P11452 (CLCB_PSEPU) 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:

clcB

Encoded on

Plasmid pAC27

Organism

Pseudomonas putida (Arthrobacter siderocapsulatus)

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas putida group

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Highly active toward chlorinated substrates but retains diminished activity toward the non-chlorinated substrates.
Catalytic activity	2-chloro-2,5-dihydro-5-oxofuran-2-acetate = 3-chloro-cis,cis-muconate.
Cofactor	Manganese By similarity.
Pathway	Aromatic compound metabolism; 3-chlorocatechol degradation.
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	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_0000171253
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 By similarity
	Metal binding	245	1	Manganese By similarity
Experimental info
	Sequence conflict	42	1	V → C Ref.1
	Sequence conflict	42	1	V → C Ref.2
	Sequence conflict	114	1	R → H Ref.1
	Sequence conflict	114	1	R → H Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P11452 [UniParc]. Last modified August 1, 1990. Version 2. Checksum: 9279DD393F42BBCD	FASTA	370	39,847
	10 20 30 40 50 60 MKIEAIDVTL VDVPASRPIQ MSFTTVQKQS YAIVQIRAGG LVGIGEGSSV GGPTWSSECA 70 80 90 100 110 120 ETIKVIIETY LAPLLIGKDA TNLRELQHLM ERAVTGNYSA KAAIDVALHD LKARSLNLPL 130 140 150 160 170 180 SDLIGGAIQQ GIPIAWTLAS GDTQRDIAIA EEMIERRRHN RFKIKLGVRS PADDLRHIEK 190 200 210 220 230 240 IIERVGDRAA VRVDINQAWD ENTASVWIPR LEAAGVELVE QPVARSNFDA LRRLSADNGV 250 260 270 280 290 300 AILADESLSS LASAFELARH HCVDAFSLKL CNMGGVANTL KVAAIAEASG IASYGGTMLD 310 320 330 340 350 360 SSIGTAAALH VYATLPTMPF ECELLGPWVL ADTLTQTQLE IKDFEIRLPS GPGLGVDIDP 370 DKLRHFTRAG

References

[1]	"Organization and nucleotide sequence determination of a gene cluster involved in 3-chlorocatechol degradation." Frantz B., Chakrabarty A.M. Proc. Natl. Acad. Sci. U.S.A. 84:4460-4464(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning and complete nucleotide sequence determination of the catB gene encoding cis,cis-muconate lactonizing enzyme." Aldrich T.L., Frantz B., Gill J.F., Kilbane J.J., Chakrabarty A.M. Gene 52:185-195(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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]. Strain: AC867.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M16964 Genomic DNA. Translation: AAA98282.1. M31457 Genomic DNA. Translation: AAA98260.1.
PIR	JQ0176.
3D structure databases
ProteinModelPortal	P11452.
SMR	P11452. Positions 1-369.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
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	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...

Entry information

Entry name

CLCB_PSEPU

Accession

Primary (citable) accession number: P11452
Secondary accession number(s): P15741

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	August 1, 1990
Last modified:	April 3, 2013
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program