ID PCXB_PSEPU Reviewed; 239 AA. AC P00437; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 04-NOV-2026, entry version 138. DE RecName: Full=Protocatechuate 3,4-dioxygenase beta chain {ECO:0000303|PubMed:8407791}; DE EC=1.13.11.3 {ECO:0000269|PubMed:16101286, ECO:0000269|PubMed:8407791, ECO:0000269|PubMed:9485360}; DE AltName: Full=3,4-PCD {ECO:0000303|PubMed:8407791}; GN Name=pcaH {ECO:0000303|PubMed:8407791}; OS Pseudomonas putida (Arthrobacter siderocapsulatus). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY. RC STRAIN=ATCC 23975 / NCIMB 12602 / B-10 / Biotype A; RX PubMed=8407791; DOI=10.1128/jb.175.19.6194-6202.1993; RA Frazee R.W., Livingston D.M., Laporte D.C., Lipscomb J.D.; RT "Cloning, sequencing, and expression of the Pseudomonas putida RT protocatechuate 3,4-dioxygenase genes."; RL J. Bacteriol. 175:6194-6202(1993). RN [2] RP PROTEIN SEQUENCE OF 2-239. RX PubMed=115853; DOI=10.1093/oxfordjournals.jbchem.a132612; RA Iwaki M., Kagamiyama H., Nozaki M.; RT "The complete amino acid sequence of the beta-subunit of protocatechuate RT 3,4-dioxygenase from Pseudomonas aeruginosa."; RL J. Biochem. 86:1159-1162(1979). RN [3] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=3194022; DOI=10.1038/336403a0; RA Ohlendorf D.H., Lipscomb J.D., Weber P.C.; RT "Structure and assembly of protocatechuate 3,4-dioxygenase."; RL Nature 336:403-405(1988). RN [4] {ECO:0007744|PDB:2PCD} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH FE(3+), COFACTOR, AND SUBUNIT. RC STRAIN=ATCC 23975 / NCIMB 12602 / B-10 / Biotype A; RX PubMed=7990141; DOI=10.1006/jmbi.1994.1754; RA Ohlendorf D.H., Orville A.M., Lipscomb J.D.; RT "Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa RT at 2.15-A resolution."; RL J. Mol. Biol. 244:586-608(1994). RN [5] {ECO:0007744|PDB:3PCB, ECO:0007744|PDB:3PCC, ECO:0007744|PDB:3PCE, ECO:0007744|PDB:3PCF, ECO:0007744|PDB:3PCG, ECO:0007744|PDB:3PCH, ECO:0007744|PDB:3PCI} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH 3-HYDROXYBENZOATE AND FE(3+), RP COFACTOR, AND SUBUNIT. RC STRAIN=ATCC 23975 / NCIMB 12602 / B-10 / Biotype A; RX PubMed=9254599; DOI=10.1021/bi970468n; RA Orville A.M., Elango N., Lipscomb J.D., Ohlendorf D.H.; RT "Structures of competitive inhibitor complexes of protocatechuate 3,4- RT dioxygenase: multiple exogenous ligand binding orientations within the RT active site."; RL Biochemistry 36:10039-10051(1997). RN [6] {ECO:0007744|PDB:3PCA, ECO:0007744|PDB:3PCJ, ECO:0007744|PDB:3PCK, ECO:0007744|PDB:3PCL, ECO:0007744|PDB:3PCM} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH 3,4-DIHYDROXYBENZOATE AND FE(3+), RP COFACTOR, AND SUBUNIT. RC STRAIN=ATCC 23975 / NCIMB 12602 / B-10 / Biotype A; RX PubMed=9254600; DOI=10.1021/bi970469f; RA Orville A.M., Lipscomb J.D., Ohlendorf D.H.; RT "Crystal structures of substrate and substrate analog complexes of RT protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in RT response to substrate binding."; RL Biochemistry 36:10052-10066(1997). RN [7] {ECO:0007744|PDB:3PCN} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH FE(3+), COFACTOR, AND SUBUNIT. RC STRAIN=ATCC 23975 / NCIMB 12602 / B-10 / Biotype A; RX PubMed=9298971; DOI=10.1021/bi970691k; RA Elgren T.E., Orville A.M., Kelly K.A., Lipscomb J.D., Ohlendorf D.H., RA Que L. Jr.; RT "Crystal structure and resonance Raman studies of protocatechuate 3,4- RT dioxygenase complexed with 3,4-dihydroxyphenylacetate."; RL Biochemistry 36:11504-11513(1997). RN [8] {ECO:0007744|PDB:3PCD} RP X-RAY CRYSTALLOGRAPHY OF MUTANT HIS-148 IN COMPLEX WITH FE(3+), FUNCTION, RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND RP MUTAGENESIS OF TYR-148. RX PubMed=9485360; DOI=10.1021/bi972047b; RA Frazee R.W., Orville A.M., Dolbeare K.B., Yu H., Ohlendorf D.H., RA Lipscomb J.D.; RT "The axial tyrosinate Fe3+ ligand in protocatechuate 3,4-dioxygenase RT influences substrate binding and product release: evidence for new reaction RT cycle intermediates."; RL Biochemistry 37:2131-2144(1998). RN [9] {ECO:0007744|PDB:1YKK, ECO:0007744|PDB:1YKL, ECO:0007744|PDB:1YKM, ECO:0007744|PDB:1YKN, ECO:0007744|PDB:1YKO, ECO:0007744|PDB:1YKP} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH 3,4-DIHYDROXYBENZOATE AND FE(3+), RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, RP SUBUNIT, AND MUTAGENESIS OF TYR-109. RX PubMed=16101286; DOI=10.1021/bi050902i; RA Valley M.P., Brown C.K., Burk D.L., Vetting M.W., Ohlendorf D.H., RA Lipscomb J.D.; RT "Roles of the equatorial tyrosyl iron ligand of protocatechuate 3,4- RT dioxygenase in catalysis."; RL Biochemistry 44:11024-11039(2005). RN [10] {ECO:0007744|PDB:3LKT, ECO:0007744|PDB:3LMX, ECO:0007744|PDB:3LXV} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH 3,4-DIHYDROXYBENZOATE AND FE(3+), RP COFACTOR, AND SUBUNIT. RA Purpero V.M., Valley M.P., Ohlendorf D.H., Lipscomb J.D., Burk D., RA Dolbeare K.B., Brown K.C.; RT "Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient RT Progress Through Catalysis."; RL Submitted (JAN-2010) to the PDB data bank. RN [11] {ECO:0007744|PDB:3MFL, ECO:0007744|PDB:3MI1, ECO:0007744|PDB:3MI5, ECO:0007744|PDB:3MV4, ECO:0007744|PDB:3MV6, ECO:0007744|PDB:3T63, ECO:0007744|PDB:3T67} RP X-RAY CRYSTALLOGRAPHY OF MUTANT HIS-148 AND TYR-163 IN COMPLEX WITH RP 3,4-DIHYDROXYBENZOATE AND FE(3+), COFACTOR, AND SUBUNIT. RA Purpero V.M., Lipscomb J.D.; RT "Axial Ligand Swapping In Double Mutant Maintains Intradiol-cleavage RT Chemistry in Protocatechuate 3,4-Dioxygenase."; RL Submitted (APR-2010) to the PDB data bank. RN [12] {ECO:0007744|PDB:4WHO, ECO:0007744|PDB:4WHP, ECO:0007744|PDB:4WHQ, ECO:0007744|PDB:4WHR, ECO:0007744|PDB:4WHS} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH 4-FLUOROCATECHOL AND FE(3+), RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND RP SUBUNIT. RX PubMed=25548185; DOI=10.1073/pnas.1419118112; RA Knoot C.J., Purpero V.M., Lipscomb J.D.; RT "Crystal structures of alkylperoxo and anhydride intermediates in an RT intradiol ring-cleaving dioxygenase."; RL Proc. Natl. Acad. Sci. U.S.A. 112:388-393(2015). CC -!- FUNCTION: Part of the protocatechuate 3,4-dioxygenase complex that CC catalyzes the oxidative cleavage of protocatechuate (3,4- CC dihydroxybenzoate) to 3-carboxy-cis,cis-muconate (PubMed:16101286, CC PubMed:9485360). Can also use 4-fluorocatechol as a substrate CC (PubMed:25548185). Plays an essential role in the utilization of CC numerous aromatic compounds via the beta-ketoadipate pathway CC (Probable). {ECO:0000269|PubMed:16101286, ECO:0000269|PubMed:25548185, CC ECO:0000269|PubMed:9485360, ECO:0000305|PubMed:8407791}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate + 2 CC H(+); Xref=Rhea:RHEA:10084, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:36241, ChEBI:CHEBI:57496; EC=1.13.11.3; CC Evidence={ECO:0000269|PubMed:16101286, ECO:0000269|PubMed:8407791, CC ECO:0000269|PubMed:9485360}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10085; CC Evidence={ECO:0000269|PubMed:16101286, ECO:0000269|PubMed:8407791, CC ECO:0000269|PubMed:9485360}; CC -!- COFACTOR: CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; CC Evidence={ECO:0000269|PubMed:16101286, ECO:0000269|PubMed:25548185, CC ECO:0000269|PubMed:7990141, ECO:0000269|PubMed:8407791, CC ECO:0000269|PubMed:9254599, ECO:0000269|PubMed:9254600, CC ECO:0000269|PubMed:9298971, ECO:0000269|PubMed:9485360, CC ECO:0000269|Ref.10, ECO:0000269|Ref.11}; CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000269|PubMed:16101286, CC ECO:0000269|PubMed:25548185, ECO:0000269|PubMed:7990141, CC ECO:0000269|PubMed:8407791, ECO:0000269|PubMed:9254599, CC ECO:0000269|PubMed:9254600, ECO:0000269|PubMed:9298971, CC ECO:0000269|PubMed:9485360, ECO:0000269|Ref.10, ECO:0000269|Ref.11}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=450 nm; CC Note=Absorption spectra results from ligand-to-metal charge transfer CC between the two tyrosinate ligands and Fe(3+), with a shoulder peak CC at 500nm. {ECO:0000269|PubMed:16101286}; CC Kinetic parameters: CC KM=30 uM for 3,4-dihydroxybenzoate (at pH 8.5 and 25 degrees Celsius CC for the native enzyme) {ECO:0000269|PubMed:8407791, CC ECO:0000269|PubMed:9485360}; CC KM=29 uM for 3,4-dihydroxybenzoate (at pH 8.5 and 25 degrees Celsius CC for the recombinant enzyme) {ECO:0000269|PubMed:8407791, CC ECO:0000269|PubMed:9485360}; CC KM=40 uM for O(2) (at pH 8.5 and 25 degrees Celsius for the native CC enzyme) {ECO:0000269|PubMed:9485360}; CC KM=56 uM for O(2) (at pH 8.5 and 25 degrees Celsius for the CC recombinant enzyme) {ECO:0000269|PubMed:9485360}; CC KM=240 uM for 4-fluorocatechol (at pH 7.5 and 22 degrees Celsius) CC {ECO:0000269|PubMed:25548185}; CC KM=270 uM for O(2) (at pH 7.5 and 22 degrees Celsius) CC {ECO:0000269|PubMed:25548185}; CC Note=kcat is 70 sec(-1) with 3,4-dihydroxybenzoate as substrate (at CC pH 8.5 and 25 degrees Celsius for the native enzyme) CC (PubMed:9485360). kcat is 68 sec(-1) with 3,4-dihydroxybenzoate as CC substrate (at pH 8.5 and 25 degrees Celsius for the recombinant CC enzyme) (PubMed:9485360). kcat is 100 sec(-1) with CC 3,4-dihydroxybenzoate as substrate (at pH 8.5 and 25 degrees Celsius) CC (PubMed:16101286). kcat is 81.4 sec(-1) with 3,4-dihydroxybenzoate as CC substrate (at pH 7.5 and 22 degrees Celsius) (PubMed:25548185). kcat CC is 106 sec(-1) with 3,4-dihydroxybenzoate as substrate (at pH 8.5 and CC 22 degrees Celsius) (PubMed:25548185). kcat is 53.5 sec(-1) with CC 3,4-dihydroxybenzoate as substrate (at pH 6.5 and 22 degrees Celsius) CC (PubMed:25548185). kcat is 0.708 sec(-1) with 4-fluorocatechol as CC substrate (at pH 7.5 and 22 degrees Celsius) (PubMed:25548185). kcat CC is 0.507 sec(-1) with 4-fluorocatechol as substrate (at pH 8.5 and 22 CC degrees Celsius) (PubMed:25548185). kcat is 0.698 sec(-1) with CC 4-fluorocatechol as substrate (at pH 6.5 and 22 degrees Celsius) CC (PubMed:25548185). {ECO:0000269|PubMed:16101286, CC ECO:0000269|PubMed:25548185, ECO:0000269|PubMed:9485360}; CC -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway; 3- CC carboxy-cis,cis-muconate from 3,4-dihydroxybenzoate: step 1/1. CC {ECO:0000305|PubMed:8407791}. CC -!- SUBUNIT: Heteromultimer composed of 12 alpha and 12 beta chains CC (PubMed:16101286, PubMed:25548185, PubMed:3194022, PubMed:7990141, CC PubMed:9254599, PubMed:9254600, PubMed:9298971, PubMed:9485360, Ref.10, CC Ref.11). The beta subunit contains most of the catalytic machinery and CC is primarily responsible for enzymatic activity, although the active CC site is formed at the alpha-beta interface (Probable). CC {ECO:0000269|PubMed:16101286, ECO:0000269|PubMed:25548185, CC ECO:0000269|PubMed:3194022, ECO:0000269|PubMed:7990141, CC ECO:0000269|PubMed:9254599, ECO:0000269|PubMed:9254600, CC ECO:0000269|PubMed:9298971, ECO:0000269|PubMed:9485360, CC ECO:0000269|Ref.10, ECO:0000269|Ref.11, ECO:0000305|PubMed:3194022}. CC -!- MISCELLANEOUS: According to protocatechuate 3,4-dioxygenase numbering CC convention, the alpha chain is started from residue 1, whereas the beta CC chain is numbered beginning from residue 301, if the N-terminal CC methionine is excised. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family. CC {ECO:0000305}. CC -!- CAUTION: Strain ATCC 23975 was originally classified as being from CC Pseudomonas aeruginosa. {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; L14836; AAB41024.1; -; Genomic_DNA. DR PIR; A36930; DAPSBA. DR RefSeq; WP_274092290.1; NZ_JANHLF010000009.1. DR PDB; 1YKK; X-ray; 2.06 A; B/D/F/H/J/L=2-239. DR PDB; 1YKL; X-ray; 2.25 A; B/D/F/H/J/L=2-239. DR PDB; 1YKM; X-ray; 2.22 A; B/D/F/H/J/L=2-239. DR PDB; 1YKN; X-ray; 2.06 A; B/D/F/H/J/L=2-239. DR PDB; 1YKO; X-ray; 2.54 A; B/D/F/H/J/L=2-239. DR PDB; 1YKP; X-ray; 2.41 A; B/D/F/H/J/L=2-239. DR PDB; 2PCD; X-ray; 2.15 A; M/N/O/P/Q/R=2-239. DR PDB; 3LKT; X-ray; 1.65 A; M/N/O/P/Q/R=2-239. DR PDB; 3LMX; X-ray; 2.20 A; M/N/O=2-239. DR PDB; 3LXV; X-ray; 1.90 A; M/N/O=2-239. DR PDB; 3MFL; X-ray; 1.78 A; M/N/O=2-239. DR PDB; 3MI1; X-ray; 1.74 A; M/N/O=2-239. DR PDB; 3MI5; X-ray; 1.78 A; M/N/O/P/Q/R=2-239. DR PDB; 3MV4; X-ray; 1.59 A; M/N/O=2-239. DR PDB; 3MV6; X-ray; 1.86 A; M/N/O=2-239. DR PDB; 3PCA; X-ray; 2.20 A; M/N/O/P/Q/R=2-239. DR PDB; 3PCB; X-ray; 2.19 A; M/N/O/P/Q/R=2-239. DR PDB; 3PCC; X-ray; 1.98 A; M/N/O/P/Q/R=2-239. DR PDB; 3PCD; X-ray; 2.10 A; M/N/O/P/Q/R=2-239. DR PDB; 3PCE; X-ray; 2.06 A; M/N/O/P/Q/R=2-239. DR PDB; 3PCF; X-ray; 2.15 A; M/N/O/P/Q/R=2-239. DR PDB; 3PCG; X-ray; 1.96 A; M/N/O/P/Q/R=2-239. DR PDB; 3PCH; X-ray; 2.05 A; M/N/O/P/Q/R=2-239. DR PDB; 3PCI; X-ray; 2.21 A; M/N/O/P/Q/R=2-239. DR PDB; 3PCJ; X-ray; 2.13 A; M/N/O/P/Q/R=2-239. DR PDB; 3PCK; X-ray; 2.13 A; M/N/O/P/Q/R=2-239. DR PDB; 3PCL; X-ray; 2.15 A; M/N/O/P/Q/R=2-239. DR PDB; 3PCM; X-ray; 2.25 A; M/N/O/P/Q/R=2-239. DR PDB; 3PCN; X-ray; 2.40 A; M/N/O/P/Q/R=2-239. DR PDB; 3T63; X-ray; 1.54 A; M/N/O=2-239. DR PDB; 3T67; X-ray; 1.67 A; M/N/O=2-239. DR PDB; 4WHO; X-ray; 1.83 A; B/D/F=2-239. DR PDB; 4WHP; X-ray; 1.54 A; B/D/F=2-239. DR PDB; 4WHQ; X-ray; 1.78 A; B/D/F=2-239. DR PDB; 4WHR; X-ray; 1.58 A; B/D/F=2-239. DR PDB; 4WHS; X-ray; 1.35 A; B/D/F=2-239. DR AlphaFoldDB; P00437; -. DR MDRepo; P00437; -. DR SMR; P00437; -. DR IntAct; P00437; 1. DR DrugBank; DB01702; 2-(3,4-Dihydroxyphenyl)Acetic Acid. DR eggNOG; COG3485; Bacteria. DR BioCyc; MetaCyc:MONOMER-3185; -. DR UniPathway; UPA00157; UER00264. DR EvolutionaryTrace; P00437; -. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0018578; F:protocatechuate 3,4-dioxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IEA:InterPro. DR GO; GO:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway. DR CDD; cd03464; 3_4-PCD_beta; 1. DR FunFam; 2.60.130.10:FF:000002; Protocatechuate 3,4-dioxygenase beta chain; 1. DR Gene3D; 2.60.130.10; Aromatic compound dioxygenase; 1. DR InterPro; IPR000627; Intradiol_dOase_C. DR InterPro; IPR015889; Intradiol_dOase_core. DR InterPro; IPR050770; Intradiol_RC_Dioxygenase. DR InterPro; IPR024756; PCDO_beta_N. DR InterPro; IPR012785; Protocat_dOase_b. DR NCBIfam; TIGR02422; protocat_beta; 1. DR PANTHER; PTHR33711; DIOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02910)-RELATED; 1. DR PANTHER; PTHR33711:SF10; INTRADIOL RING-CLEAVAGE DIOXYGENASES DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00775; Dioxygenase_C; 1. DR Pfam; PF12391; PCDO_beta_N; 1. DR SUPFAM; SSF49482; Aromatic compound dioxygenase; 1. DR PROSITE; PS00083; INTRADIOL_DIOXYGENAS; 1. PE 1: Evidence at protein level; KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase; KW Direct protein sequencing; Iron; Metal-binding; Oxidoreductase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:115853" FT CHAIN 2..239 FT /note="Protocatechuate 3,4-dioxygenase beta chain" FT /id="PRO_0000085098" FT BINDING 25 FT /ligand="3,4-dihydroxybenzoate" FT /ligand_id="ChEBI:CHEBI:36241" FT /evidence="ECO:0000269|PubMed:16101286, FT ECO:0000269|PubMed:9254599, ECO:0000269|PubMed:9254600, FT ECO:0007744|PDB:1YKL, ECO:0007744|PDB:1YKN, FT ECO:0007744|PDB:1YKP, ECO:0007744|PDB:3LMX, FT ECO:0007744|PDB:3PCA, ECO:0007744|PDB:3PCB" FT BINDING 109 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:25548185, FT ECO:0000269|PubMed:7990141, ECO:0000269|PubMed:9254599, FT ECO:0000269|Ref.10, ECO:0000269|Ref.11, FT ECO:0007744|PDB:2PCD, ECO:0007744|PDB:3LKT, FT ECO:0007744|PDB:3LMX, ECO:0007744|PDB:3LXV, FT ECO:0007744|PDB:3MFL, ECO:0007744|PDB:3MI5, FT ECO:0007744|PDB:3MV4, ECO:0007744|PDB:3MV6, FT ECO:0007744|PDB:3PCA, ECO:0007744|PDB:3PCB, FT ECO:0007744|PDB:3PCC, ECO:0007744|PDB:3PCD, FT ECO:0007744|PDB:3PCE, ECO:0007744|PDB:3PCF, FT ECO:0007744|PDB:3PCG, ECO:0007744|PDB:3PCH, FT ECO:0007744|PDB:3PCI, ECO:0007744|PDB:3PCJ, FT ECO:0007744|PDB:3PCK, ECO:0007744|PDB:3PCL, FT ECO:0007744|PDB:3PCM, ECO:0007744|PDB:3PCN, FT ECO:0007744|PDB:3T63, ECO:0007744|PDB:3T67, FT ECO:0007744|PDB:4WHO, ECO:0007744|PDB:4WHP, FT ECO:0007744|PDB:4WHQ, ECO:0007744|PDB:4WHR, FT ECO:0007744|PDB:4WHS" FT BINDING 148 FT /ligand="3,4-dihydroxybenzoate" FT /ligand_id="ChEBI:CHEBI:36241" FT /evidence="ECO:0000269|PubMed:16101286, FT ECO:0007744|PDB:1YKL, ECO:0007744|PDB:1YKN, FT ECO:0007744|PDB:1YKP" FT BINDING 148 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:16101286, FT ECO:0000269|PubMed:25548185, ECO:0000269|PubMed:7990141, FT ECO:0000269|PubMed:9254599, ECO:0000269|Ref.11, FT ECO:0007744|PDB:1YKK, ECO:0007744|PDB:1YKL, FT ECO:0007744|PDB:1YKM, ECO:0007744|PDB:1YKN, FT ECO:0007744|PDB:1YKO, ECO:0007744|PDB:1YKP, FT ECO:0007744|PDB:2PCD, ECO:0007744|PDB:3PCB, FT ECO:0007744|PDB:3PCC, ECO:0007744|PDB:3PCE, FT ECO:0007744|PDB:3PCF, ECO:0007744|PDB:3PCG, FT ECO:0007744|PDB:3PCH, ECO:0007744|PDB:3PCI, FT ECO:0007744|PDB:3T67, ECO:0007744|PDB:4WHO, FT ECO:0007744|PDB:4WHP, ECO:0007744|PDB:4WHQ, FT ECO:0007744|PDB:4WHR, ECO:0007744|PDB:4WHS" FT BINDING 158 FT /ligand="3,4-dihydroxybenzoate" FT /ligand_id="ChEBI:CHEBI:36241" FT /evidence="ECO:0000269|PubMed:16101286, FT ECO:0000269|PubMed:9254599, ECO:0000269|PubMed:9254600, FT ECO:0000269|Ref.10, ECO:0000269|Ref.11, FT ECO:0007744|PDB:1YKL, ECO:0007744|PDB:1YKN, FT ECO:0007744|PDB:1YKP, ECO:0007744|PDB:3LMX, FT ECO:0007744|PDB:3MV6, ECO:0007744|PDB:3PCA, FT ECO:0007744|PDB:3PCB" FT BINDING 161 FT /ligand="3,4-dihydroxybenzoate" FT /ligand_id="ChEBI:CHEBI:36241" FT /evidence="ECO:0000305|Ref.10, ECO:0007744|PDB:3LMX" FT BINDING 161 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:16101286, FT ECO:0000269|PubMed:25548185, ECO:0000269|PubMed:7990141, FT ECO:0000269|PubMed:9254599, ECO:0000269|PubMed:9254600, FT ECO:0000269|PubMed:9298971, ECO:0000269|PubMed:9485360, FT ECO:0000269|Ref.10, ECO:0000269|Ref.11, FT ECO:0007744|PDB:1YKK, ECO:0007744|PDB:1YKL, FT ECO:0007744|PDB:1YKM, ECO:0007744|PDB:1YKN, FT ECO:0007744|PDB:1YKO, ECO:0007744|PDB:1YKP, FT ECO:0007744|PDB:2PCD, ECO:0007744|PDB:3LKT, FT ECO:0007744|PDB:3LMX, ECO:0007744|PDB:3LXV, FT ECO:0007744|PDB:3MFL, ECO:0007744|PDB:3MI5, FT ECO:0007744|PDB:3MV4, ECO:0007744|PDB:3MV6, FT ECO:0007744|PDB:3PCA, ECO:0007744|PDB:3PCB, FT ECO:0007744|PDB:3PCC, ECO:0007744|PDB:3PCD, FT ECO:0007744|PDB:3PCE, ECO:0007744|PDB:3PCF, FT ECO:0007744|PDB:3PCG, ECO:0007744|PDB:3PCH, FT ECO:0007744|PDB:3PCJ, ECO:0007744|PDB:3PCK, FT ECO:0007744|PDB:3PCL, ECO:0007744|PDB:3PCM, FT ECO:0007744|PDB:3PCN, ECO:0007744|PDB:3T63, FT ECO:0007744|PDB:3T67, ECO:0007744|PDB:4WHO, FT ECO:0007744|PDB:4WHP, ECO:0007744|PDB:4WHQ, FT ECO:0007744|PDB:4WHR, ECO:0007744|PDB:4WHS" FT BINDING 163 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:16101286, FT ECO:0000269|PubMed:25548185, ECO:0000269|PubMed:7990141, FT ECO:0000269|PubMed:9254599, ECO:0000269|PubMed:9254600, FT ECO:0000269|PubMed:9298971, ECO:0000269|PubMed:9485360, FT ECO:0000269|Ref.10, ECO:0000269|Ref.11, FT ECO:0007744|PDB:1YKK, ECO:0007744|PDB:1YKL, FT ECO:0007744|PDB:1YKM, ECO:0007744|PDB:1YKN, FT ECO:0007744|PDB:1YKO, ECO:0007744|PDB:1YKP, FT ECO:0007744|PDB:2PCD, ECO:0007744|PDB:3LKT, FT ECO:0007744|PDB:3LMX, ECO:0007744|PDB:3LXV, FT ECO:0007744|PDB:3PCA, ECO:0007744|PDB:3PCB, FT ECO:0007744|PDB:3PCC, ECO:0007744|PDB:3PCD, FT ECO:0007744|PDB:3PCE, ECO:0007744|PDB:3PCF, FT ECO:0007744|PDB:3PCG, ECO:0007744|PDB:3PCH, FT ECO:0007744|PDB:3PCJ, ECO:0007744|PDB:3PCK, FT ECO:0007744|PDB:3PCL, ECO:0007744|PDB:3PCM, FT ECO:0007744|PDB:3PCN, ECO:0007744|PDB:3T67, FT ECO:0007744|PDB:4WHO, ECO:0007744|PDB:4WHP, FT ECO:0007744|PDB:4WHQ, ECO:0007744|PDB:4WHR, FT ECO:0007744|PDB:4WHS" FT BINDING 178 FT /ligand="3,4-dihydroxybenzoate" FT /ligand_id="ChEBI:CHEBI:36241" FT /evidence="ECO:0000269|PubMed:16101286, FT ECO:0000269|PubMed:9254599, ECO:0007744|PDB:1YKL, FT ECO:0007744|PDB:1YKN, ECO:0007744|PDB:1YKP, FT ECO:0007744|PDB:3PCB" FT MUTAGEN 109 FT /note="Y->H,E,C,F: Abolishes direct ligation of this FT residue to Fe(3+) but instead interacts through the FT solvent, which results in significant shifts in the FT ligand-to-metal charge transfer spectra. Reduces the FT turnover rate by more than 700-fold, probably due to the FT inability of the axial Tyr-148 to dissociate from Fe(3+) FT during the catalytic cycle." FT /evidence="ECO:0000269|PubMed:16101286" FT MUTAGEN 148 FT /note="Y->H: Abolishes coordination of this residue to FT Fe(3+). Alters the rate of substrate binding and product FT release, which increases the affinity for FT 3,4-dihydroxybenzoate and O(2) by about 10-fold, and FT reduces the turnover rate by about 600-fold." FT /evidence="ECO:0000269|PubMed:9485360" FT CONFLICT 62 FT /note="H -> D (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 70 FT /note="N -> D (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 72 FT /note="Missing (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 218 FT /note="D -> N (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 7..9 FT /evidence="ECO:0007829|PDB:4WHS" FT TURN 14..16 FT /evidence="ECO:0007829|PDB:4WHS" FT HELIX 26..28 FT /evidence="ECO:0007829|PDB:4WHS" FT TURN 29..31 FT /evidence="ECO:0007829|PDB:4WHR" FT HELIX 44..47 FT /evidence="ECO:0007829|PDB:4WHS" FT HELIX 55..58 FT /evidence="ECO:0007829|PDB:3T63" FT TURN 59..62 FT /evidence="ECO:0007829|PDB:4WHS" FT TURN 64..68 FT /evidence="ECO:0007829|PDB:4WHS" FT STRAND 70..72 FT /evidence="ECO:0007829|PDB:4WHS" FT STRAND 78..87 FT /evidence="ECO:0007829|PDB:4WHS" FT STRAND 97..101 FT /evidence="ECO:0007829|PDB:4WHS" FT STRAND 127..131 FT /evidence="ECO:0007829|PDB:4WHS" FT STRAND 136..143 FT /evidence="ECO:0007829|PDB:4WHS" FT HELIX 144..147 FT /evidence="ECO:0007829|PDB:4WHS" FT STRAND 148..153 FT /evidence="ECO:0007829|PDB:4WHS" FT STRAND 156..158 FT /evidence="ECO:0007829|PDB:4WHS" FT STRAND 160..166 FT /evidence="ECO:0007829|PDB:4WHS" FT TURN 171..173 FT /evidence="ECO:0007829|PDB:4WHS" FT STRAND 175..181 FT /evidence="ECO:0007829|PDB:4WHS" FT HELIX 187..189 FT /evidence="ECO:0007829|PDB:4WHS" FT HELIX 193..195 FT /evidence="ECO:0007829|PDB:4WHS" FT HELIX 199..203 FT /evidence="ECO:0007829|PDB:4WHS" FT STRAND 206..209 FT /evidence="ECO:0007829|PDB:4WHS" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:4WHS" FT TURN 216..218 FT /evidence="ECO:0007829|PDB:4WHS" FT STRAND 219..223 FT /evidence="ECO:0007829|PDB:4WHS" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:4WHS" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:4WHS" SQ SEQUENCE 239 AA; 26793 MW; 8F8CC293B6E434CE CRC64; MPAQDNSRFV IRDRNWHPKA LTPDYKTSIA RSPRQALVSI PQSISETTGP NFSHLGFGAH DHDLLLNFNN GGLPIGERII VAGRVVDQYG KPVPNTLVEM WQANAGGRYR HKNDRYLAPL DPNFGGVGRC LTDSDGYYSF RTIKPGPYPW RNGPNDWRPA HIHFGISGPS IATKLITQLY FEGDPLIPMC PIVKSIANPE AVQQLIAKLD MNNANPMDCL AYRFDIVLRG QRKTHFENC //