ID MPC2_CUPNE Reviewed; 320 AA.
AC P17296;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Metapyrocatechase 2;
DE Short=MPC;
DE EC=1.13.11.2;
DE AltName: Full=CatO2ase;
DE AltName: Full=Catechol 2,3-dioxygenase II;
GN Name=mcpII;
OS Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=106590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JMP222;
RX PubMed=2216726; DOI=10.1093/nar/18.18.5543;
RA Kabisch M., Fortnagel P.;
RT "Nucleotide sequence of the metapyrocatechase II (catechol 2,3-oxygenase
RT II) gene mpcII from Alcaligenes eutrophus JMP 222.";
RL Nucleic Acids Res. 18:5543-5543(1990).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=catechol + O2 = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate +
CC H(+); Xref=Rhea:RHEA:17337, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:18135, ChEBI:CHEBI:71198; EC=1.13.11.2;
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; X52415; CAA36666.1; -; Genomic_DNA.
DR PIR; S14691; DAAL2E.
DR RefSeq; WP_011300792.1; NZ_CAIGKG010000001.1.
DR AlphaFoldDB; P17296; -.
DR SMR; P17296; -.
DR GO; GO:0018577; F:catechol 2,3-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08360; MhqB_like_C; 1.
DR CDD; cd08344; MhqB_like_N; 1.
DR Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 2.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR037523; VOC.
DR InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2.
DR PANTHER; PTHR21366:SF22; GLYOXALASE DOMAIN-CONTAINING PROTEIN 5; 1.
DR PANTHER; PTHR21366; GLYOXALASE FAMILY PROTEIN; 1.
DR Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR PROSITE; PS51819; VOC; 2.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Repeat.
FT CHAIN 1..320
FT /note="Metapyrocatechase 2"
FT /id="PRO_0000085030"
FT DOMAIN 25..131
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 167..282
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 170
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 320 AA; 35387 MW; B08D6929FDB92D7B CRC64;
MDTHRADASQ RSQAPAARPR HAVHSIDHYA LEVPDLAVAE RFLDAFGLTV ARTPECLEVY
AADQRCWARF YEGERKRLAY LSFSCFEGDF AGIRQQLAAS GATLVEDPRY GDESGVWFFD
PDGNLVQVKI GPKTSPSSKS PARLEGAPGG QRGAVVRSQV QRVLPRRLSH VLLFTPSVQR
ALDFYRDALG LRLSDRSDDV IAFTHAPYGS DHHLLALVKS SARGWHHAAW DVADVNEVGQ
GASQMAKAGY TQGWGTGRHV LGSNYFFYVL DPWGSFCEYS ADIDYIPAGQ AWPAGDFAAE
DSLYQWGPDV PEYFVRNTEA
//
