ID YGID_ECOLI Reviewed; 262 AA. AC P24197; Q2M9G1; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 24-NOV-2009, sequence version 3. DT 16-MAR-2016, entry version 117. 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; Enterobacteriales; 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: L-dopa + O(2) = 4-(L-alanin-3-yl)-2-hydroxy- CC cis,cis-muconate 6-semialdehyde. {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 -!- SEQUENCE CAUTION: CC Sequence=AAA69207.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC Sequence=AAA71877.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC Sequence=BAE77095.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; 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; ALT_INIT; Genomic_DNA. DR EMBL; U28377; AAA69207.1; ALT_INIT; Genomic_DNA. DR EMBL; U00096; AAC76075.2; -; Genomic_DNA. DR EMBL; AP009048; BAE77095.1; ALT_INIT; Genomic_DNA. DR PIR; E65091; E65091. DR RefSeq; NP_417511.2; NC_000913.3. DR RefSeq; WP_001320780.1; NZ_LN832404.1. DR PDB; 2PW6; X-ray; 2.27 A; A=1-262. DR PDBsum; 2PW6; -. DR ProteinModelPortal; P24197; -. DR SMR; P24197; 5-262. DR BioGrid; 4263035; 3. DR IntAct; P24197; 3. DR STRING; 511145.b3039; -. DR EPD; P24197; -. DR PaxDb; P24197; -. DR EnsemblBacteria; AAC76075; AAC76075; b3039. DR EnsemblBacteria; BAE77095; BAE77095; BAE77095. DR GeneID; 946447; -. DR KEGG; ecj:JW3007; -. DR KEGG; eco:b3039; -. DR PATRIC; 32121488; VBIEscCol129921_3131. 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 OrthoDB; EOG6JDW8T; -. DR PhylomeDB; P24197; -. DR BioCyc; EcoCyc:EG11166-MONOMER; -. DR BioCyc; ECOL316407:JW3007-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:0005886; C:plasma membrane; 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 Gene3D; 3.40.830.10; -; 1. DR InterPro; IPR014436; Extradiol_dOase_DODA. DR InterPro; IPR004183; Xdiol_dOase_suB. DR Pfam; PF02900; LigB; 1. DR PIRSF; PIRSF006157; Doxgns_DODA; 1. DR SUPFAM; SSF53213; SSF53213; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Dioxygenase; KW Metal-binding; Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1 262 4,5-DOPA dioxygenase extradiol. FT /FTId=PRO_0000169405. FT METAL 13 13 Zinc. {ECO:0000269|Ref.5}. FT METAL 48 48 Zinc. {ECO:0000269|Ref.5}. FT METAL 168 168 Zinc. {ECO:0000269|Ref.5}. FT METAL 225 225 Zinc. {ECO:0000269|Ref.5}. FT CONFLICT 234 261 GAWDGQEPITIPVEGIEMGSLSMLSVQI -> RYVGWAGAN FT YHS (in Ref. 1; AAA71877). {ECO:0000305}. FT STRAND 8 12 {ECO:0000244|PDB:2PW6}. FT HELIX 24 35 {ECO:0000244|PDB:2PW6}. FT STRAND 40 57 {ECO:0000244|PDB:2PW6}. FT HELIX 86 96 {ECO:0000244|PDB:2PW6}. FT STRAND 101 106 {ECO:0000244|PDB:2PW6}. FT HELIX 112 121 {ECO:0000244|PDB:2PW6}. FT STRAND 129 135 {ECO:0000244|PDB:2PW6}. FT HELIX 140 150 {ECO:0000244|PDB:2PW6}. FT HELIX 151 156 {ECO:0000244|PDB:2PW6}. FT STRAND 158 164 {ECO:0000244|PDB:2PW6}. FT STRAND 175 177 {ECO:0000244|PDB:2PW6}. FT HELIX 183 193 {ECO:0000244|PDB:2PW6}. FT TURN 194 197 {ECO:0000244|PDB:2PW6}. FT HELIX 202 204 {ECO:0000244|PDB:2PW6}. FT TURN 206 208 {ECO:0000244|PDB:2PW6}. FT HELIX 210 212 {ECO:0000244|PDB:2PW6}. FT HELIX 216 219 {ECO:0000244|PDB:2PW6}. FT STRAND 221 223 {ECO:0000244|PDB:2PW6}. FT TURN 224 226 {ECO:0000244|PDB:2PW6}. FT HELIX 227 234 {ECO:0000244|PDB:2PW6}. FT STRAND 238 240 {ECO:0000244|PDB:2PW6}. FT TURN 251 253 {ECO:0000244|PDB:2PW6}. FT STRAND 259 261 {ECO:0000244|PDB:2PW6}. SQ SEQUENCE 262 AA; 28892 MW; 7CFF9150AD49D50C CRC64; MSSTRMPALF LGHGSPMNVL EDNLYTRSWQ KLGMTLPRPQ AIVVVSAHWF TRGTGVTAME TPPTIHDFGG FPQALYDTHY PAPGSPALAQ RLVELLAPIP VTLDKEAWGF DHGSWGVLIK MYPDADIPMV QLSIDSSKPA AWHFEMGRKL AALRDEGIML VASGNVVHNL RTVKWHGDSS PYPWATSFNE YVKANLTWQG PVEQHPLVNY LDHEGGTLSN PTPEHYLPLL YVLGAWDGQE PITIPVEGIE MGSLSMLSVQ IG //