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Protein

Selenate reductase subunit beta

Gene

serB

Organism
Thauera selenatis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Electron transfer subunit of the terminal reductase during anaerobic growth on selenate and nitrate.By similarity

Catalytic activityi

Selenite + H2O + acceptor = selenate + reduced acceptor.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi15 – 151Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi18 – 181Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi21 – 211Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi25 – 251Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi133 – 1331Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi136 – 1361Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi141 – 1411Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi145 – 1451Iron-sulfur 4 (3Fe-4S)By similarity
Metal bindingi166 – 1661Iron-sulfur 4 (3Fe-4S)By similarity
Metal bindingi172 – 1721Iron-sulfur 4 (3Fe-4S)By similarity
Metal bindingi176 – 1761Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi193 – 1931Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi196 – 1961Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi208 – 2081Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi212 – 2121Iron-sulfur 1 (4Fe-4S)By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BRENDAi1.97.1.9. 6272.

Protein family/group databases

TCDBi5.A.3.8.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Selenate reductase subunit beta (EC:1.97.1.9)
Alternative name(s):
Selenate reductase iron-sulfur subunit
Gene namesi
Name:serB
OrganismiThauera selenatis
Taxonomic identifieri33058 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeThauera

Subcellular locationi

  • Periplasm

  • Note: Probably translocated together with SerA, which possesses a Tat-type signal.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Biotechnological usei

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 327326Selenate reductase subunit betaPRO_0000159293Add
BLAST

Interactioni

Subunit structurei

Heterotrimer of alpha, beta and gamma subunits.

Structurei

3D structure databases

ProteinModelPortaliQ9S1G9.
SMRiQ9S1G9. Positions 3-326.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 35304Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini124 – 155324Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini157 – 186304Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 4Fe-4S ferredoxin-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017839. DMSO_Rdtase_II_Fe-S_su.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03478. DMSO_red_II_bet. 1 hit.
PROSITEiPS51379. 4FE4S_FER_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9S1G9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQRQLAYVF DLNKCIGCHT CTMACKQLWT NRDGREYMYW NNVESRPGKG
60 70 80 90 100
YPKNWEQKGG GFDKDGKLKT NGIIPIRADY GGTWNYNLLE TLVEGKSNQV
110 120 130 140 150
VPDEKPTWGP NWDEDEGKGE FPNNHYFYLP RICNHCSNPA CLAACPTKAI
160 170 180 190 200
YKREEDGLVV VDQSRCKGYR YCVKACPYGK MYFNLQKGTS EKCIGCYPRV
210 220 230 240 250
EKGEAPACVK QCSGRIRFWG YRDDKDGPIY KLVDQWKVAL PLHAEYGTEP
260 270 280 290 300
NVFYVPPMNT TPPPFEEDGR LGDKPRIPIE DLEALFGPGV KQALATLGGE
310 320
MAKRRKAQAS ELTDILIGYT NKDRYGI
Length:327
Mass (Da):37,122
Last modified:January 23, 2007 - v4
Checksum:i2BD215051403E931
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007744 Genomic DNA. Translation: CAB53373.1.

Genome annotation databases

KEGGiag:CAB53373.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007744 Genomic DNA. Translation: CAB53373.1.

3D structure databases

ProteinModelPortaliQ9S1G9.
SMRiQ9S1G9. Positions 3-326.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi5.A.3.8.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAB53373.

Enzyme and pathway databases

BRENDAi1.97.1.9. 6272.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017839. DMSO_Rdtase_II_Fe-S_su.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03478. DMSO_red_II_bet. 1 hit.
PROSITEiPS51379. 4FE4S_FER_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSERB_THASE
AccessioniPrimary (citable) accession number: Q9S1G9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 76 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.