AMNA_COMTE
ID AMNA_COMTE Reviewed; 271 AA.
AC Q6J1Z5; Q38M40;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=2-aminophenol 1,6-dioxygenase subunit alpha {ECO:0000303|PubMed:15580337};
DE AltName: Full=2-amino-5-chlorophenol 1,6-dioxygenase subunit alpha {ECO:0000312|EMBL:ABB13578.1};
GN Name=cnbCa {ECO:0000312|EMBL:ABB13578.1};
GN Synonyms=amnA {ECO:0000312|EMBL:AAT35227.1};
OS Comamonas testosteroni (Pseudomonas testosteroni).
OG Plasmid pCNB1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAT35227.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-9, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=CNB-1 {ECO:0000269|PubMed:15580337}; PLASMID=pCNB1;
RX PubMed=15580337; DOI=10.1007/s00203-004-0738-5;
RA Wu J.F., Sun C.W., Jiang C.Y., Liu Z.P., Liu S.J.;
RT "A novel 2-aminophenol 1,6-dioxygenase involved in the degradation of p-
RT chloronitrobenzene by Comamonas strain CNB-1: purification, properties,
RT genetic cloning and expression in Escherichia coli.";
RL Arch. Microbiol. 183:1-8(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ABB13578.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=CNB-1 {ECO:0000269|PubMed:16517619}; PLASMID=pCNB1;
RX PubMed=16517619; DOI=10.1128/aem.72.3.1759-1765.2006;
RA Wu J.F., Jiang C.Y., Wang B.J., Ma Y.F., Liu Z.P., Liu S.J.;
RT "Novel partial reductive pathway for 4-chloronitrobenzene and nitrobenzene
RT degradation in Comamonas sp. strain CNB-1.";
RL Appl. Environ. Microbiol. 72:1759-1765(2006).
RN [3] {ECO:0000305, ECO:0000312|EMBL:ABB13578.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=CNB-1 {ECO:0000269|PubMed:17526790}; PLASMID=pCNB1;
RX PubMed=17526790; DOI=10.1128/aem.00616-07;
RA Ma Y.F., Wu J.F., Wang S.Y., Jiang C.Y., Zhang Y., Qi S.W., Liu L.,
RA Zhao G.P., Liu S.J.;
RT "Nucleotide sequence of plasmid pCNB1 from Comamonas strain CNB-1 reveals
RT novel genetic organization and evolution for 4-chloronitrobenzene
RT degradation.";
RL Appl. Environ. Microbiol. 73:4477-4483(2007).
RN [4] {ECO:0000305, ECO:0000312|PDB:3VSG}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT, AND
RP SUBUNIT.
RC STRAIN=CNB-1 {ECO:0000269|PubMed:23275161}; PLASMID=pCNB1;
RX PubMed=23275161; DOI=10.1107/s0907444912042072;
RA Li de F., Zhang J.Y., Hou Y.J., Liu L., Hu Y., Liu S.J., Wang da C.,
RA Liu W.;
RT "Structures of aminophenol dioxygenase in complex with intermediate,
RT product and inhibitor.";
RL Acta Crystallogr. D 69:32-43(2013).
CC -!- FUNCTION: Component of the 2-aminophenol 1,6-dioxygenase (APD) complex
CC that catalyzes the ring fission of 2-aminophenol to produce 2-
CC aminomuconic semialdehyde. CnbCa may have a role in the stability of
CC the complex. The complex is also active on other substrates such as 2-
CC amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and
CC catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol
CC are likely native substrates for this dioxygenase which is involved in
CC the reductive degradation pathway of both nitrobenzene (NB) and 4-
CC chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to
CC grow on these compounds as sole source of carbon, nitrogen, and energy.
CC {ECO:0000269|PubMed:15580337, ECO:0000269|PubMed:16517619}.
CC -!- PATHWAY: Xenobiotic degradation; nitrobenzene degradation.
CC {ECO:0000269|PubMed:16517619, ECO:0000269|PubMed:17526790}.
CC -!- PATHWAY: Xenobiotic degradation; 4-chloronitrobenzene degradation.
CC -!- SUBUNIT: The APD complex is a heterotetramer of 2 alpha (CnbCa) and 2
CC beta (CnbCb) subunits. {ECO:0000269|PubMed:15580337,
CC ECO:0000269|PubMed:23275161}.
CC -!- MISCELLANEOUS: Not active on 4-methylcatechol, 4-chlorocatechol, 2,4-
CC dihydroxybenzoate, o-nitrophenol, p-nitrophenol or 4-nitrocatechol.
CC -!- SIMILARITY: Belongs to the LigB/MhpB extradiol dioxygenase family.
CC {ECO:0000255}.
CC -!- CAUTION: In contrast to other members of the family, lacks the
CC conserved iron-binding sites, suggesting that the alpha subunit has no
CC oxidoreductase activity. {ECO:0000305}.
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DR EMBL; AY605054; AAT35227.1; -; Genomic_DNA.
DR EMBL; EF079106; ABB13578.1; -; Genomic_DNA.
DR RefSeq; YP_001967697.1; NC_010935.1.
DR PDB; 3VSG; X-ray; 2.40 A; A/C=1-271.
DR PDB; 3VSH; X-ray; 2.70 A; A/C=1-271.
DR PDB; 3VSI; X-ray; 2.50 A; A/C=1-271.
DR PDB; 3VSJ; X-ray; 2.30 A; A/C=1-271.
DR PDBsum; 3VSG; -.
DR PDBsum; 3VSH; -.
DR PDBsum; 3VSI; -.
DR PDBsum; 3VSJ; -.
DR AlphaFoldDB; Q6J1Z5; -.
DR SMR; Q6J1Z5; -.
DR KEGG; ag:AAT35227; -.
DR BioCyc; MetaCyc:MON-13345; -.
DR BRENDA; 1.13.11.74; 1590.
DR BRENDA; 1.13.11.76; 1590.
DR UniPathway; UPA00923; -.
DR UniPathway; UPA01033; -.
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 3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW Plasmid.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15580337"
FT CHAIN 2..271
FT /note="2-aminophenol 1,6-dioxygenase subunit alpha"
FT /evidence="ECO:0000269|PubMed:15580337"
FT /id="PRO_0000422780"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:3VSJ"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:3VSJ"
FT HELIX 22..40
FT /evidence="ECO:0007829|PDB:3VSJ"
FT STRAND 44..62
FT /evidence="ECO:0007829|PDB:3VSJ"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:3VSJ"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3VSJ"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3VSJ"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:3VSJ"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:3VSJ"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:3VSJ"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:3VSJ"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:3VSJ"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:3VSJ"
FT HELIX 148..164
FT /evidence="ECO:0007829|PDB:3VSJ"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:3VSJ"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3VSJ"
FT HELIX 196..211
FT /evidence="ECO:0007829|PDB:3VSJ"
FT HELIX 214..227
FT /evidence="ECO:0007829|PDB:3VSJ"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:3VSJ"
FT HELIX 235..243
FT /evidence="ECO:0007829|PDB:3VSJ"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:3VSJ"
FT STRAND 249..259
FT /evidence="ECO:0007829|PDB:3VSJ"
FT STRAND 262..270
FT /evidence="ECO:0007829|PDB:3VSJ"
SQ SEQUENCE 271 AA; 29266 MW; 7BECCAF5A68DA7A8 CRC64;
MTVVSAFLVP GTPLPQLKPE VPSWGQLAAA TERAGKALAA SRPDVVLVYS TQWLAVLDQQ
WLTRPRSEGV HVDENWYEFG DLAYDIRADT ALAEACVTSS PLHGVHARGV NYDGFPIDTG
TITACTLMGI GTDAFPLVVG SNNLYHSGEI TEKLAALAVD CAKDQNKRVA VVGVGGLSGS
LFREEIDPRE DRIANEEDDK WNRRVLKLIE AGDVSALREA MPVYAKEARV DMGFKHLHWI
LGALKGKFSG ANVLGYGPSY GSGAAVIEFR L
