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P0A6L8 (UXAB_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Altronate oxidoreductase

EC=1.1.1.58
Alternative name(s):
Tagaturonate dehydrogenase
Tagaturonate reductase
Gene names
Name:uxaB
Ordered Locus Names:Z2184, ECs2128
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

D-altronate + NAD+ = D-tagaturonate + NADH. HAMAP-Rule MF_00670

Pathway

Carbohydrate metabolism; pentose and glucuronate interconversion. HAMAP-Rule MF_00670

Sequence similarities

Belongs to the mannitol dehydrogenase family. UxaB subfamily.

Ontologies

Keywords
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular_functioncoenzyme binding

Inferred from electronic annotation. Source: InterPro

tagaturonate reductase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 483483Altronate oxidoreductase HAMAP-Rule MF_00670
PRO_0000170743

Regions

Nucleotide binding18 – 2912NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A6L8 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: AFA4677CF35BC2E0

FASTA48354,808
        10         20         30         40         50         60 
MKTLNRRDFP GAQYPERIIQ FGEGNFLRAF VDWQIDLLNE HTDLNSGVVV VRPIETSFPP 

        70         80         90        100        110        120 
SLSTQDGLYT TIIRGLNEKG EAVSDARLIR SVNREISVYS EYDEFLKLAH NPEMRFVFSN 

       130        140        150        160        170        180 
TTEAGISYHA GDKFDDAPAV SYPAKLTRLL FERFSHFNGA LDKGWIIIPC ELIDYNGDAL 

       190        200        210        220        230        240 
RELVLRYAQE WALPEAFIQW LDQANSFCST LVDRIVTGYP RDEVAKLEEE LGYHDGFLDT 

       250        260        270        280        290        300 
AEHFYLFVIQ GPKSLATELR LDKYPLNVLI VDDIKPYKER KVAILNGAHT ALVPVAFQAG 

       310        320        330        340        350        360 
LDTVGEAMND AEICAFVEKA IYEEIIPVLD LPRDELESFA SAVTGRFRNP YIKHQLLSIA 

       370        380        390        400        410        420 
LNGMTKFRTR ILPQLLAGQK ANGTLPARLT FALAALIAFY RGERNGETYP VQDDAHWLER 

       430        440        450        460        470        480 
YQQLWSQHRD RVIGTQELVA IVLAEKDHWE QDLTQVPGLV EQVANDLDAI LEKGMREAVR 


PLC 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG56245.2.
BA000007 Genomic DNA. Translation: BAB35551.1.
PIRH90894.
RefSeqNP_287633.2. NC_002655.2.
NP_310155.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0A6L8.
SMRP0A6L8. Positions 2-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z2184.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG56245; AAG56245; Z2184.
BAB35551; BAB35551; BAB35551.
GeneID917329.
960645.
KEGGece:Z2184.
ecs:ECs2128.
PATRIC18353087. VBIEscCol44059_1763.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0246.
HOGENOMHOG000029586.
KOK00041.
OMARVIQFGE.
OrthoDBEOG6CVVB8.
ProtClustDBPRK03643.

Enzyme and pathway databases

BioCycECOL386585:GJFA-2096-MONOMER.
ECOO157:UXAB-MONOMER.
UniPathwayUPA00246.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPMF_00670. Altron_oxidoreduct.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR023668. Altronate_OxRdtase.
IPR013328. DH_multihelical.
IPR013118. Mannitol_DH_C.
IPR013131. Mannitol_DH_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF01232. Mannitol_dh. 1 hit.
PF08125. Mannitol_dh_C. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 1 hit.
ProtoNetSearch...

Entry information

Entry nameUXAB_ECO57
AccessionPrimary (citable) accession number: P0A6L8
Secondary accession number(s): P24214, P78064
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: March 19, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways