P05404 (TFDD1_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chloromuconate cycloisomerase
EC=5.5.1.7

Alternative name(s):
Muconate cycloisomerase II

Gene names

Name:	tfdDI
Synonyms:	tfdD
Ordered Locus Names:	Reut_D6465

Encoded on

Plasmid pJP4 Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.7
Plasmid pReut1 Ref.4

Organism

Cupriavidus pinatubonensis (strain JMP134 / LMG 1197) (Alcaligenes eutrophus) (Ralstonia eutropha) [Complete proteome] [HAMAP]

Taxonomic identifier

264198 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus › Cupriavidus pinatubonensis

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	2-chloro-2,5-dihydro-5-oxofuran-2-acetate = 3-chloro-cis,cis-muconate.
Cofactor	Manganese.
Pathway	Aromatic compound metabolism; 3-chlorocatechol degradation.
Miscellaneous	Chloromuconate cycloisomerase II is highly active toward chlorinated substrates but retains diminished activity toward the non-chlorinated substrates.
Sequence similarities	Belongs to the mandelate racemase/muconate lactonizing enzyme family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Manganese Metal-binding
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Plasmid
Gene Ontology (GO)
Biological_process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW cellular amino acid catabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	chloromuconate cycloisomerase activity Inferred from electronic annotation. Source: EC manganese ion binding Inferred from electronic annotation. Source: InterPro muconate cycloisomerase activity 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 – 370

370

Chloromuconate cycloisomerase

PRO_0000171256

Sites

Active site

165

1

Proton acceptor By similarity

Active site

323

1

Proton donor By similarity

Metal binding

194

1

Manganese By similarity

Metal binding

220

1

Manganese

Metal binding

245

1

Manganese

Experimental info

Sequence conflict

306 – 325

20

SVALQ…GCELI → RLHSAYLRFHASVRLRTV in AAA98267. Ref.2

Secondary structure

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370

Helix Strand Turn

Details...

Beta strand

5 – 20

16

Beta strand

25 – 38

14

Beta strand

44 – 46

3

Turn

51 – 55

5

Helix

60 – 70

11

Helix

72 – 75

4

Helix

83 – 91

9

Helix

98 – 115

18

Helix

120 – 123

4

Beta strand

130 – 138

9

Helix

143 – 155

13

Beta strand

161 – 165

5

Beta strand

167 – 169

3

Helix

171 – 184

14

Turn

185 – 188

4

Beta strand

189 – 194

6

Helix

202 – 212

11

Turn

213 – 215

3

Beta strand

218 – 220

3

Helix

228 – 237

10

Beta strand

239 – 247

9

Helix

251 – 258

8

Turn

259 – 261

3

Beta strand

264 – 266

3

Helix

270 – 273

4

Helix

276 – 289

14

Helix

302 – 312

11

Helix

326 – 329

4

Beta strand

334 – 336

3

Beta strand

343 – 347

5

Beta strand

351 – 353

3

Helix

360 – 366

7

Sequences

	Sequence		Length	Mass (Da)
	P05404 [UniParc]. Last modified August 1, 1992. Version 4. Checksum: C08032835D42EBDD	FASTA	370	39,722
	10 20 30 40 50 60 MKIDAIEAVI VDVPTKRPIQ MSITTVHQQS YVIVRVYSEG LVGVGEGGSV GGPVWSAECA 70 80 90 100 110 120 ETIKIIVERY LAPHLLGTDA FNVSGALQTM ARAVTGNASA KAAVEMALLD LKARALGVSI 130 140 150 160 170 180 AELLGGPLRS AIPIAWTLAS GDTKRDLDSA VEMIERRRHN RFKVKLGFRS PQDDLIHMEA 190 200 210 220 230 240 LSNSLGSKAY LRVDVNQAWD EQVASVYIPE LEALGVELIE QPVGRENTQA LRRLSDNNRV 250 260 270 280 290 300 AIMADESLST LASAFDLARD RSVDVFSLKL CNMGGVSATQ KIAAVAEASG IASYGGTMLD 310 320 330 340 350 360 STIGTSVALQ LYSTVPSLPF GCELIGPFVL ADTLSHEPLE IRDYELQVPT GVGHGMTLDE 370 DKVRQYARVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4." Perkins E.J., Gordon M.P., Caceres O., Lurquin P.F. J. Bacteriol. 172:2351-2359(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Operon structure and nucleotide homology of the chlorocatechol oxidation genes of plasmids pJP4 and pAC27." Ghosal D., You I.-S. Gene 83:225-232(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants and evolution of specialized chloroaromatic degradation pathways." Trefault N., De la Iglesia R., Molina A.M., Manzano M., Ledger T., Perez-Pantoja D., Sanchez M.A., Stuardo M., Gonzalez B. Environ. Microbiol. 6:655-668(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Complete sequence of plasmid 1 of Ralstonia eutropha JMP134." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JMP134 / LMG 1197.
[5]	"Partial nucleotide sequence of the chlorocatechol degradative operon tfdCDEF of pJP4 and similarity to promoters of the chlorinated aromatic degradative operons tfdA and clcABD." Perkins E.J., Bolton G., Gordon M.P., Lurquin P.F. Nucleic Acids Res. 16:7200-7200(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-166.
[6]	"Crystal structure of chloromuconate cycloisomerase from Alcaligenes eutrophus JMP134 (pJP4) at 3-A resolution." Hoier H., Schloemann M., Hammer A., Glusker J.P., Carrell H.L., Goldman A., Stezowski J.J., Heinemann U. Acta Crystallogr. D 50:75-84(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS.
[7]	"A re-evaluation of the crystal structure of chloromuconate cycloisomerase." Kleywegt G.J., Jones T.A. Acta Crystallogr. D 52:858-863(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M35097 Genomic DNA. Translation: AAA98263.1.
M31458 Genomic DNA. Translation: AAA98267.1.
AY365053 Genomic DNA. Translation: AAR31038.1.
CP000093 Genomic DNA. Translation: AAZ65763.1.

PIR

B35255.

RefSeq

YP_025386.1. NC_005912.1.
YP_293620.1. NC_007337.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CHR	X-ray	3.00	A	1-370	[»]

ProteinModelPortal

P05404.

SMR

P05404. Positions 1-370.

ModBase

Search...

Protein-protein interaction databases

STRING

264198.Reut_D6465.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAZ65763; AAZ65763; Reut_D6465.

GeneID

2847421.
3607311.

KEGG

reu:Reut_D6465.

PATRIC

20225306. VBIRalEut24049_0532.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG4948.

HOGENOM

HOG000185904.

KO

K01860.

OMA

GRENTQA.

ProtClustDB

CLSK926389.

Enzyme and pathway databases

BioCyc

CPIN264198:GIW3-6551-MONOMER.
MetaCyc:MONOMER-14403.

UniPathway

UPA00083.

Family and domain databases

InterPro

IPR013370. Chloromuconate_cycloisomerase.
IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N.
IPR001354. MR_MLE.
[Graphical view]

PANTHER

PTHR13794. PTHR13794. 1 hit.
PTHR13794:SF12. PTHR13794:SF12. 1 hit.

Pfam

PF01188. MR_MLE. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]

SMART

SM00922. MR_MLE. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02534. mucon_cyclo. 1 hit.

PROSITE

PS00908. MR_MLE_1. 1 hit.
PS00909. MR_MLE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P05404.

Entry information

Entry name

TFDD1_CUPPJ

Accession

Primary (citable) accession number: P05404
Secondary accession number(s): Q46M67

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	August 1, 1992
Last modified:	May 1, 2013
This is version 114 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program