ID YGID_ECOLI Reviewed; 271 AA. AC P24197; Q2M9G1; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2016, sequence version 4. DT 27-MAR-2024, entry version 158. DE RecName: Full=4,5-DOPA dioxygenase extradiol {ECO:0000305}; DE EC=1.13.11.29 {ECO:0000269|PubMed:23666480}; GN Name=ygiD; OrderedLocusNames=b3039, JW3007; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1314093; DOI=10.1016/0167-4781(92)90535-8; RA Yang T.-P., Depew R.E.; RT "Nucleotide sequence of a region duplicated in Escherichia coli toc RT mutants."; RL Biochim. Biophys. Acta 1130:227-228(1992). 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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND RP SUBCELLULAR LOCATION. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=23666480; DOI=10.1007/s00253-013-4961-3; RA Gandia-Herrero F., Garcia-Carmona F.; RT "Escherichia coli protein YgiD produces the structural unit of plant RT pigments betalains: characterization of a prokaryotic enzyme with DOPA- RT extradiol-dioxygenase activity."; RL Appl. Microbiol. Biotechnol. 98:1165-1174(2014). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS), AND ZINC BINDING. RG Southeast collaboratory for structural genomics (SECSG); RT "Crystal structure of uncharacterized protein JW3007 from Escherichia coli RT K12."; RL Submitted (JUN-2007) to the PDB data bank. CC -!- FUNCTION: In vitro, opens the cyclic ring of dihydroxy-phenylalanine CC (DOPA) between carbons 4 and 5, thus producing an unstable seco-DOPA CC that rearranges nonenzymatically to betalamic acid. The physiological CC substrate is unknown. {ECO:0000269|PubMed:23666480}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-dopa + O2 = 4-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6- CC semialdehyde + H(+); Xref=Rhea:RHEA:21220, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, ChEBI:CHEBI:57639; CC EC=1.13.11.29; Evidence={ECO:0000269|PubMed:23666480}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=7.9 mM for L-DOPA {ECO:0000269|PubMed:23666480}; CC Note=kcat is 0.17 min(-1) with L-DOPA. {ECO:0000269|PubMed:23666480}; CC pH dependence: CC Optimum pH is 8.0. {ECO:0000269|PubMed:23666480}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23666480}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23666480}. CC -!- MISCELLANEOUS: Betalamic acid is the structural unit of the betalains, CC natural nitrogen-containing water-soluble pigments with high colorant CC and bioactive properties, characteristic of plants of the order CC Caryophyllales. {ECO:0000305|PubMed:23666480}. CC -!- SIMILARITY: Belongs to the DODA-type extradiol aromatic ring-opening CC dioxygenase family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-10 is the initiator. CC {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; M77129; AAA71877.1; -; Genomic_DNA. DR EMBL; U28377; AAA69207.1; -; Genomic_DNA. DR EMBL; U00096; AAC76075.3; -; Genomic_DNA. DR EMBL; AP009048; BAE77095.1; -; Genomic_DNA. DR PIR; E65091; E65091. DR RefSeq; NP_417511.2; NC_000913.3. DR PDB; 2PW6; X-ray; 2.27 A; A=1-271. DR PDBsum; 2PW6; -. DR AlphaFoldDB; P24197; -. DR SMR; P24197; -. DR BioGRID; 4263035; 3. DR IntAct; P24197; 3. DR STRING; 511145.b3039; -. DR PaxDb; 511145-b3039; -. DR EnsemblBacteria; AAC76075; AAC76075; b3039. DR GeneID; 946447; -. DR KEGG; ecj:JW3007; -. DR KEGG; eco:b3039; -. DR PATRIC; fig|1411691.4.peg.3693; -. DR EchoBASE; EB1154; -. DR eggNOG; COG3384; Bacteria. DR HOGENOM; CLU_046582_2_0_6; -. DR InParanoid; P24197; -. DR OMA; EWGFDHG; -. DR OrthoDB; 9790889at2; -. DR BioCyc; EcoCyc:EG11166-MONOMER; -. DR BioCyc; MetaCyc:EG11166-MONOMER; -. DR EvolutionaryTrace; P24197; -. DR PRO; PR:P24197; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046566; F:DOPA dioxygenase activity; IDA:EcoCyc. DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro. DR GO; GO:0050297; F:stizolobate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro. DR CDD; cd07363; 45_DOPA_Dioxygenase; 1. DR Gene3D; 3.40.830.10; LigB-like; 1. DR InterPro; IPR014436; Extradiol_dOase_DODA. DR InterPro; IPR004183; Xdiol_dOase_suB. DR PANTHER; PTHR30096:SF0; 4,5-DOPA DIOXYGENASE EXTRADIOL-LIKE PROTEIN; 1. DR PANTHER; PTHR30096; UNCHARACTERIZED; 1. DR Pfam; PF02900; LigB; 1. DR PIRSF; PIRSF006157; Doxgns_DODA; 1. DR SUPFAM; SSF53213; LigB-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Dioxygenase; Metal-binding; Oxidoreductase; KW Reference proteome; Zinc. FT CHAIN 1..271 FT /note="4,5-DOPA dioxygenase extradiol" FT /id="PRO_0000169405" FT BINDING 22 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|Ref.5" FT BINDING 57 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|Ref.5" FT BINDING 177 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|Ref.5" FT BINDING 234 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|Ref.5" FT CONFLICT 243..270 FT /note="GAWDGQEPITIPVEGIEMGSLSMLSVQI -> RYVGWAGANYHS (in FT Ref. 1; AAA71877)" FT /evidence="ECO:0000305" FT STRAND 17..21 FT /evidence="ECO:0007829|PDB:2PW6" FT HELIX 33..44 FT /evidence="ECO:0007829|PDB:2PW6" FT STRAND 49..66 FT /evidence="ECO:0007829|PDB:2PW6" FT HELIX 95..105 FT /evidence="ECO:0007829|PDB:2PW6" FT STRAND 110..115 FT /evidence="ECO:0007829|PDB:2PW6" FT HELIX 121..130 FT /evidence="ECO:0007829|PDB:2PW6" FT STRAND 138..144 FT /evidence="ECO:0007829|PDB:2PW6" FT HELIX 149..159 FT /evidence="ECO:0007829|PDB:2PW6" FT HELIX 160..165 FT /evidence="ECO:0007829|PDB:2PW6" FT STRAND 167..173 FT /evidence="ECO:0007829|PDB:2PW6" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:2PW6" FT HELIX 192..202 FT /evidence="ECO:0007829|PDB:2PW6" FT TURN 203..206 FT /evidence="ECO:0007829|PDB:2PW6" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:2PW6" FT TURN 215..217 FT /evidence="ECO:0007829|PDB:2PW6" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:2PW6" FT HELIX 225..228 FT /evidence="ECO:0007829|PDB:2PW6" FT STRAND 230..232 FT /evidence="ECO:0007829|PDB:2PW6" FT TURN 233..235 FT /evidence="ECO:0007829|PDB:2PW6" FT HELIX 236..243 FT /evidence="ECO:0007829|PDB:2PW6" FT STRAND 247..249 FT /evidence="ECO:0007829|PDB:2PW6" FT TURN 260..262 FT /evidence="ECO:0007829|PDB:2PW6" FT STRAND 268..270 FT /evidence="ECO:0007829|PDB:2PW6" SQ SEQUENCE 271 AA; 29903 MW; A74E9035BAF6EB0F CRC64; MTPLVKDIIM SSTRMPALFL GHGSPMNVLE DNLYTRSWQK LGMTLPRPQA IVVVSAHWFT RGTGVTAMET PPTIHDFGGF PQALYDTHYP APGSPALAQR LVELLAPIPV TLDKEAWGFD HGSWGVLIKM YPDADIPMVQ LSIDSSKPAA WHFEMGRKLA ALRDEGIMLV ASGNVVHNLR TVKWHGDSSP YPWATSFNEY VKANLTWQGP VEQHPLVNYL DHEGGTLSNP TPEHYLPLLY VLGAWDGQEP ITIPVEGIEM GSLSMLSVQI G //