OORD_MOOTA
ID OORD_MOOTA Reviewed; 315 AA.
AC Q2RI40;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Oxalate oxidoreductase subunit delta {ECO:0000303|PubMed:20956531};
DE Short=OOR delta subunit {ECO:0000303|PubMed:20956531};
DE EC=1.2.7.10 {ECO:0000269|PubMed:20956531};
GN OrderedLocusNames=Moth_1593 {ECO:0000312|EMBL:ABC19899.1};
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; 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:0000269|PubMed:20956531};
CC Note=Binds 2 [4Fe-4S] clusters per subunit.
CC {ECO:0000269|PubMed:20956531};
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; ABC19899.1; -; Genomic_DNA.
DR RefSeq; YP_430442.1; NC_007644.1.
DR PDB; 5C4I; X-ray; 2.27 A; B/E=1-315.
DR PDB; 5EXD; X-ray; 2.50 A; B/E/H/K=1-315.
DR PDB; 5EXE; X-ray; 1.88 A; B/E=1-315.
DR PDBsum; 5C4I; -.
DR PDBsum; 5EXD; -.
DR PDBsum; 5EXE; -.
DR AlphaFoldDB; Q2RI40; -.
DR SMR; Q2RI40; -.
DR STRING; 264732.Moth_1593; -.
DR PRIDE; Q2RI40; -.
DR EnsemblBacteria; ABC19899; ABC19899; Moth_1593.
DR KEGG; mta:Moth_1593; -.
DR PATRIC; fig|264732.11.peg.1723; -.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG1144; Bacteria.
DR HOGENOM; CLU_060916_0_0_9; -.
DR BioCyc; MetaCyc:MON-16173; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA: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:0033611; P:oxalate catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.920.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR011898; PorD_KorD.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR PANTHER; PTHR43724; PTHR43724; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF01558; POR; 1.
DR SUPFAM; SSF53323; SSF53323; 1.
DR TIGRFAMs; TIGR02179; PorD_KorD; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Repeat.
FT CHAIN 1..315
FT /note="Oxalate oxidoreductase subunit delta"
FT /id="PRO_0000430799"
FT DOMAIN 252..280
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 281..310
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 261
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 264
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 267
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 271
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 290
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 293
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 296
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 300
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT TURN 4..7
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:5EXE"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 25..40
FT /evidence="ECO:0007829|PDB:5EXE"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:5C4I"
FT STRAND 61..72
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:5EXE"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:5C4I"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:5EXE"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:5EXE"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 295..299
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:5EXE"
SQ SEQUENCE 315 AA; 33931 MW; 488A111A1E1E808C CRC64;
MSTKDLFAEP NLKQITVWAR GVVMNKDARD IVVALTEAAA KEGKYVQAWE NYVDLPDRIY
VPVRAYARIS SDPIESKYIY ENETPDIVVL VEESLIKGVP ILKGIRPGST LVVNTKRSID
TILEFLGDTG NLAQIVTVDA NSMAEAVMTL SGAEGATDAT GIGAGIAAPI AGAVVKATGI
VDVENLAAVV KNPAAMRRGY AEAQVRQLPP HEAVEEAAVS ATELLRQMPF AGTVPSPVTE
NEGMVTGNWR IQRPIIDREA CTECYTCWIY CPDSCITRTE EGPVFNMKYC KGCGLCTAVC
PSGALTNVPE LDFKD
