GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

FMN-dependent NADH-azoreductase (EC 1.7.-.-) (Azo-dye reductase) (FMN-dependent NADH-azo compound oxidoreductase)

 AZOR_ECOLI              Reviewed;         201 AA.
P41407; P77143; Q93V21;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
13-FEB-2019, entry version 143.
RecName: Full=FMN-dependent NADH-azoreductase;
EC=1.7.-.-;
AltName: Full=Azo-dye reductase;
AltName: Full=FMN-dependent NADH-azo compound oxidoreductase;
Name=azoR; Synonyms=acpD; OrderedLocusNames=b1412, JW1409;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
Kitakawa M., Kasai H., Baba T., Honjo A., Isono K.;
"Nucleotide sequence of the replication terminus region of Escherichia
coli.";
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-144.
STRAIN=K12;
PubMed=7899078; DOI=10.1093/nar/23.4.595;
Moriya H., Kasai H., Isono K.;
"Cloning and characterization of the hrpA gene in the terC region of
Escherichia coli that is highly similar to the DEAH family RNA
helicase genes of Saccharomyces cerevisiae.";
Nucleic Acids Res. 23:595-598(1995).
[6]
PROTEIN SEQUENCE OF 2-16, AND PRELIMINARY FUNCTION.
PubMed=2168383; DOI=10.1128/jb.172.9.5445-5449.1990;
Fischl A.S., Kennedy E.P.;
"Isolation and properties of acyl carrier protein phosphodiesterase of
Escherichia coli.";
J. Bacteriol. 172:5445-5449(1990).
[7]
PROTEIN SEQUENCE OF 2-8, COFACTOR, SUBUNIT, AND CHARACTERIZATION.
STRAIN=K12 / JM109 / ATCC 53323;
PubMed=11583992; DOI=10.1074/jbc.M104483200;
Nakanishi M., Yatome C., Ishida N., Kitade Y.;
"Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase.";
J. Biol. Chem. 276:46394-46399(2001).
[8]
CRYSTALLIZATION.
PubMed=16511052; DOI=10.1107/S1744309105007918;
Ito K., Nakanishi M., Lee W.-C., Sasaki H., Zenno S., Saigo K.,
Kitade Y., Tanokura M.;
"Crystallization and preliminary X-ray analysis of azoR (azoreductase)
from Escherichia coli.";
Acta Crystallogr. F 61:399-402(2005).
[9]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
New York structural genomics research consortium (NYSGRC);
"Crystal structure of acyl carrier protein phosphodiesterase.";
Submitted (JUN-2004) to the PDB data bank.
[10]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FMN.
Ito K., Tanokura M.;
"The crystal structure of AzoR (Azo Reductase) from Escherichia coli:
oxidized form.";
Submitted (JAN-2005) to the PDB data bank.
-!- FUNCTION: Catalyzes the reductive cleavage of azo bond in aromatic
azo compounds to the corresponding amines. Requires NADH, but not
NADPH, as an electron donor for its activity. The enzyme can
reduce ethyl red and methyl red, but is not able to convert
sulfonated azo dyes.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:11583992};
Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:11583992};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=17.9 uM for methyl red;
KM=31.6 uM for NADH;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11583992,
ECO:0000269|Ref.10}.
-!- MISCELLANEOUS: The stoichiometry implies that 2 cycles of the
ping-pong mechanism are required for the cleavage.
-!- SIMILARITY: Belongs to the azoreductase type 1 family.
{ECO:0000305}.
-!- CAUTION: Was originally thought to be an ACP phosphodiesterase.
{ECO:0000305|PubMed:2168383}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; D85081; BAA25408.1; -; Genomic_DNA.
EMBL; U00096; AAC74494.1; -; Genomic_DNA.
EMBL; AP009048; BAA15024.1; -; Genomic_DNA.
EMBL; D42105; BAA07684.1; -; Genomic_DNA.
PIR; G64892; G64892.
RefSeq; NP_415930.1; NC_000913.3.
RefSeq; WP_000048950.1; NZ_LN832404.1.
PDB; 1TIK; X-ray; 2.30 A; A=2-201.
PDB; 1V4B; X-ray; 1.80 A; A=2-201.
PDB; 2D5I; X-ray; 2.20 A; A=2-201.
PDB; 2Z98; X-ray; 1.40 A; A=2-201.
PDB; 2Z9B; X-ray; 1.70 A; A=2-201.
PDB; 2Z9C; X-ray; 2.30 A; A=2-201.
PDB; 2Z9D; X-ray; 2.10 A; A/B=2-201.
PDBsum; 1TIK; -.
PDBsum; 1V4B; -.
PDBsum; 2D5I; -.
PDBsum; 2Z98; -.
PDBsum; 2Z9B; -.
PDBsum; 2Z9C; -.
PDBsum; 2Z9D; -.
ProteinModelPortal; P41407; -.
SMR; P41407; -.
BioGrid; 4261518; 20.
STRING; 316385.ECDH10B_1538; -.
DrugBank; DB02325; Isopropyl Alcohol.
DrugBank; DB03247; Riboflavin Monophosphate.
jPOST; P41407; -.
PaxDb; P41407; -.
PRIDE; P41407; -.
EnsemblBacteria; AAC74494; AAC74494; b1412.
EnsemblBacteria; BAA15024; BAA15024; BAA15024.
GeneID; 947569; -.
KEGG; ecj:JW1409; -.
KEGG; eco:b1412; -.
PATRIC; fig|1411691.4.peg.859; -.
EchoBASE; EB2558; -.
EcoGene; EG12695; azoR.
eggNOG; ENOG4108V3G; Bacteria.
eggNOG; COG1182; LUCA.
HOGENOM; HOG000247892; -.
InParanoid; P41407; -.
KO; K01118; -.
PhylomeDB; P41407; -.
BioCyc; EcoCyc:G6731-MONOMER; -.
BioCyc; ECOL316407:JW1409-MONOMER; -.
BioCyc; MetaCyc:G6731-MONOMER; -.
BRENDA; 1.7.1.6; 2026.
SABIO-RK; P41407; -.
EvolutionaryTrace; P41407; -.
PRO; PR:P41407; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0050446; F:azobenzene reductase activity; IDA:EcoCyc.
GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
GO; GO:0008752; F:FMN reductase activity; IEA:UniProtKB-UniRule.
GO; GO:0016652; F:oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor; IEA:UniProtKB-UniRule.
GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:EcoCyc.
GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
Gene3D; 3.40.50.360; -; 1.
HAMAP; MF_01216; Azoreductase_type1; 1.
InterPro; IPR003680; Flavodoxin_fold.
InterPro; IPR029039; Flavoprotein-like_sf.
InterPro; IPR023048; NADH-azoreductase_FMN-depdnt.
Pfam; PF02525; Flavodoxin_2; 1.
SUPFAM; SSF52218; SSF52218; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Flavoprotein; FMN; NAD; Oxidoreductase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:11583992,
ECO:0000269|PubMed:2168383}.
CHAIN 2 201 FMN-dependent NADH-azoreductase.
/FTId=PRO_0000166310.
NP_BIND 16 18 FMN. {ECO:0000269|Ref.10}.
NP_BIND 96 99 FMN. {ECO:0000269|Ref.10}.
NP_BIND 140 145 FMN. {ECO:0000269|Ref.10}.
BINDING 10 10 FMN. {ECO:0000269|Ref.10}.
CONFLICT 23 35 DYFVEQWREKHSA -> IILLNNGAKSTPR (in Ref.
1; BAA25408 and 5; BAA07684).
{ECO:0000305}.
STRAND 3 8 {ECO:0000244|PDB:2Z98}.
HELIX 13 15 {ECO:0000244|PDB:2Z98}.
HELIX 17 32 {ECO:0000244|PDB:2Z98}.
STRAND 36 42 {ECO:0000244|PDB:2Z98}.
TURN 43 47 {ECO:0000244|PDB:2Z98}.
HELIX 53 58 {ECO:0000244|PDB:2Z98}.
HELIX 68 86 {ECO:0000244|PDB:2Z98}.
STRAND 88 93 {ECO:0000244|PDB:2Z98}.
HELIX 103 112 {ECO:0000244|PDB:2Z98}.
TURN 115 117 {ECO:0000244|PDB:2Z98}.
STRAND 118 122 {ECO:0000244|PDB:2Z98}.
STRAND 125 128 {ECO:0000244|PDB:2Z98}.
STRAND 134 140 {ECO:0000244|PDB:2Z98}.
HELIX 153 163 {ECO:0000244|PDB:2Z98}.
STRAND 169 174 {ECO:0000244|PDB:2Z98}.
HELIX 177 179 {ECO:0000244|PDB:2Z9D}.
HELIX 181 199 {ECO:0000244|PDB:2Z98}.
SEQUENCE 201 AA; 21658 MW; E28D30DC4DA42297 CRC64;
MSKVLVLKSS ILAGYSQSNQ LSDYFVEQWR EKHSADEITV RDLAANPIPV LDGELVGALR
PSDAPLTPRQ QEALALSDEL IAELKAHDVI VIAAPMYNFN ISTQLKNYFD LVARAGVTFR
YTENGPEGLV TGKKAIVITS RGGIHKDGPT DLVTPYLSTF LGFIGITDVK FVFAEGIAYG
PEMAAKAQSD AKAAIDSIVS A


Related products :

Catalog number Product name Quantity
EIAAB26662 Homo sapiens,Human,NADPH-dependent diflavin oxidoreductase 1,NADPH-dependent FMN and FAD-containing oxidoreductase,NDOR1,Novel reductase 1,NR1
EIAAB28138 Mouse,Mtnd4,mt-Nd4,Mus musculus,NADH dehydrogenase subunit 4,NADH-ubiquinone oxidoreductase chain 4,Nd4
EIAAB28103 MTND1,MT-ND1,NADH dehydrogenase subunit 1,NADH1,NADH-ubiquinone oxidoreductase chain 1,ND1,Pig,Sus scrofa
EIAAB28155 Mtnd6,mt-Nd6,NADH dehydrogenase subunit 6,NADH-ubiquinone oxidoreductase chain 6,Nd6,Rat,Rattus norvegicus
EIAAB28151 MTND6,MT-ND6,NADH dehydrogenase subunit 6,NADH6,NADH-ubiquinone oxidoreductase chain 6,ND6,Pig,Sus scrofa
EIAAB28158 Mouse,Mtnd6,mt-Nd6,Mus musculus,NADH dehydrogenase subunit 6,NADH-ubiquinone oxidoreductase chain 6,Nd6
EIAAB28100 Mouse,Mtnd1,mt-Nd1,Mus musculus,NADH dehydrogenase subunit 1,NADH-ubiquinone oxidoreductase chain 1,Nd1
EIAAB28150 MTND5,MT-ND5,NADH dehydrogenase subunit 5,NADH5,NADH-ubiquinone oxidoreductase chain 5,ND5,Pig,Sus scrofa
EIAAB28146 Mtnd5,mt-Nd5,NADH dehydrogenase subunit 5,NADH-ubiquinone oxidoreductase chain 5,Nd5,Rat,Rattus norvegicus
EIAAB28147 Mouse,Mtnd5,mt-Nd5,Mus musculus,NADH dehydrogenase subunit 5,NADH-ubiquinone oxidoreductase chain 5,Nd5
EIAAB28135 MTND4,MT-ND4,NADH dehydrogenase subunit 4,NADH4,NADH-ubiquinone oxidoreductase chain 4,ND4,Pig,Sus scrofa
EIAAB28137 Mtnd4,mt-Nd4,NADH dehydrogenase subunit 4,NADH-ubiquinone oxidoreductase chain 4,Nd4,Rat,Rattus norvegicus
EIAAB28106 Mtnd1,mt-Nd1,NADH dehydrogenase subunit 1,NADH-ubiquinone oxidoreductase chain 1,Nd1,Rat,Rattus norvegicus
EIAAB28124 MTND3,MT-ND3,NADH dehydrogenase subunit 3,NADH3,NADH-ubiquinone oxidoreductase chain 3,ND3,Pig,Sus scrofa
EIAAB28120 Mtnd3,mt-Nd3,NADH dehydrogenase subunit 3,NADH-ubiquinone oxidoreductase chain 3,Nd3,Rat,Rattus norvegicus
EIAAB28114 Mouse,Mtnd2,mt-Nd2,Mus musculus,NADH dehydrogenase subunit 2,NADH-ubiquinone oxidoreductase chain 2,Nd2
EIAAB28122 Mouse,Mtnd3,mt-Nd3,Mus musculus,NADH dehydrogenase subunit 3,NADH-ubiquinone oxidoreductase chain 3,Nd3
EIAAB28117 MTND2,MT-ND2,NADH dehydrogenase subunit 2,NADH2,NADH-ubiquinone oxidoreductase chain 2,ND2,Pig,Sus scrofa
EIAAB28113 Mtnd2,mt-Nd2,NADH dehydrogenase subunit 2,NADH-ubiquinone oxidoreductase chain 2,Nd2,Rat,Rattus norvegicus
EIAAB28136 Bos taurus,Bovine,MTND4,MT-ND4,NADH dehydrogenase subunit 4,NADH4,NADH-ubiquinone oxidoreductase chain 4,ND4
EIAAB28152 Bos taurus,Bovine,MTND6,MT-ND6,NADH dehydrogenase subunit 6,NADH6,NADH-ubiquinone oxidoreductase chain 6,ND6
EIAAB28145 Bos taurus,Bovine,MTND5,MT-ND5,NADH dehydrogenase subunit 5,NADH5,NADH-ubiquinone oxidoreductase chain 5,ND5
EIAAB28125 Bos taurus,Bovine,MTND3,MT-ND3,NADH dehydrogenase subunit 3,NADH3,NADH-ubiquinone oxidoreductase chain 3,ND3
EIAAB28116 Bos taurus,Bovine,MTND2,MT-ND2,NADH dehydrogenase subunit 2,NADH2,NADH-ubiquinone oxidoreductase chain 2,ND2
EIAAB28105 Bos taurus,Bovine,MTND1,MT-ND1,NADH dehydrogenase subunit 1,NADH1,NADH-ubiquinone oxidoreductase chain 1,ND1

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP1493: Carbon assimilation C4 pathway
WP1566: Citrate cycle (TCA cycle)
WP1619: Amino sugar and nucleotide sugar metabolism
WP1625: Base excision repair
WP1672: Mismatch repair
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair
WP2344: vitamin B6 (pyridoxine, pyridoxal, pyridoxamine) biosynthesis and salvage pathway
WP710: DNA damage response (only ATM dependent)
WP1006: metapathway biotransformation
WP1124: metapathway biotransformation
WP1212: metapathway biotransformation
WP1251: metapathway biotransformation
WP1286: metapathway biotransformation
WP1403: AMPK signaling
WP1461: Photosynthetic Carbon Reduction
WP1567: Glycolysis and Gluconeogenesis
WP1611: 1,1,1-Trichloro-2,2-bis(4-chlorophenyl)ethane (DDT
WP1626: Benzoate degradation via CoA ligation
WP1627: Benzoate degradation via hydroxylation
WP1634: Butanoate metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1665: Limonene and pinene degradation
WP1680: Oxidative phosphorylation

Related Genes :
[azoR acpD b1412 JW1409] FMN-dependent NADH-azoreductase (EC 1.7.-.-) (Azo-dye reductase) (FMN-dependent NADH-azo compound oxidoreductase)
[azoR2 yvaB BSU33540] FMN-dependent NADH-azoreductase 2 (EC 1.7.-.-) (Azo-dye reductase 2) (FMN-dependent NADH-azo compound oxidoreductase 2)
[nfrA2 ycnD BSU03860] FMN reductase [NAD(P)H] (EC 1.5.1.39) (NAD(P)H-dependent FMN reductase) (NAD(P)H-dependent nitro/flavin reductase) (NAD(P)H-dependent nitroreductase) (NAD(P)H-dependent oxidoreductase)
[azoR1 yocJ BSU19230] FMN-dependent NADH-azoreductase 1 (EC 1.7.-.-) (Azo-dye reductase 1) (FMN-dependent NADH-azo compound oxidoreductase 1)
[azoR1 PA0785] FMN-dependent NADH-azoreductase 1 (EC 1.7.-.-) (Azo-dye reductase 1) (FMN-dependent NADH-azo compound oxidoreductase 1)
[nfsB dprA nfnB nfsI ntr b0578 JW0567] Oxygen-insensitive NAD(P)H nitroreductase (EC 1.-.-.-) (Dihydropteridine reductase) (EC 1.5.1.34) (FMN-dependent nitroreductase)
[azoR2 PA1962] FMN-dependent NADH-azoreductase 2 (EC 1.7.-.-) (Azo-dye reductase 2) (FMN-dependent NADH-azo compound oxidoreductase 2)
[azoR3 PA3223] FMN-dependent NADH-azoreductase 3 (EC 1.7.-.-) (Azo-dye reductase 3) (FMN-dependent NADH-azo compound oxidoreductase 3)
[NDOR1 NR1] NADPH-dependent diflavin oxidoreductase 1 (EC 1.18.1.-) (NADPH-dependent FMN and FAD-containing oxidoreductase) (Novel reductase 1)
[rutF ycdH b1007 JW5138] FMN reductase (NADH) RutF (EC 1.5.1.42) (FMN reductase) (NADH-flavin reductase RutF) (NADH:flavin oxidoreductase)
[NDUFV1 UQOR1] NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial (EC 1.6.99.3) (EC 7.1.1.2) (Complex I-51kD) (CI-51kD) (NADH dehydrogenase flavoprotein 1) (NADH-ubiquinone oxidoreductase 51 kDa subunit)
[inhA Rv1484 MTCY277.05] Enoyl-[acyl-carrier-protein] reductase [NADH] (ENR) (Enoyl-ACP reductase) (EC 1.3.1.9) (FAS-II enoyl-ACP reductase) (NADH-dependent 2-trans-enoyl-ACP reductase)
[ATR3 At3g02280 F14P3.7] NADPH-dependent diflavin oxidoreductase 1 (EC 1.18.1.-) (NADPH-dependent FMN and FAD-containing oxidoreductase)
[TAH18 YPR048W YP9499.06] NADPH-dependent diflavin oxidoreductase 1 (EC 1.18.1.-) (NADPH-dependent FMN and FAD-containing oxidoreductase)
[azrA azoR] FMN-dependent NADH-azoreductase (EC 1.7.-.-) (Azo-dye reductase) (FMN-dependent NADH-azo compound oxidoreductase)
[azrC azoR] FMN-dependent NADH-azoreductase (EC 1.7.-.-) (Azo-dye reductase) (FMN-dependent NADH-azo compound oxidoreductase)
[NDUFV1 UQOR1] NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial (EC 1.6.99.3) (EC 7.1.1.2) (Complex I-51kD) (CI-51kD) (NADH dehydrogenase flavoprotein 1) (NADH-ubiquinone oxidoreductase 51 kDa subunit)
[nqrB nqr2] Na(+)-translocating NADH-quinone reductase subunit B (Na(+)-NQR subunit B) (Na(+)-translocating NQR subunit B) (EC 7.2.1.1) (NQR complex subunit B) (NQR-1 subunit B)
[Tkfc Dak] Triokinase/FMN cyclase (Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)) [Includes: ATP-dependent dihydroxyacetone kinase (DHA kinase) (EC 2.7.1.28) (EC 2.7.1.29) (Glycerone kinase) (Triokinase) (Triose kinase); FAD-AMP lyase (cyclizing) (EC 4.6.1.15) (FAD-AMP lyase (cyclic FMN forming)) (FMN cyclase)]
[TKFC DAK] Triokinase/FMN cyclase (Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)) [Includes: ATP-dependent dihydroxyacetone kinase (DHA kinase) (EC 2.7.1.28) (EC 2.7.1.29) (Glycerone kinase) (Triokinase) (Triose kinase); FAD-AMP lyase (cyclizing) (EC 4.6.1.15) (FAD-AMP lyase (cyclic FMN forming)) (FMN cyclase)]
[nqrB VC0395_A1883 VC395_2410] Na(+)-translocating NADH-quinone reductase subunit B (Na(+)-NQR subunit B) (Na(+)-translocating NQR subunit B) (EC 7.2.1.1) (NQR complex subunit B) (NQR-1 subunit B)
[nqo1 TTHA0089] NADH-quinone oxidoreductase subunit 1 (EC 7.1.1.-) (NADH dehydrogenase I chain 1) (NDH-1 subunit 1)
[MT-ND1 MTND1 NADH1 ND1] NADH-ubiquinone oxidoreductase chain 1 (EC 7.1.1.2) (NADH dehydrogenase subunit 1)
[nuo-51 B10H18.210 NCU04044] NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrial (EC 1.6.99.3) (EC 7.1.1.2) (Complex I-51kD) (CI-51kD)
[nuoF b2284 JW2279] NADH-quinone oxidoreductase subunit F (EC 7.1.1.-) (NADH dehydrogenase I subunit F) (NDH-1 subunit F) (NUO6)
[nqrC nqr3] Na(+)-translocating NADH-quinone reductase subunit C (Na(+)-NQR subunit C) (Na(+)-translocating NQR subunit C) (EC 7.2.1.1) (NQR complex subunit C) (NQR-1 subunit C)
[azoR DNK77_05485] FMN-dependent NADH-azoreductase (EC 1.7.-.-) (Azo-dye reductase) (FMN-dependent NADH-azo compound oxidoreductase)
[TKFC DAK] Triokinase/FMN cyclase (Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)) [Includes: ATP-dependent dihydroxyacetone kinase (DHA kinase) (EC 2.7.1.28) (EC 2.7.1.29) (Glycerone kinase) (Triokinase) (Triose kinase); FAD-AMP lyase (cyclizing) (EC 4.6.1.15) (FAD-AMP lyase (cyclic FMN forming)) (FMN cyclase)]
[Tkfc Dak] Triokinase/FMN cyclase (Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)) [Includes: ATP-dependent dihydroxyacetone kinase (DHA kinase) (EC 2.7.1.28) (EC 2.7.1.29) (Glycerone kinase) (Triokinase) (Triose kinase); FAD-AMP lyase (cyclizing) (EC 4.6.1.15) (FAD-AMP lyase (cyclic FMN forming)) (FMN cyclase)]
[NDUFS7] NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial (EC 1.6.99.3) (EC 7.1.1.2) (Complex I-20kD) (CI-20kD) (NADH-ubiquinone oxidoreductase 20 kDa subunit) (PSST subunit)

Bibliography :
No related Items
?>