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Protein

Mercuric reductase

Gene

merA

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

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 bindingi544 – 5441MercuryPROSITE-ProRule annotation
Metal bindingi545 – 5451MercuryPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi115 – 1239FADBy 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
Encoded oniPlasmid pI2580 Publication
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547Mercuric reductasePRO_0000068002Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi123 ↔ 128Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP0A0E5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 6864HMAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HMA domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

KOiK00520.

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.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HMA_dom.
IPR021179. Mercury_reductase_MerA.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF00403. HMA. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55008. SSF55008. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR02053. MerA. 1 hit.
PROSITEiPS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A0E5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQNSYKIPI QGMTCTGCEE HVTEALEQAG AKDVSADFRR GEAIFELSDD
60 70 80 90 100
QIEKAKQNIS AAGYQPGEEE SQPSENSVDF NRDGDYDLLI IGSGGAAFSA
110 120 130 140 150
AIKANENGAK VAMVERGTVG GTCVNIGCVP SKTMLRAGEI NGLAQNNPFT
160 170 180 190 200
GLQTSTGAAD LAQLTEQKDG LVSQMRQEKY IDLIEEYGFD LIRGEASFID
210 220 230 240 250
DKTIQVNGQN ITSKSFLIAT GASPAVPEIP GMNEVDYLTS TSALELKEVP
260 270 280 290 300
QRLAVIGSGY IAAELGQMFH NLGTEVTLMQ RSERLFKTYD PEISEAIDES
310 320 330 340 350
LTEQGLNLIT GVTYQKVEQN GKSTSIYIEV NGQEQVIEAD QVLVATGRKP
360 370 380 390 400
NTETLNLESA GVKTGKKGEV LTNEYLQTSN NRIYAAGDVT LGPQFVYVAA
410 420 430 440 450
YEGGIVANNA LGLAKRKIDL RFVPGVTFTN PSIATVGLTE QQAKEKGYDV
460 470 480 490 500
KTSVLPLDAV PRALVNHETT GVYKLVVNAQ TQKLIGAHIV SENAGDVIYA
510 520 530 540
ATLAVQFGLT IEDLTDSFAP YLTMAEGLKL AALTFDKDVS KLSCCAG
Length:547
Mass (Da):58,566
Last modified:January 1, 1988 - v1
Checksum:iB0BEA5FCFA99C049
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29436 Genomic DNA. Translation: AAA98245.1.
PIRiE29504.
RefSeqiWP_000193219.1. NZ_LMZC01000074.1.
YP_006937593.1. NC_013319.1.
YP_006938295.1. NC_013337.1.
YP_006938628.1. NC_013347.1.
YP_006938790.1. NC_013352.1.
YP_006958467.1. NC_018968.1.

Genome annotation databases

GeneIDi13874741.
13875462.
13875805.
13875971.
13913500.
KEGGipg:13874741.
pg:13875462.
pg:13875805.
pg:13875971.
pg:13913500.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29436 Genomic DNA. Translation: AAA98245.1.
PIRiE29504.
RefSeqiWP_000193219.1. NZ_LMZC01000074.1.
YP_006937593.1. NC_013319.1.
YP_006938295.1. NC_013337.1.
YP_006938628.1. NC_013347.1.
YP_006938790.1. NC_013352.1.
YP_006958467.1. NC_018968.1.

3D structure databases

ProteinModelPortaliP0A0E5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi13874741.
13875462.
13875805.
13875971.
13913500.
KEGGipg:13874741.
pg:13875462.
pg:13875805.
pg:13875971.
pg:13913500.

Phylogenomic databases

KOiK00520.

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.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HMA_dom.
IPR021179. Mercury_reductase_MerA.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF00403. HMA. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55008. SSF55008. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR02053. MerA. 1 hit.
PROSITEiPS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMERA_STAAU
AccessioniPrimary (citable) accession number: P0A0E5
Secondary accession number(s): P08663
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: May 11, 2016
This is version 60 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.By similarity

Keywords - Technical termi

Plasmid

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.