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 13-SEP-2023, entry version 60. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:MONOMER-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 CDD; cd07373; 2A5CPDO_A; 1. DR Gene3D; 3.40.830.10; LigB-like; 1. DR InterPro; IPR004183; Xdiol_dOase_suB. DR Pfam; PF02900; LigB; 1. DR SUPFAM; SSF53213; LigB-like; 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 //