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Protein

Mercuric reductase

Gene

merA

Organism
Shigella flexneri
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)DescriptionActionsGraphical viewLength
Metal bindingi561MercuryPROSITE-ProRule annotation1
Metal bindingi562MercuryPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi127 – 135FADBy similarity9

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 IncFII R100 (NR1)0 Publication
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000680011 – 564Mercuric reductaseAdd BLAST564

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi135 ↔ 140Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP08332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 66HMAPROSITE-ProRule annotationAdd BLAST66

Sequence similaritiesi

Contains 1 HMA domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Family and domain databases

CDDicd00371. HMA. 1 hit.
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.

P08332-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTLKITGMT CDSCAVHVKD ALEKVPGVQS ADVSYAKGSA KLAIEVGTSP
60 70 80 90 100
DALTAAVAGL GYRATLADAP SVSTPGGLLD KMRDLLGRND KTGSSGALHI
110 120 130 140 150
AVIGSGGAAM AAALKAVEQG ARVTLIERGT IGGTCVNVGC VPSKIMIRAA
160 170 180 190 200
HIAHLRRESP FDGGIAATTP TIQRTALLAQ QQARVDELRH AKYEGILEGN
210 220 230 240 250
PAITVLHGSA RFKDNRNLIV QLNDGGERVV AFDRCLIATG ASPAVPPIPG
260 270 280 290 300
LKDTPYWTST EALVSETIPK RLAVIGSSVV ALELAQAFAR LGAKVTILAR
310 320 330 340 350
STLFFREDPA IGEAVTAAFR MEGIEVREHT QASQVAYING VRDGEFVLTT
360 370 380 390 400
AHGELRADKL LVATGRAPNT RKLALDATGV TLTPQGAIVI DPGMRTSVEH
410 420 430 440 450
IYAAGDCTDQ PQFVYVAAAA GTRAAINMTG GDAALNLTAM PAVVFTDPQV
460 470 480 490 500
ATVGYSEAEA HHDGIKTDSR TLTLDNVPRA LANFDTRGFI KLVVEEGSGR
510 520 530 540 550
LIGVQAVAPE AGELIQTAAL AIRNRMTVQE LADQLFPYLT MVEGLKLAAQ
560
TFNKDVKQLS CCAG
Length:564
Mass (Da):58,975
Last modified:August 1, 1988 - v1
Checksum:i582E74333BDA88EF
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti70P → A in plasmid NR1. 1
Natural varianti341 – 342VR → EG in plasmid NR1. 2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01730 Genomic DNA. Translation: AAA92263.1.
K03089 Genomic DNA. Translation: AAB59078.1.
PIRiA22799. RDEBHA.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01730 Genomic DNA. Translation: AAA92263.1.
K03089 Genomic DNA. Translation: AAB59078.1.
PIRiA22799. RDEBHA.

3D structure databases

ProteinModelPortaliP08332.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd00371. HMA. 1 hit.
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...

Entry informationi

Entry nameiMERA_SHIFL
AccessioniPrimary (citable) accession number: P08332
Secondary accession number(s): P07045
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: August 1, 1988
Last modified: November 30, 2016
This is version 116 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, Transposable element

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.