ID   NICA_PSEPU              Reviewed;         618 AA.
AC   B1N1A3;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Putative nicotine oxidoreductase;
GN   Name=nicA;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S16;
RX   PubMed=18203859; DOI=10.1128/aem.02529-07;
RA   Tang H., Wang S., Ma L., Meng X., Deng Z., Zhang D., Ma C., Xu P.;
RT   "A novel gene, encoding 6-hydroxy-3-succinoylpyridine hydroxylase, involved
RT   in nicotine degradation by Pseudomonas putida strain S16.";
RL   Appl. Environ. Microbiol. 74:1567-1574(2008).
RN   [2]
RP   FUNCTION, AND COFACTOR.
RX   PubMed=19060159; DOI=10.1128/aem.02300-08;
RA   Tang H., Wang L., Meng X., Ma L., Wang S., He X., Wu G., Xu P.;
RT   "Novel nicotine oxidoreductase-encoding gene involved in nicotine
RT   degradation by Pseudomonas putida strain S16.";
RL   Appl. Environ. Microbiol. 75:772-778(2009).
CC   -!- FUNCTION: It is hypothesized that the pyrrolidine ring of nicotine is
CC       oxidized by NicA to form N-methylmyosmine. The spontaneous ring opening
CC       of N-methylmyosmine due to the addition of water generates
CC       pseudooxynicotine, which is further oxidized to 3-succinoylpyridine
CC       (SP) by NicA through two hypothesized unstable compounds and the
CC       removal of methylamine. {ECO:0000269|PubMed:19060159}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:19060159};
CC   -!- PATHWAY: Alkaloid degradation; nicotine degradation.
CC   -!- MISCELLANEOUS: No similarities to sequences of bacterial dehydrogenase
CC       or oxidase are found. Moreover, the reverse transcriptase catalytic
CC       domain analysis revealed three possible magnesium binding sites in the
CC       nicA sequence. In addition, NicA has no significant homology with other
CC       genes for degradation of heterocyclic compounds. Therefore, the
CC       sequence of NicA seems to be unique among the sequences of bacterial
CC       nicotine catabolic genes and more closely related to sequences of
CC       higher organisms (PubMed:19060159). {ECO:0000305|PubMed:19060159}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the bacterial reverse
CC       transcriptase family. {ECO:0000305}.
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DR   EMBL; DQ988162; ABM05922.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1N1A3; -.
DR   SMR; B1N1A3; -.
DR   BioCyc; MetaCyc:MON-17156; -.
DR   UniPathway; UPA00106; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   GO; GO:0019608; P:nicotine catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR024937; Domain_X.
DR   InterPro; IPR000477; RT_dom.
DR   Pfam; PF01348; Intron_maturas2; 1.
DR   Pfam; PF00078; RVT_1; 2.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   3: Inferred from homology;
KW   Alkaloid metabolism; Magnesium; Metal-binding; NAD; Oxidoreductase.
FT   CHAIN           1..618
FT                   /note="Putative nicotine oxidoreductase"
FT                   /id="PRO_0000422326"
FT   DOMAIN          72..367
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         314
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         315
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
SQ   SEQUENCE   618 AA;  70539 MW;  CB55A5DDE17ADC60 CRC64;
     MRDAEQSFTR IEAIRKANSD PSYVNDRIYR LMYKEDLYIA AYEKIKSKPG NMTPGQDGTT
     LDEFSIRTIR NIINKMKDES FTFRGARRVL IPKANGKTRP LSVAPPTDKV VQEVIRSILE
     AIYEPTFSKN SHGFRAGKSC HTALKQVRES WSGVTWVIEG DIKGCFDNIS HSKLIDQLRL
     RIKDERFINL IRKALNAGYF ENGAFFSATL GTPQGSIISP ILANVFLDQL DRKVEQLIKD
     HHQGEEGDKI TDPAYRKLQR QKTSLRKKAE KQEGAERDAT LSLAREANSK LLSMSPYLTR
     NNGFIRVKYV RYADDWIIGV NGPKLLAEEL RSVVGEFLEN AGLELSIEKT HIRHAKSETA
     KFLGTNLRIG SENSKIMKVL RNGKKFPKRV AGWTPVMYAP MNELIAKLHS RGFCDPKGNP
     TTVNKWIFLD DNQIVEQIGS VWRGIMNYYS FIDQFSMLSR IQFILQHAAA KTLATKHRSS
     RSKIFSKHGA NLRVRIRDKA GNVIRQVEFP LIKSWKTSPK RFKIGTVDTN FLERSLRLRT
     RSKLYSPCVI CESGDRVAMH HVRHIRKMGQ EIKGFKRVLV SLNRKQIPVC HECHLKIHQG
     KYDGISLKDF ALPHTAAA