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Protein

Muconate cycloisomerase 1

Gene

catB

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes a syn cycloisomerization.

Catalytic activityi

+-muconolactone = cis,cis-muconate.1 Publication

Cofactori

Pathwayi: beta-ketoadipate pathway

This protein is involved in step 2 of the subpathway that synthesizes 5-oxo-4,5-dihydro-2-furylacetate from catechol.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Muconate cycloisomerase 1 (catB)
  3. Muconolactone Delta-isomerase (catC), Muconolactone Delta-isomerase (catC), Muconolactone Delta-isomerase (A3L25_20555), Muconolactone Delta-isomerase (catC), Muconolactone Delta-isomerase, Muconolactone Delta-isomerase (AL481_22130), Muconolactone Delta-isomerase (PU99_13590), Muconolactone Delta-isomerase (catC), Muconolactone Delta-isomerase (HB4184_27310), Muconolactone Delta-isomerase (HA62_11725), Muconolactone Delta-isomerase
This subpathway is part of the pathway beta-ketoadipate pathway, which is itself part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-oxo-4,5-dihydro-2-furylacetate from catechol, the pathway beta-ketoadipate pathway and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei171 – 1711Proton acceptor
Metal bindingi200 – 2001Manganese
Metal bindingi226 – 2261Manganese
Metal bindingi251 – 2511Manganese
Active sitei329 – 3291Proton donor

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3423.
BRENDAi5.5.1.1. 5092.
SABIO-RKP08310.
UniPathwayiUPA00157; UER00259.

Names & Taxonomyi

Protein namesi
Recommended name:
Muconate cycloisomerase 1 (EC:5.5.1.11 Publication)
Alternative name(s):
Cis,cis-muconate lactonizing enzyme I
Short name:
MLE
Muconate cycloisomerase I
Gene namesi
Name:catB
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 375374Muconate cycloisomerase 1PRO_0000171251Add
BLAST

Interactioni

Subunit structurei

Homooctamer.

Protein-protein interaction databases

STRINGi160488.PP_3715.

Structurei

Secondary structure

1
375
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1410Combined sources
Beta strandi16 – 194Combined sources
Beta strandi33 – 4311Combined sources
Beta strandi48 – 547Combined sources
Turni57 – 615Combined sources
Helixi66 – 7510Combined sources
Helixi77 – 815Combined sources
Helixi89 – 9911Combined sources
Helixi104 – 12219Combined sources
Helixi126 – 1294Combined sources
Beta strandi136 – 1405Combined sources
Beta strandi142 – 1443Combined sources
Helixi149 – 16113Combined sources
Beta strandi166 – 1716Combined sources
Beta strandi173 – 1753Combined sources
Helixi177 – 19115Combined sources
Helixi192 – 1943Combined sources
Beta strandi195 – 2006Combined sources
Helixi207 – 21913Combined sources
Helixi234 – 24310Combined sources
Beta strandi248 – 2514Combined sources
Helixi257 – 26610Combined sources
Beta strandi270 – 2745Combined sources
Helixi276 – 2794Combined sources
Helixi282 – 29514Combined sources
Beta strandi298 – 3014Combined sources
Helixi308 – 31811Combined sources
Helixi332 – 3354Combined sources
Beta strandi336 – 3383Combined sources
Beta strandi340 – 3434Combined sources
Beta strandi346 – 3483Combined sources
Beta strandi351 – 3533Combined sources
Helixi366 – 3727Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MUCX-ray1.85A/B1-375[»]
2MUCX-ray2.30A/B1-375[»]
3MUCX-ray2.30A/B5-374[»]
ProteinModelPortaliP08310.
SMRiP08310. Positions 5-374.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08310.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105DTQ. Bacteria.
COG4948. LUCA.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
InterProiIPR013370. Chloromuconate_cycloisomerase.
IPR029065. Enolase_C-like.
IPR029017. Enolase_N-like.
IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N_dom.
IPR001354. MR/MLE/MAL.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PfamiPF13378. MR_MLE_C. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]
SMARTiSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR02534. mucon_cyclo. 1 hit.
PROSITEiPS00908. MR_MLE_1. 1 hit.
PS00909. MR_MLE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08310-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSVLIERIE AIIVHDLPTI RPPHKLAMHT MQTQTLVLIR VRCSDGVEGI
60 70 80 90 100
GEATTIGGLA YGYESPEGIK ANIDAHLAPA LVGLPADNIN AAMLKLDKLA
110 120 130 140 150
KGNTFAKSGI ESALLDAQGK RLGLPVSELL GGRVRDSLEV AWTLASGDTA
160 170 180 190 200
RDIAEAQHML EIRRHRVFKL KIGANPLAQD LKHVVAIKRE LGDSASVRVD
210 220 230 240 250
VNQYWDESQA IRACQVLGDN GIDLIEQPIS RINRSGQVRL NQRSPAPIMA
260 270 280 290 300
DESIESVEDA FSLAADGAAS IFALKIAKNG GPRAVLRTAQ IAEAAGIALY
310 320 330 340 350
GGTMLEGSIG TLASAHAFLT LRQLTWGTEL FGPLLLTEEI VNEPPQYRDF
360 370
QLHIPRTPGL GLTLDEQRLA RFARR
Length:375
Mass (Da):40,510
Last modified:January 23, 2007 - v4
Checksum:i4C8668BF6765D061
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331T → S in AAA25766 (PubMed:2449420).Curated
Sequence conflicti65 – 651S → T in AAA25766 (PubMed:2449420).Curated
Sequence conflicti244 – 2441Missing in AAA25765 (PubMed:3609743).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19460 Genomic DNA. Translation: AAA25766.1.
M16236 Genomic DNA. Translation: AAA25765.1.
PIRiA28630.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19460 Genomic DNA. Translation: AAA25766.1.
M16236 Genomic DNA. Translation: AAA25765.1.
PIRiA28630.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MUCX-ray1.85A/B1-375[»]
2MUCX-ray2.30A/B1-375[»]
3MUCX-ray2.30A/B5-374[»]
ProteinModelPortaliP08310.
SMRiP08310. Positions 5-374.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi160488.PP_3715.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105DTQ. Bacteria.
COG4948. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00157; UER00259.
BioCyciMetaCyc:MONOMER-3423.
BRENDAi5.5.1.1. 5092.
SABIO-RKP08310.

Miscellaneous databases

EvolutionaryTraceiP08310.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
InterProiIPR013370. Chloromuconate_cycloisomerase.
IPR029065. Enolase_C-like.
IPR029017. Enolase_N-like.
IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N_dom.
IPR001354. MR/MLE/MAL.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PfamiPF13378. MR_MLE_C. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]
SMARTiSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR02534. mucon_cyclo. 1 hit.
PROSITEiPS00908. MR_MLE_1. 1 hit.
PS00909. MR_MLE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCATB_PSEPU
AccessioniPrimary (citable) accession number: P08310
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 114 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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.