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UniProtKB/Swiss-Prot entry Q9HGY2

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

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Entry information
Entry name GPD1_ZYGRO
Primary accession number Q9HGY2
Secondary accession numbers None
Integrated into Swiss-Prot on June 1, 2001
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 40)
Name and origin of the protein
Protein name Glycerol-3-phosphate dehydrogenase [NAD+] 1
Synonyms EC 1.1.1.8
ZrGPD1
Gene name
Name: GPD1
From
Zygosaccharomyces rouxii (Candida mogii) [TaxID: 4956] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 42981;
DOI=10.1002/yea.722; PubMed=11378901 [NCBI, ExPASy, EBI, Israel, Japan]
Iwaki T., Kurono S., Yokose Y., Kubota K., Tamai Y., Watanabe Y.;
"Cloning of glycerol-3-phosphate dehydrogenase genes (ZrGPD1 and ZrGPD2) and glycerol dehydrogenase genes (ZrGCY1 and ZrGCY2) from the salt-tolerant yeast Zygosaccharomyces rouxii.";
Yeast 18:737-744(2001).
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
AB047394; BAB11957.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P90551; 1EVY. [HSSP ENTRY / PDB]
ModBase Q9HGY2.
Ontologies
GO
GO:0009331; Cellular component: glycerol-3-phosphate dehydrogenase complex (inferred from electronic annotation from InterPro).
GO:0004367; Molecular function: glycerol-3-phosphate dehydrogenase (NAD+) activity (inferred from electronic annotation from InterPro).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0005975; Biological process: carbohydrate metabolic process (inferred from electronic annotation from InterPro).
GO:0046168; Biological process: glycerol-3-phosphate catabolic process (inferred from electronic annotation from InterPro).
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.
ProtoNet Q9HGY2.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   401  401     Glycerol-3-phosphate dehydrogenase [NAD+] 1. PRO_0000138101
NP_BIND   40    45  6     NAD (By similarity). 
REGION   309   310  2     Substrate binding (By similarity). 
ACT_SITE   244   244        Proton acceptor (By similarity). 
BINDING   128   128        NAD (By similarity). 
BINDING   151   151        NAD; via amide nitrogen (By similarity). 
BINDING   151   151        Substrate (By similarity). 
BINDING   184   184        NAD; via amide nitrogen (By similarity). 
BINDING   309   309        NAD (By similarity). 
BINDING   338   338        NAD (By similarity). 
Sequence information
Length: 401 AA [This is the length of the unprocessed precursor] Molecular weight: 43791 Da [This is the MW of the unprocessed precursor] CRC64: E698797A2AA20A16 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAATDRLNQT SDILSQSMKK TDSSMSVVTA ENPYKVSVVG SGNWGTTIAK VVAENTKEKP 

        70         80         90        100        110        120 
ELFQERVDMW VFEEQIDGTP LAQIINTKHQ NVKYLPNIDL PDNLVANPDL IATTKDADVI 

       130        140        150        160        170        180 
VFNVPHQFLG RIVAQMKGQI KPTARAVSCL KGFEVGPKGV QLLSDYVTQE LGIECGALSG 

       190        200        210        220        230        240 
ANLAPEVAKE HWSETTVAYH IPDDFKGDGK DIDHRVLKQL FHRPYFHVNV IDDVAGISIA 

       250        260        270        280        290        300 
GALKNVVALG CGFVTGLGWG NNAAAAIQRV GLGEIIKFGR MFFPESKVET YYQESAGVAD 

       310        320        330        340        350        360 
LITTCSGGRN VRVATEMAKT GKSGEQVEKD ILNGQSAQGL VTCKEVHQWL ESSGNTEDFP 

       370        380        390        400 
LFEAVYQITY ENVPMKELPS MIEELDIDST SKCVLSYKMG L
Q9HGY2 in FASTA format

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