PCYB_SPHSK
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 03-AUG-2022, entry version 87.
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; Proteobacteria; 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.
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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:MON-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 InterPro; IPR034937; PCA_45_Dioxygenase_B.
DR InterPro; IPR004183; Xdiol_dOase_suB.
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
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
