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Q9S1H0 (SERA_THASE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Selenate reductase subunit alpha

EC=1.97.1.9
Alternative name(s):
Selenate reductase molybdenum subunit
Gene names
Name:serA
OrganismThauera selenatis
Taxonomic identifier33058 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeThauera

Protein attributes

Sequence length918 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Terminal reductase that allows anaerobic growth on selenate as the sole respiratory oxidant.

Catalytic activity

Selenite + H2O + acceptor = selenate + reduced acceptor.

Cofactor

Binds 1 4Fe-4S cluster Potential.

Molybdenum (molybdopterin).

Enzyme regulation

Inhibited by O2.

Subunit structure

Heterotrimer of alpha, beta and gamma subunits.

Subcellular location

Periplasm.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Biotechnological use

Has potential use in bioremediation of waste sites contaminated with selenate, such as agricultural drainage waters.

Sequence similarities

Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
Molybdenum
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

molybdenum ion binding

Inferred from electronic annotation. Source: InterPro

selenate reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636Tat-type signal Ref.2
Chain37 – 918882Selenate reductase subunit alpha
PRO_0000019175

Sites

Metal binding731Iron-sulfur (4Fe-4S); via pros nitrogen By similarity
Metal binding771Iron-sulfur (4Fe-4S) By similarity
Metal binding811Iron-sulfur (4Fe-4S) By similarity
Metal binding1151Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9S1H0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 995D6134B107798F

FASTA918103,407
        10         20         30         40         50         60 
MRKVMNSPDD GNGRRRFLQF SMAALASAAA PSSVWAFSKI QPIEDPLKSY PYRDWEDLYR 

        70         80         90        100        110        120 
KEWTWDSTGF ITHSNGCVAG CAWRVFVKNG VPMREEQVSE YPQLPGVPDM NPRGCQKGAV 

       130        140        150        160        170        180 
YCSWSKQPDF LKYPLKRVGE RGERKWKRIS WDEAFTEIAD KIIDTTVKRG PGNVCMPKRP 

       190        200        210        220        230        240 
FAVITSAGYS RLANLIGAIK PDVSSMTGDL YPGIQTVRMP ARTVSTFDDW FTSDLILMWH 

       250        260        270        280        290        300 
KNPIVTRIPD AHFLTEARYN GARLVNISPD YNPSSVHADL HLPVTTGTDS HLAAAIVNVL 

       310        320        330        340        350        360 
IADKKYKADY LKEQTDLPFL VRTDNGKFLR EKDFNKDGSD EVFYIWDSKS GKAVLAPGSM 

       370        380        390        400        410        420 
GSKDKTLKLG AVEPALEGTF DANGIEVTTV FARLKAEIAP YTPEATHKTT GIHPSVVRQL 

       430        440        450        460        470        480 
AGWIGDCKAL RILDGYNNQK HFDGFQCGRL KILILTLIGH HGTTGSIDTT YEGWVLEGNK 

       490        500        510        520        530        540 
ALGGVKGRPG RSVSMVLAQW VWGEQYRRSK AYFDDTELRE QIGFGVDEME ALRKESEANG 

       550        560        570        580        590        600 
WMPNWQSIKD PVVYINAGIN TFATSTGYQH LRENFLKRCE LYVVVDFRLN SGAMYADIVL 

       610        620        630        640        650        660 
PAATNLEKLD IRETSSTRFI HAFGQPIKPM YDRRTDWQIS VGLARKIQER ARARGITRVD 

       670        680        690        700        710        720 
DPEIKSFIDF DKVYDEFTMN GAVEKDEDAL RFVMEKSKAL GPGSYEEVLK RGFVGVGPSA 

       730        740        750        760        770        780 
GKTGPVPADK PYRPFTVNVS EKVPYKTLTG RLQFYIDHDW YQRFGATVPK PQYGGGVLGP 

       790        800        810        820        830        840 
KKYPFVYNTP HTRWGVHSFA RTDQWMLRHQ RGEPDVRLNP AAMARKGIKD GDQVRIFNSS 

       850        860        870        880        890        900 
GEFFAMAKAW PGLPENMLFS EHGWEQYLYK NMTHYNSVNA ELINPLELVG GYGHVKFAAG 

       910 
GFNPNRIFHE TTVDVEKA 

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References

[1]"Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis."
Krafft T., Bowen A., Theis F., Macy J.M.
DNA Seq. 10:365-377(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Purification and characterization of the selenate reductase from Thauera selenatis."
Schroeder I., Rech S., Krafft T., Macy J.M.
J. Biol. Chem. 272:23765-23768(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 37-51, CHARACTERIZATION.
[3]"Crystallization and preliminary X-ray analysis of the selenate reductase from Thauera selenatis."
Maher M.J., Macy J.M.
Acta Crystallogr. D 58:706-708(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CRYSTALLIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ007744 Genomic DNA. Translation: CAB53372.1.

3D structure databases

ProteinModelPortalQ9S1H0.
ModBaseSearch...

Protein family/group databases

TCDB5.A.3.8.1. prokaryotic molybdopterin-containing oxidoreductase (PMO) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.40.40.20. 1 hit.
InterProIPR009010. Asp_de-COase-like_dom.
IPR017840. DMSO_Rdtase_II_Mopterin_su.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006311. TAT_signal.
[Graphical view]
PfamPF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SUPFAMSSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMsTIGR03479. DMSO_red_II_alp. 1 hit.
PROSITEPS00551. MOLYBDOPTERIN_PROK_1. False negative.
PS00490. MOLYBDOPTERIN_PROK_2. False negative.
PS00932. MOLYBDOPTERIN_PROK_3. False negative.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERA_THASE
AccessionPrimary (citable) accession number: Q9S1H0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families