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UniProtKB/Swiss-Prot entry Q56839


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

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Entry information
Entry name XECC_XANP2
Primary accession number Q56839
Secondary accession number A7IPY2
Integrated into Swiss-Prot on January 16, 2004
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 51)
Name and origin of the protein
Protein name 2-oxopropyl-CoM reductase, carboxylating
Synonyms EC 1.8.1.5
NADPH:2-ketopropyl-CoM carboxylase/oxidoreductase
2-KPCC
Aliphatic epoxide carboxylation component II
Gene name
Name: xecC
OrderedLocusNames: Xaut_4867
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]
CHARACTERIZATION.
PubMed=9150202 [NCBI, ExPASy, EBI, Israel, Japan]
Allen J.R., Ensign S.A.;
"Characterization of three protein components required for functional reconstitution of the epoxide carboxylase multienzyme complex from Xanthobacter strain Py2.";
J. Bacteriol. 179:3110-3115(1997).
[4]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), AND DISULFIDE BOND.
DOI=10.1021/bi026580p; PubMed=12390015 [NCBI, ExPASy, EBI, Israel, Japan]
Nocek B., Jang S.B., Jeong M.S., Clark D.D., Ensign S.A., Peters J.W.;
"Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.";
Biochemistry 41:12907-12913(2002).
[5]
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; CAA56243.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000782; ABS70078.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S47053; S47053.
RefSeq YP_001409314.1; -.
3D structure databases
PDB
1MO9; X-ray; 1.65 A; A/B=1-523.[ExPASy / RCSB / EBI]
1MOK; X-ray; 2.80 A; A/B/C/D=1-523.[ExPASy / RCSB / EBI]
2C3C; X-ray; 2.15 A; A/B=1-523.[ExPASy / RCSB / EBI]
2C3D; X-ray; 2.15 A; A/B=1-523.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1MO9; -.
1MOK; -.
2C3C; -.
2C3D; -.
ModBase Q56839.
Enzyme and pathway databases
BioCyc MetaCyc:MON-8022; -.
Family and domain databases
InterPro IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.30.390.30; Pyr_redox_dim; 1.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00411; PNDRDTASEI.
BLOCKS Q56839.
Genome annotation databases
GeneID 5420640; -.
GenomeReviews CP000782_GR; Xaut_4867.
KEGG xau:Xaut_4867; -.
CMR Q56839; Xaut_4867.
Other
ProtoNet Q56839.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; FAD; NADP; Oxidoreductase; Plasmid; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   523  523     2-oxopropyl-CoM reductase, carboxylating. PRO_0000068006
DISULFID   82    87        Redox-active. 
STRAND   3     5  3      
HELIX   13    25  13      
STRAND   32    35  4      
STRAND   44    49  6      
HELIX   53    64  12      
STRAND   69    79  11      
HELIX   81    85  5      
HELIX   87   105  19      
TURN   106   108  3      
HELIX   122   132  11      
HELIX   134   146  13      
STRAND   152   156  5      
STRAND   159   162  4      
STRAND   165   168  4      
STRAND   171   176  6      
STRAND   178   180  3      
TURN   192   195  4      
STRAND   199   201  3      
HELIX   202   208  7      
STRAND   215   220  6      
HELIX   224   235  12      
STRAND   239   243  5      
TURN   248   251  4      
HELIX   255   267  13      
STRAND   271   275  5      
STRAND   277   283  7      
STRAND   287   296  10      
STRAND   299   304  6      
STRAND   308   310  3      
HELIX   319   325  7      
STRAND   348   350  3      
HELIX   352   355  4      
HELIX   361   375  15      
STRAND   389   401  13      
HELIX   404   409  6      
STRAND   414   420  7      
TURN   424   427  4      
TURN   435   437  3      
HELIX   438   442  5      
TURN   444   446  3      
HELIX   447   450  4      
STRAND   452   458  7      
TURN   459   461  3      
STRAND   463   473  11      
HELIX   475   486  12      
HELIX   491   495  5      
HELIX   507   514  8      
Sequence information
Length: 523 AA [This is the length of the unprocessed precursor] Molecular weight: 57348 Da [This is the MW of the unprocessed precursor] CRC64: 01962978B88E2015 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKVWNARNDH LTINQWATRI DEILEAPDGG EVIYNVDEND PREYDAIFIG GGAAGRFGSA 

        70         80         90        100        110        120 
YLRAMGGRQL IVDRWPFLGG SCPHNACVPH HLFSDCAAEL MLARTFSGQY WFPDMTEKVV 

       130        140        150        160        170        180 
GIKEVVDLFR AGRNGPHGIM NFQSKEQLNL EYILNCPAKV IDNHTVEAAG KVFKAKNLIL 

       190        200        210        220        230        240 
AVGAGPGTLD VPGVNAKGVF DHATLVEELD YEPGSTVVVV GGSKTAVEYG CFFNATGRRT 

       250        260        270        280        290        300 
VMLVRTEPLK LIKDNETRAY VLDRMKEQGM EIISGSNVTR IEEDANGRVQ AVVAMTPNGE 

       310        320        330        340        350        360 
MRIETDFVFL GLGEQPRSAE LAKILGLDLG PKGEVLVNEY LQTSVPNVYA VGDLIGGPME 

       370        380        390        400        410        420 
MFKARKSGCY AARNVMGEKI SYTPKNYPDF LHTHYEVSFL GMGEEEARAA GHEIVTIKMP 

       430        440        450        460        470        480 
PDTENGLNVA LPASDRTMLY AFGKGTAHMS GFQKIVIDAK TRKVLGAHHV GYGAKDAFQY 

       490        500        510        520 
LNVLIKQGLT VDELGDMDEL FLNPTHFIQL SRLRAGSKNL VSL 

Q56839 in FASTA format

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