SERC_THASE
ID SERC_THASE Reviewed; 239 AA.
AC Q9S1G7;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Selenate reductase subunit gamma;
DE EC=1.97.1.9;
DE AltName: Full=Selenate reductase heme subunit;
DE Flags: Precursor;
GN Name=serC;
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 29-48, 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).
CC -!- FUNCTION: May transfer electrons to the iron-sulfur centers of SerB.
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=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000305};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000305};
CC -!- SUBUNIT: Heterotrimer of alpha, beta and gamma subunits.
CC -!- SUBCELLULAR LOCATION: Periplasm.
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; CAB53375.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9S1G7; -.
DR SMR; Q9S1G7; -.
DR TCDB; 5.A.3.8.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR KEGG; ag:CAB53375; -.
DR BRENDA; 1.97.1.9; 6272.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033797; F:selenate reductase activity; IEA:UniProtKB-EC.
DR CDD; cd09623; DOMON_EBDH; 1.
DR InterPro; IPR019020; Cyt-c552/DMSO_Rdtase_haem-bd.
DR InterPro; IPR017838; DMSO_Rdtase_II_haem_b-bd_su.
DR Pfam; PF09459; EB_dh; 1.
DR TIGRFAMs; TIGR03477; DMSO_red_II_gam; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Oxidoreductase; Periplasm; Signal; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:9295321"
FT CHAIN 29..239
FT /note="Selenate reductase subunit gamma"
FT /id="PRO_0000022320"
FT BINDING 74
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 138
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
SQ SEQUENCE 239 AA; 25564 MW; CCDCBDDDEC346D47 CRC64;
MRTSSMMKRM AAMSLAAAAA WATGAAAAAD GAPAAQRTIQ VLSVKGGDAA SPQAAVWKKA
PTGQVALQTA FPGHASIVGT ALTQQMTAQA VRAGDRLFVR LAWRDATANT EIKDTDQFVD
GAAVQFPVNG KDTTLAFMGD PDNPVNVWHW RADGRTRNLV AKGFGTATPV PAEGLRSTAT
RTRDGWEVVI SRPLRVKAEE GADLQGRRTM PIAFAAWDGE NQERDGLKAV TMEWWQLNF
