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Protein

Mercuric reductase

Gene

merA

Organism
Shewanella putrefaciens (Pseudomonas putrefaciens)
Status
Reviewed-Annotation score: Annotation score: 4 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.

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 bindingi554 – 5541MercuryPROSITE-ProRule annotation
Metal bindingi555 – 5551MercuryPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi124 – 13310FADBy 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 IncJ pMERPH0 Publication
OrganismiShewanella putrefaciens (Pseudomonas putrefaciens)
Taxonomic identifieri24 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 557557Mercuric reductasePRO_0000067999Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi133 ↔ 138Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ54465.
SMRiQ54465. Positions 96-557.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6666HMAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HMA domain.PROSITE-ProRule annotation

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.
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. 3 hits.
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.

Q54465-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILLSIEGMT CPSCVAHVKE ALDAIEGVNK VEISYENARA TITTNGGVSV
60 70 80 90 100
TVLIGAIEAL GYIAKESTGT AKEITSPNDC CDNENASNTE SNQTQHVAII
110 120 130 140 150
GTGSGAFACA IKAAEGGAKV TLIEGADVIG GCCVNVGCVP SKILIRAAQL
160 170 180 190 200
AQQQRNNPFT GLENHAPQLS RALLTQQQTA RVEELRAAKY QNILETNPAL
210 220 230 240 250
SLLKGWAQFK NANTLIVRKN DGTEQAVHAD KILIATGSTP TIPPIDGLTE
260 270 280 290 300
TPYWTSTEAL FAQELPQHLV VIGSSVVALE IAQAYRRLGS EVTILARHTL
310 320 330 340 350
LYREDPLLGE KLTGCFEKEG IRVLNSTQAT KVTHDGSQFT LETNAGDLRC
360 370 380 390 400
DRLLVSTGRH ANTCQLNLGA VGVTTNKKGE IVVNERMETN VPGIYAAGDC
410 420 430 440 450
CNMPQFVYVA AAAGSRSGIN MTGGYAKLDL STMPAVIFTD PQVATVGLTE
460 470 480 490 500
EQANAQDIET DSRVLEMENV PRALANFETD GFIKLVTEKA TGRLIGAQIL
510 520 530 540 550
AHEGGELIQS AALAIRNRMT VTELADQLFP YLTMVEGLKL CAQTFNKDVK

ELSCCAG
Length:557
Mass (Da):59,336
Last modified:November 1, 1996 - v1
Checksum:iEE3D6E1C2ACD473C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49196 Genomic DNA. Translation: CAA89057.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49196 Genomic DNA. Translation: CAA89057.1.

3D structure databases

ProteinModelPortaliQ54465.
SMRiQ54465. Positions 96-557.
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.
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. 3 hits.
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...

Publicationsi

  1. "Distribution, diversity and evolution of the bacterial mercury resistance (mer) operon."
    Osborn A.M., Bruce K.D., Strike P., Ritchie D.A.
    FEMS Microbiol. Rev. 19:239-262(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiMERA_SHEPU
AccessioniPrimary (citable) accession number: Q54465
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 11, 2015
This is version 98 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.

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.