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Protein

Mercuric reductase

Gene

merA

Organism
Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)
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 bindingi558 – 5581MercuryPROSITE-ProRule annotation
Metal bindingi559 – 5591MercuryPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi128 – 1369FADBy 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 pKLH2720 Publication
OrganismiEnterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)
Taxonomic identifieri549 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePantoeaPantoea agglomerans group

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 561561Mercuric reductasePRO_0000067996Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi136 ↔ 141Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP94702.
SMRiP94702. Positions 98-550.
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.

P94702-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTLKITGMT CDSCAAHVKE ALEKVPGVQS ALVSYPKGTA QLAIEAGTSS
60 70 80 90 100
DALTTAVAGL GYEATLADAP PTDNRAGLLD KMRGWIGAAD KPSGNERPLQ
110 120 130 140 150
VVVIGSGGAA MAAALKAVEQ GAQVTLIERG TIGGTCVNVG CVPSKIMIRV
160 170 180 190 200
AHIAHLRRES PFDGGMPPTS PTILRERLLA QQQARVEELR HAKYEGILDG
210 220 230 240 250
NSAITVLHGE ARFKDDQSLI VSLNEGGERV VMFDRCLVAT GASPAVPPIP
260 270 280 290 300
GLKESPYWTS TEALASDTIP ERLAVIGSSV VALELAQAFA RLGSKVTALA
310 320 330 340 350
RNTLFFREDP AIGEAVTAAF RAEGIEVLEH TQASQVAHMD GEFVLTTTHG
360 370 380 390 400
ELRADKLLVA TGRTPNTRSL ALEAAGVAVN AQGAIVIDKG MRTSSPNIYA
410 420 430 440 450
AGDCTDQPQF VYVAAAAGTR AAINMTGGDA ALDLTAMPAV VFTDPQVATV
460 470 480 490 500
GYSEAEAHHD GIETDSRLLT LDNVPRALAN FDTRGFIKLV IEEGSGRLIG
510 520 530 540 550
VQAVAPEAGE LIQTAVLAIR NRMTVQELAD QLFPYLTMVE GLKLAAQTFS
560
KDVKQLSCCA G
Length:561
Mass (Da):58,785
Last modified:May 1, 1997 - v1
Checksum:iFABA07D7EC2F13C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08992 Genomic DNA. Translation: CAA70184.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08992 Genomic DNA. Translation: CAA70184.1.

3D structure databases

ProteinModelPortaliP94702.
SMRiP94702. Positions 98-550.
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...

Entry informationi

Entry nameiMERA_ENTAG
AccessioniPrimary (citable) accession number: P94702
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: May 11, 2016
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.

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.