Reviewed, UniProtKB/Swiss-Prot Q56839 (XECC_XANP2)

Names and origin

Protein names

Recommended name:
    2-oxopropyl-CoM reductase, carboxylating
    EC=1.8.1.5
Alternative name(s):
    NADPH:2-ketopropyl-CoM carboxylase/oxidoreductase
      Short name=2-KPCC
    Aliphatic epoxide carboxylation component II

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.
Sequence processing	The displayed sequence is not processed.
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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	2-oxopropyl-CoM reductase (carboxylating) activity Inferred from electronic annotation. Source: EC FAD 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

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523

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Helix

13 – 25

13

Beta strand

32 – 35

4

Beta strand

44 – 49

6

Helix

53 – 64

12

Beta strand

69 – 79

11

Helix

81 – 85

5

Helix

87 – 105

19

Turn

106 – 108

3

Helix

122 – 132

11

Helix

134 – 146

13

Beta strand

152 – 156

5

Beta strand

159 – 162

4

Beta strand

165 – 168

4

Beta strand

171 – 176

6

Beta strand

178 – 180

3

Turn

192 – 195

4

Beta strand

199 – 201

3

Helix

202 – 208

7

Beta strand

215 – 220

6

Helix

224 – 235

12

Beta strand

239 – 243

5

Turn

248 – 251

4

Helix

255 – 267

13

Beta strand

271 – 275

5

Beta strand

277 – 283

7

Beta strand

287 – 296

10

Beta strand

299 – 304

6

Beta strand

308 – 310

3

Helix

319 – 325

7

Beta strand

348 – 350

3

Helix

352 – 355

4

Helix

361 – 375

15

Beta strand

389 – 401

13

Helix

404 – 409

6

Beta strand

414 – 420

7

Turn

424 – 427

4

Turn

435 – 437

3

Helix

438 – 442

5

Turn

444 – 446

3

Helix

447 – 450

4

Beta strand

452 – 458

7

Turn

459 – 461

3

Beta strand

463 – 473

11

Helix

475 – 486

12

Helix

491 – 495

5

Helix

507 – 514

8

Sequences

	Sequence		Length	Mass (Da)
	Q56839-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 01962978B88E2015	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

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." 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. Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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

EMBLGenBankDDBJ

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

PIR

S47053.

RefSeq

YP_001409314.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Genome annotation databases

GeneID

5420640.

GenomeReviews

Gene locus Xaut_4867 in contig CP000782_GR.

KEGG

xau:Xaut_4867.

Organism-specific databases

CMR

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-8022.

Family and domain databases

InterPro

IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR001327. Pyr_OxRdtase_NAD_bd.
[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.

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:	March 24, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)