ID   AMNA_PSESP              Reviewed;         271 AA.
AC   O33478;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=2-aminophenol 1,6-dioxygenase alpha subunit;
GN   Name=amnA;
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 2-30, FUNCTION, AND
RP   SUBUNIT.
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. AmnA seems to have a role in the stability of the
CC       complex. {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}.
CC   -!- CAUTION: In contrast to other members of the family, lacks the
CC       conserved iron-binding sites, suggesting it has no oxidoreductase
CC       activity. {ECO:0000305}.
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DR   EMBL; AB020521; BAB03532.1; -; Genomic_DNA.
DR   AlphaFoldDB; O33478; -.
DR   SMR; O33478; -.
DR   BioCyc; MetaCyc:MON-14739; -.
DR   SABIO-RK; O33478; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProt.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR004183; Xdiol_dOase_suB.
DR   Pfam; PF02900; LigB; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9169437"
FT   CHAIN           2..271
FT                   /note="2-aminophenol 1,6-dioxygenase alpha subunit"
FT                   /id="PRO_0000383021"
SQ   SEQUENCE   271 AA;  29416 MW;  096838E6BDD5587D CRC64;
     MTIVSAFLVP GSPLPHLRPD VKSWESFKVA MQNVGEKLRA SKPDVVLIYS TQWFAVLDEI
     WLTRQRSLDI HVDENWHEFG ELPYDIYSDV DLANACIESC RAAGVNARGA DYESFPIDTG
     TIVACNALKV GTSDLPVVVA SNNLYDDQAA TERLAALAVA CISEKGKRIA VIGVGGLSGS
     VFTTAIDPAE DRVVKAVEDD CNKNILSLME SGNIQALREA LKSYSKEARA EMGFKHFHWL
     LGALDGHFKG ATVHHYGALY GSGAAVVEFS I