ID OORB_MOOTA Reviewed; 314 AA.
AC Q2RI42;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Oxalate oxidoreductase subunit beta {ECO:0000303|PubMed:20956531};
DE Short=OOR subunit beta {ECO:0000303|PubMed:20956531};
DE EC=1.2.7.10 {ECO:0000269|PubMed:20956531};
GN OrderedLocusNames=Moth_1591 {ECO:0000312|EMBL:ABC19897.1};
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=20956531; DOI=10.1074/jbc.m110.155739;
RA Pierce E., Becker D.F., Ragsdale S.W.;
RT "Identification and characterization of oxalate oxidoreductase, a novel
RT thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables
RT anaerobic growth on oxalate.";
RL J. Biol. Chem. 285:40515-40524(2010).
CC -!- FUNCTION: Catalyzes the anaerobic oxidation of oxalate using a broad
CC range of electron acceptors, including ferredoxin and the nickel-
CC dependent carbon monoxide dehydrogenase. Does not require coenzyme A as
CC cosubstrate. Enables anaerobic growth on oxalate which is used as
CC energy source by the bacteria. {ECO:0000269|PubMed:20956531}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=oxalate + oxidized 2[4Fe-4S]-[ferredoxin] = 2 CO2 + reduced
CC 2[4Fe-4S]-[ferredoxin]; Xref=Rhea:RHEA:30179, Rhea:RHEA-COMP:10002,
CC Rhea:RHEA-COMP:10004, ChEBI:CHEBI:16526, ChEBI:CHEBI:30623,
CC ChEBI:CHEBI:33722, ChEBI:CHEBI:33723; EC=1.2.7.10;
CC Evidence={ECO:0000269|PubMed:20956531};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P94692};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P94692};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=58 uM for oxalate {ECO:0000269|PubMed:20956531};
CC Note=Kinetic parameters determined with the heterodimer oxalate
CC oxidoreductase complex. {ECO:0000269|PubMed:20956531};
CC pH dependence:
CC Optimum pH is 8.7. {ECO:0000269|PubMed:20956531};
CC -!- SUBUNIT: Dimer of heterotrimer of one alpha, one beta and one delta
CC subunit. {ECO:0000269|PubMed:20956531}.
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DR EMBL; CP000232; ABC19897.1; -; Genomic_DNA.
DR RefSeq; YP_430440.1; NC_007644.1.
DR PDB; 5C4I; X-ray; 2.27 A; C/F=1-314.
DR PDB; 5EXD; X-ray; 2.50 A; C/F/I/L=1-314.
DR PDB; 5EXE; X-ray; 1.88 A; C/F=1-314.
DR PDBsum; 5C4I; -.
DR PDBsum; 5EXD; -.
DR PDBsum; 5EXE; -.
DR AlphaFoldDB; Q2RI42; -.
DR SMR; Q2RI42; -.
DR STRING; 264732.Moth_1591; -.
DR EnsemblBacteria; ABC19897; ABC19897; Moth_1591.
DR KEGG; mta:Moth_1591; -.
DR PATRIC; fig|264732.11.peg.1721; -.
DR eggNOG; COG1013; Bacteria.
DR HOGENOM; CLU_058423_0_0_9; -.
DR OrthoDB; 9794954at2; -.
DR BioCyc; MetaCyc:MONOMER-16174; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; TAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IDA:UniProtKB.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0033611; P:oxalate catabolic process; IDA:UniProtKB.
DR CDD; cd03376; TPP_PFOR_porB_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR42897; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR PANTHER; PTHR42897:SF2; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase.
FT CHAIN 1..314
FT /note="Oxalate oxidoreductase subunit beta"
FT /id="PRO_0000430798"
FT BINDING 24
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 27
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 225
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT HELIX 28..40
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 42..51
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:5EXE"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 77..93
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:5EXE"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:5C4I"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 200..212
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 286..302
FT /evidence="ECO:0007829|PDB:5EXE"
SQ SEQUENCE 314 AA; 34234 MW; BF600D9A20E895F7 CRC64;
MLDRIASIKK APDEEYYVPG HRTCAGCGPA LTYRLVAKAA GPNTIFIGPT GCMYVANTSY
GCGPWRVPWI HAQITNGGAV ASGIEAAYKA MIRKKKTDAE FPNIIVMAGD GGAVDIGLQA
LSAMLYRGHD VLFICYDNES YANTGIQTSP TTPYGANTTF TPPGEVVPEG KKLFPKDNPK
VIAHGHPELK YVATASIGWP VDLMNKVRKG LNQEGPAYIH IHAPCPKGWQ FPADKTIEMA
KLAVQTGMFQ LYEYENGEYK LSVKVDKRKP VSEYMKLQKR FAHLKPEHIA KMQAFVDARC
AEVGITVPVV ASNA
//
