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Protein

Glycerol dehydrogenase 1

Gene

gld1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Glycerol dehydrogenase involved in the assimilation of glycerol.1 Publication

Catalytic activityi

Glycerol + NAD+ = glycerone + NADH.1 Publication

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Pathwayi: glycerol fermentation

This protein is involved in step 1 of the subpathway that synthesizes glycerone phosphate from glycerol (oxidative route).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glycerol dehydrogenase 1 (gld1)
  2. Dihydroxyacetone kinase 1 (dak1), Dihydroxyacetone kinase 2 (dak2)
This subpathway is part of the pathway glycerol fermentation, which is itself part of Polyol metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycerone phosphate from glycerol (oxidative route), the pathway glycerol fermentation and in Polyol metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991NADBy similarity
Binding sitei182 – 1821SubstrateBy similarity
Binding sitei186 – 1861NADBy similarity
Binding sitei188 – 1881NAD; via carbonyl oxygenBy similarity
Binding sitei192 – 1921NADBy similarity
Metal bindingi232 – 2321Zinc; catalytic1 Publication
Binding sitei232 – 2321SubstrateBy similarity
Metal bindingi315 – 3151Zinc; catalytic1 Publication
Binding sitei315 – 3151Substrate1 Publication
Metal bindingi333 – 3331Zinc; catalytic1 Publication
Binding sitei333 – 3331Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi155 – 1595NADBy similarity
Nucleotide bindingi177 – 1804NADBy similarity

GO - Molecular functioni

  • glycerol dehydrogenase [NAD+] activity Source: PomBase
  • zinc ion binding Source: PomBase

GO - Biological processi

  • aerobic glycerol catabolic process Source: PomBase
  • glycerol metabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycerol metabolism

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BRENDAi1.1.1.6. 5613.
UniPathwayiUPA00617; UER00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol dehydrogenase 1 (EC:1.1.1.6)
Short name:
GDH
Short name:
GLDH
Gene namesi
Name:gld1
ORF Names:SPAC13F5.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC13F5.03c.
PomBaseiSPAC13F5.03c. gld1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Glycerol dehydrogenase 1PRO_0000314770Add
BLAST

Proteomic databases

MaxQBiO13702.

Expressioni

Inductioni

Repressed by glucose.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi279326. 69 interactions.
MINTiMINT-4667285.

Structurei

Secondary structure

1
450
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi62 – 676Combined sources
Beta strandi70 – 756Combined sources
Helixi78 – 814Combined sources
Helixi82 – 865Combined sources
Turni87 – 893Combined sources
Beta strandi91 – 999Combined sources
Helixi100 – 1056Combined sources
Helixi107 – 11610Combined sources
Beta strandi120 – 1267Combined sources
Helixi132 – 1398Combined sources
Beta strandi148 – 1547Combined sources
Helixi155 – 16713Combined sources
Beta strandi172 – 1787Combined sources
Beta strandi187 – 1915Combined sources
Beta strandi200 – 2034Combined sources
Beta strandi209 – 2146Combined sources
Helixi215 – 2206Combined sources
Helixi223 – 24523Combined sources
Beta strandi253 – 2553Combined sources
Helixi258 – 28427Combined sources
Helixi289 – 30719Combined sources
Helixi313 – 3219Combined sources
Helixi322 – 3243Combined sources
Helixi326 – 3305Combined sources
Helixi333 – 34715Combined sources
Helixi352 – 36413Combined sources
Helixi371 – 3744Combined sources
Helixi381 – 39111Combined sources
Helixi397 – 4004Combined sources
Beta strandi401 – 4033Combined sources
Helixi407 – 42822Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TA9X-ray1.90A/B1-450[»]
ProteinModelPortaliO13702.
SMRiO13702. Positions 57-450.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO13702.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000031784.
InParanoidiO13702.
OMAiQFNGEAS.
OrthoDBiEOG092C2KC9.
PhylomeDBiO13702.

Family and domain databases

InterProiIPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
[Graphical view]
PfamiPF00465. Fe-ADH. 1 hit.
[Graphical view]
PROSITEiPS00913. ADH_IRON_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O13702-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIGPRLCAAT PRFPLVSLAH RNSKVFALAS SNAVAQRWGK RFYAPIETET
60 70 80 90 100
PHKVGVEFEE SKDRIFTSPQ KYVQGRHAFT RSYMYVKKWA TKSAVVLADQ
110 120 130 140 150
NVWNICANKI VDSLSQNGMT VTKLVFGGEA SLVELDKLRK QCPDDTQVII
160 170 180 190 200
GVGGGKTMDS AKYIAHSMNL PSIICPTTAS SDAATSSLSV IYTPDGQFQK
210 220 230 240 250
YSFYPLNPNL IFIDTDVIVR APVRFLISGI GDALSTWVET ESVIRSNSTS
260 270 280 290 300
FAGGVASIAG RYIARACKDT LEKYALSAIL SNTRGVCTEA FENVVEANTL
310 320 330 340 350
MSGLGFENGG LAAAHAIHNG MTAIHGPVHR LMHGEKVAYG TLVQVVLEDW
360 370 380 390 400
PLEDFNNLAS FMAKCHLPIT LEELGIPNVT DEELLMVGRA TLRPDESIHN
410 420 430 440 450
MSKKFNPSQI ADAIKAVDSY SQKWQEQTGW TERFRLPPSR HSPHLTDIHP
Length:450
Mass (Da):49,433
Last modified:January 1, 1998 - v1
Checksum:iE25248204A92E33A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11766.1.
PIRiT37628.
RefSeqiNP_593651.1. NM_001019083.2.

Genome annotation databases

EnsemblFungiiSPAC13F5.03c.1; SPAC13F5.03c.1:pep; SPAC13F5.03c.
GeneIDi2542881.
KEGGispo:SPAC13F5.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11766.1.
PIRiT37628.
RefSeqiNP_593651.1. NM_001019083.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TA9X-ray1.90A/B1-450[»]
ProteinModelPortaliO13702.
SMRiO13702. Positions 57-450.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279326. 69 interactions.
MINTiMINT-4667285.

Proteomic databases

MaxQBiO13702.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC13F5.03c.1; SPAC13F5.03c.1:pep; SPAC13F5.03c.
GeneIDi2542881.
KEGGispo:SPAC13F5.03c.

Organism-specific databases

EuPathDBiFungiDB:SPAC13F5.03c.
PomBaseiSPAC13F5.03c. gld1.

Phylogenomic databases

HOGENOMiHOG000031784.
InParanoidiO13702.
OMAiQFNGEAS.
OrthoDBiEOG092C2KC9.
PhylomeDBiO13702.

Enzyme and pathway databases

UniPathwayiUPA00617; UER00668.
BRENDAi1.1.1.6. 5613.

Miscellaneous databases

EvolutionaryTraceiO13702.
PROiO13702.

Family and domain databases

InterProiIPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
[Graphical view]
PfamiPF00465. Fe-ADH. 1 hit.
[Graphical view]
PROSITEiPS00913. ADH_IRON_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLD1_SCHPO
AccessioniPrimary (citable) accession number: O13702
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 1, 1998
Last modified: September 7, 2016
This is version 100 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.