CLRA_IDEDE
ID CLRA_IDEDE Reviewed; 914 AA.
AC P60068;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Chlorate reductase subunit alpha;
DE EC=1.97.1.1;
DE AltName: Full=Chlorate reductase molybdenum subunit;
DE Flags: Precursor;
GN Name=clrA;
OS Ideonella dechloratans.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Ideonella.
OX NCBI_TaxID=36863;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=12957948; DOI=10.1128/aem.69.9.5585-5592.2003;
RA Danielsson Thorell H., Stenklo K., Karlsson J., Nilsson T.;
RT "A gene cluster for chlorate metabolism in Ideonella dechloratans.";
RL Appl. Environ. Microbiol. 69:5585-5592(2003).
CC -!- FUNCTION: Terminal reductase that allows anaerobic growth on chlorate
CC as the sole respiratory oxidant.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + chlorate = A + chlorite + H2O; Xref=Rhea:RHEA:16349,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17441,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:49709; EC=1.97.1.1;
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 -!- 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 not been experimentally proven.
CC -!- BIOTECHNOLOGY: Has potential use in bioremediation of waste sites
CC contaminated with chlorate, such as pulp and paper industry wastewater.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AJ566363; CAD97447.1; -; Genomic_DNA.
DR AlphaFoldDB; P60068; -.
DR SMR; P60068; -.
DR TCDB; 5.A.3.8.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR PRIDE; P60068; -.
DR BioCyc; MetaCyc:MON-15697; -.
DR BRENDA; 1.97.1.1; 2756.
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:0047143; F:chlorate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR017840; DMSO_Rdtase_II_Mopterin_su.
DR InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-like.
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; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase;
KW Periplasm; Signal.
FT SIGNAL 1..32
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 33..914
FT /note="Chlorate reductase subunit alpha"
FT /id="PRO_0000019173"
FT DOMAIN 62..125
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
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 111
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 205
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
SQ SEQUENCE 914 AA; 102823 MW; 372B1FDE26E06499 CRC64;
MNSPDEHNGR RRFLQFSAAA LASAAASPSL WAFSKIQPIE DPLKDYPYRD WEDLYRKEWT
WDSVGVMTHS NGCVAGCAWN VFVKNGIPMR EEQISKYPQL PGIPDMNPRG CQKGAVYCSW
SKQPDHIKWP LKRVGERGER KWKRISWDEA LTEIADKIID TTVKRGPGNI YIPKRPFAVI
TNTAYTRMTK LLGAISPDAT SMTGDLYTGI QTVRVPASTV STFDDWFTSD LILMWHKNPI
VTRIPDAHFL MEARYNGARL VNISADYNPS SIHSDLFVPV TSGTDSHLAA ALVNVLIAGK
HYKADYLKEQ TALPFLVRTD NGKFLREKDF KADGSDQVFY VWDTKAGKAV LAPGSMGSKD
KTLKLGTIDP ALEGNFETHG IKVTTVFERL KAEITPYTPE ATQATTGVHP SVVRQLAGWI
AECKALRILD GYNNQKHFDG FQCGRLKILI LTLIGHHGTT GSIDTTFEGW RLEGNSELGT
VKGKPGRSVS AVLAQWVWGE QYQRSKDYFN DAQLREELGF GVDEMESMRK ESEANGWMPN
WQSIKEPVVS ITGGINMFAT SNGYQHLRDN FLKRCELNVV VDFRLNSGAM YADIVLPAAE
NTEKLDIRET SVTRFIHAFG QPVKPMYERK TDWQIMVALA AKIQERAKAR GIARVDDPEI
KSGIDFDKIY DEFTMNGKVV TDEQAVRFVM DNSKALGPGT YEEVMKNGFV AVGPSAGKTG
PVPKDKPYRP FTVNVTDKKP YGTLTGRLQF YVDHDWFQRL GATVPKPQYR GGVLGPKKYP
FVRNSPHARW GVHSFARTEQ WMLRHQRGEP DVRMSPKAMA AKGIKDGDMV RIFNDSGEFF
AVVKAMPALP DNMLFTEHGW EQYQYKNMTH YNMVSSELIN PLELVGGYGH IKYTSGGFNP
NRIFYETTVD VEKA
