ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q56841


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name HCDS_XANP2
Primary accession number Q56841
Secondary accession number A7IPY4
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 53)
Name and origin of the protein
Protein name 2-(S)-hydroxypropyl-CoM dehydrogenase
Synonyms S-HPCDH
EC 1.1.1.269
Aliphatic epoxide carboxylation component IV
Gene name
Name: xecE
OrderedLocusNames: Xaut_4869
From
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) [TaxID: 78245] [HAMAP proteome]
Encoded on Plasmid pXAUT01.
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Xanthobacteraceae; Xanthobacter.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7704278 [NCBI, ExPASy, EBI, Israel, Japan]
Swaving J., Weijers C.A.G.M., van Ooyen A.J.J., de Bont J.A.M.;
"Complementation of Xanthobacter Py2 mutants in epoxyalkane degradation; expression and nucleotide sequence of the complementing DNA fragment.";
Microbiology 141:477-484(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
"Complete sequence of plasmid pXAUT01 of Xanthobacter autotrophicus Py2.";
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 1-10, AND CHARACTERIZATION.
DOI=10.1074/jbc.272.51.32121; PubMed=9405410 [NCBI, ExPASy, EBI, Israel, Japan]
Allen J.R., Ensign S.A.;
"Purification to homogeneity and reconstitution of the individual components of the epoxide carboxylase multiprotein enzyme complex from Xanthobacter strain Py2.";
J. Biol. Chem. 272:32121-32128(1997).
[4]
REVIEW.
DOI=10.1146/annurev.biochem.72.121801.161820; PubMed=12524213 [NCBI, ExPASy, EBI, Israel, Japan]
Ensign S.A., Allen J.R.;
"Aliphatic epoxide carboxylation.";
Annu. Rev. Biochem. 72:55-76(2003).
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
X79863; CAA56245.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000782; ABS70080.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S47055; S47055.
RefSeq YP_001409316.1; -.
3D structure databases
HSSP Q12634; 1G0N. [HSSP ENTRY / PDB]
ModBase Q56841.
Enzyme and pathway databases
BioCyc MetaCyc:MON-13284; -.
Ontologies
GO
GO:0050575; Molecular function: 2-(S)-hydroxypropyl-CoM dehydrogenase activity (inferred from electronic annotation from EC).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
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 Q56841.
Genome annotation databases
GeneID 5420357; -.
GenomeReviews CP000782_GR; Xaut_4869.
KEGG xau:Xaut_4869; -.
CMR Q56841; Xaut_4869.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; NAD; Oxidoreductase; Plasmid.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   249  249     2-(S)-hydroxypropyl-CoM dehydrogenase. PRO_0000054706
ACT_SITE   150   150        Proton acceptor (By similarity). 
BINDING   137   137        Substrate (By similarity). 
CONFLICT   4     4        A -> N (in Ref. 3; AA sequence). 
Sequence information
Length: 249 AA [This is the length of the unprocessed precursor] Molecular weight: 24941 Da [This is the MW of the unprocessed precursor] CRC64: B5E0B82C1D8D9782 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLDAEVIAIT GGAAGIGLAV AHAAIRAGAR VALIDRDGAC AQRAAAEFGA AAWGVGADVT 

        70         80         90        100        110        120 
DEAAITAAMA GAQRALGPLT GLVNNAGIAG FGSVHATEVE TWSRIMAVNV TGTFLASKAA 

       130        140        150        160        170        180 
LFGMLERGRG AIVNFGSVAG LVGIPTMAAY CAAKGAVVNL TRQMAADYSG RGIRVNVVCP 

       190        200        210        220        230        240 
GTVAGTDMGR QLLGTDCDPE LEARRLAKYP MGRFGTPEDI AEAAVFLLST KAAFVTGSVL 


AVDGGMTAI 

Q56841 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!