SERA_THASE
ID SERA_THASE Reviewed; 918 AA.
AC Q9S1H0;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Selenate reductase subunit alpha;
DE EC=1.97.1.9;
DE AltName: Full=Selenate reductase molybdenum subunit;
DE Flags: Precursor;
GN Name=serA;
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 37-51, 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: Terminal reductase that allows anaerobic growth on selenate
CC as the sole respiratory oxidant.
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000305};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000305};
CC -!- ACTIVITY REGULATION: Inhibited by O(2).
CC -!- SUBUNIT: Heterotrimer of alpha, beta and gamma subunits.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- BIOTECHNOLOGY: Has potential use in bioremediation of waste sites
CC contaminated with selenate, such as agricultural drainage waters.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AJ007744; CAB53372.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9S1H0; -.
DR SMR; Q9S1H0; -.
DR TCDB; 5.A.3.8.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR KEGG; ag:CAB53372; -.
DR BRENDA; 1.97.1.9; 6272.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0033797; F:selenate reductase activity; IEA:UniProtKB-EC.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR017840; DMSO_Rdtase_II_Mopterin_su.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR03479; DMSO_red_II_alp; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW Molybdenum; Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..36
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:9295321"
FT CHAIN 37..918
FT /note="Selenate reductase subunit alpha"
FT /id="PRO_0000019175"
FT DOMAIN 66..129
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 77
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
SQ SEQUENCE 918 AA; 103407 MW; 995D6134B107798F CRC64;
MRKVMNSPDD GNGRRRFLQF SMAALASAAA PSSVWAFSKI QPIEDPLKSY PYRDWEDLYR
KEWTWDSTGF ITHSNGCVAG CAWRVFVKNG VPMREEQVSE YPQLPGVPDM NPRGCQKGAV
YCSWSKQPDF LKYPLKRVGE RGERKWKRIS WDEAFTEIAD KIIDTTVKRG PGNVCMPKRP
FAVITSAGYS RLANLIGAIK PDVSSMTGDL YPGIQTVRMP ARTVSTFDDW FTSDLILMWH
KNPIVTRIPD AHFLTEARYN GARLVNISPD YNPSSVHADL HLPVTTGTDS HLAAAIVNVL
IADKKYKADY LKEQTDLPFL VRTDNGKFLR EKDFNKDGSD EVFYIWDSKS GKAVLAPGSM
GSKDKTLKLG AVEPALEGTF DANGIEVTTV FARLKAEIAP YTPEATHKTT GIHPSVVRQL
AGWIGDCKAL RILDGYNNQK HFDGFQCGRL KILILTLIGH HGTTGSIDTT YEGWVLEGNK
ALGGVKGRPG RSVSMVLAQW VWGEQYRRSK AYFDDTELRE QIGFGVDEME ALRKESEANG
WMPNWQSIKD PVVYINAGIN TFATSTGYQH LRENFLKRCE LYVVVDFRLN SGAMYADIVL
PAATNLEKLD IRETSSTRFI HAFGQPIKPM YDRRTDWQIS VGLARKIQER ARARGITRVD
DPEIKSFIDF DKVYDEFTMN GAVEKDEDAL RFVMEKSKAL GPGSYEEVLK RGFVGVGPSA
GKTGPVPADK PYRPFTVNVS EKVPYKTLTG RLQFYIDHDW YQRFGATVPK PQYGGGVLGP
KKYPFVYNTP HTRWGVHSFA RTDQWMLRHQ RGEPDVRLNP AAMARKGIKD GDQVRIFNSS
GEFFAMAKAW PGLPENMLFS EHGWEQYLYK NMTHYNSVNA ELINPLELVG GYGHVKFAAG
GFNPNRIFHE TTVDVEKA
