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Protein

Mercuric reductase

Gene

merA

Organism
Pseudomonas aeruginosa
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 Hg0.1 Publication

Catalytic activityi

Hg + NADP+ + H+ = Hg2+ + NADPH.1 Publication

Cofactori

FADNote: Binds 1 FAD per subunit.

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 pVS10 Publication
OrganismiPseudomonas aeruginosa
Taxonomic identifieri287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 561560Mercuric reductasePRO_0000067997Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi136 ↔ 141Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
561
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi13 – 2412Combined sources
Beta strandi28 – 347Combined sources
Turni35 – 384Combined sources
Beta strandi39 – 446Combined sources
Helixi50 – 589Combined sources
Turni59 – 613Combined sources
Beta strandi62 – 654Combined sources
Beta strandi100 – 1045Combined sources
Helixi108 – 11912Combined sources
Beta strandi123 – 1319Combined sources
Helixi134 – 1396Combined sources
Helixi141 – 15818Combined sources
Turni161 – 1655Combined sources
Helixi175 – 19319Combined sources
Helixi195 – 1995Combined sources
Beta strandi204 – 21512Combined sources
Beta strandi218 – 2236Combined sources
Beta strandi226 – 2327Combined sources
Beta strandi234 – 2385Combined sources
Beta strandi242 – 2443Combined sources
Turni250 – 2545Combined sources
Helixi260 – 2656Combined sources
Beta strandi271 – 2766Combined sources
Helixi280 – 29112Combined sources
Beta strandi295 – 2995Combined sources
Beta strandi301 – 3033Combined sources
Turni304 – 3074Combined sources
Helixi310 – 32213Combined sources
Beta strandi326 – 3283Combined sources
Beta strandi333 – 3397Combined sources
Beta strandi342 – 3476Combined sources
Beta strandi350 – 35910Combined sources
Beta strandi363 – 3664Combined sources
Helixi368 – 3703Combined sources
Helixi372 – 3754Combined sources
Beta strandi398 – 4003Combined sources
Turni403 – 4064Combined sources
Helixi411 – 42515Combined sources
Beta strandi438 – 4414Combined sources
Beta strandi443 – 4519Combined sources
Helixi454 – 4596Combined sources
Beta strandi464 – 4707Combined sources
Helixi471 – 4733Combined sources
Helixi475 – 4795Combined sources
Beta strandi486 – 4927Combined sources
Turni493 – 4953Combined sources
Beta strandi497 – 5059Combined sources
Helixi508 – 52013Combined sources
Helixi525 – 5295Combined sources
Helixi540 – 5478Combined sources
Turni548 – 5503Combined sources
Helixi553 – 5553Combined sources
Turni556 – 5583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZK7X-ray1.60A96-561[»]
1ZX9X-ray1.90A96-561[»]
2KT2NMR-A1-69[»]
2KT3NMR-A1-69[»]
4K7ZX-ray1.50A96-561[»]
4K8DX-ray1.86A96-561[»]
ProteinModelPortaliP00392.
SMRiP00392. Positions 96-561.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00392.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 6665HMAPROSITE-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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00392-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHLKITGMT CDSCAAHVKE ALEKVPGVQS ALVSYPKGTA QLAIVPGTSP
60 70 80 90 100
DALTAAVAGL GYKATLADAP LADNRVGLLD KVRGWMAAAE KHSGNEPPVQ
110 120 130 140 150
VAVIGSGGAA MAAALKAVEQ GAQVTLIERG TIGGTCVNVG CVPSKIMIRA
160 170 180 190 200
AHIAHLRRES PFDGGIAATV PTIDRSKLLA QQQARVDELR HAKYEGILGG
210 220 230 240 250
NPAITVVHGE ARFKDDQSLT VRLNEGGERV VMFDRCLVAT GASPAVPPIP
260 270 280 290 300
GLKESPYWTS TEALASDTIP ERLAVIGSSV VALELAQAFA RLGSKVTVLA
310 320 330 340 350
RNTLFFREDP AIGEAVTAAF RAEGIEVLEH TQASQVAHMD GEFVLTTTHG
360 370 380 390 400
ELRADKLLVA TGRTPNTRSL ALDAAGVTVN AQGAIVIDQG MRTSNPNIYA
410 420 430 440 450
AGDCTDQPQF VYVAAAAGTR AAINMTGGDA ALDLTAMPAV VFTDPQVATV
460 470 480 490 500
GYSEAEAHHD GIETDSRTLT LDNVPRALAN FDTRGFIKLV IEEGSHRLIG
510 520 530 540 550
VQAVAPEAGE LIQTAALAIR NRMTVQELAD QLFPYLTMVE GLKLAAQTFN
560
KDVKQLSCCA G
Length:561
Mass (Da):58,728
Last modified:July 21, 1986 - v1
Checksum:i858669A67A490065
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z00027 Genomic DNA. Translation: CAA77323.1.
PIRiA00406. RDPSHA.
RefSeqiWP_003156770.1. NZ_LOHK01000073.1.

Genome annotation databases

KEGGiag:CAA77323.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z00027 Genomic DNA. Translation: CAA77323.1.
PIRiA00406. RDPSHA.
RefSeqiWP_003156770.1. NZ_LOHK01000073.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZK7X-ray1.60A96-561[»]
1ZX9X-ray1.90A96-561[»]
2KT2NMR-A1-69[»]
2KT3NMR-A1-69[»]
4K7ZX-ray1.50A96-561[»]
4K8DX-ray1.86A96-561[»]
ProteinModelPortaliP00392.
SMRiP00392. Positions 96-561.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA77323.

Phylogenomic databases

KOiK00520.

Miscellaneous databases

EvolutionaryTraceiP00392.

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...

Publicationsi

  1. "Nucleotide sequence of a gene from the Pseudomonas transposon Tn501 encoding mercuric reductase."
    Brown N.L., Ford S.J., Pridmore R.D., Fritzinger D.C.
    Biochemistry 22:4089-4095(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Transposon: Tn501.
  2. "Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide."
    Fox B.S., Walsh C.T.
    Biochemistry 22:4082-4088(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12 AND 130-143, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DISULFIDE BOND.

Entry informationi

Entry nameiMERA_PSEAI
AccessioniPrimary (citable) accession number: P00392
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 6, 2016
This is version 129 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

3D-structure, Direct protein sequencing, Plasmid, Transposable element

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.