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Protein

Glycerol-3-phosphate dehydrogenase, mitochondrial

Gene

gut2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.

Cofactori

FADBy similarity

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi69 – 9729FADSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. glycerol-3-phosphate dehydrogenase activity Source: PomBase
  2. sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycerol-3-phosphate metabolic process Source: PomBase
  2. glycerol catabolic process Source: UniProtKB-UniPathway
  3. NADH oxidation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_353129. Fatty acid, triacylglycerol, and ketone body metabolism.
UniPathwayiUPA00618; UER00673.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate dehydrogenase, mitochondrial (EC:1.1.5.3)
Short name:
GPD-M
Short name:
GPDH-M
Gene namesi
Name:gut2
ORF Names:SPCC1223.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1223.03c.
PomBaseiSPCC1223.03c.

Subcellular locationi

  1. Mitochondrion By similarity

GO - Cellular componenti

  1. glycerol-3-phosphate dehydrogenase complex Source: PomBase
  2. mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 649Glycerol-3-phosphate dehydrogenase, mitochondrialPRO_0000010433
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

MaxQBiO14400.

Interactioni

Protein-protein interaction databases

BioGridi275787. 12 interactions.
MINTiMINT-4672763.
STRINGi4896.SPCC1223.03c-1.

Structurei

3D structure databases

ProteinModelPortaliO14400.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0578.
HOGENOMiHOG000004813.
InParanoidiO14400.
KOiK00111.
OMAiKHLTESY.
OrthoDBiEOG7NSBB6.
PhylomeDBiO14400.

Family and domain databases

InterProiIPR006076. FAD-dep_OxRdtase.
IPR000447. G3P_DH_FAD-dep.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
[Graphical view]
PRINTSiPR01001. FADG3PDH.
PROSITEiPS00977. FAD_G3PDH_1. 1 hit.
PS00978. FAD_G3PDH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O14400-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSIFKRRSV QAALAASGLV GGAVFYSDFI KRPAPSHFNP QFTPFTKSLA
60 70 80 90 100
PPPSRETLLK NVEDISKFDV LIIGGGATGT GVAVDASTRG LNVCLLEKTD
110 120 130 140 150
FASETSSKST KMAHGGVRYL EKAVFQLSKA QLDLVIEALN ERANMLRTAP
160 170 180 190 200
HLCTVLPIMI PVYKWWQVPY FFVGCKIYDW VAGSKNLRAS TIFSKETTVA
210 220 230 240 250
IAPMLDDSNL KASCVYHDGS FNDTRMNTTL AVTAIDNGAT VLNYMEVKKL
260 270 280 290 300
LKSKDNKLEG VLAIDRETGK EYQIKATSVV NATGPFSDKI LEMDADPQGE
310 320 330 340 350
PPKTAQFPRM VVPSAGVHVV LPEYYCPPNI GILDPSTSDN RVMFFLPWQG
360 370 380 390 400
KVIAGTTDKP LSSVPTNPTP SEDDIQLILK ELQKYLVFPV DREDVLSAWC
410 420 430 440 450
GIRPLVRDPS TVPPGTDPTT GETQGLVRSH FIFKSDTGLL TISGGKWTTY
460 470 480 490 500
REMAEETVNE LIKDHDFGKA LKPCQTKKLI LVGGENYYKN YSARLIHEYH
510 520 530 540 550
IPLRLAKHLS HNYGSRAPLI LELYSKTDFN KLPVTLADKE VFAPSSDASS
560 570 580 590 600
DKSVSYASFD EPFTVAELKY SIKYEYTRTP TDFLARRTRL AFLDARQALQ
610 620 630 640
AVAGVTHVMK EEFGWDDATT DKLAQEARDY IGGMGVSSDR FDVKQFEVK
Length:649
Mass (Da):71,873
Last modified:January 1, 1998 - v1
Checksum:i65702D1FDE831E6A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14993 Genomic DNA. Translation: CAA75227.1.
CU329672 Genomic DNA. Translation: CAA20872.1.
PIRiT40863.
RefSeqiNP_588348.1. NM_001023339.2.

Genome annotation databases

EnsemblFungiiSPCC1223.03c.1; SPCC1223.03c.1:pep; SPCC1223.03c.
GeneIDi2539217.
KEGGispo:SPCC1223.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14993 Genomic DNA. Translation: CAA75227.1.
CU329672 Genomic DNA. Translation: CAA20872.1.
PIRiT40863.
RefSeqiNP_588348.1. NM_001023339.2.

3D structure databases

ProteinModelPortaliO14400.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275787. 12 interactions.
MINTiMINT-4672763.
STRINGi4896.SPCC1223.03c-1.

Proteomic databases

MaxQBiO14400.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1223.03c.1; SPCC1223.03c.1:pep; SPCC1223.03c.
GeneIDi2539217.
KEGGispo:SPCC1223.03c.

Organism-specific databases

EuPathDBiFungiDB:SPCC1223.03c.
PomBaseiSPCC1223.03c.

Phylogenomic databases

eggNOGiCOG0578.
HOGENOMiHOG000004813.
InParanoidiO14400.
KOiK00111.
OMAiKHLTESY.
OrthoDBiEOG7NSBB6.
PhylomeDBiO14400.

Enzyme and pathway databases

UniPathwayiUPA00618; UER00673.
ReactomeiREACT_353129. Fatty acid, triacylglycerol, and ketone body metabolism.

Miscellaneous databases

NextBioi20800387.
PROiO14400.

Family and domain databases

InterProiIPR006076. FAD-dep_OxRdtase.
IPR000447. G3P_DH_FAD-dep.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
[Graphical view]
PRINTSiPR01001. FADG3PDH.
PROSITEiPS00977. FAD_G3PDH_1. 1 hit.
PS00978. FAD_G3PDH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Hansen K.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    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.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiGPDM_SCHPO
AccessioniPrimary (citable) accession number: O14400
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: April 29, 2015
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.