ID OXC_ECOLI Reviewed; 564 AA. AC P0AFI0; P78093; P78194; P78195; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 02-SEP-2026, entry version 137. DE RecName: Full=Oxalyl-CoA decarboxylase; DE EC=4.1.1.8; GN Name=oxc; Synonyms=yfdU; OrderedLocusNames=b2373, JW2370; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9205837; DOI=10.1093/dnares/4.2.91; RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S., RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.; RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of RT its sequence features."; RL DNA Res. 4:91-113(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP INDUCTION. RX PubMed=23335415; DOI=10.1128/jb.01936-12; RA Fontenot E.M., Ezelle K.E., Gabreski L.N., Giglio E.R., McAfee J.M., RA Mills A.C., Qureshi M.N., Salmon K.M., Toyota C.G.; RT "YfdW and YfdU are required for oxalate-induced acid tolerance in RT Escherichia coli K-12."; RL J. Bacteriol. 195:1446-1455(2013). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) IN COMPLEX WITH THIAMINE RP PYROPHOSPHATE; SUBSTRATE ANALOGS; ADP AND MAGNESIUM, FUNCTION, CATALYTIC RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, AND RP SUBUNIT. RX PubMed=20553497; DOI=10.1111/j.1742-464x.2010.07673.x; RA Werther T., Zimmer A., Wille G., Golbik R., Weiss M.S., Konig S.; RT "New insights into structure-function relationships of oxalyl CoA RT decarboxylase from Escherichia coli."; RL FEBS J. 277:2628-2640(2010). CC -!- FUNCTION: Involved in the catabolism of oxalate and in the adapatation CC to low pH via the induction of the oxalate-dependent acid tolerance CC response (ATR). Catalyzes the decarboxylation of oxalyl-CoA to yield CC carbon dioxide and formyl-CoA. {ECO:0000269|PubMed:20553497}. CC -!- CATALYTIC ACTIVITY: CC Reaction=oxalyl-CoA + H(+) = formyl-CoA + CO2; Xref=Rhea:RHEA:19333, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57376, CC ChEBI:CHEBI:57388; EC=4.1.1.8; CC Evidence={ECO:0000269|PubMed:20553497}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:20553497}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:20553497}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000269|PubMed:20553497}; CC Note=Binds 1 thiamine pyrophosphate per subunit. CC {ECO:0000269|PubMed:20553497}; CC -!- ACTIVITY REGULATION: Activated by ADP. {ECO:0000269|PubMed:20553497}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.17 uM for oxalyl-CoA (with 300 uM ADP at pH 6.5 and 30 degrees CC Celsius) {ECO:0000269|PubMed:20553497}; CC KM=4.8 uM for oxalyl-CoA (at pH 6.5 and 30 degrees Celsius) CC {ECO:0000269|PubMed:20553497}; CC Note=kcat is 69.7 sec(-1) for decarboxylase activity with oxalyl-CoA CC as substrate (with 300 uM ADP at pH 6.5 and 30 degrees Celsius). kcat CC is 60.7 sec(-1) for decarboxylase activity with oxalyl-CoA as CC substrate (at pH 6.5 and 30 degrees Celsius).; CC pH dependence: CC Optimum pH is between 5.5 and 7. {ECO:0000269|PubMed:20553497}; CC -!- PATHWAY: Metabolic intermediate degradation; oxalate degradation; CO(2) CC and formate from oxalate: step 2/2. CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000269|PubMed:20553497}. CC -!- INTERACTION: CC P0AFI0; P0AFI0: oxc; NbExp=4; IntAct=EBI-557143, EBI-557143; CC -!- INDUCTION: By the acid response regulator EvgA. CC {ECO:0000269|PubMed:23335415}. CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}. 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; U00096; AAC75432.1; -; Genomic_DNA. DR EMBL; AP009048; BAA16245.2; -; Genomic_DNA. DR PIR; B65011; B65011. DR RefSeq; NP_416874.1; NC_000913.3. DR RefSeq; WP_001283490.1; NZ_CP009789.1. DR PDB; 2Q27; X-ray; 2.12 A; A/B=1-564. DR PDB; 2Q28; X-ray; 1.74 A; A/B=1-564. DR PDB; 2Q29; X-ray; 1.82 A; A/B=1-564. DR AlphaFoldDB; P0AFI0; -. DR SMR; P0AFI0; -. DR BioGRID; 4260862; 20. DR BioGRID; 851186; 1. DR DIP; DIP-48075N; -. DR FunCoup; P0AFI0; 485. DR IntAct; P0AFI0; 6. DR MINT; P0AFI0; -. DR STRING; 511145.b2373; -. DR PaxDb; 511145-b2373; -. DR EnsemblBacteria; AAC75432; AAC75432; b2373. DR GeneID; 93774756; -. DR GeneID; 946845; -. DR KEGG; ecj:JW2370; -. DR KEGG; eco:b2373; -. DR KEGG; ecoc:C3026_13195; -. DR PATRIC; fig|1411691.4.peg.4356; -. DR EchoBASE; EB3895; -. DR eggNOG; COG0028; Bacteria. DR InParanoid; P0AFI0; -. DR OMA; QGPWIGS; -. DR OrthoDB; 3194735at2; -. DR PhylomeDB; P0AFI0; -. DR BioCyc; EcoCyc:G7236-MONOMER; -. DR BioCyc; MetaCyc:G7236-MONOMER; -. DR BRENDA; 4.1.1.8; 2026. DR UniPathway; UPA00540; UER00599. DR EvolutionaryTrace; P0AFI0; -. DR PRO; PR:P0AFI0; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P0AFI0; -. DR GO; GO:0043531; F:ADP binding; IDA:EcoCyc. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0008949; F:oxalyl-CoA decarboxylase activity; IDA:EcoCyc. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:EcoCyc. DR GO; GO:0071468; P:cellular response to acidic pH; IMP:EcoCyc. DR GO; GO:0033611; P:oxalate catabolic process; IDA:UniProtKB. DR CDD; cd02004; TPP_BZL_OCoD_HPCL; 1. DR CDD; cd07035; TPP_PYR_POX_like; 1. DR DisProt; DP03810; -. DR FunFam; 3.40.50.1220:FF:000006; 2-hydroxyacyl-CoA lyase 1; 1. DR FunFam; 3.40.50.970:FF:000040; Oxalyl-CoA decarboxylase; 1. DR FunFam; 3.40.50.970:FF:000042; Oxalyl-CoA decarboxylase; 1. DR Gene3D; 3.40.50.970; -; 2. DR Gene3D; 3.40.50.1220; TPP-binding domain; 1. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR045025; HACL1-like. DR InterPro; IPR017660; Oxalyl-CoA_decarboxylase. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom. DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom. DR InterPro; IPR011766; TPP_enzyme_TPP-bd. DR NCBIfam; TIGR03254; oxalate_oxc; 1. DR NCBIfam; NF006721; PRK09259.1; 1. DR PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1. DR PANTHER; PTHR43710:SF2; 2-HYDROXYACYL-COA LYASE 1; 1. DR Pfam; PF02775; TPP_enzyme_C; 1. DR Pfam; PF00205; TPP_enzyme_M; 1. DR Pfam; PF02776; TPP_enzyme_N; 1. DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2. DR PDBsum; 2Q27; -. DR PDBsum; 2Q28; -. DR PDBsum; 2Q29; -. PE 1: Evidence at protein level; KW 3D-structure; Decarboxylase; Lyase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome; Thiamine pyrophosphate. FT CHAIN 1..564 FT /note="Oxalyl-CoA decarboxylase" FT /id="PRO_0000090824" FT BINDING 32 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 118 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 158 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:20553497" FT BINDING 220 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:20553497" FT BINDING 261..265 FT /ligand="substrate" FT /evidence="ECO:0000305" FT BINDING 280 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:20553497" FT BINDING 302 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:20553497" FT BINDING 322 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:20553497" FT BINDING 355 FT /ligand="substrate" FT BINDING 372 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000269|PubMed:20553497" FT BINDING 396..398 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT BINDING 403..404 FT /ligand="substrate" FT BINDING 421..423 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT BINDING 447 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:20553497" FT BINDING 448..449 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT BINDING 474 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:20553497" FT BINDING 476 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:20553497" FT BINDING 478 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000269|PubMed:20553497" FT BINDING 550..552 FT /ligand="substrate" FT /evidence="ECO:0000250" FT STRAND 7..9 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 10..20 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 25..28 FT /evidence="ECO:0007829|PDB:2Q28" FT TURN 32..34 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 35..43 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 47..50 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 54..68 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 72..76 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 79..95 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 99..105 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 108..112 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 123..127 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 128..130 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 131..136 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 143..155 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 156..158 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 161..167 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 168..172 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 177..182 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 188..191 FT /evidence="ECO:0007829|PDB:2Q29" FT STRAND 194..196 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 198..210 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 212..218 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 220..225 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 228..238 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 246..248 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 261..263 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 264..270 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 272..278 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 283..288 FT /evidence="ECO:0007829|PDB:2Q28" FT TURN 289..291 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 297..303 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 310..312 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 315..320 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 322..335 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 342..363 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 368..370 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 372..383 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 390..396 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 397..405 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 410..412 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 414..417 FT /evidence="ECO:0007829|PDB:2Q28" FT TURN 418..421 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 426..437 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 441..446 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 447..451 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 454..456 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 457..462 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 467..473 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 475..478 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 490..492 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 502..509 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 512..516 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 519..532 FT /evidence="ECO:0007829|PDB:2Q28" FT STRAND 536..542 FT /evidence="ECO:0007829|PDB:2Q28" FT HELIX 548..550 FT /evidence="ECO:0007829|PDB:2Q27" SQ SEQUENCE 564 AA; 60581 MW; 94418B2BE7D40C17 CRC64; MSDQLQMTDG MHIIVEALKQ NNIDTIYGVV GIPVTDMARH AQAEGIRYIG FRHEQSAGYA AAASGFLTQK PGICLTVSAP GFLNGLTALA NATVNGFPMI MISGSSDRAI VDLQQGDYEE LDQMNAAKPY AKAAFRVNQP QDLGIALARA IRVSVSGRPG GVYLDLPANV LAATMEKDEA LTTIVKVENP SPALLPCPKS VTSAISLLAK AERPLIILGK GAAYSQADEQ LREFIESAQI PFLPMSMAKG ILEDTHPLSA AAARSFALAN ADVVMLVGAR LNWLLAHGKK GWAADTQFIQ LDIEPQEIDS NRPIAVPVVG DIASSMQGML AELKQNTFTT PLVWRDILNI HKQQNAQKMH EKLSTDTQPL NYFNALSAVR DVLRENQDIY LVNEGANTLD NARNIIDMYK PRRRLDCGTW GVMGIGMGYA IGASVTSGSP VVAIEGDSAF GFSGMEIETI CRYNLPVTIV IFNNGGIYRG DGVDLSGAGA PSPTDLLHHA RYDKLMDAFR GVGYNVTTTD ELRHALTTGI QSRKPTIINV VIDPAAGTES GHITKLNPKQ VAGN //