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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)DescriptionActionsGraphical viewLength
Binding sitei139SubstrateBy similarity1
Active sitei152Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi5 – 34NADBy similarityAdd BLAST30

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000546551 – 256Sorbitol dehydrogenaseAdd BLAST256

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi272943.RSP_0095.

Structurei

Secondary structure

1256
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni2 – 5Combined sources4
Beta strandi6 – 11Combined sources6
Helixi16 – 27Combined sources12
Beta strandi30 – 37Combined sources8
Helixi39 – 49Combined sources11
Beta strandi53 – 57Combined sources5
Helixi63 – 77Combined sources15
Beta strandi82 – 85Combined sources4
Helixi95 – 97Combined sources3
Helixi100 – 110Combined sources11
Helixi112 – 128Combined sources17
Beta strandi132 – 137Combined sources6
Helixi140 – 142Combined sources3
Helixi150 – 170Combined sources21
Helixi171 – 173Combined sources3
Beta strandi175 – 182Combined sources8
Helixi190 – 201Combined sources12
Helixi207 – 215Combined sources9
Helixi224 – 233Combined sources10
Helixi237 – 239Combined sources3
Beta strandi246 – 250Combined sources5

3D structure databases

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

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: November 2, 2016
This is version 74 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.