ID PCYA_SPHSK Reviewed; 139 AA. AC P22635; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 13-SEP-2023, entry version 90. DE RecName: Full=Protocatechuate 4,5-dioxygenase alpha chain; DE EC=1.13.11.8; DE AltName: Full=4,5-PCD; GN Name=ligA; OS Sphingobium sp. (strain NBRC 103272 / SYK-6). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=627192; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-34. RC STRAIN=NBRC 103272 / SYK-6; RX PubMed=2185230; DOI=10.1128/jb.172.5.2704-2709.1990; RA Noda Y., Nishikawa S., Shiozuka K., Kadokura H., Nakajima H., Yoda K., RA Katayama Y., Morohoshi N., Haraguchi T., Yamasaki M.; RT "Molecular cloning of the protocatechuate 4,5-dioxygenase genes of RT Pseudomonas paucimobilis."; RL J. Bacteriol. 172:2704-2709(1990). CC -!- FUNCTION: Responsible for the aromatic ring fission of protocatechuate. CC -!- CATALYTIC ACTIVITY: CC Reaction=3,4-dihydroxybenzoate + O2 = 4-carboxy-2-hydroxy-cis,cis- CC muconate 6-semialdehyde + H(+); Xref=Rhea:RHEA:24044, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:36241, CC ChEBI:CHEBI:58358; EC=1.13.11.8; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC -!- SUBUNIT: Composed of two subunits (alpha and beta) in a 1:1 ratio. 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; M34835; AAA17727.1; -; Unassigned_DNA. DR PIR; A35271; A35271. DR RefSeq; WP_014075577.1; NC_015976.1. DR PDB; 1B4U; X-ray; 2.20 A; A/C=1-139. DR PDB; 1BOU; X-ray; 2.20 A; A/C=1-139. DR PDBsum; 1B4U; -. DR PDBsum; 1BOU; -. DR AlphaFoldDB; P22635; -. DR SMR; P22635; -. DR IntAct; P22635; 1. DR STRING; 627192.SLG_12510; -. DR KEGG; ag:AAA17727; -. DR OrthoDB; 7864521at2; -. DR BioCyc; MetaCyc:MONOMER-15116; -. DR EvolutionaryTrace; P22635; -. DR GO; GO:0018579; F:protocatechuate 4,5-dioxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW. DR CDD; cd07924; PCA_45_Doxase_A; 1. DR Gene3D; 1.10.700.10; Dioxygenase LigAB, LigA subunit; 1. DR InterPro; IPR036622; LigA_sf. DR InterPro; IPR014159; PCA_LigA. DR InterPro; IPR011986; Xdiol_dOase_LigA. DR NCBIfam; TIGR02792; PCA_ligA; 1. DR Pfam; PF07746; LigA; 1. DR SUPFAM; SSF48076; LigA subunit of an aromatic-ring-opening dioxygenase LigAB; 1. PE 1: Evidence at protein level; KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase; KW Direct protein sequencing; Iron; Oxidoreductase. FT CHAIN 1..139 FT /note="Protocatechuate 4,5-dioxygenase alpha chain" FT /id="PRO_0000085100" FT HELIX 10..15 FT /evidence="ECO:0007829|PDB:1B4U" FT HELIX 16..19 FT /evidence="ECO:0007829|PDB:1B4U" FT HELIX 28..33 FT /evidence="ECO:0007829|PDB:1B4U" FT HELIX 35..43 FT /evidence="ECO:0007829|PDB:1B4U" FT HELIX 47..55 FT /evidence="ECO:0007829|PDB:1B4U" FT HELIX 57..62 FT /evidence="ECO:0007829|PDB:1B4U" FT TURN 63..65 FT /evidence="ECO:0007829|PDB:1B4U" FT HELIX 68..76 FT /evidence="ECO:0007829|PDB:1B4U" FT HELIX 79..84 FT /evidence="ECO:0007829|PDB:1B4U" FT HELIX 89..98 FT /evidence="ECO:0007829|PDB:1B4U" FT HELIX 103..109 FT /evidence="ECO:0007829|PDB:1B4U" FT TURN 110..112 FT /evidence="ECO:0007829|PDB:1B4U" FT HELIX 115..123 FT /evidence="ECO:0007829|PDB:1B4U" FT TURN 135..137 FT /evidence="ECO:0007829|PDB:1B4U" SQ SEQUENCE 139 AA; 15549 MW; E6CFEF0499A3FD26 CRC64; MTEKKERIDV HAYLAEFDDI PGTRVFTAQR ARKGYNLNQF AMSLMKAENR ERFKADESAY LDEWNLTPAA KAAVLARDYN AMIDEGGNVY FLSKLFSTDG KSFQFAAGSM TGMTQEEYAQ MMIDGGRSPA GVRSIKGGY //