet Q6FN96.
Genome annotation databases
GeneID 2890024; -.
KEGG cgr:CAGL0K01683g; -.
Phylogenomic databases
HOGENOM Q6FN96; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   400  400     Glycerol-3-phosphate dehydrogenase [NAD+] 1. PRO_0000138086
NP_BIND   50    55  6     NAD (By similarity). 
REGION   319   320  2     Substrate binding (By similarity). 
ACT_SITE   254   254        Proton acceptor (By similarity). 
BINDING   138   138        NAD (By similarity). 
BINDING   161   161        NAD; via amide nitrogen (By similarity). 
BINDING   161   161        Substrate (By similarity). 
BINDING   194   194        NAD; via amide nitrogen (By similarity). 
BINDING   319   319        NAD (By similarity). 
BINDING   348   348        NAD (By similarity). 
Sequence information
Length: 400 AA [This is the length of the unprocessed precursor] Molecular weight: 43988 Da [This is the MW of the unprocessed precursor] CRC64: DE850B128571D8E5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSNSAAGRLN QTSHILNESI KNDDISLRRS QPSTTSLQAL EHPFKVTVIG SGNWGTTIAK 

        70         80         90        100        110        120 
VVAENTALNP HLFVSRVDMW VFEEKIDGKN LTEIINEQHE NVKYLPDIKL PENLVANPNL 

       130        140        150        160        170        180 
IDSVKGADIL IFNIPHQFLP RIVSNLKNHV GPHVRAISCL KGFEVGKKGV QLLSSYVTDE 

       190        200        210        220        230        240 
LGIQCGALSG ANLAPEVAKE HWSETTVAYH IPKDFRGEGK DVDHKLLKAL FHRPYFHVNV 

       250        260        270        280        290        300 
IEDVAGISIA GALKNVVALG CGFVEGLGWG NNAAAAIQRV GLGEIIKFGQ MFFPESRVQT 

       310        320        330        340        350        360 
YYQESAGVAD LITTCSGGRN VRVAKHMAKT GKSALDAEKE LLNGQSAQGI ITCKEVHEWL 

       370        380        390        400 
ETCEMTHEFP LFEAVYQIVY NNVPMKNLPD MIEELECIAD 

Q6FN96 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!