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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.
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 databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000680061 – 5232-oxopropyl-CoM reductase, carboxylatingAdd BLAST523

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1523
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Turni7 – 9Combined sources3
Helixi13 – 25Combined sources13
Beta strandi32 – 35Combined sources4
Beta strandi44 – 49Combined sources6
Helixi53 – 64Combined sources12
Beta strandi69 – 79Combined sources11
Helixi81 – 85Combined sources5
Helixi87 – 105Combined sources19
Turni106 – 108Combined sources3
Helixi122 – 132Combined sources11
Helixi134 – 146Combined sources13
Beta strandi152 – 156Combined sources5
Beta strandi159 – 162Combined sources4
Beta strandi165 – 168Combined sources4
Beta strandi171 – 176Combined sources6
Beta strandi178 – 180Combined sources3
Beta strandi184 – 186Combined sources3
Turni192 – 195Combined sources4
Beta strandi199 – 201Combined sources3
Helixi202 – 208Combined sources7
Beta strandi215 – 220Combined sources6
Helixi224 – 235Combined sources12
Beta strandi239 – 243Combined sources5
Turni248 – 251Combined sources4
Helixi255 – 267Combined sources13
Beta strandi271 – 275Combined sources5
Beta strandi277 – 283Combined sources7
Beta strandi287 – 296Combined sources10
Beta strandi299 – 304Combined sources6
Beta strandi308 – 310Combined sources3
Beta strandi314 – 316Combined sources3
Helixi319 – 325Combined sources7
Beta strandi348 – 350Combined sources3
Helixi352 – 355Combined sources4
Helixi361 – 375Combined sources15
Beta strandi389 – 401Combined sources13
Helixi404 – 409Combined sources6
Beta strandi414 – 420Combined sources7
Turni424 – 427Combined sources4
Turni435 – 437Combined sources3
Helixi438 – 442Combined sources5
Turni444 – 446Combined sources3
Helixi447 – 450Combined sources4
Beta strandi452 – 458Combined sources7
Turni459 – 461Combined sources3
Beta strandi463 – 473Combined sources11
Helixi475 – 486Combined sources12
Helixi491 – 495Combined sources5
Helixi507 – 514Combined sources8
Beta strandi517 – 519Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
3.40.50.720. 1 hit.
3.50.50.60. 4 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR016040. NAD(P)-bd_dom.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-8081882.

Chemistry databases

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.
BRENDAi1.8.1.5. 1641.

Miscellaneous databases

EvolutionaryTraceiQ56839.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.40.50.720. 1 hit.
3.50.50.60. 4 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR016040. NAD(P)-bd_dom.
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: November 30, 2016
This is version 105 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.