OORA_MOOTA
ID OORA_MOOTA Reviewed; 395 AA.
AC Q2RI41;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Oxalate oxidoreductase subunit alpha {ECO:0000303|PubMed:20956531};
DE Short=OOR subunit alpha {ECO:0000303|PubMed:20956531};
DE EC=1.2.7.10 {ECO:0000269|PubMed:20956531};
GN OrderedLocusNames=Moth_1592 {ECO:0000312|EMBL:ABC19898.1};
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 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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000232; ABC19898.1; -; Genomic_DNA.
DR RefSeq; WP_011393098.1; NC_007644.1.
DR RefSeq; YP_430441.1; NC_007644.1.
DR PDB; 5C4I; X-ray; 2.27 A; A/D=1-395.
DR PDB; 5EXD; X-ray; 2.50 A; A/D/G/J=1-395.
DR PDB; 5EXE; X-ray; 1.88 A; A/D=1-395.
DR PDBsum; 5C4I; -.
DR PDBsum; 5EXD; -.
DR PDBsum; 5EXE; -.
DR AlphaFoldDB; Q2RI41; -.
DR SMR; Q2RI41; -.
DR STRING; 264732.Moth_1592; -.
DR EnsemblBacteria; ABC19898; ABC19898; Moth_1592.
DR KEGG; mta:Moth_1592; -.
DR PATRIC; fig|264732.11.peg.1722; -.
DR eggNOG; COG0674; Bacteria.
DR HOGENOM; CLU_002569_5_0_9; -.
DR OMA; IQGWAST; -.
DR BioCyc; MetaCyc:MON-16172; -.
DR BRENDA; 1.2.7.10; 1528.
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 CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase.
FT CHAIN 1..395
FT /note="Oxalate oxidoreductase subunit alpha"
FT /id="PRO_0000430797"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:5EXE"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:5EXD"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:5EXE"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 140..155
FT /evidence="ECO:0007829|PDB:5EXE"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:5EXE"
FT TURN 169..174
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 217..229
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 231..246
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 272..285
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 303..309
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:5EXD"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 333..341
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:5EXE"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:5EXE"
FT HELIX 365..381
FT /evidence="ECO:0007829|PDB:5EXE"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:5EXE"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:5EXE"
SQ SEQUENCE 395 AA; 43687 MW; BFF45784726830DC CRC64;
MGKVRNISGC VAVAHGVRLA DVDVICSYPI RPYTGIMSEL ARMVADGELD AEFVHGEGEH
AQLSVVYGAS AAGARVFTGS SGVGVTYAME VYSPISGERL PVQMAIADRT LDPPGDFGEE
HTDAECCRDQ GWIQGWASTP QEALDNTLIY YRVGEDQRVL LPQYACLDGY FVSHILGPVD
IPDEAQVKEF LPPYKNHHVL DPRKPQIIGP QIEPAMGPPL QYQRYQAVKG VHKVLEEACD
EFARIFGRKY DPYLDEYLTD DAEVIIFGQG AHMETAKAVA RRLRNLGEKV GVARLRTFRP
FPTEQIKERL SKFKAIGVLD VSANFGISCS GGVLLSELRA ALYDYGDKVK TVGFVAGLGG
EVVTHDEFYR MFQKLKEIAK TGKVEQTSYW IPFEL
