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Protein

Sorbitol dehydrogenase 2

Gene

SOR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

L-iditol + NAD+ = L-sorbose + NADH.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431Zinc; catalyticBy similarity
Binding sitei49 – 491SubstrateBy similarity
Metal bindingi68 – 681Zinc; catalyticBy similarity
Metal bindingi69 – 691Zinc; catalyticBy similarity
Binding sitei154 – 1541SubstrateBy similarity
Binding sitei301 – 3011SubstrateBy similarity
Binding sitei302 – 3021SubstrateBy similarity

GO - Molecular functioni

  • L-iditol 2-dehydrogenase activity Source: SGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • hexose metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29621-MONOMER.
ReactomeiR-SCE-5652227. Fructose biosynthesis.
R-SCE-5661270. Catabolism of glucuronate to xylulose-5-phosphate.

Names & Taxonomyi

Protein namesi
Recommended name:
Sorbitol dehydrogenase 2 (EC:1.1.1.14)
Alternative name(s):
L-iditol 2-dehydrogenase 2
Gene namesi
Name:SOR2
Ordered Locus Names:YDL246C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL246C.
SGDiS000002405. SOR2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 357357Sorbitol dehydrogenase 2PRO_0000160822Add
BLAST

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi31866. 45 interactions.
DIPiDIP-1512N.
IntActiQ07786. 6 interactions.
MINTiMINT-390932.

Structurei

3D structure databases

ProteinModelPortaliQ07786.
SMRiQ07786. Positions 2-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00840000130391.
HOGENOMiHOG000294670.
InParanoidiQ07786.
KOiK00008.
OMAiIGHEYTG.
OrthoDBiEOG79CZ8G.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q07786-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQNSNPAVV LEKVGDIAIE QRPIPTIKDP HYVKLAIKAT GICGSDIHYY
60 70 80 90 100
RSGGIGKYIL KAPMVLGHES SGQVVEVGDA VTRVKVGDRV AIEPGVPSRY
110 120 130 140 150
SDETKEGSYN LCPHMAFAAT PPIDGTLVKY YLSPEDFLVK LPEGVSYEEG
160 170 180 190 200
ACVEPLSVGV HSNKLAGVRF GTKVVVFGAG PVGLLTGAVA RAFGATDVIF
210 220 230 240 250
VDVFDNKLQR AKDFGATNTF NSSQFSTDKA QDLADGVQKL LGGNHADVVF
260 270 280 290 300
ECSGADVCID AAVKTTKVGG TMVQVGMGKN YTNFPIAEVS GKEMKLIGCF
310 320 330 340 350
RYSFGDYRDA VNLVATGKVN VKPLITHKFK FEDAAKAYDY NIAHGGEVVK

TIIFGPE
Length:357
Mass (Da):38,097
Last modified:November 1, 1996 - v1
Checksum:i1684792040A3834A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74294 Genomic DNA. Translation: CAA98826.1.
BK006938 Genomic DNA. Translation: DAA11621.1.
PIRiS67811.
RefSeqiNP_010035.1. NM_001180306.1.

Genome annotation databases

EnsemblFungiiYDL246C; YDL246C; YDL246C.
GeneIDi851351.
KEGGisce:YDL246C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74294 Genomic DNA. Translation: CAA98826.1.
BK006938 Genomic DNA. Translation: DAA11621.1.
PIRiS67811.
RefSeqiNP_010035.1. NM_001180306.1.

3D structure databases

ProteinModelPortaliQ07786.
SMRiQ07786. Positions 2-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31866. 45 interactions.
DIPiDIP-1512N.
IntActiQ07786. 6 interactions.
MINTiMINT-390932.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL246C; YDL246C; YDL246C.
GeneIDi851351.
KEGGisce:YDL246C.

Organism-specific databases

EuPathDBiFungiDB:YDL246C.
SGDiS000002405. SOR2.

Phylogenomic databases

GeneTreeiENSGT00840000130391.
HOGENOMiHOG000294670.
InParanoidiQ07786.
KOiK00008.
OMAiIGHEYTG.
OrthoDBiEOG79CZ8G.

Enzyme and pathway databases

BioCyciYEAST:G3O-29621-MONOMER.
ReactomeiR-SCE-5652227. Fructose biosynthesis.
R-SCE-5661270. Catabolism of glucuronate to xylulose-5-phosphate.

Miscellaneous databases

NextBioi968441.
PROiQ07786.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.

Entry informationi

Entry nameiDHSO2_YEAST
AccessioniPrimary (citable) accession number: Q07786
Secondary accession number(s): D6VRB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 125 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. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.