OXDD_BACSU
ID OXDD_BACSU Reviewed; 392 AA.
AC O34767;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Oxalate decarboxylase OxdD {ECO:0000303|PubMed:11546787};
DE EC=4.1.1.2 {ECO:0000269|PubMed:11546787};
GN Name=oxdD {ECO:0000303|PubMed:11546787}; Synonyms=yoaN {ECO:0000303|Ref.1};
GN OrderedLocusNames=BSU18670;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT terC and odhAB loci cloned in a yeast artificial chromosome.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PROBABLE SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=11546787; DOI=10.1074/jbc.m107202200;
RA Tanner A., Bowater L., Fairhurst S.A., Bornemann S.;
RT "Oxalate decarboxylase requires manganese and dioxygen for activity.
RT Overexpression and characterization of Bacillus subtilis YvrK and YoaN.";
RL J. Biol. Chem. 276:43627-43634(2001).
CC -!- FUNCTION: Converts oxalate to formate and CO(2).
CC {ECO:0000269|PubMed:11546787}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxalate = CO2 + formate; Xref=Rhea:RHEA:16509,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30623; EC=4.1.1.2;
CC Evidence={ECO:0000269|PubMed:11546787};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11546787};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:O34714};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:11546787}.
CC -!- SIMILARITY: To B.subtilis OxdC. {ECO:0000305}.
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DR EMBL; AF027868; AAB84450.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13759.1; -; Genomic_DNA.
DR PIR; G69896; G69896.
DR RefSeq; NP_389748.1; NC_000964.3.
DR RefSeq; WP_003231409.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34767; -.
DR SMR; O34767; -.
DR IntAct; O34767; 1.
DR STRING; 224308.BSU18670; -.
DR PaxDb; O34767; -.
DR PRIDE; O34767; -.
DR EnsemblBacteria; CAB13759; CAB13759; BSU_18670.
DR GeneID; 940006; -.
DR KEGG; bsu:BSU18670; -.
DR PATRIC; fig|224308.179.peg.2036; -.
DR eggNOG; COG2140; Bacteria.
DR InParanoid; O34767; -.
DR OMA; HPNNDEW; -.
DR PhylomeDB; O34767; -.
DR BioCyc; BSUB:BSU18670-MON; -.
DR BRENDA; 4.1.1.2; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046564; F:oxalate decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0033609; P:oxalate metabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR017774; Bicupin_oxalate_deCO2ase/Oxase.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 2.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 1.
DR TIGRFAMs; TIGR03404; bicupin_oxalic; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Decarboxylase; Lyase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..392
FT /note="Oxalate decarboxylase OxdD"
FT /id="PRO_0000058107"
FT DOMAIN 59..200
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 236..377
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 341
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 106
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 110
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 149
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 281
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 283
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 288
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34714"
FT BINDING 327
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34714"
SQ SEQUENCE 392 AA; 43554 MW; 54642A8AD727DC30 CRC64;
MLLEQQPINH EDRNVPQPIR SDGAGAIDTG PRNIIRDIQN PNIFVPPVTD EGMIPNLRFS
FSDAPMKLDH GGWSREITVR QLPISTAIAG VNMSLTAGGV RELHWHKQAE WAYMLLGRAR
ITAVDQDGRN FIADVGPGDL WYFPAGIPHS IQGLEHCEFL LVFDDGNFSE FSTLTISDWL
AHTPKDVLSA NFGVPENAFN SLPSEQVYIY QGNVPGSVAS EDIQSPYGKV PMTFKHELLN
QPPIQMPGGS VRIVDSSNFP ISKTIAAALV QIEPGAMREL HWHPNSDEWQ YYLTGQGRMT
VFIGNGTART FDYRAGDVGY VPSNAGHYIQ NTGTETLWFL EMFKSNRYAD VSLNQWMALT
PKELVQSNLN AGSVMLDSLR KKKVPVVKYP GT
