ID OXDC_BACSU Reviewed; 385 AA. AC O34714; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 13-NOV-2013, entry version 105. DE RecName: Full=Oxalate decarboxylase OxdC; DE EC=4.1.1.2; GN Name=oxdC; Synonyms=yvrK; OrderedLocusNames=BSU33240; OS Bacillus subtilis (strain 168). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX PubMed=9639930; RA Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., RA Harwood C.R.; RT "The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus RT subtilis chromosome containing genes involved in metal ion uptake and RT a putative sigma factor."; RL Microbiology 144:1593-1600(1998). 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., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA 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., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA 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 PROTEIN SEQUENCE OF 1-15, AND CHARACTERIZATION. RX PubMed=10960116; DOI=10.1128/JB.182.18.5271-5273.2000; RA Tanner A., Bornemann S.; RT "Bacillus subtilis YvrK is an acid-induced oxalate decarboxylase."; RL J. Bacteriol. 182:5271-5273(2000). RN [4] RP CHARACTERIZATION. 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 RT YoaN."; RL J. Biol. Chem. 276:43627-43634(2001). RN [5] RP INDUCTION. RC STRAIN=168 / CU1065; RX PubMed=18573182; DOI=10.1111/j.1365-2958.2008.06331.x; RA MacLellan S.R., Wecke T., Helmann J.D.; RT "A previously unidentified sigma factor and two accessory proteins RT regulate oxalate decarboxylase expression in Bacillus subtilis."; RL Mol. Microbiol. 69:954-967(2008). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND MUTAGENESIS OF GLU-333. RX PubMed=12056897; DOI=10.1021/bi0200965; RA Anand R., Dorrestein P.C., Kinsland C., Begley T.P., Ealick S.E.; RT "Structure of oxalate decarboxylase from Bacillus subtilis at 1.75 A RT resolution."; RL Biochemistry 41:7659-7669(2002). CC -!- FUNCTION: Converts oxalate to formate and CO(2) in an O(2)- CC dependent reaction. Can also catalyze minor side reactions: CC oxalate oxidation to produce H(2)O(2), and oxalate-dependent, CC H(2)O(2)-independent dye oxidations. CC -!- CATALYTIC ACTIVITY: Oxalate = formate + CO(2). CC -!- COFACTOR: Binds 2 manganese ions per subunit. CC -!- SUBUNIT: Homohexamer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- INDUCTION: Induced by acid pH but not by oxalate. Positively CC regulated by SigO and its coactivator RsoA. CC -!- SIMILARITY: To B.subtilis OxdD. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ223978; CAA11727.1; -; Genomic_DNA. DR EMBL; AL009126; CAB15314.1; -; Genomic_DNA. DR PIR; E70047; E70047. DR RefSeq; NP_391204.1; NC_000964.3. DR PDB; 1J58; X-ray; 1.75 A; A=1-385. DR PDB; 1L3J; X-ray; 1.90 A; A=1-385. DR PDB; 1UW8; X-ray; 2.00 A; A=1-385. DR PDB; 2UY8; X-ray; 2.80 A; A=1-385. DR PDB; 2UY9; X-ray; 3.10 A; A=1-385. DR PDB; 2UYA; X-ray; 2.00 A; A=1-385. DR PDB; 2UYB; X-ray; 2.10 A; A=1-385. DR PDB; 2V09; X-ray; 1.80 A; A=1-385. DR PDB; 3S0M; X-ray; 2.31 A; A=6-382. DR PDBsum; 1J58; -. DR PDBsum; 1L3J; -. DR PDBsum; 1UW8; -. DR PDBsum; 2UY8; -. DR PDBsum; 2UY9; -. DR PDBsum; 2UYA; -. DR PDBsum; 2UYB; -. DR PDBsum; 2V09; -. DR PDBsum; 3S0M; -. DR ProteinModelPortal; O34714; -. DR SMR; O34714; 8-379. DR STRING; 224308.BSU33240; -. DR PaxDb; O34714; -. DR EnsemblBacteria; CAB15314; CAB15314; BSU33240. DR GeneID; 938620; -. DR KEGG; bsu:BSU33240; -. DR PATRIC; 18978646; VBIBacSub10457_3486. DR GenoList; BSU33240; -. DR eggNOG; COG2140; -. DR HOGENOM; HOG000200624; -. DR KO; K01569; -. DR OMA; ITDSTNF; -. DR OrthoDB; EOG689HPG; -. DR ProtClustDB; CLSK2301483; -. DR BioCyc; BSUB:BSU33240-MONOMER; -. DR BioCyc; MetaCyc:BSU33240-MONOMER; -. DR BRENDA; 4.1.1.2; 700. DR SABIO-RK; O34714; -. DR EvolutionaryTrace; O34714; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0045735; F:nutrient reservoir activity; IEA:InterPro. DR GO; GO:0046564; F:oxalate decarboxylase activity; IEA:UniProtKB-EC. 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. 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 3D-structure; Complete proteome; Cytoplasm; Decarboxylase; KW Direct protein sequencing; Lyase; Manganese; Metal-binding; KW Reference proteome. FT CHAIN 1 385 Oxalate decarboxylase OxdC. FT /FTId=PRO_0000058106. FT ACT_SITE 333 333 Proton donor. FT METAL 95 95 Manganese 1. FT METAL 97 97 Manganese 1. FT METAL 101 101 Manganese 1. FT METAL 140 140 Manganese 1. FT METAL 273 273 Manganese 2. FT METAL 275 275 Manganese 2. FT METAL 280 280 Manganese 2. FT METAL 319 319 Manganese 2. FT MUTAGEN 333 333 E->A: 25-fold reduction of activity. FT STRAND 10 12 FT HELIX 25 30 FT HELIX 32 35 FT STRAND 49 51 FT HELIX 52 54 FT STRAND 58 60 FT STRAND 63 68 FT TURN 70 72 FT STRAND 80 86 FT STRAND 91 99 FT STRAND 101 115 FT STRAND 121 127 FT STRAND 130 134 FT STRAND 140 156 FT HELIX 162 164 FT STRAND 165 167 FT HELIX 168 173 FT HELIX 177 184 FT HELIX 189 191 FT STRAND 200 202 FT HELIX 210 213 FT STRAND 226 229 FT HELIX 230 232 FT STRAND 236 238 FT STRAND 239 247 FT TURN 248 250 FT STRAND 258 264 FT STRAND 269 274 FT STRAND 276 278 FT STRAND 280 296 FT STRAND 299 308 FT STRAND 310 313 FT STRAND 318 323 FT STRAND 325 327 FT STRAND 329 339 FT HELIX 345 350 FT HELIX 354 361 FT HELIX 365 368 FT STRAND 377 379 SQ SEQUENCE 385 AA; 43566 MW; A301F5A75E53F4FB CRC64; MKKQNDIPQP IRGDKGATVK IPRNIERDRQ NPDMLVPPET DHGTVSNMKF SFSDTHNRLE KGGYAREVTV RELPISENLA SVNMRLKPGA IRELHWHKEA EWAYMIYGSA RVTIVDEKGR SFIDDVGEGD LWYFPSGLPH SIQALEEGAE FLLVFDDGSF SENSTFQLTD WLAHTPKEVI AANFGVTKEE ISNLPGKEKY IFENQLPGSL KDDIVEGPNG EVPYPFTYRL LEQEPIESEG GKVYIADSTN FKVSKTIASA LVTVEPGAMR ELHWHPNTHE WQYYISGKAR MTVFASDGHA RTFNYQAGDV GYVPFAMGHY VENIGDEPLV FLEIFKDDHY ADVSLNQWLA MLPETFVQAH LDLGKDFTDV LSKEKHPVVK KKCSK //