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UniProtKB/Swiss-Prot entry P23102


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name XYLL_PSEPU
Primary accession number P23102
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on November 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 56)
Name and origin of the protein
Protein name 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase
Synonyms EC 1.3.1.25
Cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase
Cis-1,2-dihydroxy-3,4-cyclohexadiene-1-carboxylate dehydrogenase
2-hydro-1,2-dihydroxybenzoate dehydrogenase
DHB dehydrogenase
Gene name
Name: xylL
From
Pseudomonas putida [TaxID: 303] 
Encoded on Plasmid TOL pWW0.
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1111/j.1432-1033.1992.tb16612.x; PubMed=1740120 [NCBI, ExPASy, EBI, Israel, Japan]
Neidle E.L., Hartnett C., Ornston L.N., Bairoch A., Rekik M., Harayama S.;
"Cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily.";
Eur. J. Biochem. 204:113-120(1992).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M64747; AAA26050.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S23485; S23485.
RefSeq NP_542868.1; -.
3D structure databases
HSSP Q9LBG2; 1IY8. [HSSP ENTRY / PDB]
ModBase P23102.
Enzyme and pathway databases
BioCyc MetaCyc:MON-2964; -.
Ontologies
GO
GO:0047116; Molecular function: 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase activity (inferred from electronic annotation from EC).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0019439; Biological process: aromatic compound catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR19410; ADH_short_C2; 1.
Pfam PF00106; adh_short; 1.
Pfam graphical view of domain structure.
PRINTS PR00081; GDHRDH.
PR00080; SDRFAMILY.
PROSITE PS00061; ADH_SHORT; 1.
ProtoNet P23102.
Genome annotation databases
GeneID 1218753; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Aromatic hydrocarbons catabolism; NAD; Oxidoreductase; Plasmid.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   269  269     1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase. PRO_0000054814
NP_BIND   11    35  25     NAD (By similarity). 
ACT_SITE   153   153        Proton acceptor (By similarity). 
BINDING   142   142        Substrate (By similarity). 
Sequence information
Length: 269 AA [This is the length of the unprocessed precursor] Molecular weight: 28883 Da [This is the MW of the unprocessed precursor] CRC64: 23708B9757C6FC41 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNKRFQGKVA VITGAAQGIG RRVAERMAAE GGRLLLVDRS ELIHELADEL VGVAEVLTLT 

        70         80         90        100        110        120 
ADLEQFAECQ RVMAAALERF GRLDILINNV GGTIWAKPFE HYQEREIEAE VRRSLFPTLW 

       130        140        150        160        170        180 
CCHAALAPMI EQGSGAIVNV SSVATRGIHR VPYGAAKGGV NALTACLAFE TAERGIRVNA 

       190        200        210        220        230        240 
TAPGGTEARH GGFRNSAEPS EQEKVWYQQI VDQSLDSSLM KRYGSIDEQV EAILFLASDA 

       250        260 
ASYITGITLP VAGGDLGCQS CSVMFSVSG 

P23102 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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