2-oxopropyl-CoM reductase, carboxylating

Details

Name

2-oxopropyl-CoM reductase, carboxylating

Synonyms

• 1.8.1.5
• 2-KPCC
• Aliphatic epoxide carboxylation component II
• NADPH:2-ketopropyl-CoM carboxylase/oxidoreductase

Gene Name

xecC

Organism

Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)

Amino acid sequence

>lcl|BSEQ0011272|2-oxopropyl-CoM reductase, carboxylating
MKVWNARNDHLTINQWATRIDEILEAPDGGEVIYNVDENDPREYDAIFIGGGAAGRFGSA
YLRAMGGRQLIVDRWPFLGGSCPHNACVPHHLFSDCAAELMLARTFSGQYWFPDMTEKVV
GIKEVVDLFRAGRNGPHGIMNFQSKEQLNLEYILNCPAKVIDNHTVEAAGKVFKAKNLIL
AVGAGPGTLDVPGVNAKGVFDHATLVEELDYEPGSTVVVVGGSKTAVEYGCFFNATGRRT
VMLVRTEPLKLIKDNETRAYVLDRMKEQGMEIISGSNVTRIEEDANGRVQAVVAMTPNGE
MRIETDFVFLGLGEQPRSAELAKILGLDLGPKGEVLVNEYLQTSVPNVYAVGDLIGGPME
MFKARKSGCYAARNVMGEKISYTPKNYPDFLHTHYEVSFLGMGEEEARAAGHEIVTIKMP
PDTENGLNVALPASDRTMLYAFGKGTAHMSGFQKIVIDAKTRKVLGAHHVGYGAKDAFQY
LNVLIKQGLTVDELGDMDELFLNPTHFIQLSRLRAGSKNLVSL

Number of residues

523

Molecular Weight

57347.19

Theoretical pI

5.9

GO Classification

Functions

2-oxopropyl-CoM reductase (carboxylating) activity / flavin adenine dinucleotide binding

Processes

cell redox homeostasis / propylene catabolic process

Components

cell

General Function

Flavin adenine dinucleotide binding

Specific 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.

Pfam Domain Function

• Pyr_redox_2 (PF07992)
• Pyr_redox_dim (PF02852)

Transmembrane Regions

Not Available

Cellular Location

Not Available

Gene sequence

>lcl|BSEQ0011273|2-oxopropyl-CoM reductase, carboxylating (xecC)
GTGAAAGTCTGGAACGCCCGAAACGACCATCTCACCATCAATCAATGGGCCACGCGGATC
GATGAGATCCTCGAGGCGCCCGATGGCGGAGAGGTCATCTACAACGTGGACGAGAACGAT
CCACGCGAATACGACGCCATCTTCATCGGCGGCGGCGCCGCCGGGCGCTTCGGCTCGGCC
TATCTGCGCGCCATGGGCGGCCGGCAGCTCATCGTCGACCGCTGGCCGTTCCTGGGCGGC
TCGTGCCCGCACAATGCGTGCGTGCCGCACCATCTGTTCTCCGACTGCGCGGCCGAGCTG
ATGCTCGCGCGCACCTTCTCGGGCCAGTACTGGTTCCCGGACATGACCGAGAAGGTGGTC
GGCATCAAGGAGGTGGTCGATCTGTTCCGCGCCGGGCGCAACGGCCCGCACGGCATCATG
AACTTCCAGTCCAAGGAACAGCTCAACCTCGAATACATCCTCAACTGCCCGGCCAAGGTG
ATCGATAATCACACCGTCGAGGCGGCCGGCAAGGTGTTCAAGGCCAAGAACCTGATCCTC
GCGGTGGGCGCGGGGCCGGGCACGCTCGACGTGCCGGGCGTCAACGCCAAGGGCGTCTTC
GACCACGCGACGCTGGTGGAGGAGCTCGACTACGAGCCCGGCAGCACCGTGGTCGTGGTG
GGCGGCTCGAAGACCGCGGTCGAATATGGCTGCTTCTTCAACGCCACCGGCCGGCGCACC
GTGATGCTGGTGCGCACCGAGCCGCTCAAGCTCATCAAGGACAACGAGACCCGCGCCTAC
GTGCTCGACCGCATGAAGGAGCAGGGCATGGAGATCATCTCCGGCTCCAACGTCACGCGC
ATCGAGGAGGACGCCAACGGCCGCGTTCAGGCGGTGGTGGCCATGACGCCCAACGGCGAG
ATGCGCATCGAGACCGACTTCGTCTTCCTCGGCCTCGGCGAGCAGCCCCGCTCGGCGGAG
CTGGCGAAGATCCTGGGCCTCGATCTCGGCCCCAAGGGCGAGGTGCTGGTCAACGAATAT
CTTCAGACCAGCGTGCCCAACGTCTACGCGGTGGGCGACCTCATCGGCGGGCCCATGGAG
ATGTTCAAGGCCCGCAAGTCCGGCTGCTATGCCGCGCGCAACGTCATGGGCGAGAAGATC
TCCTACACGCCCAAGAATTATCCCGACTTCCTGCACACCCATTACGAGGTCAGCTTCCTC
GGCATGGGCGAGGAGGAAGCCCGCGCGGCGGGGCACGAGATCGTCACCATCAAGATGCCG
CCGGACACGGAGAACGGCCTCAACGTGGCGCTGCCGGCCTCCGACCGCACCATGCTCTAC
GCCTTCGGCAAGGGCACGGCCCACATGTCGGGCTTCCAGAAGATCGTCATCGACGCCAAG
ACCCGCAAGGTGCTCGGCGCCCATCACGTGGGCTATGGCGCGAAGGACGCGTTCCAATAC
CTGAACGTGCTCATCAAGCAGGGGCTCACCGTCGACGAACTGGGGGACATGGACGAATTG
TTCCTCAATCCGACCCACTTCATCCAGCTCTCGCGCCTGCGCGCGGGCTCGAAGAATCTG
GTGAGCCTGTGA

Chromosome Location

Not Available

Locus

Not Available

External Identifiers

Resource	Link
UniProtKB ID	Q56839
UniProtKB Entry Name	XECC_XANP2
GenBank Protein ID	929914
GenBank Gene ID	X79863

General References

1. Swaving J, Weijers CA, van Ooyen AJ, de Bont JA: Complementation of Xanthobacter Py2 mutants defective in epoxyalkane degradation, and expression and nucleotide sequence of the complementing DNA fragment. Microbiology. 1995 Feb;141 ( Pt 2):477-84. [Article]
2. Allen JR, Ensign SA: Characterization of three protein components required for functional reconstitution of the epoxide carboxylase multienzyme complex from Xanthobacter strain Py2. J Bacteriol. 1997 May;179(10):3110-5. [Article]
3. Nocek B, Jang SB, Jeong MS, Clark DD, Ensign SA, Peters JW: Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase. Biochemistry. 2002 Oct 29;41(43):12907-13. [Article]
4. Ensign SA, Allen JR: Aliphatic epoxide carboxylation. Annu Rev Biochem. 2003;72:55-76. Epub 2003 Jan 8. [Article]

Drug Relations

Drug Relations

DrugBank ID	Name	Drug group	Pharmacological action?	Actions	Details
DB03147	Flavin adenine dinucleotide	approved	unknown		Details
DB03163	2-oxopropyl-CoM	experimental	unknown		Details