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Protein

Sorbitol dehydrogenase

Gene

SORD

Organism
Ovis aries (Sheep)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm.By similarity

Catalytic activityi

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

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431Zinc; catalytic1 Publication
Binding sitei49 – 491Substrate1 Publication
Metal bindingi67 – 671Zinc; catalytic1 Publication
Metal bindingi68 – 681Zinc; catalytic1 Publication
Binding sitei153 – 1531Substrate1 Publication
Binding sitei296 – 2961Substrate1 Publication
Binding sitei297 – 2971Substrate1 Publication

GO - Molecular functioni

  1. L-iditol 2-dehydrogenase activity Source: UniProtKB
  2. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. sperm motility Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

SABIO-RKP07846.

Names & Taxonomyi

Protein namesi
Recommended name:
Sorbitol dehydrogenase (EC:1.1.1.14)
Alternative name(s):
L-iditol 2-dehydrogenase
Gene namesi
Name:SORD
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
ProteomesiUP000002356 Componenti: Unplaced

Subcellular locationi

  1. Mitochondrion membrane By similarity; Peripheral membrane protein By similarity
  2. Cell projectionciliumflagellum By similarity

  3. Note: Associated with mitochondria of the midpiece and near the plasma membrane in the principal piece of the flagellum. Also found in the epididymosome, secreted by the epididymal epithelium and that transfers proteins from the epididymal fluid to the sperm surface.By similarity

GO - Cellular componenti

  1. mitochondrial membrane Source: UniProtKB-SubCell
  2. motile cilium Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Flagellum, Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354Sorbitol dehydrogenasePRO_0000160819Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylalanineBy similarity
Modified residuei208 – 2081PhosphoserineBy similarity
Modified residuei222 – 2221PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
354
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 147Combined sources
Beta strandi17 – 226Combined sources
Beta strandi32 – 4211Combined sources
Helixi44 – 518Combined sources
Beta strandi52 – 543Combined sources
Beta strandi68 – 769Combined sources
Beta strandi88 – 914Combined sources
Beta strandi93 – 953Combined sources
Helixi101 – 1044Combined sources
Helixi108 – 1103Combined sources
Beta strandi127 – 1337Combined sources
Helixi134 – 1363Combined sources
Beta strandi137 – 1393Combined sources
Helixi146 – 16520Combined sources
Beta strandi172 – 1765Combined sources
Helixi180 – 19112Combined sources
Beta strandi195 – 2028Combined sources
Helixi204 – 21310Combined sources
Beta strandi216 – 2205Combined sources
Helixi226 – 23712Combined sources
Beta strandi242 – 2465Combined sources
Helixi251 – 26010Combined sources
Beta strandi266 – 2694Combined sources
Helixi281 – 2866Combined sources
Beta strandi290 – 2934Combined sources
Helixi301 – 3099Combined sources
Helixi316 – 3183Combined sources
Beta strandi319 – 3246Combined sources
Helixi325 – 3273Combined sources
Helixi328 – 33710Combined sources
Beta strandi339 – 3468Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SDGmodel-A1-347[»]
3QE3X-ray1.90A1-354[»]
ProteinModelPortaliP07846.
SMRiP07846. Positions 1-354.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07846.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG005484.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P07846-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AKPAAENLSL VVHGPGDLRL ENYPIPEPGP NEVLLKMHSV GICGSDVHYW
60 70 80 90 100
QGRIGDFVVK KPMVLGHEAS GTVVKVGSLV RHLQPGDRVA IQPGAPRQTD
110 120 130 140 150
EFCKIGRYNL SPTIFFCATP PDDGNLCRFY KHNANFCYKL PDNVTFEEGA
160 170 180 190 200
LIEPLSVGIH ACRRAGVTLG NKVLVCGAGP IGLVNLLAAK AMGAAQVVVT
210 220 230 240 250
DLSASRLSKA KEVGADFILE ISNESPEEIA KKVEGLLGSK PEVTIECTGV
260 270 280 290 300
ETSIQAGIYA THSGGTLVLV GLGSEMTSVP LVHAATREVD IKGVFRYCNT
310 320 330 340 350
WPMAISMLAS KSVNVKPLVT HRFPLEKALE AFETSKKGLG LKVMIKCDPS

DQNP
Length:354
Mass (Da):37,831
Last modified:August 1, 1988 - v1
Checksum:iD5FE56BC06F87389
GO

Sequence databases

PIRiS10065.

Cross-referencesi

Sequence databases

PIRiS10065.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SDGmodel-A1-347[»]
3QE3X-ray1.90A1-354[»]
ProteinModelPortaliP07846.
SMRiP07846. Positions 1-354.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL1075154.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005484.

Enzyme and pathway databases

SABIO-RKP07846.

Miscellaneous databases

EvolutionaryTraceiP07846.

Family and domain databases

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

Publicationsi

  1. "Sorbitol dehydrogenase. The primary structure of the sheep-liver enzyme."
    Jeffery J., Cederlund E., Joernvall H.
    Eur. J. Biochem. 140:7-16(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Liver.
  2. "Extensive variations and basic features in the alcohol dehydrogenase-sorbitol dehydrogenase family."
    Joernvall H., von Bahr-Lindstroem H., Jeffery J.
    Eur. J. Biochem. 140:17-23(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO ZINC ALCOHOL DEHYDROGENASES.
  3. "Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases."
    Eklund H., Horjales E., Joernvall H., Branden C.I., Jeffery J.
    Biochemistry 24:8005-8012(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  4. "X-ray crystal structure and small-angle X-ray scattering of sheep liver sorbitol dehydrogenase."
    Yennawar H., Moller M., Gillilan R., Yennawar N.
    Acta Crystallogr. D 67:440-446(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT, ZINC-BINDING SITES, SUBSTRATE-BINDING SITES, ENZYME MECHANISM.

Entry informationi

Entry nameiDHSO_SHEEP
AccessioniPrimary (citable) accession number: P07846
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: March 4, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.