ID   NTAB_AMIAI              Reviewed;         322 AA.
AC   P54990;
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=FMN reductase (NADH) NtaB;
DE            EC=1.5.1.42;
DE   AltName: Full=Nitrilotriacetate monooxygenase component B;
DE            Short=NTA monooxygenase component B;
DE            Short=NTA-MO B;
GN   Name=ntaB; Synonyms=nmoB;
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 1-14, 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, AND SUBUNIT.
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: Catalyzes the NADH-dependent reduction of the FMN cofactor of
CC       the nitrilotriacetate monooxygenase subunit A.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FMNH2 + NAD(+) = FMN + 2 H(+) + NADH; Xref=Rhea:RHEA:21620,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58210; EC=1.5.1.42;
CC         Evidence={ECO:0000269|PubMed:1735711, ECO:0000269|PubMed:9023192};
CC   -!- SUBUNIT: Heterodimer of two subunits, A and B.
CC       {ECO:0000269|PubMed:1735711}.
CC   -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase 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; AAB05944.1; -; Genomic_DNA.
DR   EMBL; L49438; AAB47921.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54990; -.
DR   SMR; P54990; -.
DR   KEGG; ag:AAB05944; -.
DR   BioCyc; MetaCyc:MON-14048; -.
DR   SABIO-RK; P54990; -.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0052874; F:FMN reductase (NADH) activity; IEA:RHEA.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 2.30.110.10; -; 1.
DR   InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF01613; Flavin_Reduct; 1.
DR   SMART; SM00903; Flavin_Reduct; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Flavoprotein; FMN; NAD; Oxidoreductase.
FT   CHAIN           1..322
FT                   /note="FMN reductase (NADH) NtaB"
FT                   /id="PRO_0000057970"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   322 AA;  34496 MW;  2539C08A0B2F964A CRC64;
     MADQIRSATE GGDPTSDPKG FRRALGTFPT GVTIVTAPGV DGPAGVTANS FASVSLDPPL
     VLWSIGHTSR SHSKFQQSAT FAINILADDQ VGVSQVFAGG SADKFSLVDW HTGRTGAPLI
     DNALAYFDCV CEARHEGGDH TIMIGRVVDF GRAEGSPLAF SQGRYGVTLD HPEAAKARDH
     KSEEYGLDDL PFLSLIAKAH YKEDADLEEQ RSAAGCTPVG SKILAGLYGS APLTADELAR
     RMYLDRREVV DSLNEFVADG HVESCDSGRF ALTESGKQRR RRMIEYVSRY QDEQLASISR
     SDLGVATRVL QAFLAGPGRG SS