Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mercuric reductase

Gene

merA

Organism
Streptomyces lividans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Resistance to Hg2+ in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg0.

Catalytic activityi

Hg + NADP+ + H+ = Hg2+ + NADPH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi471 – 4711MercurySequence analysis
Metal bindingi472 – 4721MercurySequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi37 – 459FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Mercuric resistance

Keywords - Ligandi

FAD, Flavoprotein, Mercury, Metal-binding, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Mercuric reductase (EC:1.16.1.1)
Alternative name(s):
Hg(II) reductase
Gene namesi
Name:merA
OrganismiStreptomyces lividans
Taxonomic identifieri1916 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 474474Mercuric reductasePRO_0000068004Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi45 ↔ 50Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

By mercuric ions. Negatively regulated by MerR.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP30341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR021179. Mercury_reductase_MerA.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 3 hits.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR02053. MerA. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30341-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQAHTGYDL AIIGSGAGAF AAAIAARNKG RSVVMVERGT TGGTCVNVGC
60 70 80 90 100
VPSKALLAAA EARHGAQAAS RFPGIQATEP ALDFPALISG KDTLVGQLRA
110 120 130 140 150
EKYTDLAAEY GWQIVHGTAT FADGPMLEVA LNDGGTATVE AAHYLIATGS
160 170 180 190 200
APTAPHIDGL DQVDYLTSTT AMELQQLPEH LLILGGGYVG LEQAQLFARL
210 220 230 240 250
GSRVTLAVRS RLASREEPEI SAGIENIFRE EGITVHTRTQ LRAVRRDGEG
260 270 280 290 300
ILATLTGPDG DQQVRASHLL IATGRRSVTN GLGLERVGVK TGERGEVVVD
310 320 330 340 350
EYLRTDNPRI WAAGDVTCHP DFVYVAAAHG TLVADNALDG AERTLDYTAL
360 370 380 390 400
PKVTFTSPAI ASVGLTEAQL TEAGIAHQTR TLSLENVPRA LVNRDTRGLV
410 420 430 440 450
KLIAERGTGK LLAAHVLAEG AGDVITAATY AITAGLTVDQ LARTWHPYLT
460 470
MAEALKLAAQ TFTSDVAKLS CCAG
Length:474
Mass (Da):49,671
Last modified:April 1, 1993 - v1
Checksum:i3C85E89D0062215E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65467 Genomic DNA. Translation: CAA46460.1.
PIRiS30168.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65467 Genomic DNA. Translation: CAA46460.1.
PIRiS30168.

3D structure databases

ProteinModelPortaliP30341.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR021179. Mercury_reductase_MerA.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 3 hits.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR02053. MerA. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and DNA sequence analysis of the mercury resistance genes of Streptomyces lividans."
    Sedlmeier R., Altenbuchner J.
    Mol. Gen. Genet. 236:76-85(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 66 / 1326.
  2. "Regulation of the operon responsible for broad-spectrum mercury resistance in Streptomyces lividans 1326."
    Brunker P., Rother D., Sedlmeier R., Klein J., Mattes R., Altenbuchner J.
    Mol. Gen. Genet. 251:307-315(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION.
    Strain: 66 / 1326.

Entry informationi

Entry nameiMERA_STRLI
AccessioniPrimary (citable) accession number: P30341
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 11, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Documents

  1. 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.