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Major NAD(P)H-flavin oxidoreductase (EC 1.6.99.-) (FRASE I)

 FRA1_ALIFS              Reviewed;         218 AA.
P46072;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-JUL-2017, entry version 79.
RecName: Full=Major NAD(P)H-flavin oxidoreductase;
EC=1.6.99.-;
AltName: Full=FRASE I;
Aliivibrio fischeri (Vibrio fischeri).
Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
Vibrionaceae; Aliivibrio.
NCBI_TaxID=668;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 7744 / DSM 507 / NCIMB 1281 / 398;
PubMed=8206830; DOI=10.1128/jb.176.12.3536-3543.1994;
Zenno S., Saigo K., Kanoh H., Inouye S.;
"Identification of the gene encoding the major NAD(P)H-flavin
oxidoreductase of the bioluminescent bacterium Vibrio fischeri ATCC
7744.";
J. Bacteriol. 176:3536-3543(1994).
[2]
SEQUENCE REVISION TO 61 AND 213.
Zenno S., Saigo K., Kanoh H., Inouye S.;
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[3]
CHARACTERIZATION.
STRAIN=ATCC 7744 / DSM 507 / NCIMB 1281 / 398;
PubMed=8033996; DOI=10.1016/0014-5793(94)00528-1;
Inouye S.;
"NAD(P)H-flavin oxidoreductase from the bioluminescent bacterium,
Vibrio fischeri ATCC 7744, is a flavoprotein.";
FEBS Lett. 347:163-168(1994).
[4]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH FMN AND
SUBSTRATE ANALOGS, AND SUBUNIT.
STRAIN=ATCC 7744 / DSM 507 / NCIMB 1281 / 398;
PubMed=9654450; DOI=10.1006/jmbi.1998.1871;
Koike H., Sasaki H., Kobori T., Zenno S., Saigo K., Murphy M.E.,
Adman E.T., Tanokura M.;
"1.8-A crystal structure of the major NAD(P)H:FMN oxidoreductase of a
bioluminescent bacterium, Vibrio fischeri: overall structure, cofactor
and substrate-analog binding, and comparison with related
flavoproteins.";
J. Mol. Biol. 280:259-273(1998).
-!- FUNCTION: Involved in bioluminescence. It is a good supplier of
reduced flavin mononucleotide (FMNH2) to the bioluminescence
reaction. Major FMN reductase. It is capable of using both NADH
and NADPH as electron donors. As electron acceptor, FMN is the
most effective, FAD is considerably effective, and riboflavin is
the least effective.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9654450}.
-!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
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EMBL; D17743; BAA04595.2; -; Genomic_DNA.
PIR; S46241; S46241.
PDB; 1V5Y; X-ray; 1.90 A; A/B=2-218.
PDB; 1V5Z; X-ray; 2.00 A; A/B=2-218.
PDB; 1VFR; X-ray; 1.80 A; A/B=1-218.
PDBsum; 1V5Y; -.
PDBsum; 1V5Z; -.
PDBsum; 1VFR; -.
ProteinModelPortal; P46072; -.
SMR; P46072; -.
DrugBank; DB03410; 4-hydroxycoumarin.
DrugBank; DB03247; Riboflavin Monophosphate.
DrugBank; DB01650; trans-2-hydroxycinnamic acid.
eggNOG; ENOG4108RCM; Bacteria.
eggNOG; COG0778; LUCA.
EvolutionaryTrace; P46072; -.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
CDD; cd02149; NfsB_like_nitroreductase; 1.
Gene3D; 3.40.109.10; -; 1.
InterPro; IPR033878; NfsB-like.
InterPro; IPR029479; Nitroreductase.
InterPro; IPR000415; Nitroreductase-like.
Pfam; PF00881; Nitroreductase; 1.
SUPFAM; SSF55469; SSF55469; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; FAD; Flavoprotein; FMN;
Luminescence; NAD; NADP; Oxidoreductase.
INIT_MET 1 1 Removed.
CHAIN 2 218 Major NAD(P)H-flavin oxidoreductase.
/FTId=PRO_0000072714.
NP_BIND 12 16 FMN.
NP_BIND 154 159 NAD or NADP. {ECO:0000250}.
NP_BIND 165 166 FMN.
NP_BIND 206 208 FMN.
BINDING 73 73 FMN.
HELIX 4 11 {ECO:0000244|PDB:1VFR}.
STRAND 16 18 {ECO:0000244|PDB:1VFR}.
HELIX 26 37 {ECO:0000244|PDB:1VFR}.
HELIX 42 44 {ECO:0000244|PDB:1VFR}.
STRAND 48 53 {ECO:0000244|PDB:1VFR}.
HELIX 56 64 {ECO:0000244|PDB:1VFR}.
STRAND 67 69 {ECO:0000244|PDB:1VFR}.
HELIX 71 75 {ECO:0000244|PDB:1VFR}.
HELIX 76 79 {ECO:0000244|PDB:1VFR}.
STRAND 80 90 {ECO:0000244|PDB:1VFR}.
HELIX 94 106 {ECO:0000244|PDB:1VFR}.
HELIX 112 118 {ECO:0000244|PDB:1VFR}.
HELIX 119 122 {ECO:0000244|PDB:1VFR}.
HELIX 123 127 {ECO:0000244|PDB:1VFR}.
STRAND 131 133 {ECO:0000244|PDB:1V5Y}.
HELIX 136 157 {ECO:0000244|PDB:1VFR}.
STRAND 160 164 {ECO:0000244|PDB:1VFR}.
HELIX 169 175 {ECO:0000244|PDB:1VFR}.
TURN 176 182 {ECO:0000244|PDB:1VFR}.
STRAND 183 192 {ECO:0000244|PDB:1VFR}.
TURN 196 198 {ECO:0000244|PDB:1VFR}.
HELIX 200 203 {ECO:0000244|PDB:1VFR}.
HELIX 211 214 {ECO:0000244|PDB:1VFR}.
STRAND 215 217 {ECO:0000244|PDB:1VFR}.
SEQUENCE 218 AA; 24721 MW; AC223CF8CEE5A636 CRC64;
MTHPIIHDLE NRYTSKKYDP SKKVSQEDLA VLLEALRLSA SSINSQPWKF IVIESDAAKQ
RMHDSFANMH QFNQPHIKAC SHVILFANKL SYTRDDYDVV LSKAVADKRI TEEQKEAAFA
SFKFVELNCD ENGEHKAWTK PQAYLALGNA LHTLARLNID STTMEGIDPE LLSEIFADEL
KGYECHVALA IGYHHPSEDY NASLPKSRKA FEDVITIL


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