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Protein

2-oxopropyl-CoM reductase, carboxylating

Gene

xecC

Organism
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

2-mercaptoethanesulfonate + acetoacetate + NADP+ = 2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH.

Cofactori

FADNote: Binds 1 FAD per subunit.

Pathwayi: propylene degradation

This protein is involved in the pathway propylene degradation, which is part of Alkene metabolism.
View all proteins of this organism that are known to be involved in the pathway propylene degradation and in Alkene metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8022.
XAUT78245:GHS6-4926-MONOMER.
BRENDAi1.8.1.5. 1641.
UniPathwayiUPA00776.

Names & Taxonomyi

Protein namesi
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 namesi
Name:xecC
Ordered Locus Names:Xaut_4867
Encoded oniPlasmid pXAUT010 Publication
OrganismiXanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Taxonomic identifieri78245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeXanthobacter
Proteomesi
  • UP000002417 Componenti: Plasmid pXAUT01

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5235232-oxopropyl-CoM reductase, carboxylatingPRO_0000068006Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi82 ↔ 87Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer. Component II of the aliphatic epoxide carboxylation complex together with components I, III and IV.

Protein-protein interaction databases

MINTiMINT-8081882.

Structurei

Secondary structure

1
523
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Turni7 – 93Combined sources
Helixi13 – 2513Combined sources
Beta strandi32 – 354Combined sources
Beta strandi44 – 496Combined sources
Helixi53 – 6412Combined sources
Beta strandi69 – 7911Combined sources
Helixi81 – 855Combined sources
Helixi87 – 10519Combined sources
Turni106 – 1083Combined sources
Helixi122 – 13211Combined sources
Helixi134 – 14613Combined sources
Beta strandi152 – 1565Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi165 – 1684Combined sources
Beta strandi171 – 1766Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi184 – 1863Combined sources
Turni192 – 1954Combined sources
Beta strandi199 – 2013Combined sources
Helixi202 – 2087Combined sources
Beta strandi215 – 2206Combined sources
Helixi224 – 23512Combined sources
Beta strandi239 – 2435Combined sources
Turni248 – 2514Combined sources
Helixi255 – 26713Combined sources
Beta strandi271 – 2755Combined sources
Beta strandi277 – 2837Combined sources
Beta strandi287 – 29610Combined sources
Beta strandi299 – 3046Combined sources
Beta strandi308 – 3103Combined sources
Beta strandi314 – 3163Combined sources
Helixi319 – 3257Combined sources
Beta strandi348 – 3503Combined sources
Helixi352 – 3554Combined sources
Helixi361 – 37515Combined sources
Beta strandi389 – 40113Combined sources
Helixi404 – 4096Combined sources
Beta strandi414 – 4207Combined sources
Turni424 – 4274Combined sources
Turni435 – 4373Combined sources
Helixi438 – 4425Combined sources
Turni444 – 4463Combined sources
Helixi447 – 4504Combined sources
Beta strandi452 – 4587Combined sources
Turni459 – 4613Combined sources
Beta strandi463 – 47311Combined sources
Helixi475 – 48612Combined sources
Helixi491 – 4955Combined sources
Helixi507 – 5148Combined sources
Beta strandi517 – 5193Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MO9X-ray1.65A/B1-523[»]
1MOKX-ray2.80A/B/C/D1-523[»]
2C3CX-ray2.15A/B1-523[»]
2C3DX-ray2.15A/B1-523[»]
3Q6JX-ray1.92A/B1-523[»]
ProteinModelPortaliQ56839.
SMRiQ56839. Positions 2-523.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ56839.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

HOGENOMiHOG000223613.
OrthoDBiPOG091H2XGL.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 4 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 3 hits.
SSF55424. SSF55424. 1 hit.

Sequencei

Sequence statusi: Complete.

Q56839-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVWNARNDH LTINQWATRI DEILEAPDGG EVIYNVDEND PREYDAIFIG
60 70 80 90 100
GGAAGRFGSA YLRAMGGRQL IVDRWPFLGG SCPHNACVPH HLFSDCAAEL
110 120 130 140 150
MLARTFSGQY WFPDMTEKVV GIKEVVDLFR AGRNGPHGIM NFQSKEQLNL
160 170 180 190 200
EYILNCPAKV IDNHTVEAAG KVFKAKNLIL AVGAGPGTLD VPGVNAKGVF
210 220 230 240 250
DHATLVEELD YEPGSTVVVV GGSKTAVEYG CFFNATGRRT VMLVRTEPLK
260 270 280 290 300
LIKDNETRAY VLDRMKEQGM EIISGSNVTR IEEDANGRVQ AVVAMTPNGE
310 320 330 340 350
MRIETDFVFL GLGEQPRSAE LAKILGLDLG PKGEVLVNEY LQTSVPNVYA
360 370 380 390 400
VGDLIGGPME MFKARKSGCY AARNVMGEKI SYTPKNYPDF LHTHYEVSFL
410 420 430 440 450
GMGEEEARAA GHEIVTIKMP PDTENGLNVA LPASDRTMLY AFGKGTAHMS
460 470 480 490 500
GFQKIVIDAK TRKVLGAHHV GYGAKDAFQY LNVLIKQGLT VDELGDMDEL
510 520
FLNPTHFIQL SRLRAGSKNL VSL
Length:523
Mass (Da):57,348
Last modified:November 1, 1996 - v1
Checksum:i01962978B88E2015
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79863 Genomic DNA. Translation: CAA56243.1.
CP000782 Genomic DNA. Translation: ABS70078.1.
PIRiS47053.
RefSeqiWP_011992982.1. NC_009717.1.

Genome annotation databases

EnsemblBacteriaiABS70078; ABS70078; Xaut_4867.
KEGGixau:Xaut_4867.
PATRICi24041515. VBIXanAut29526_0069.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79863 Genomic DNA. Translation: CAA56243.1.
CP000782 Genomic DNA. Translation: ABS70078.1.
PIRiS47053.
RefSeqiWP_011992982.1. NC_009717.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MO9X-ray1.65A/B1-523[»]
1MOKX-ray2.80A/B/C/D1-523[»]
2C3CX-ray2.15A/B1-523[»]
2C3DX-ray2.15A/B1-523[»]
3Q6JX-ray1.92A/B1-523[»]
ProteinModelPortaliQ56839.
SMRiQ56839. Positions 2-523.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-8081882.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS70078; ABS70078; Xaut_4867.
KEGGixau:Xaut_4867.
PATRICi24041515. VBIXanAut29526_0069.

Phylogenomic databases

HOGENOMiHOG000223613.
OrthoDBiPOG091H2XGL.

Enzyme and pathway databases

UniPathwayiUPA00776.
BioCyciMetaCyc:MONOMER-8022.
XAUT78245:GHS6-4926-MONOMER.
BRENDAi1.8.1.5. 1641.

Miscellaneous databases

EvolutionaryTraceiQ56839.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 4 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 3 hits.
SSF55424. SSF55424. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiXECC_XANP2
AccessioniPrimary (citable) accession number: Q56839
Secondary accession number(s): A7IPY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

3D-structure, Complete proteome, Plasmid, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.