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UniProtKB/Swiss-Prot entry P32191


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

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Entry information
Entry name GPDM_YEAST
Primary accession number P32191
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on February 1, 1995 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 77)
Name and origin of the protein
Protein name Glycerol-3-phosphate dehydrogenase, mitochondrial [Precursor]
Synonyms GPDH-M
GPD-M
EC 1.1.99.5
Gene name
Name: GUT2
OrderedLocusNames: YIL155C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=S288c / GRF88;
PubMed=8256521 [NCBI, ExPASy, EBI, Israel, Japan]
Roennow B., Kielland-Brandt M.C.;
"GUT2, a gene for mitochondrial glycerol 3-phosphate dehydrogenase of Saccharomyces cerevisiae.";
Yeast 9:1121-1130(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169870 [NCBI, ExPASy, EBI, Israel, Japan]
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
Nature 387:84-87(1997).
[3]
SUBCELLULAR LOCATION.
DOI=10.1021/bi010277r; PubMed=11502169 [NCBI, ExPASy, EBI, Israel, Japan]
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.;
"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex.";
Biochemistry 40:9758-9769(2001).
[4]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
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
Z38059; CAA86123.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X71660; CAA50652.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S38190; S48379.
RefSeq NP_012111.1; -.
3D structure databases
ModBase P32191.
Organism-specific databases
CYGD YIL155c; -.
SGD S000001417; GUT2.
Yeast-GFP YIL155C.
Gene expression databases
ArrayExpress P32191; -.
GermOnline YIL155C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0009331; Cellular component: glycerol-3-phosphate dehydrogenase complex (inferred from electronic annotation from InterPro).
GO:0031307; Cellular component: integral to mitochondrial outer membrane (inferred from direct assay from SGD).
GO:0005743; Cellular component: mitochondrial inner membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004368; Molecular function: glycerol-3-phosphate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0005975; Biological process: carbohydrate metabolic process (inferred from mutant phenotype from SGD).
GO:0006072; Biological process: glycerol-3-phosphate metabolic process (inferred from electronic annotation from InterPro).
GO:0006116; Biological process: NADH oxidation (inferred from direct assay from SGD).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0001302; Biological process: replicative cell aging (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000447; FAD-dep_Gly3P_DHase.
IPR006076; FAD-dep_OxRdtase.
Graphical view of domain structure.
Pfam PF01266; DAO; 1.
Pfam graphical view of domain structure.
PRINTS PR01001; FADG3PDH.
PROSITE PS00977; FAD_G3PDH_1; 1.
PS00978; FAD_G3PDH_2; 1.
BLOCKS P32191.
ProtoNet P32191.
Proteomic databases
PeptideAtlas P32191; -.
Genome annotation databases
Ensembl YIL155C; Saccharomyces cerevisiae. [Contig view]
GeneID 854651; -.
GenomeReviews Z47047_GR; YIL155C.
KEGG sce:YIL155C; -.
NMPDR fig|4932.3.peg.1633; -.
Phylogenomic databases
HOGENOM P32191; -.
Other
LinkHub P32191; -.
NextBio 977202; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion (Potential). 
CHAIN   ?   649        Glycerol-3-phosphate dehydrogenase, mitochondrial. PRO_0000010434
NP_BIND   69    97  29     FAD (Potential). 
CONFLICT   1    51        MFSVTRRRAAGAAAAMATATGTLYWMTSQGDRPLVHNDPS YMVQFPTAAPP -> MTRATWCNSPPPLHR (in Ref. 1). 
CONFLICT   63    63        A -> D (in Ref. 1; CAA50652). 
CONFLICT   182   182        A -> G (in Ref. 1; CAA50652). 
CONFLICT   234   234        A -> G (in Ref. 1; CAA50652). 
CONFLICT   243   243        N -> I (in Ref. 1; CAA50652). 
CONFLICT   320   320        A -> S (in Ref. 1; CAA50652). 
CONFLICT   342   342        C -> S (in Ref. 1; CAA50652). 
CONFLICT   645   646        KT -> QGR (in Ref. 1; CAA50652). 
Sequence information
Length: 649 AA [This is the length of the unprocessed precursor] Molecular weight: 72389 Da [This is the MW of the unprocessed precursor] CRC64: FE6B25F5B21EF8DA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFSVTRRRAA GAAAAMATAT GTLYWMTSQG DRPLVHNDPS YMVQFPTAAP PQVSRRDLLD 

        70         80         90        100        110        120 
RLAKTHQFDV LIIGGGATGT GCALDAATRG LNVALVEKGD FASGTSSKST KMIHGGVRYL 

       130        140        150        160        170        180 
EKAFWEFSKA QLDLVIEALN ERKHLINTAP HLCTVLPILI PIYSTWQVPY IYMGCKFYDF 

       190        200        210        220        230        240 
FAGSQNLKKS YLLSKSATVE KAPMLTTDNL KASLVYHDGS FNDSRLNATL AITAVENGAT 

       250        260        270        280        290        300 
VLNYVEVQKL IKDPTSGKVI GAEARDVETN ELVRINAKCV VNATGPYSDA ILQMDRNPSG 

       310        320        330        340        350        360 
LPDSPLNDNS KIKSTFNQIA VMDPKMVIPS IGVHIVLPSF YCPKDMGLLD VRTSDGRVMF 

       370        380        390        400        410        420 
FLPWQGKVLA GTTDIPLKQV PENPMPTEAD IQDILKELQH YIEFPVKRED VLSAWAGVRP 

       430        440        450        460        470        480 
LVRDPRTIPA DGKKGSATQG VVRSHFLFTS DNGLITIAGG KWTTYRQMAE ETVDKVVEVG 

       490        500        510        520        530        540 
GFHNLKPCHT RDIKLAGAEE WTQNYVALLA QNYHLSSKMS NYLVQNYGTR SSIICEFFKE 

       550        560        570        580        590        600 
SMENKLPLSL ADKENNVIYS SEENNLVNFD TFRYPFTIGE LKYSMQYEYC RTPLDFLLRR 

       610        620        630        640 
TRFAFLDAKE ALNAVHATVK VMGDEFNWSE KKRQWELEKT VNFIKTFGV 

P32191 in FASTA format

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View entry in raw text format (no links)
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