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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)DescriptionActionsGraphical viewLength
Metal bindingi558MercuryPROSITE-ProRule annotation1
Metal bindingi559MercuryPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi128 – 136FADBy 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 pVS10 Publication
OrganismiPseudomonas aeruginosa
Taxonomic identifieri287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000679972 – 561Mercuric reductaseAdd BLAST560

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi136 ↔ 141Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1561
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi13 – 24Combined sources12
Beta strandi28 – 34Combined sources7
Turni35 – 38Combined sources4
Beta strandi39 – 44Combined sources6
Helixi50 – 58Combined sources9
Turni59 – 61Combined sources3
Beta strandi62 – 65Combined sources4
Beta strandi100 – 104Combined sources5
Helixi108 – 119Combined sources12
Beta strandi123 – 131Combined sources9
Helixi134 – 139Combined sources6
Helixi141 – 158Combined sources18
Turni161 – 165Combined sources5
Helixi175 – 193Combined sources19
Helixi195 – 199Combined sources5
Beta strandi204 – 215Combined sources12
Beta strandi218 – 223Combined sources6
Beta strandi226 – 232Combined sources7
Beta strandi234 – 238Combined sources5
Beta strandi242 – 244Combined sources3
Turni250 – 254Combined sources5
Helixi260 – 265Combined sources6
Beta strandi271 – 276Combined sources6
Helixi280 – 291Combined sources12
Beta strandi295 – 299Combined sources5
Beta strandi301 – 303Combined sources3
Turni304 – 307Combined sources4
Helixi310 – 322Combined sources13
Beta strandi326 – 328Combined sources3
Beta strandi333 – 339Combined sources7
Beta strandi342 – 347Combined sources6
Beta strandi350 – 359Combined sources10
Beta strandi363 – 366Combined sources4
Helixi368 – 370Combined sources3
Helixi372 – 375Combined sources4
Beta strandi398 – 400Combined sources3
Turni403 – 406Combined sources4
Helixi411 – 425Combined sources15
Beta strandi438 – 441Combined sources4
Beta strandi443 – 451Combined sources9
Helixi454 – 459Combined sources6
Beta strandi464 – 470Combined sources7
Helixi471 – 473Combined sources3
Helixi475 – 479Combined sources5
Beta strandi486 – 492Combined sources7
Turni493 – 495Combined sources3
Beta strandi497 – 505Combined sources9
Helixi508 – 520Combined sources13
Helixi525 – 529Combined sources5
Helixi540 – 547Combined sources8
Turni548 – 550Combined sources3
Helixi553 – 555Combined sources3
Turni556 – 558Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00392.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 66HMAPROSITE-ProRule annotationAdd BLAST65

Sequence similaritiesi

Contains 1 HMA domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

KOiK00520.

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. 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_LYLY01000036.1.

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_LYLY01000036.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA77323.

Phylogenomic databases

KOiK00520.

Miscellaneous databases

EvolutionaryTraceiP00392.

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. 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_PSEAI
AccessioniPrimary (citable) accession number: P00392
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 132 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.