ID   AMNB_PSESP              Reviewed;         305 AA.
AC   O33477;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=2-aminophenol 1,6-dioxygenase beta subunit;
DE            EC=1.13.11.74;
GN   Name=amnB;
OS   Pseudomonas sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, FUNCTION,
RP   CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP   SUBSTRATE SPECIFICITY, AND ACTIVITY REGULATION.
RC   STRAIN=AP-3;
RX   PubMed=9169437; DOI=10.1074/jbc.272.23.14727;
RA   Takenaka S., Murakami S., Shinke R., Hatakeyama K., Yukawa H., Aoki K.;
RT   "Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas
RT   species AP-3 growing on 2-aminophenol and catalytic properties of the
RT   purified enzyme.";
RL   J. Biol. Chem. 272:14727-14732(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AP-3;
RX   PubMed=11081795; DOI=10.1007/s002030000203;
RA   Takenaka S., Murakami S., Kim Y.J., Aoki K.;
RT   "Complete nucleotide sequence and functional analysis of the genes for 2-
RT   aminophenol metabolism from Pseudomonas sp. AP-3.";
RL   Arch. Microbiol. 174:265-272(2000).
CC   -!- FUNCTION: Component of the 2-aminophenol 1,6-dioxygenase complex that
CC       catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic
CC       6-semialdehyde. AmnB seems to be the catalytic subunit of the complex.
CC       The enzyme is also active toward 2-amino-p-cresol, 6-amino-m-cresol, 2-
CC       amino-m-cresol, 2-amino-4,5-dimethylphenol, 2-amino-4-chlorophenol, and
CC       catechol. {ECO:0000269|PubMed:9169437}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-aminophenol + O2 = 2-aminomuconate 6-semialdehyde;
CC         Xref=Rhea:RHEA:26305, ChEBI:CHEBI:15379, ChEBI:CHEBI:18112,
CC         ChEBI:CHEBI:77634; EC=1.13.11.74;
CC         Evidence={ECO:0000269|PubMed:9169437};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:9169437};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:9169437};
CC   -!- ACTIVITY REGULATION: Strongly inhibited by CuSO(4), FeCl(3),
CC       K(3)[Fe(CN)(6)], AgNO3, HgCl(2) and MnCl(2).
CC       {ECO:0000269|PubMed:9169437}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=46.7 uM for 2-aminophenol {ECO:0000269|PubMed:9169437};
CC         Vmax=0.1 umol/sec/mg enzyme {ECO:0000269|PubMed:9169437};
CC   -!- SUBUNIT: Heterotetramer of 2 alpha and 2 beta subunits.
CC       {ECO:0000269|PubMed:9169437}.
CC   -!- SIMILARITY: Belongs to the LigB/MhpB extradiol dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AB020521; BAB03531.1; -; Genomic_DNA.
DR   AlphaFoldDB; O33477; -.
DR   SMR; O33477; -.
DR   KEGG; ag:BAB03531; -.
DR   BioCyc; MetaCyc:MON-14740; -.
DR   SABIO-RK; O33477; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07372; 2A5CPDO_B; 1.
DR   InterPro; IPR034943; 2A5CPDO_B.
DR   InterPro; IPR004183; Xdiol_dOase_suB.
DR   Pfam; PF02900; LigB; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing;
KW   Iron; Metal-binding; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9169437"
FT   CHAIN           2..305
FT                   /note="2-aminophenol 1,6-dioxygenase beta subunit"
FT                   /id="PRO_0000383022"
FT   BINDING         14
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  34441 MW;  321A2570D7A61F67 CRC64;
     MANGEIISGF IAPHPPHLVY GENPPQNEPK STGGWEQLRW AYERARASIE ELKPDVLLVH
     SPHWITSVGH HFIGVDHLQG RSVDPIFPNL FRFDYSINFD VELSEACCEE GRKAGLVTKM
     MRNPRFRPDY GTITTLHMIR PQWDIPVVSI SANNTPYYLS MEEGLGEMDV LGKATREAIL
     KSGKRAVLLA SNTLSHWHFH EEPVPPEDMS KEHPQTKIGY EWDMRMIELM RQGRMEEVFQ
     LLPQFIEEAF AEVKSGAFTW MHAAMQYPNL PAELHGYGTV IGTGNAVVEW NLVKAGLARV
     AGKAA