ID   PCYB_SPHSK              Reviewed;         302 AA.
AC   P22636;
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 beta chain;
DE            EC=1.13.11.8;
DE   AltName: Full=4,5-PCD;
GN   Name=ligB;
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 1-9.
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; 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   AlphaFoldDB; P22636; -.
DR   SMR; P22636; -.
DR   IntAct; P22636; 1.
DR   STRING; 627192.SLG_12500; -.
DR   KEGG; ag:AAA17728; -.
DR   BioCyc; MetaCyc:MONOMER-15117; -.
DR   EvolutionaryTrace; P22636; -.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
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; cd07364; PCA_45_Dioxygenase_B; 1.
DR   Gene3D; 3.40.830.10; LigB-like; 1.
DR   InterPro; IPR034937; PCA_45_Dioxygenase_B.
DR   InterPro; IPR004183; Xdiol_dOase_suB.
DR   Pfam; PF02900; LigB; 1.
DR   SUPFAM; SSF53213; LigB-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase;
KW   Direct protein sequencing; Iron; Oxidoreductase.
FT   CHAIN           1..302
FT                   /note="Protocatechuate 4,5-dioxygenase beta chain"
FT                   /id="PRO_0000085101"
FT   STRAND          3..10
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   HELIX           14..21
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   TURN            28..30
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   HELIX           31..44
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   STRAND          52..58
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   STRAND          69..76
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   HELIX           100..112
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   STRAND          118..122
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   HELIX           127..137
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   STRAND          144..152
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   HELIX           162..177
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   STRAND          184..190
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   TURN            200..203
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   HELIX           207..219
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   HELIX           221..224
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   HELIX           229..236
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   HELIX           240..243
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   HELIX           244..251
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   STRAND          257..268
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   STRAND          271..280
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   HELIX           281..283
FT                   /evidence="ECO:0007829|PDB:1B4U"
FT   STRAND          289..296
FT                   /evidence="ECO:0007829|PDB:1B4U"
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
//