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Conserved domains on  [gi|1673034483|gb|TMP18633|]
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flavodoxin [Pseudoalteromonas sp. S2721]

Protein Classification

NAD(P)H-dependent oxidoreductase( domain architecture ID 10495002)

NAD(P)H-dependent oxidoreductase which catalyzes the reduction or oxidation of a substrate coupled to the oxidation or reduction, respectively, of a nicotinamide adenine dinucleotide cofactor NAD(P)H or NAD(P)+

CATH:  3.40.50.360
EC:  1.-.-.-
Gene Ontology:  GO:0050136|GO:0008753|GO:0010181
SCOP:  3001217

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
2-189 8.81e-29

Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyze the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP. This family is related to pfam03358 and pfam00258.


:

Pssm-ID: 426816 [Multi-domain]  Cd Length: 193  Bit Score: 105.88  E-value: 8.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673034483   2 KNVLILNAHHYYPFSEGKLNAALIAKAdaffQAKGYQTRVVN-------------------TQDEFDVETELENHQWADI 62
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEAL----KAAGHEVTVRDlyalflpvldaedladltyPQGAADVESEQEELLAADV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673034483  63 VFLQSPINWMGMTWSFKKYMDEVYTAGMGgalchgdgrHQDNPkaNYGKGGTLTNTQYMMSLTLNAPAESFadAADFFEG 142
Cdd:pfam02525  77 IVFQFPLYWFSVPALLKGWIDRVLRAGFA---------FKYEE--GGPGGGGLLGKKVLVIVTTGGPEYAY--GKGGYNG 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1673034483 143 KSVDDLVFPMHMNFKFFGMQAMPTFACYDVM---KNADIDSDFARFEKHL 189
Cdd:pfam02525 144 FSLDELLPYLRGILGFCGITDLPPFAVEGTAgpeDEAALAEALERYEERL 193
 
Name Accession Description Interval E-value
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
2-189 8.81e-29

Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyze the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP. This family is related to pfam03358 and pfam00258.


Pssm-ID: 426816 [Multi-domain]  Cd Length: 193  Bit Score: 105.88  E-value: 8.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673034483   2 KNVLILNAHHYYPFSEGKLNAALIAKAdaffQAKGYQTRVVN-------------------TQDEFDVETELENHQWADI 62
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEAL----KAAGHEVTVRDlyalflpvldaedladltyPQGAADVESEQEELLAADV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673034483  63 VFLQSPINWMGMTWSFKKYMDEVYTAGMGgalchgdgrHQDNPkaNYGKGGTLTNTQYMMSLTLNAPAESFadAADFFEG 142
Cdd:pfam02525  77 IVFQFPLYWFSVPALLKGWIDRVLRAGFA---------FKYEE--GGPGGGGLLGKKVLVIVTTGGPEYAY--GKGGYNG 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1673034483 143 KSVDDLVFPMHMNFKFFGMQAMPTFACYDVM---KNADIDSDFARFEKHL 189
Cdd:pfam02525 144 FSLDELLPYLRGILGFCGITDLPPFAVEGTAgpeDEAALAEALERYEERL 193
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
3-191 7.10e-17

Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction only];


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 74.49  E-value: 7.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673034483   3 NVLILNAHHYypfsEGKLNAALIAKADAFFQAKGYQTRVV------------------NTQDEFDVETELENHQWADIVF 64
Cdd:COG2249     1 KILIIYAHPD----PSSFNAALAEAAAEGLEAAGHEVTVHdlyaegfdpvlsaadfyrDGPLPIDVAAEQELLLWADHLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673034483  65 LQSPINWMGMTWSFKKYMDEVYTAGmggaLCHGDGRHqdnpkanyGKGGTLTNTQYMMSLTLNAPAESFadAADFFeGKS 144
Cdd:COG2249    77 FQFPLWWYSMPALLKGWIDRVLTPG----FAYGYGGG--------YPGGLLKGKKALLVVTTGGPEEAY--SRLGY-GGP 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1673034483 145 VDDLVFpmHMNFKFFGMQAMPTFACYDVMKnadidSDFARFEKHLNE 191
Cdd:COG2249   142 IEELLF--RGTLGYCGMKVLPPFVLYGVDR-----SSDEERAAWLER 181
PRK00871 PRK00871
glutathione-regulated potassium-efflux system oxidoreductase KefF;
49-168 7.75e-03

glutathione-regulated potassium-efflux system oxidoreductase KefF;


Pssm-ID: 234852  Cd Length: 176  Bit Score: 35.53  E-value: 7.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673034483  49 DVETELENHQWADIVFLQSPINWMGMTWSFKKYMDEVYTAGMGgalchgdgrhqdnpkanYGKGGTLTNTQYMMSLTLNA 128
Cdd:PRK00871   45 DIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVLSHGWA-----------------YGHGGTALHGKHLLWAVTTG 107
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1673034483 129 PAESFADAADFfegKSVDDLVFPMHMNFKFFGMQAMPTFA 168
Cdd:PRK00871  108 GGESHFEIGAH---PGFDVLSQPLQATALYCGLNWLPPFA 144
 
Name Accession Description Interval E-value
Flavodoxin_2 pfam02525
Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family ...
2-189 8.81e-29

Flavodoxin-like fold; This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyze the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP. This family is related to pfam03358 and pfam00258.


Pssm-ID: 426816 [Multi-domain]  Cd Length: 193  Bit Score: 105.88  E-value: 8.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673034483   2 KNVLILNAHHYYPFSEGKLNAALIAKAdaffQAKGYQTRVVN-------------------TQDEFDVETELENHQWADI 62
Cdd:pfam02525   1 MKILIINAHPRPGSFSSRLADALVEAL----KAAGHEVTVRDlyalflpvldaedladltyPQGAADVESEQEELLAADV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673034483  63 VFLQSPINWMGMTWSFKKYMDEVYTAGMGgalchgdgrHQDNPkaNYGKGGTLTNTQYMMSLTLNAPAESFadAADFFEG 142
Cdd:pfam02525  77 IVFQFPLYWFSVPALLKGWIDRVLRAGFA---------FKYEE--GGPGGGGLLGKKVLVIVTTGGPEYAY--GKGGYNG 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1673034483 143 KSVDDLVFPMHMNFKFFGMQAMPTFACYDVM---KNADIDSDFARFEKHL 189
Cdd:pfam02525 144 FSLDELLPYLRGILGFCGITDLPPFAVEGTAgpeDEAALAEALERYEERL 193
MdaB COG2249
Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction ...
3-191 7.10e-17

Putative NADPH-quinone reductase (modulator of drug activity B) [General function prediction only];


Pssm-ID: 441850 [Multi-domain]  Cd Length: 190  Bit Score: 74.49  E-value: 7.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673034483   3 NVLILNAHHYypfsEGKLNAALIAKADAFFQAKGYQTRVV------------------NTQDEFDVETELENHQWADIVF 64
Cdd:COG2249     1 KILIIYAHPD----PSSFNAALAEAAAEGLEAAGHEVTVHdlyaegfdpvlsaadfyrDGPLPIDVAAEQELLLWADHLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673034483  65 LQSPINWMGMTWSFKKYMDEVYTAGmggaLCHGDGRHqdnpkanyGKGGTLTNTQYMMSLTLNAPAESFadAADFFeGKS 144
Cdd:COG2249    77 FQFPLWWYSMPALLKGWIDRVLTPG----FAYGYGGG--------YPGGLLKGKKALLVVTTGGPEEAY--SRLGY-GGP 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1673034483 145 VDDLVFpmHMNFKFFGMQAMPTFACYDVMKnadidSDFARFEKHLNE 191
Cdd:COG2249   142 IEELLF--RGTLGYCGMKVLPPFVLYGVDR-----SSDEERAAWLER 181
PRK00871 PRK00871
glutathione-regulated potassium-efflux system oxidoreductase KefF;
49-168 7.75e-03

glutathione-regulated potassium-efflux system oxidoreductase KefF;


Pssm-ID: 234852  Cd Length: 176  Bit Score: 35.53  E-value: 7.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673034483  49 DVETELENHQWADIVFLQSPINWMGMTWSFKKYMDEVYTAGMGgalchgdgrhqdnpkanYGKGGTLTNTQYMMSLTLNA 128
Cdd:PRK00871   45 DIAAEQEALSRADLIVWQHPMQWYSIPPLLKLWIDKVLSHGWA-----------------YGHGGTALHGKHLLWAVTTG 107
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1673034483 129 PAESFADAADFfegKSVDDLVFPMHMNFKFFGMQAMPTFA 168
Cdd:PRK00871  108 GGESHFEIGAH---PGFDVLSQPLQATALYCGLNWLPPFA 144
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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