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Database: UniProt
Entry: OXC_ECOLI
LinkDB: OXC_ECOLI
Original site: OXC_ECOLI 
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   24-JAN-2024, entry version 127.
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; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   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=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         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}.
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DR   EMBL; U00096; AAC75432.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16245.1; -; Genomic_DNA.
DR   PIR; B65011; B65011.
DR   RefSeq; NP_416874.1; NC_000913.3.
DR   RefSeq; WP_001283490.1; NZ_LN832404.1.
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   PDBsum; 2Q27; -.
DR   PDBsum; 2Q28; -.
DR   PDBsum; 2Q29; -.
DR   AlphaFoldDB; P0AFI0; -.
DR   SMR; P0AFI0; -.
DR   BioGRID; 4260862; 15.
DR   BioGRID; 851186; 1.
DR   DIP; DIP-48075N; -.
DR   IntAct; P0AFI0; 6.
DR   MINT; P0AFI0; -.
DR   STRING; 511145.b2373; -.
DR   PaxDb; 511145-b2373; -.
DR   EnsemblBacteria; AAC75432; AAC75432; b2373.
DR   GeneID; 946845; -.
DR   KEGG; ecj:JW2370; -.
DR   KEGG; eco:b2373; -.
DR   PATRIC; fig|1411691.4.peg.4356; -.
DR   EchoBASE; EB3895; -.
DR   eggNOG; COG0028; Bacteria.
DR   InParanoid; P0AFI0; -.
DR   OMA; PGPYGCL; -.
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; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
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:0001561; P:fatty acid alpha-oxidation; IBA:GO_Central.
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   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   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.
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           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"
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
//
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