PCYA_SPHSK
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 03-AUG-2022, entry version 86.
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; Proteobacteria; 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.
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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 BioCyc; MetaCyc:MON-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; -; 1.
DR InterPro; IPR036622; LigA_sf.
DR InterPro; IPR014159; PCA_LigA.
DR InterPro; IPR011986; Xdiol_dOase_LigA.
DR Pfam; PF07746; LigA; 1.
DR SUPFAM; SSF48076; SSF48076; 1.
DR TIGRFAMs; TIGR02792; PCA_ligA; 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
