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Protein

Alkylmercury lyase

Gene

merB

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves the carbon-mercury bond of organomercurials such as phenylmercuric acetate. One product is Hg2+, which is subsequently detoxified by the mercuric reductase (By similarity).By similarity

Catalytic activityi

An alkylmercury + H+ = an alkane + Hg2+.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Mercuric resistance

Keywords - Ligandi

Mercury

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3304.
BRENDAi4.99.1.2. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkylmercury lyase (EC:4.99.1.2)
Alternative name(s):
Organomercurial lyase
Gene namesi
Name:merB
Encoded oniPlasmid IncM R831b0 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Alkylmercury lyasePRO_0000220356Add
BLAST

Proteomic databases

PRIDEiP77072.

Structurei

Secondary structure

1
212
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1411Combined sources
Helixi20 – 3112Combined sources
Turni32 – 343Combined sources
Helixi39 – 468Combined sources
Helixi50 – 5910Combined sources
Turni67 – 693Combined sources
Beta strandi71 – 799Combined sources
Beta strandi82 – 876Combined sources
Beta strandi90 – 967Combined sources
Helixi97 – 10711Combined sources
Beta strandi111 – 1166Combined sources
Turni118 – 1203Combined sources
Beta strandi123 – 1286Combined sources
Beta strandi133 – 1386Combined sources
Beta strandi142 – 1454Combined sources
Beta strandi150 – 1523Combined sources
Helixi154 – 1574Combined sources
Helixi159 – 1613Combined sources
Beta strandi164 – 1663Combined sources
Helixi168 – 1758Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi185 – 1884Combined sources
Helixi189 – 20416Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S6LNMR-A1-212[»]
3F0OX-ray1.76A/B1-212[»]
3F0PX-ray1.64A/B1-212[»]
3F2FX-ray1.98A/B1-212[»]
3F2GX-ray1.78A/B1-212[»]
3F2HX-ray2.00A/B1-212[»]
3FN8X-ray1.88A/B1-212[»]
5C0TX-ray1.96A/B1-212[»]
5C0UX-ray1.87A/B1-212[»]
5DSFX-ray1.95A/B1-212[»]
DisProtiDP00575.
ProteinModelPortaliP77072.
SMRiP77072. Positions 21-212.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77072.

Family & Domainsi

Sequence similaritiesi

Belongs to the MerB family.Curated

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_00714. MerB.
InterProiIPR004927. MerB.
IPR024259. MerB_HTH_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF12324. HTH_15. 1 hit.
PF03243. MerB. 1 hit.
[Graphical view]
PIRSFiPIRSF001458. MerB. 1 hit.
PRINTSiPR01699. ORGNOHGLYASE.
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequencei

Sequence statusi: Complete.

P77072-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLAPYILEL LTSVNRTNGT ADLLVPLLRE LAKGRPVSRT TLAGILDWPA
60 70 80 90 100
ERVAAVLEQA TSTEYDKDGN IIGYGLTLRE TSYVFEIDDR RLYAWCALDT
110 120 130 140 150
LIFPALIGRT ARVSSHCAAT GAPVSLTVSP SEIQAVEPAG MAVSLVLPQE
160 170 180 190 200
AADVRQSFCC HVHFFASVPT AEDWASKHQG LEGLAIVSVH EAFGLGQEFN
210
RHLLQTMSSR TP
Length:212
Mass (Da):23,035
Last modified:February 1, 1997 - v1
Checksum:i7FE9DFA8A95F490A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77087 Genomic DNA. Translation: AAB49639.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77087 Genomic DNA. Translation: AAB49639.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S6LNMR-A1-212[»]
3F0OX-ray1.76A/B1-212[»]
3F0PX-ray1.64A/B1-212[»]
3F2FX-ray1.98A/B1-212[»]
3F2GX-ray1.78A/B1-212[»]
3F2HX-ray2.00A/B1-212[»]
3FN8X-ray1.88A/B1-212[»]
5C0TX-ray1.96A/B1-212[»]
5C0UX-ray1.87A/B1-212[»]
5DSFX-ray1.95A/B1-212[»]
DisProtiDP00575.
ProteinModelPortaliP77072.
SMRiP77072. Positions 21-212.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP77072.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3304.
BRENDAi4.99.1.2. 2026.

Miscellaneous databases

EvolutionaryTraceiP77072.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_00714. MerB.
InterProiIPR004927. MerB.
IPR024259. MerB_HTH_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF12324. HTH_15. 1 hit.
PF03243. MerB. 1 hit.
[Graphical view]
PIRSFiPIRSF001458. MerB. 1 hit.
PRINTSiPR01699. ORGNOHGLYASE.
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of the organomercury resistance (OMR) locus."
    Tolle C., Totis P., Summers A.O.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiMERB_ECOLX
AccessioniPrimary (citable) accession number: P77072
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: February 1, 1997
Last modified: May 11, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.