2-oxopropyl-CoM reductase, carboxylating - Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)

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Q56839 (XECC_XANP2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
2-oxopropyl-CoM reductase, carboxylating
EC=1.8.1.5

Alternative name(s):
Aliphatic epoxide carboxylation component II
NADPH:2-ketopropyl-CoM carboxylase/oxidoreductase
Short name=2-KPCC

Gene names

Name:	xecC
Ordered Locus Names:	Xaut_4867

Encoded on

Plasmid pXAUT01

Organism

Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) [Complete proteome] [HAMAP]

Taxonomic identifier

78245 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Xanthobacteraceae › Xanthobacter

Protein attributes

Sequence length	523 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M.
Catalytic activity	2-mercaptoethanesulfonate + acetoacetate + NADP⁺ = 2-(2-oxopropylthio)ethanesulfonate + CO₂ + NADPH.
Cofactor	Binds 1 FAD per subunit.
Pathway	Alkene metabolism; propylene degradation.
Subunit structure	Homodimer. Component II of the aliphatic epoxide carboxylation complex together with components I, III and IV.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Domain	Redox-active center
Ligand	FAD NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Plasmid
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	2-oxopropyl-CoM reductase (carboxylating) activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 523

523

2-oxopropyl-CoM reductase, carboxylating

PRO_0000068006

Amino acid modifications

Disulfide bond

82 ↔ 87

Redox-active Ref.4

Secondary structure

523

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q56839 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 01962978B88E2015
Show »

FASTA

523

57,348

        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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complementation of Xanthobacter Py2 mutants in epoxyalkane degradation; expression and nucleotide sequence of the complementing DNA fragment." Swaving J., Weijers C.A.G.M., van Ooyen A.J.J., de Bont J.A.M. Microbiology 141:477-484(1995) [PubMed: 7704278] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequence of plasmid pXAUT01 of Xanthobacter autotrophicus Py2." US DOE Joint Genome Institute 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. Richardson P. Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-1158 / Py2.
[3]	"Characterization of three protein components required for functional reconstitution of the epoxide carboxylase multienzyme complex from Xanthobacter strain Py2." Allen J.R., Ensign S.A. J. Bacteriol. 179:3110-3115(1997) [PubMed: 9150202] [Abstract] Cited for: CHARACTERIZATION.
[4]	"Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase." Nocek B., Jang S.B., Jeong M.S., Clark D.D., Ensign S.A., Peters J.W. Biochemistry 41:12907-12913(2002) [PubMed: 12390015] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), DISULFIDE BOND.
[5]	"Aliphatic epoxide carboxylation." Ensign S.A., Allen J.R. Annu. Rev. Biochem. 72:55-76(2003) [PubMed: 12524213] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X79863 Genomic DNA. Translation: CAA56243.1.
CP000782 Genomic DNA. Translation: ABS70078.1.

PIR

S47053.

RefSeq

YP_001409314.1. NC_009717.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MO9	X-ray	1.65	A/B	1-523	[»]
1MOK	X-ray	2.80	A/B/C/D	1-523	[»]
2C3C	X-ray	2.15	A/B	1-523	[»]
2C3D	X-ray	2.15	A/B	1-523	[»]
3Q6J	X-ray	1.92	A/B	1-523	[»]

ProteinModelPortal

Q56839.

SMR

Q56839. Positions 2-523.

ModBase

Search...

Protein-protein interaction databases

STRING

Q56839.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

5420640.

GenomeReviews

Gene locus Xaut_4867 in contig CP000782_GR.

KEGG

xau:Xaut_4867.

PATRIC

24041515. VBIXanAut29526_0069.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG1249.

HOGENOM

HBG579391.

OMA

SICENIK.

ProtClustDB

CLSK962048.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-8022.
XAUT78245:XAUT_4867-MONOMER.

Family and domain databases

InterPro

IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.

Pfam

PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.

SUPFAM

SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.

ProtoNet

Search...

Entry information

Entry name

XECC_XANP2

Accession

Primary (citable) accession number: Q56839
Secondary accession number(s): A7IPY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents