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 10-APR-2019, entry version 134. 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; Proteobacteria; 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., RA Mau B., 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 RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, RP AND 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 RT DOPA-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 RT coli K12."; RL Submitted (JUN-2007) to the PDB data bank. CC -!- FUNCTION: In vitro, opens the cyclic ring of dihydroxy- CC phenylalanine (DOPA) between carbons 4 and 5, thus producing an CC unstable seco-DOPA that rearranges nonenzymatically to betalamic CC acid. The physiological substrate is unknown. CC {ECO:0000269|PubMed:23666480}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-dopa + O2 = 4-(L-alanin-3-yl)-2-hydroxy-cis,cis- CC muconate 6-semialdehyde + H(+); Xref=Rhea:RHEA:21220, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, CC ChEBI:CHEBI:57639; EC=1.13.11.29; CC 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. CC {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 CC betalains, natural nitrogen-containing water-soluble pigments with CC high colorant and bioactive properties, characteristic of plants CC of the order Caryophyllales. {ECO:0000305|PubMed:23666480}. CC -!- SIMILARITY: Belongs to the DODA-type extradiol aromatic ring- CC opening dioxygenase family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-10 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC76075.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={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; AAC76075.2; ALT_INIT; 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 ProteinModelPortal; P24197; -. DR SMR; P24197; -. DR BioGrid; 4263035; 3. DR IntAct; P24197; 3. DR STRING; 511145.b3039; -. DR PaxDb; P24197; -. DR PRIDE; P24197; -. DR EnsemblBacteria; AAC76075; AAC76075; b3039. DR EnsemblBacteria; BAE77095; BAE77095; BAE77095. DR GeneID; 946447; -. DR KEGG; ecj:JW3007; -. DR KEGG; eco:b3039; -. DR PATRIC; fig|1411691.4.peg.3693; -. DR EchoBASE; EB1154; -. DR EcoGene; EG11166; ygiD. DR eggNOG; ENOG4105C8E; Bacteria. DR eggNOG; COG3384; LUCA. DR HOGENOM; HOG000236850; -. DR InParanoid; P24197; -. DR KO; K15777; -. DR PhylomeDB; P24197; -. DR BioCyc; EcoCyc:EG11166-MONOMER; -. DR BioCyc; ECOL316407:JW3007-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 InterPro; IPR014436; Extradiol_dOase_DODA. DR InterPro; IPR004183; Xdiol_dOase_suB. DR Pfam; PF02900; LigB; 1. DR PIRSF; PIRSF006157; Doxgns_DODA; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Dioxygenase; KW Metal-binding; Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1 271 4,5-DOPA dioxygenase extradiol. FT /FTId=PRO_0000169405. FT METAL 22 22 Zinc. {ECO:0000269|Ref.5}. FT METAL 57 57 Zinc. {ECO:0000269|Ref.5}. FT METAL 177 177 Zinc. {ECO:0000269|Ref.5}. FT METAL 234 234 Zinc. {ECO:0000269|Ref.5}. FT CONFLICT 243 270 GAWDGQEPITIPVEGIEMGSLSMLSVQI -> RYVGWAGAN FT YHS (in Ref. 1; AAA71877). {ECO:0000305}. FT STRAND 17 21 {ECO:0000244|PDB:2PW6}. FT HELIX 33 44 {ECO:0000244|PDB:2PW6}. FT STRAND 49 66 {ECO:0000244|PDB:2PW6}. FT HELIX 95 105 {ECO:0000244|PDB:2PW6}. FT STRAND 110 115 {ECO:0000244|PDB:2PW6}. FT HELIX 121 130 {ECO:0000244|PDB:2PW6}. FT STRAND 138 144 {ECO:0000244|PDB:2PW6}. FT HELIX 149 159 {ECO:0000244|PDB:2PW6}. FT HELIX 160 165 {ECO:0000244|PDB:2PW6}. FT STRAND 167 173 {ECO:0000244|PDB:2PW6}. FT STRAND 184 186 {ECO:0000244|PDB:2PW6}. FT HELIX 192 202 {ECO:0000244|PDB:2PW6}. FT TURN 203 206 {ECO:0000244|PDB:2PW6}. FT HELIX 211 213 {ECO:0000244|PDB:2PW6}. FT TURN 215 217 {ECO:0000244|PDB:2PW6}. FT HELIX 219 221 {ECO:0000244|PDB:2PW6}. FT HELIX 225 228 {ECO:0000244|PDB:2PW6}. FT STRAND 230 232 {ECO:0000244|PDB:2PW6}. FT TURN 233 235 {ECO:0000244|PDB:2PW6}. FT HELIX 236 243 {ECO:0000244|PDB:2PW6}. FT STRAND 247 249 {ECO:0000244|PDB:2PW6}. FT TURN 260 262 {ECO:0000244|PDB:2PW6}. FT STRAND 268 270 {ECO:0000244|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 //