ID PCYB_PSEPA Reviewed; 302 AA. AC P22636; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 04-NOV-2008, entry version 44. DE RecName: Full=Protocatechuate 4,5-dioxygenase beta chain; DE EC=1.13.11.8; DE AltName: Full=4,5-PCD; GN Name=ligB; OS Pseudomonas paucimobilis (Sphingomonas paucimobilis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=13689; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-9. RC STRAIN=SYK-6; RX MEDLINE=90236935; PubMed=2185230; 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 CC protocatechuate. CC -!- CATALYTIC ACTIVITY: Protocatechuate + O(2) = 4-carboxy-2- CC hydroxymuconate semialdehyde. CC -!- COFACTOR: Fe(2+) ion. CC -!- SUBUNIT: Composed of two subunits (alpha and beta) in a 1:1 ratio. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M34835; AAA17728.1; -; Unassigned_DNA. DR PIR; B35271; B35271. DR PDB; 1B4U; X-ray; 2.20 A; B/D=1-302. DR PDB; 1BOU; X-ray; 2.20 A; B/D=1-302. DR PDBsum; 1B4U; -. DR PDBsum; 1BOU; -. DR GO; GO:0018579; F:protocatechuate 4,5-dioxygenase activity; IEA:EC. DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR004183; Xdiol_dOase_3B. DR Gene3D; G3DSA:3.40.830.10; Xdiol_dOase_3B; 1. DR Pfam; PF02900; LigB; 1. PE 1: Evidence at protein level; KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase; KW Direct protein sequencing; Iron; Oxidoreductase. FT CHAIN 1 302 Protocatechuate 4,5-dioxygenase beta FT chain. FT /FTId=PRO_0000085101. FT STRAND 3 10 FT HELIX 14 21 FT TURN 28 30 FT HELIX 31 44 FT TURN 47 49 FT STRAND 52 58 FT STRAND 62 64 FT STRAND 69 76 FT STRAND 78 81 FT STRAND 87 90 FT HELIX 100 112 FT STRAND 118 122 FT HELIX 127 137 FT STRAND 144 152 FT STRAND 155 157 FT HELIX 162 177 FT STRAND 179 181 FT STRAND 184 190 FT TURN 200 203 FT HELIX 207 219 FT HELIX 221 224 FT HELIX 229 236 FT HELIX 240 243 FT HELIX 244 251 FT STRAND 257 268 FT STRAND 271 280 FT HELIX 281 283 FT STRAND 289 296 SQ SEQUENCE 302 AA; 33292 MW; 0552B3B0E59702E5 CRC64; MARVTTGITS SHIPALGAAI QTGTSDNDYW GPVFKGYQPI RDWIKQPGNM PDVVILVYND HASAFDMNII PTFAIGCAET FKPADEGWGP RPVPDVKGHP DLAWHIAQSL ILDEFDMTIM NQMDVDHGCT VPLSMIFGEP EEWPCKVIPF PVNVVTYPPP SGKRCFALGD SIRAAVESFP EDLNVHVWGT GGMSHQLQGP RAGLINKEFD LNFIDKLISD PEELSKMPHI QYLRESGSEG VELVMWLIMR GALPEKVRDL YTFYHIPASN TALGAMILQP EETAGTPLEP RKVMSGHSLA QA //