SERB_THASE
ID SERB_THASE Reviewed; 327 AA.
AC Q9S1G9;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Selenate reductase subunit beta;
DE EC=1.97.1.9;
DE AltName: Full=Selenate reductase iron-sulfur subunit;
GN Name=serB;
OS Thauera selenatis.
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=33058;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10826693; DOI=10.3109/10425170009015604;
RA Krafft T., Bowen A., Theis F., Macy J.M.;
RT "Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-
RT containing selenate reductase of Thauera selenatis.";
RL DNA Seq. 10:365-377(2000).
RN [2]
RP PROTEIN SEQUENCE OF 2-31, AND CHARACTERIZATION.
RX PubMed=9295321; DOI=10.1074/jbc.272.38.23765;
RA Schroeder I., Rech S., Krafft T., Macy J.M.;
RT "Purification and characterization of the selenate reductase from Thauera
RT selenatis.";
RL J. Biol. Chem. 272:23765-23768(1997).
RN [3]
RP CRYSTALLIZATION.
RX PubMed=11914503; DOI=10.1107/s0907444902002640;
RA Maher M.J., Macy J.M.;
RT "Crystallization and preliminary X-ray analysis of the selenate reductase
RT from Thauera selenatis.";
RL Acta Crystallogr. D 58:706-708(2002).
CC -!- FUNCTION: Electron transfer subunit of the terminal reductase during
CC anaerobic growth on selenate and nitrate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H2O + selenite = AH2 + selenate; Xref=Rhea:RHEA:14029,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15075, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:18212; EC=1.97.1.9;
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 3 [4Fe-4S] clusters. {ECO:0000250};
CC -!- SUBUNIT: Heterotrimer of alpha, beta and gamma subunits.
CC -!- SUBCELLULAR LOCATION: Periplasm. Note=Probably translocated together
CC with SerA, which possesses a Tat-type signal.
CC -!- BIOTECHNOLOGY: Has potential use in bioremediation of waste sites
CC contaminated with selenate, such as agricultural drainage waters.
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DR EMBL; AJ007744; CAB53373.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9S1G9; -.
DR SMR; Q9S1G9; -.
DR TCDB; 5.A.3.8.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR KEGG; ag:CAB53373; -.
DR BRENDA; 1.97.1.9; 6272.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033797; F:selenate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0009061; P:anaerobic respiration; IEA:InterPro.
DR CDD; cd10555; EBDH_beta; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017839; DMSO_Rdtase_II_Fe-S_su.
DR Pfam; PF13247; Fer4_11; 1.
DR TIGRFAMs; TIGR03478; DMSO_red_II_bet; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 1: Evidence at protein level;
KW 3Fe-4S; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Oxidoreductase; Periplasm; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9295321"
FT CHAIN 2..327
FT /note="Selenate reductase subunit beta"
FT /id="PRO_0000159293"
FT DOMAIN 6..35
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 124..155
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 157..186
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 327 AA; 37122 MW; 2BD215051403E931 CRC64;
MSQRQLAYVF DLNKCIGCHT CTMACKQLWT NRDGREYMYW NNVESRPGKG YPKNWEQKGG
GFDKDGKLKT NGIIPIRADY GGTWNYNLLE TLVEGKSNQV VPDEKPTWGP NWDEDEGKGE
FPNNHYFYLP RICNHCSNPA CLAACPTKAI YKREEDGLVV VDQSRCKGYR YCVKACPYGK
MYFNLQKGTS EKCIGCYPRV EKGEAPACVK QCSGRIRFWG YRDDKDGPIY KLVDQWKVAL
PLHAEYGTEP NVFYVPPMNT TPPPFEEDGR LGDKPRIPIE DLEALFGPGV KQALATLGGE
MAKRRKAQAS ELTDILIGYT NKDRYGI
