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Protein

Sorbitol dehydrogenase

Gene

polS

Organism
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of D-glucitol (sorbitol) to D-fructose, galactitol to D-tagatose and of L-iditol.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391SubstrateBy similarity
Active sitei152 – 1521Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi5 – 3430NADBy similarityAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Sorbitol dehydrogenase (EC:1.1.1.14)
Alternative name(s):
L-iditol 2-dehydrogenase
Polyol dehydrogenase
Gene namesi
Name:polS
Synonyms:smoS
OrganismiRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Taxonomic identifieri1063 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 256256Sorbitol dehydrogenasePRO_0000054655Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi272943.RSP_0095.

Structurei

Secondary structure

1
256
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni2 – 54Combined sources
Beta strandi6 – 116Combined sources
Helixi16 – 2712Combined sources
Beta strandi30 – 378Combined sources
Helixi39 – 4911Combined sources
Beta strandi53 – 575Combined sources
Helixi63 – 7715Combined sources
Beta strandi82 – 854Combined sources
Helixi95 – 973Combined sources
Helixi100 – 11011Combined sources
Helixi112 – 12817Combined sources
Beta strandi132 – 1376Combined sources
Helixi140 – 1423Combined sources
Helixi150 – 17021Combined sources
Helixi171 – 1733Combined sources
Beta strandi175 – 1828Combined sources
Helixi190 – 20112Combined sources
Helixi207 – 2159Combined sources
Helixi224 – 23310Combined sources
Helixi237 – 2393Combined sources
Beta strandi246 – 2505Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K2WX-ray2.40A/B1-256[»]
1UZOmodel-A1-256[»]
ProteinModelPortaliQ59787.
SMRiQ59787. Positions 1-256.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59787.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CHR. Bacteria.
ENOG410XNW1. LUCA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59787-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLDGKTALI TGSARGIGRA FAEAYVREGA RVAIADINLE AARATAAEIG
60 70 80 90 100
PAACAIALDV TDQASIDRCV AELLDRWGSI DILVNNAALF DLAPIVEITR
110 120 130 140 150
ESYDRLFAIN VSGTLFMMQA VARAMIAGGR GGKIINMASQ AGRRGEALVG
160 170 180 190 200
VYCATKAAVI SLTQSAGLNL IRHGINVNAI APGVVDGEHW DGVDAKFADY
210 220 230 240 250
ENLPRGEKKR QVGAAVPFGR MGRAEDLTGM AIFLATPEAD YIVAQTYNVD

GGNWMS
Length:256
Mass (Da):27,014
Last modified:November 1, 1997 - v1
Checksum:i33CD7BC17598B02A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF018073 Genomic DNA. Translation: AAC45770.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF018073 Genomic DNA. Translation: AAC45770.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K2WX-ray2.40A/B1-256[»]
1UZOmodel-A1-256[»]
ProteinModelPortaliQ59787.
SMRiQ59787. Positions 1-256.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272943.RSP_0095.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CHR. Bacteria.
ENOG410XNW1. LUCA.

Miscellaneous databases

EvolutionaryTraceiQ59787.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Polyol metabolism of Rhodobacter sphaeroides: biochemical characterization of a short-chain sorbitol dehydrogenase."
    Schauder S., Schneider K.-H., Giffhorn F.
    Microbiology 141:1857-1863(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: SI-4.
  2. "Structure of zinc-independent sorbitol dehydrogenase from Rhodobacter sphaeroides at 2.4 A resolution."
    Philippsen A., Schirmer T., Stein M.A., Giffhorn F., Stetefeld J.
    Acta Crystallogr. D 61:374-379(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Entry informationi

Entry nameiDHSO_RHOSH
AccessioniPrimary (citable) accession number: Q59787
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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