ID   NTAA_AMIAI              Reviewed;         453 AA.
AC   P54989;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Nitrilotriacetate monooxygenase component A;
DE            Short=NTA monooxygenase component A;
DE            Short=NTA-MO A;
DE            EC=1.14.14.10;
GN   Name=ntaA; Synonyms=nmoA;
OS   Aminobacter aminovorans (Chelatobacter heintzii).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Aminobacter.
OX   NCBI_TaxID=83263;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12.
RC   STRAIN=ATCC 29600 / DSM 10368 / NCIMB 13986;
RX   PubMed=8892809; DOI=10.1128/jb.178.21.6123-6132.1996;
RA   Knobel H.R., Egli T., van der Meer J.R.;
RT   "Cloning and characterization of the genes encoding nitrilotriacetate
RT   monooxygenase of Chelatobacter heintzii ATCC 29600.";
RL   J. Bacteriol. 178:6123-6132(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, AND CATALYTIC
RP   ACTIVITY.
RC   STRAIN=ATCC 29600 / DSM 10368 / NCIMB 13986;
RX   PubMed=9023192; DOI=10.1128/jb.179.4.1112-1116.1997;
RA   Xu Y., Mortimer M.W., Fisher T.S., Kahn M.L., Brockman F.J., Xun L.;
RT   "Cloning, sequencing, and analysis of a gene cluster from Chelatobacter
RT   heintzii ATCC 29600 encoding nitrilotriacetate monooxygenase and
RT   NADH:flavin mononucleotide oxidoreductase.";
RL   J. Bacteriol. 179:1112-1116(1997).
RN   [3]
RP   CATALYTIC ACTIVITY, SUBUNIT, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=ATCC 29600 / DSM 10368 / NCIMB 13986;
RX   PubMed=1735711; DOI=10.1128/jb.174.4.1179-1188.1992;
RA   Uetz T., Schneider R., Snozzi M., Egli T.;
RT   "Purification and characterization of a two-component monooxygenase that
RT   hydroxylates nitrilotriacetate from 'Chelatobacter' strain ATCC 29600.";
RL   J. Bacteriol. 174:1179-1188(1992).
CC   -!- FUNCTION: Hydroxylation of nitrilotriacetate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FMNH2 + nitrilotriacetate + O2 = ammoniodiacetate + FMN +
CC         glyoxylate + H2O; Xref=Rhea:RHEA:31359, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:25548, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:62745;
CC         EC=1.14.14.10; Evidence={ECO:0000269|PubMed:1735711,
CC         ECO:0000269|PubMed:9023192};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.5 mM for nitriloacetate {ECO:0000269|PubMed:1735711};
CC         KM=350 uM for NADH {ECO:0000269|PubMed:1735711};
CC   -!- SUBUNIT: Heterodimer of two subunits, A and B.
CC       {ECO:0000269|PubMed:1735711}.
CC   -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family.
CC       {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; U39411; AAB05943.1; -; Genomic_DNA.
DR   EMBL; L49438; AAB47922.1; -; Genomic_DNA.
DR   PIR; I40750; I40750.
DR   RefSeq; WP_067969613.1; NZ_CP015007.1.
DR   AlphaFoldDB; P54989; -.
DR   SMR; P54989; -.
DR   PRIDE; P54989; -.
DR   KEGG; ag:AAB05943; -.
DR   OrthoDB; 1591714at2; -.
DR   BioCyc; MetaCyc:MON-14047; -.
DR   BRENDA; 1.14.14.10; 5090.
DR   SABIO-RK; P54989; -.
DR   GO; GO:0018529; F:nitrilotriacetate monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102977; F:nitrilotriacetate monooxygenase activity (FMN-dependent); IEA:UniProtKB-EC.
DR   CDD; cd01095; Nitrilotriacetate_monoxgenase; 1.
DR   Gene3D; 3.20.20.30; -; 1.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   InterPro; IPR016215; NTA_MOA.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   PIRSF; PIRSF000337; NTA_MOA; 1.
DR   SUPFAM; SSF51679; SSF51679; 1.
DR   TIGRFAMs; TIGR03860; FMN_nitrolo; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Flavoprotein; FMN; Monooxygenase;
KW   Oxidoreductase.
FT   CHAIN           1..453
FT                   /note="Nitrilotriacetate monooxygenase component A"
FT                   /id="PRO_0000057969"
FT   BINDING         58
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:O34974"
FT   BINDING         107
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:O34974"
FT   BINDING         157..161
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:O34974"
FT   BINDING         229..232
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:O34974"
SQ   SEQUENCE   453 AA;  50529 MW;  44AA0A57683E5861 CRC64;
     MGANKQMNLG FLFQISGVHY GGWRYPSAQP HRATDIQYYA EIVRTAERGK LDFCFLADSI
     AAYEGSADQQ DRSKDALMAA EPKRLLEPFT LLAALAMVTE HIGLVTTATT TYNEPYTMAR
     LFASLDHITN GRAGWNVVTS ANLAEAHNFG RDGHVEHGDR YARAEEFINV VFKLWDSIED
     GAYLRDKLAG RYGLSEKIHF INHIGEHFKV RGPLNVPRPP QGHPVIVQAG SSHPGKELAA
     RTAEVVFTAQ QTLADGKAFY SDVKGRMAKY GRSSENLKVL PGVVVYVAET ESEAKAKYET
     VSNLVPPDFG LFMLSDLLGE IDLKQFDIDG PLPEDLPEAK GSQSRREVII NLARRENLTI
     RQLYQRVSGA SGHRSIWGTP KQIADQFEQW VYEEAADGFN ILPPYLPESM NDFVNFVVPE
     LQRRGIFRTE YEGSTLRDHL GLARPKNSVA KPS