OXC_ECO57
ID OXC_ECO57 Reviewed; 564 AA.
AC P0AFI1; P78093; P78194; P78195;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Oxalyl-CoA decarboxylase;
DE EC=4.1.1.8;
GN Name=oxc; OrderedLocusNames=Z3637, ECs3253;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxalyl-CoA = CO2 + formyl-CoA; Xref=Rhea:RHEA:19333,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57376,
CC ChEBI:CHEBI:57388; EC=4.1.1.8;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- PATHWAY: Metabolic intermediate degradation; oxalate degradation; CO(2)
CC and formate from oxalate: step 2/2.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; AE005174; AAG57499.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36676.1; -; Genomic_DNA.
DR PIR; E91035; E91035.
DR PIR; G85879; G85879.
DR RefSeq; NP_311280.1; NC_002695.1.
DR RefSeq; WP_001283490.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AFI1; -.
DR SMR; P0AFI1; -.
DR STRING; 155864.EDL933_3542; -.
DR EnsemblBacteria; AAG57499; AAG57499; Z3637.
DR EnsemblBacteria; BAB36676; BAB36676; ECs_3253.
DR GeneID; 915646; -.
DR KEGG; ece:Z3637; -.
DR KEGG; ecs:ECs_3253; -.
DR PATRIC; fig|386585.9.peg.3397; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_3_6; -.
DR OMA; PGPYGCL; -.
DR UniPathway; UPA00540; UER00599.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0043531; F:ADP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0008949; F:oxalyl-CoA decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0033611; P:oxalate catabolic process; ISS:UniProtKB.
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-bd_C.
DR PANTHER; PTHR43710; PTHR43710; 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; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR03254; oxalate_oxc; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..564
FT /note="Oxalyl-CoA decarboxylase"
FT /id="PRO_0000090825"
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:0000250"
FT BINDING 220
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 261..265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 372
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 396..398
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 403..404
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 421..423
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 448..449
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 478
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 550..552
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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
