ID   NFADR_GEOTN             Reviewed;         185 AA.
AC   A4IT49;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=NAD(P)H-dependent FAD/FMN reductase GTNG_3158 {ECO:0000250|UniProtKB:Q9USJ6, ECO:0000303|PubMed:19942660};
DE            Short=FAD/FMN reductase {ECO:0000303|PubMed:19942660};
DE            EC=1.5.1.45;
GN   OrderedLocusNames=GTNG_3158;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1] {ECO:0000312|EMBL:ABO68503.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP   SPECIFICITY, AND SUBUNIT.
RC   STRAIN=NG80-2 {ECO:0000269|PubMed:19942660};
RX   PubMed=19942660; DOI=10.1099/mic.0.031880-0;
RA   Liu X., Dong Y., Li X., Ren Y., Li Y., Wang W., Wang L., Feng L.;
RT   "Characterization of the anthranilate degradation pathway in Geobacillus
RT   thermodenitrificans NG80-2.";
RL   Microbiology 156:589-595(2010).
CC   -!- FUNCTION: Involved in the pathway of tryptophan degradation. Reduces
CC       FAD/FMN to FADH(2)/FMNH(2), which are subsequently used for the
CC       hydroxylation of anthranilate. It can reduce either FAD or flavin
CC       mononucleotide (FMN) but prefers FAD. The enzyme has a slight
CC       preference for NADPH as acceptor. {ECO:0000269|PubMed:19942660}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FADH2 + NAD(+) = FAD + 2 H(+) + NADH; Xref=Rhea:RHEA:30147,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58307; EC=1.5.1.45;
CC         Evidence={ECO:0000269|PubMed:19942660};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FADH2 + NADP(+) = FAD + 2 H(+) + NADPH; Xref=Rhea:RHEA:30151,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58307, ChEBI:CHEBI:58349; EC=1.5.1.45;
CC         Evidence={ECO:0000269|PubMed:19942660};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=58.2 umol/min/mg enzyme with FAD as substrate for the reverse
CC         reaction (with NADPH as cofactor) {ECO:0000269|PubMed:19942660};
CC         Vmax=55.5 umol/min/mg enzyme with FMN as substrate for the reverse
CC         reaction (with NADPH as cofactor) {ECO:0000269|PubMed:19942660};
CC         Note=With FAD as substrate NADH can be used as an electron donor,
CC         with 95% activity relative to NADPH. {ECO:0000269|PubMed:19942660};
CC   -!- SUBUNIT: Anthranilate 3-monooxygenase consists of a reductase component
CC       (GTNG_3158) and an oxygenase component HpaH.
CC       {ECO:0000269|PubMed:19942660}.
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DR   EMBL; CP000557; ABO68503.1; -; Genomic_DNA.
DR   RefSeq; WP_011888287.1; NC_009328.1.
DR   AlphaFoldDB; A4IT49; -.
DR   SMR; A4IT49; -.
DR   STRING; 420246.GTNG_3158; -.
DR   EnsemblBacteria; ABO68503; ABO68503; GTNG_3158.
DR   KEGG; gtn:GTNG_3158; -.
DR   eggNOG; COG0431; Bacteria.
DR   HOGENOM; CLU_055322_3_3_9; -.
DR   OMA; YAMRPLF; -.
DR   OrthoDB; 796211at2; -.
DR   Proteomes; UP000001578; Chromosome.
DR   GO; GO:0016646; F:oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR   GO; GO:0043421; P:anthranilate catabolic process; IDA:UniProtKB.
DR   GO; GO:0006569; P:tryptophan catabolic process; IDA:UniProtKB.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR005025; FMN_Rdtase-like.
DR   Pfam; PF03358; FMN_red; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; FMN; NAD; NADP; Oxidoreductase.
FT   CHAIN           1..185
FT                   /note="NAD(P)H-dependent FAD/FMN reductase GTNG_3158"
FT                   /id="PRO_0000420235"
SQ   SEQUENCE   185 AA;  20725 MW;  0F7405824A97476D CRC64;
     MKLLGISGTL VGTKTCILVE QVLVEAKRIC PEVDIQLLDL KDYQVEFCDG RQQSSYNEDT
     QKVIELVSVA DCYVIGTPIF QGSITGALKN LFDLISPQAL RHKVMGFVAN GGTYQHYLVI
     ENQLKPIASF FRAFVAPGSV YAHTDHFNEK NELVDPEVRE RVAQLAWEVV HMHWSLKSGG
     VHAHR