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Conserved domains on  [gi|6323552|ref|NP_013623|]
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cytochrome-b5 reductase [Saccharomyces cerevisiae S288C]

Protein Classification

cytochrome b5 reductase family protein( domain architecture ID 10153046)

cytochrome b5 reductase family protein such as NADH-cytochrome b5 reductase that catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor; the cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes

CATH:  3.40.50.80
EC:  1.-.-.-
Gene Ontology:  GO:0016491
PubMed:  19997042

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 75-312 1.33e-92

Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.


:

Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 274.44  E-value: 1.33e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   75 LPLSKKTRISRNTSLYCFKLKYPFERLHIPMGYHLAVRVTINGERLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKYFDK 154
Cdd:cd06183   1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYLHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  155 LKIRQYVEFKGPLGELEYDQDT-ATELGIIAGGSGITPVLQVLQEIIPSPEDLTHISLIYANETEDDILMKSQLDHMAKE 233
Cdd:cd06183  81 LKPGDTVEIRGPFGKFEYKPNGkVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKISLLYANRTEEDILLREELDELAKK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  234 YP-HFKVHYVIHKPNGKWNGDVGYVTLEEMKRYLPK-QAEDHRLLICGPPKMNEM-VLNYAKELGWSNgfhkgngtDKVF 310
Cdd:cd06183 161 HPdRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPPpPSEDTLVLVCGPPPMIEGaVKGLLKELGYKK--------DNVF 232


                ..
gi 6323552  311 VF 312
Cdd:cd06183 233 KF 234
 
Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 75-312 1.33e-92

Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 274.44  E-value: 1.33e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   75 LPLSKKTRISRNTSLYCFKLKYPFERLHIPMGYHLAVRVTINGERLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKYFDK 154
Cdd:cd06183   1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYLHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  155 LKIRQYVEFKGPLGELEYDQDT-ATELGIIAGGSGITPVLQVLQEIIPSPEDLTHISLIYANETEDDILMKSQLDHMAKE 233
Cdd:cd06183  81 LKPGDTVEIRGPFGKFEYKPNGkVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKISLLYANRTEEDILLREELDELAKK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  234 YP-HFKVHYVIHKPNGKWNGDVGYVTLEEMKRYLPK-QAEDHRLLICGPPKMNEM-VLNYAKELGWSNgfhkgngtDKVF 310
Cdd:cd06183 161 HPdRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPPpPSEDTLVLVCGPPPMIEGaVKGLLKELGYKK--------DNVF 232


                ..
gi 6323552  311 VF 312
Cdd:cd06183 233 KF 234
PLN02252 PLN02252
nitrate reductase [NADPH]
 71-312 1.85e-67

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 226.10  E-value: 1.85e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552    71 KWVALPLSKKTRISRNTSLYCFKLKYPFERLHIPMGYHLAVRVTINGERLVRYYTPVNVPNTEGHLELVVKTYKHGV--- 147
Cdd:PLN02252 633 EKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKVYFKNVhpk 712

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   148 ------VSKYFDKLKIRQYVEFKGPLGELEY----------DQDTATELGIIAGGSGITPVLQVLQEIIPSPEDLTHISL 211
Cdd:PLN02252 713 fpngglMSQYLDSLPIGDTIDVKGPLGHIEYagrgsflvngKPKFAKKLAMLAGGTGITPMYQVIQAILRDPEDKTEMSL 792

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   212 IYANETEDDILMKSQLDHMAKEYPH-FKVHYVIHKPNGK-WNGDVGYVTLEEMKRYLPKQAEDHRLLICGPPKMNEM-VL 288
Cdd:PLN02252 793 VYANRTEDDILLREELDRWAAEHPDrLKVWYVVSQVKREgWKYSVGRVTEAMLREHLPEGGDETLALMCGPPPMIEFaCQ 872

                        250       260
                 ....*....|....*....|....
gi 6323552   289 NYAKELGWSNgfhkgngtDKVFVF 312
Cdd:PLN02252 873 PNLEKMGYDK--------DSILVF 888
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
74-172 2.82e-42

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 141.18  E-value: 2.82e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552     74 ALPLSKKTRISRNTSLYCFKLKYPFERLHIPMGYHLAVRVTINGERLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKYFD 153
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVYPGGKMSQYLD 80

                          90
                  ....*....|....*....
gi 6323552    154 KLKIRQYVEFKGPLGELEY 172
Cdd:pfam00970  81 ELKIGDTIDFKGPLGRFEY 99
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
108-297 1.72e-37

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 133.38  E-value: 1.72e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  108 HLAVRVTINGERLVRYYTPVNVPNtEGHLELVVKTYKHGVVSKY-FDKLKIRQYVEFKGPLGELEYDQDTATELGIIAGG 186
Cdd:COG1018  39 FVTLRLPIDGKPLRRAYSLSSAPG-DGRLEITVKRVPGGGGSNWlHDHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGG 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  187 SGITPVLQVLQEIIPSpEDLTHISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHKPNGKWNgdvGYVTLEEMKRYL 266
Cdd:COG1018 118 IGITPFLSMLRTLLAR-GPFRPVTLVYGARSPADLAFRDELEALAARHPRLRLHPVLSREPAGLQ---GRLDAELLAALL 193

                       170       180       190
                ....*....|....*....|....*....|.
gi 6323552  267 PKQAEDHrLLICGPPKMNEMVLNYAKELGWS 297
Cdd:COG1018 194 PDPADAH-VYLCGPPPMMEAVRAALAELGVP 223
 
Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 75-312 1.33e-92

Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 274.44  E-value: 1.33e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   75 LPLSKKTRISRNTSLYCFKLKYPFERLHIPMGYHLAVRVTINGERLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKYFDK 154
Cdd:cd06183   1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYLHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  155 LKIRQYVEFKGPLGELEYDQDT-ATELGIIAGGSGITPVLQVLQEIIPSPEDLTHISLIYANETEDDILMKSQLDHMAKE 233
Cdd:cd06183  81 LKPGDTVEIRGPFGKFEYKPNGkVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKISLLYANRTEEDILLREELDELAKK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  234 YP-HFKVHYVIHKPNGKWNGDVGYVTLEEMKRYLPK-QAEDHRLLICGPPKMNEM-VLNYAKELGWSNgfhkgngtDKVF 310
Cdd:cd06183 161 HPdRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPPpPSEDTLVLVCGPPPMIEGaVKGLLKELGYKK--------DNVF 232


                ..
gi 6323552  311 VF 312
Cdd:cd06183 233 KF 234
PLN02252 PLN02252
nitrate reductase [NADPH]
 71-312 1.85e-67

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 226.10  E-value: 1.85e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552    71 KWVALPLSKKTRISRNTSLYCFKLKYPFERLHIPMGYHLAVRVTINGERLVRYYTPVNVPNTEGHLELVVKTYKHGV--- 147
Cdd:PLN02252 633 EKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKVYFKNVhpk 712

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   148 ------VSKYFDKLKIRQYVEFKGPLGELEY----------DQDTATELGIIAGGSGITPVLQVLQEIIPSPEDLTHISL 211
Cdd:PLN02252 713 fpngglMSQYLDSLPIGDTIDVKGPLGHIEYagrgsflvngKPKFAKKLAMLAGGTGITPMYQVIQAILRDPEDKTEMSL 792

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   212 IYANETEDDILMKSQLDHMAKEYPH-FKVHYVIHKPNGK-WNGDVGYVTLEEMKRYLPKQAEDHRLLICGPPKMNEM-VL 288
Cdd:PLN02252 793 VYANRTEDDILLREELDRWAAEHPDrLKVWYVVSQVKREgWKYSVGRVTEAMLREHLPEGGDETLALMCGPPPMIEFaCQ 872

                        250       260
                 ....*....|....*....|....
gi 6323552   289 NYAKELGWSNgfhkgngtDKVFVF 312
Cdd:PLN02252 873 PNLEKMGYDK--------DSILVF 888
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 42-286 1.73e-49

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 166.55  E-value: 1.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552    42 IVVVSLLQFVVLYATAFISIGTDKSLYRNkwvaLPLSKKTRISRNTSLYCFKLKYPFERLHIPMGYHLAVRVTING---- 117
Cdd:PTZ00319   7 IIALGVAAFFAFMFSRSPPVALDPDMFQH----FKLIKKTEVTHDTFIFRFALHSPTQRLGLPIGQHIVFRCDCTTpgkp 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   118 ERLVRYYTPVNVPNTEGHLELVVKTYKHGV---------VSKYFDKLKIRQYVEFKGPLGELEY---------------D 173
Cdd:PTZ00319  83 ETVQHSYTPISSDDEKGYVDFLIKVYFKGVhpsfpnggrLSQHLYHMKLGDKIEMRGPVGKFEYlgngtytvhkgkgglK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   174 QDTATELGIIAGGSGITPVLQVLQEIIPSPEDLTHISLIYANETEDDILMKSQLDHMAKEyPHFKVHYVIHKPNG-KWNG 252
Cdd:PTZ00319 163 TMHVDAFAMIAGGTGITPMLQIIHAIKKNKEDRTKVFLVYANQTEDDILLRKELDEAAKD-PRFHVWYTLDREATpEWKY 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 6323552   253 DVGYVTLEEMKRYLP----KQAEDHRL--LICGPPKMNEM 286
Cdd:PTZ00319 242 GTGYVDEEMLRAHLPvpdpQNSGIKKVmaLMCGPPPMLQM 281
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
74-172 2.82e-42

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 141.18  E-value: 2.82e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552     74 ALPLSKKTRISRNTSLYCFKLKYPFERLHIPMGYHLAVRVTINGERLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKYFD 153
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVYPGGKMSQYLD 80

                          90
                  ....*....|....*....
gi 6323552    154 KLKIRQYVEFKGPLGELEY 172
Cdd:pfam00970  81 ELKIGDTIDFKGPLGRFEY 99
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 78-295 1.40e-37

Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99778 [Multi-domain]  Cd Length: 223  Bit Score: 133.34  E-value: 1.40e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   78 SKKTRISRNTSLYCFKLKYPFErlHIPmGYHLAVRVTINGERLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKYFDKLKI 157
Cdd:cd00322   1 VATEDVTDDVRLFRLQLPNGFS--FKP-GQYVDLHLPGDGRGLRRAYSIASSPDEEGELELTVKIVPGGPFSAWLHDLKP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  158 RQYVEFKGPLGELEYDQDTATELGIIAGGSGITPVLQVLQEIIPSPEDLtHISLIYANETEDDILMKSQLDHMAKEYPHF 237
Cdd:cd00322  78 GDEVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGG-EITLLYGARTPADLLFLDELEELAKEGPNF 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6323552  238 KVHYVIHKPNGKWNGDVGYVTLEEMKRYLPKQAEDHRLLICGPPKMNEMVLNYAKELG 295
Cdd:cd00322 157 RLVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLG 214
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
108-297 1.72e-37

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 133.38  E-value: 1.72e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  108 HLAVRVTINGERLVRYYTPVNVPNtEGHLELVVKTYKHGVVSKY-FDKLKIRQYVEFKGPLGELEYDQDTATELGIIAGG 186
Cdd:COG1018  39 FVTLRLPIDGKPLRRAYSLSSAPG-DGRLEITVKRVPGGGGSNWlHDHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGG 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  187 SGITPVLQVLQEIIPSpEDLTHISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHKPNGKWNgdvGYVTLEEMKRYL 266
Cdd:COG1018 118 IGITPFLSMLRTLLAR-GPFRPVTLVYGARSPADLAFRDELEALAARHPRLRLHPVLSREPAGLQ---GRLDAELLAALL 193

                       170       180       190
                ....*....|....*....|....*....|.
gi 6323552  267 PKQAEDHrLLICGPPKMNEMVLNYAKELGWS 297
Cdd:COG1018 194 PDPADAH-VYLCGPPPMMEAVRAALAELGVP 223
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 183-287 1.19e-29

Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.


Pssm-ID: 425503 [Multi-domain]  Cd Length: 109  Bit Score: 108.89  E-value: 1.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552    183 IAGGSGITPVLQVLQEIIPSPEDLTHISLIYANETEDDILMKSQLDHMAKEYP-HFKVHYVIHKPNGKWNGDVGYVTLEE 261
Cdd:pfam00175   2 IAGGTGIAPVRSMLRAILEDPKDPTQVVLVFGNRNEDDILYREELDELAEKHPgRLTVVYVVSRPEAGWTGGKGRVQDAL 81

                          90       100
                  ....*....|....*....|....*.
gi 6323552    262 MKRYLPKQAEDHRLLICGPPKMNEMV 287
Cdd:pfam00175  82 LEDHLSLPDEETHVYVCGPPGMIKAV 107
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 106-295 7.60e-29

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99811 [Multi-domain]  Cd Length: 231  Bit Score: 110.37  E-value: 7.60e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  106 GYHLAVRVTINGERLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKYF-DKLKIRQYVEFKGPLGELEYDQDTATELGIIA 184
Cdd:cd06215  31 GQFLTLELEIDGETVYRAYTLSSSPSRPDSLSITVKRVPGGLVSNWLhDNLKVGDELWASGPAGEFTLIDHPADKLLLLS 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  185 GGSGITPVLQVLQEIIPSPEDlTHISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHKPN-GKWNGDVGYVTLEEMK 263
Cdd:cd06215 111 AGSGITPMMSMARWLLDTRPD-ADIVFIHSARSPADIIFADELEELARRHPNFRLHLILEQPApGAWGGYRGRLNAELLA 189

                       170       180       190
                ....*....|....*....|....*....|..
gi 6323552  264 RYLPKQAEDHrLLICGPPKMNEMVLNYAKELG 295
Cdd:cd06215 190 LLVPDLKERT-VFVCGPAGFMKAVKSLLAELG 220
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 102-295 1.25e-27

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99813 [Multi-domain]  Cd Length: 235  Bit Score: 107.35  E-value: 1.25e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  102 HIPmGYHLAVRVT-INGERLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKYF-DKLKIRQYVEFKGPLGELEYDQDTATE 179
Cdd:cd06217  31 FLA-GQHVDLRLTaIDGYTAQRSYSIASSPTQRGRVELTVKRVPGGEVSPYLhDEVKVGDLLEVRGPIGTFTWNPLHGDP 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  180 LGIIAGGSGITPVLQVLQEI--IPSPEDlthISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHKPNGK-WNGDVGY 256
Cdd:cd06217 110 VVLLAGGSGIVPLMSMIRYRrdLGWPVP---FRLLYSARTAEDVIFRDELEQLARRHPNLHVTEALTRAAPAdWLGPAGR 186

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 6323552  257 VTLEEMKRYLPkQAEDHRLLICGPPKMNEMVLNYAKELG 295
Cdd:cd06217 187 ITADLIAELVP-PLAGRRVYVCGPPAFVEAATRLLLELG 224
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 79-295 1.57e-27

NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 107.26  E-value: 1.57e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   79 KKTRISRNTslYCFKLKYPFERLHipmgyHLA---VRVTINGERLVRYYTPVNVPNTEGHLELVVKtyKHGVVSKYFDKL 155
Cdd:COG0543   4 SVERLAPDV--YLLRLEAPLIALK-----FKPgqfVMLRVPGDGLRRPFSIASAPREDGTIELHIR--VVGKGTRALAEL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  156 KIRQYVEFKGPLG---ELEYDQDTATelgIIAGGSGITPVLQVLQEIIpspEDLTHISLIYANETEDDILMKSQLdhmaK 232
Cdd:COG0543  75 KPGDELDVRGPLGngfPLEDSGRPVL---LVAGGTGLAPLRSLAEALL---ARGRRVTLYLGARTPEDLYLLDEL----E 144

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323552  233 EYPHFKVHYVIHKPngkWNGDVGYVTlEEMKRYLPKQaEDHRLLICGPPKMNEMVLNYAKELG 295
Cdd:COG0543 145 ALADFRVVVTTDDG---WYGRKGFVT-DALKELLAED-SGDDVYACGPPPMMKAVAELLLERG 202
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 46-297 1.23e-26

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 110.25  E-value: 1.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552     46 SLLQFVVlyataFISIGTDKS----------LYRNKWVALPLskktRISRNTSLYC-------FKLKYPFERLHIPMGYH 108
Cdd:PTZ00306  883 SLLECVV-----FGKIAGDRAatilqkkkygLSKDKWTTVVV----REVREGGQFGtgsrvlrFNLPGALQRSGLTLGQF 953

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552    109 LAVRVTINGERLVRYYTPVNVPNTEGHLELVVKTYKhGVVSKYFDKLKIRQYVEFKGpLGELEYDQDTA----------- 177
Cdd:PTZ00306  954 IAIRGDWDGQQLIGYYSPITLPDDLGVISILARGDK-GTLKEWISALRPGDSVEMKA-CGGLRIERRPAdkqfvfrghvi 1031

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552    178 TELGIIAGGSGITPVLQVLQEIIPSP--EDLTHISLIYANETEDDILMKSQLDHMAKEYP-HFKVHYVIHKPNGKWNGDV 254
Cdd:PTZ00306 1032 RKLALIAGGTGVAPMLQIIRAALKKPyvDSIESIRLIYAAEDVSELTYRELLESYRKENPgKFKCHFVLNNPPEGWTDGV 1111

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 6323552    255 GYVTLEEMKRYLPKQAEDHRLLICGPPKMNEMVLNYAKELGWS 297
Cdd:PTZ00306 1112 GFVDRALLQSALQPPSKDLLVAICGPPVMQRAVKADLLALGYN 1154
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 111-283 5.44e-26

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99784 [Multi-domain]  Cd Length: 224  Bit Score: 102.67  E-value: 5.44e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  111 VRVTINGE-RLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKY-FDKLKIRQYVEFKGPLGELEYDQDTATELGIIAGGSG 188
Cdd:cd06187  30 VNVTVPGRpRTWRAYSPANPPNEDGEIEFHVRAVPGGRVSNAlHDELKVGDRVRLSGPYGTFYLRRDHDRPVLCIAGGTG 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  189 ITPVLQVLQEIIPSPEDLThISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHKPNGKWNGDVGYVTlEEMKRYLPK 268
Cdd:cd06187 110 LAPLRAIVEDALRRGEPRP-VHLFFGARTERDLYDLEGLLALAARHPWLRVVPVVSHEEGAWTGRRGLVT-DVVGRDGPD 187

                       170
                ....*....|....*
gi 6323552  269 QAeDHRLLICGPPKM 283
Cdd:cd06187 188 WA-DHDIYICGPPAM 201
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
 122-283 5.93e-26

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 105.00  E-value: 5.93e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   122 RYYTPVNVPNTEGHLELVVKTYKHGVVSKYFDKLKIRQYVEFKGPLGELEYDQDTATELGIIAGGSGITPVLQV----LQ 197
Cdd:PTZ00274 104 RFYTPVTANHTKGYFDIIVKRKKDGLMTNHLFGMHVGDKLLFRSVTFKIQYRPNRWKHVGMIAGGTGFTPMLQIirhsLT 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   198 EIIPSPE-DLTHISLIYANETEDDILMKSQLDHMAKEYPH-FKVHYVIHKP--NGKWNGDVGYVTLEEMKRYLPKQAEDH 273
Cdd:PTZ00274 184 EPWDSGEvDRTKLSFLFCNRTERHILLKGLFDDLARRYSNrFKVYYTIDQAvePDKWNHFLGYVTKEMVRRTMPAPEEKK 263

                        170
                 ....*....|.
gi 6323552   274 R-LLICGPPKM 283
Cdd:PTZ00274 264 KiIMLCGPDQL 274
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 100-301 3.21e-25

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99812 [Multi-domain]  Cd Length: 243  Bit Score: 101.15  E-value: 3.21e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  100 RLHIPmGYHLAVRVTINGERLVRYYTPVNVPNTE-GHLELVVKTYKHGVVSKYF-DKLKIRQYVEFKGPLGELEYDQDTA 177
Cdd:cd06216  44 PGHRA-GQHVRLGVEIDGVRHWRSYSLSSSPTQEdGTITLTVKAQPDGLVSNWLvNHLAPGDVVELSQPQGDFVLPDPLP 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  178 TELGIIAGGSGITPVLQVLQEIIPSPEDlTHISLIYANETEDDILMKSQLDHMAKEYPHFKVHyVIHkpngkwngdvgyv 257
Cdd:cd06216 123 PRLLLIAAGSGITPVMSMLRTLLARGPT-ADVVLLYYARTREDVIFADELRALAAQHPNLRLH-LLY------------- 187

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 6323552  258 TLEEMKRYLPKQ--------AEDHRLLICGPPKMNEMVLNYAKELGWSNGFH 301
Cdd:cd06216 188 TREELDGRLSAAhldavvpdLADRQVYACGPPGFLDAAEELLEAAGLADRLH 239
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 92-283 9.24e-22

Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases.


Pssm-ID: 99807  Cd Length: 238  Bit Score: 91.62  E-value: 9.24e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   92 FKLKYPFERLHIPMGYhlaVRVTINGERLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKYF-DKLKIRQYVEFKGPLGEL 170
Cdd:cd06211  26 LKLDEPEEIEFQAGQY---VNLQAPGYEGTRAFSIASSPSDAGEIELHIRLVPGGIATTYVhKQLKEGDELEISGPYGDF 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  171 EYDQDTATELGIIAGGSGITPVLQVLQEIIPSPEDLThISLIYANETEDDILMKSQLDHMAKEYPHFKvhYV----IHKP 246
Cdd:cd06211 103 FVRDSDQRPIIFIAGGSGLSSPRSMILDLLERGDTRK-ITLFFGARTRAELYYLDEFEALEKDHPNFK--YVpalsREPP 179

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 6323552  247 NGKWNGDVGYVTlEEMKRYLPKQAEDHRLLICGPPKM 283
Cdd:cd06211 180 ESNWKGFTGFVH-DAAKKHFKNDFRGHKAYLCGPPPM 215
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 106-295 5.54e-21

NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation oxidoreductase. PA oxidoreductases of E. coli hydroxylate PA-CoA in the second step of PA degradation. Members of this group typically fuse a ferredoxin reductase-like domain with an iron-sulfur binding cluster domain. Ferredoxins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal portion may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99810 [Multi-domain]  Cd Length: 241  Bit Score: 89.52  E-value: 5.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  106 GYHLAVRVTINGERLVRYY----TPvnvpnTEGHLELVVKTYKHGVVSKY-FDKLKIRQYVEFKGPLGELEYDQDTATE- 179
Cdd:cd06214  36 GQFLTLRVPIDGEEVRRSYsicsSP-----GDDELRITVKRVPGGRFSNWaNDELKAGDTLEVMPPAGRFTLPPLPGARh 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  180 LGIIAGGSGITPVL----QVLQEiipspEDLTHISLIYANETEDDILMKSQLDHMAKEYP-HFKVHYVIHKPNGKWNGDV 254
Cdd:cd06214 111 YVLFAAGSGITPVLsilkTALAR-----EPASRVTLVYGNRTEASVIFREELADLKARYPdRLTVIHVLSREQGDPDLLR 185

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 6323552  255 GYVTLEEMKRYLP---KQAEDHRLLICGPPKMNEMVLNYAKELG 295
Cdd:cd06214 186 GRLDAAKLNALLKnllDATEFDEAFLCGPEPMMDAVEAALLELG 229
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 111-295 1.51e-20

Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent hydroxylation of methane to methanol. This multicomponent enzyme mediates electron transfer via a hydroxylase (MMOH), a coupling protein, and a reductase which is comprised of an N-terminal [2Fe-2S] ferredoxin domain, an FAD binding subdomain, and an NADH binding subdomain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. Dioxygenases add both atom of oxygen to the substrate, while mono-oxygenases add one atom to the substrate and one atom to water.


Pssm-ID: 99806  Cd Length: 236  Bit Score: 88.17  E-value: 1.51e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  111 VRVTINGERLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKYF-DKLKIRQYVEFKGPLGELEYDQDTATELGIIAGGSGI 189
Cdd:cd06210  41 VEIEIPGTDTRRSYSLANTPNWDGRLEFLIRLLPGGAFSTYLeTRAKVGQRLNLRGPLGAFGLRENGLRPRWFVAGGTGL 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  190 TPVLQVLQEII----PSPedlTHisLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHKPNGKWNGDVGYVtLEEMKRY 265
Cdd:cd06210 121 APLLSMLRRMAewgePQE---AR--LFFGVNTEAELFYLDELKRLADSLPNLTVRICVWRPGGEWEGYRGTV-VDALRED 194

                       170       180       190
                ....*....|....*....|....*....|
gi 6323552  266 LPKQAEDHRLLICGPPKMNEMVLNYAKELG 295
Cdd:cd06210 195 LASSDAKPDIYLCGPPGMVDAAFAAAREAG 224
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 111-295 4.92e-20

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate.


Pssm-ID: 99808 [Multi-domain]  Cd Length: 232  Bit Score: 87.00  E-value: 4.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  111 VRVTINGERLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKYFD-KLKIRQYVEFKGPLGELEYDQDTATELGIIAGGSGI 189
Cdd:cd06212  36 VDITVPGTEETRSFSMANTPADPGRLEFIIKKYPGGLFSSFLDdGLAVGDPVTVTGPYGTCTLRESRDRPIVLIGGGSGM 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  190 TPVLQVLQEIIPSPEDLThISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHK--PNGKWNGDVGYVTlEEMKRYLP 267
Cdd:cd06212 116 APLLSLLRDMAASGSDRP-VRFFYGARTARDLFYLEEIAALGEKIPDFTFIPALSEspDDEGWSGETGLVT-EVVQRNEA 193

                       170       180
                ....*....|....*....|....*...
gi 6323552  268 kQAEDHRLLICGPPKMNEMVLNYAKELG 295
Cdd:cd06212 194 -TLAGCDVYLCGPPPMIDAALPVLEMSG 220
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 102-295 5.87e-20

FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.


Pssm-ID: 99781  Cd Length: 247  Bit Score: 86.84  E-value: 5.87e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  102 HIPmGYHLAVRVTINGE--RLVRYYTPVNVPNtEGHLELVVKTYKHGVVSKYF-DKLKIRQYVEFKGPLGELEYDQDTAT 178
Cdd:cd06184  37 FLP-GQYLSVRVKLPGLgyRQIRQYSLSDAPN-GDYYRISVKREPGGLVSNYLhDNVKVGDVLEVSAPAGDFVLDEASDR 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  179 ELGIIAGGSGITPVLQVLQEIIpSPEDLTHISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHKPNGKWNGD----V 254
Cdd:cd06184 115 PLVLISAGVGITPMLSMLEALA-AEGPGRPVTFIHAARNSAVHAFRDELEELAARLPNLKLHVFYSEPEAGDREEdydhA 193

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 6323552  255 GYVTLEEMKRYLPKQaeDHRLLICGPPKMNEMVLNYAKELG 295
Cdd:cd06184 194 GRIDLALLRELLLPA--DADFYLCGPVPFMQAVREGLKALG 232
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 116-295 9.93e-20

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 88.38  E-value: 9.93e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  116 NGERLVRYYTPVNVPNTEGHLELVVK------TYKHGVVSKYFDKLKIRQYVEFKGPLGELeYDQDTATELGIIAGGSGI 189
Cdd:COG2871 195 NDEEVTRAYSMANYPAEKGIIELNIRiatppmDVPPGIGSSYIFSLKPGDKVTISGPYGEF-FLRDSDREMVFIGGGAGM 273

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  190 TPVLQVLQEIIPSPEDLTHISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIH--KPNGKWNGDVGYVT--LEEmkRY 265
Cdd:COG2871 274 APLRSHIFDLLERGKTDRKITFWYGARSLRELFYLEEFRELEKEHPNFKFHPALSepLPEDNWDGETGFIHevLYE--NY 351

                       170       180       190
                ....*....|....*....|....*....|..
gi 6323552  266 LPKQA--EDHRLLICGPPKMNEMVLNYAKELG 295
Cdd:COG2871 352 LKDHPapEDCEAYLCGPPPMIDAVIKMLDDLG 383
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
124-295 2.58e-19

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 87.64  E-value: 2.58e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  124 YTPVNVPNTEGHLELVVKT---YKHGVvskyfDKLKIRQYVEFKGPLGELEYDQ-DTATELGIIAGGSGITPVLQVLQEI 199
Cdd:COG4097 266 FSISSAPGGDGRLRFTIKAlgdFTRRL-----GRLKPGTRVYVEGPYGRFTFDRrDTAPRQVWIAGGIGITPFLALLRAL 340

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  200 IPSPEDLTHISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIhkpngkwNGDVGYVTLEEMKRYLPKQAEdHRLLICG 279
Cdd:COG4097 341 AARPGDQRPVDLFYCVRDEEDAPFLEELRALAARLAGLRLHLVV-------SDEDGRLTAERLRRLVPDLAE-ADVFFCG 412

                       170
                ....*....|....*.
gi 6323552  280 PPKMNEMVLNYAKELG 295
Cdd:COG4097 413 PPGMMDALRRDLRALG 428
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 110-295 9.30e-19

Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal region may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99793 [Multi-domain]  Cd Length: 218  Bit Score: 83.06  E-value: 9.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  110 AVRVTIN--GERL-VRYYTPVNVPNtEGHLELVVKTY-KHGVVSKYFDKLKIRQYVEFKGPLGELEYDQDtatelG-IIA 184
Cdd:cd06196  33 ATEVAIDkpGWRDeKRPFTFTSLPE-DDVLEFVIKSYpDHDGVTEQLGRLQPGDTLLIEDPWGAIEYKGP-----GvFIA 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  185 GGSGITPVLQVLQEIIPSpEDLTHISLIYANETEDDILMKSQLDHMakeyPHFKVHYVI-HKPNGKWngDVGYVTLEEMK 263
Cdd:cd06196 107 GGAGITPFIAILRDLAAK-GKLEGNTLIFANKTEKDIILKDELEKM----LGLKFINVVtDEKDPGY--AHGRIDKAFLK 179

                       170       180       190
                ....*....|....*....|....*....|..
gi 6323552  264 RYLPKQAEdhRLLICGPPKMNEMVLNYAKELG 295
Cdd:cd06196 180 QHVTDFNQ--HFYVCGPPPMEEAINGALKELG 209
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 77-283 7.11e-18

Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates toluene and forms p-cresol as part of a three component toluene-4-monoxygenase system. Electron transfer is from NADH to an NADH:ferredoxin oxidoreductase (TmoF in P. mendocina) to ferredoxin to an iron-containing oxygenase. TmoF is homologous to other mono- and dioxygenase systems within the ferredoxin reductase family.


Pssm-ID: 99787  Cd Length: 232  Bit Score: 80.76  E-value: 7.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   77 LSKKTRISRNTSLYCFKLKYPFERLhiPMGYHLavrVTINGERLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKY-FDKL 155
Cdd:cd06190   1 LVDVRELTHDVAEFRFALDGPADFL--PGQYAL---LALPGVEGARAYSMANLANASGEWEFIIKRKPGGAASNAlFDNL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  156 KIRQYVEFKGPLGELEYDQDTATELGIIAGGSGITPVLQVLQEIIPSPEDLTH-ISLIYANETEDDILMKSQLDhMAKEY 234
Cdd:cd06190  76 EPGDELELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSDRpVDLFYGGRTPSDLCALDELS-ALVAL 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 6323552  235 PH-FKVHYVI----HKPNGKWNGDVGYVTlEEMKRYLPKQAEDHRLLICGPPKM 283
Cdd:cd06190 155 GArLRVTPAVsdagSGSAAGWDGPTGFVH-EVVEATLGDRLAEFEFYFAGPPPM 207
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 107-295 1.55e-17

Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) provides a means of storing redox reaction energy via the transmembrane translocation of Na2+ ions. The C-terminal domain resembles ferredoxin:NADP+ oxidoreductase, and has NADH and FAD binding sites. (Na+-NQR) is distinct from H+-translocating NADH:quinone oxidoreductases and noncoupled NADH:quinone oxidoreductases. The NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain of this group typically contains an iron-sulfur cluster binding domain.


Pssm-ID: 99785 [Multi-domain]  Cd Length: 283  Bit Score: 80.81  E-value: 1.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  107 YHLAVRVTINGERLVRYYTPVNVPNTEGHLELVVK---------TYKHGVVSKYFDKLKIRQYVEFKGPLGELeYDQDTA 177
Cdd:cd06188  72 FGLWQLVFKHDEPVSRAYSLANYPAEEGELKLNVRiatpppgnsDIPPGIGSSYIFNLKPGDKVTASGPFGEF-FIKDTD 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  178 TELGIIAGGSGITPVLQVLQEIIPSPEDLTHISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHKP--NGKWNGDVG 255
Cdd:cd06188 151 REMVFIGGGAGMAPLRSHIFHLLKTLKSKRKISFWYGARSLKELFYQEEFEALEKEFPNFKYHPVLSEPqpEDNWDGYTG 230

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6323552  256 YVTLEEMKRYLPKQA--EDHRLLICGPPKMNEMVLNYAKELG 295
Cdd:cd06188 231 FIHQVLLENYLKKHPapEDIEFYLCGPPPMNSAVIKMLDDLG 272
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 122-283 2.07e-17

NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.


Pssm-ID: 99786 [Multi-domain]  Cd Length: 224  Bit Score: 79.52  E-value: 2.07e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  122 RYYTPVNVPNTEGHLELVVKTYKHGVVSKY-FDKLKIRQYVEFKGPLGELEYDQDTATELGIIAGGSGITPVLQVLQEII 200
Cdd:cd06189  42 RPFSIASAPHEDGEIELHIRAVPGGSFSDYvFEELKENGLVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLL 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  201 PSPEDlTHISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHKPNGKWNGDVGYVtleemkrylpKQA--------ED 272
Cdd:cd06189 122 AQGSK-RPIHLYWGARTEEDLYLDELLEAWAEAHPNFTYVPVLSEPEEGWQGRTGLV----------HEAvledfpdlSD 190

                       170
                ....*....|.
gi 6323552  273 HRLLICGPPKM 283
Cdd:cd06189 191 FDVYACGSPEM 201
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
112-293 7.71e-17

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 79.79  E-value: 7.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   112 RVTINGERLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKYF-DKLKIRQYVEFKGPLGELeYDQDTATELGIIAGGSGIT 190
Cdd:PRK11872 144 RLQIPGTDDWRSYSFANRPNATNQLQFLIRLLPDGVMSNYLrERCQVGDEILFEAPLGAF-YLREVERPLVFVAGGTGLS 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   191 PVLQVLQEIIPSPEDLThISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHKPNGKWNGDVGYVTLEEMKRYLPKQA 270
Cdd:PRK11872 223 AFLGMLDELAEQGCSPP-VHLYYGVRHAADLCELQRLAAYAERLPNFRYHPVVSKASADWQGKRGYIHEHFDKAQLRDQA 301

                        170       180
                 ....*....|....*....|...
gi 6323552   271 EDhrLLICGPPKMNEMVLNYAKE 293
Cdd:PRK11872 302 FD--MYLCGPPPMVEAVKQWLDE 322
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 130-283 8.93e-17

Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 78.42  E-value: 8.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  130 PNTEGHLELVVKtyKHGVVSKYFDKLKIRQYVEFKGPLG-----ELEYDQDtateLGIIAGGSGITPVLQVLQEIIPSPE 204
Cdd:cd06221  52 PTRRGPLELTIR--RVGRVTEALHELKPGDTVGLRGPFGngfpvEEMKGKD----LLLVAGGLGLAPLRSLINYILDNRE 125

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323552  205 DLTHISLIYANETEDDILMKSQLDHMAKEyPHFKVHYVIHKPNGKWNGDVGYVTlEEMKRYLPKQAEDhRLLICGPPKM 283
Cdd:cd06221 126 DYGKVTLLYGARTPEDLLFKEELKEWAKR-SDVEVILTVDRAEEGWTGNVGLVT-DLLPELTLDPDNT-VAIVCGPPIM 201
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 111-295 1.83e-16

Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group.


Pssm-ID: 99805 [Multi-domain]  Cd Length: 228  Bit Score: 76.86  E-value: 1.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  111 VRVTINGERLVRYYTPVNVPNtEGHLELVVKTYKHGVVSKYF-DKLKIRQYVEFKGPLGELeYDQDTATELGIIAGGSGI 189
Cdd:cd06209  37 VNLQVPGTDETRSYSFSSAPG-DPRLEFLIRLLPGGAMSSYLrDRAQPGDRLTLTGPLGSF-YLREVKRPLLMLAGGTGL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  190 TPVLQVLQEIIPSPEDLThISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHKPNgKWNGDVGYVT--LEEmkRYLP 267
Cdd:cd06209 115 APFLSMLDVLAEDGSAHP-VHLVYGVTRDADLVELDRLEALAERLPGFSFRTVVADPD-SWHPRKGYVTdhLEA--EDLN 190

                       170       180
                ....*....|....*....|....*...
gi 6323552  268 kqAEDHRLLICGPPKMNEMVLNYAKELG 295
Cdd:cd06209 191 --DGDVDVYLCGPPPMVDAVRSWLDEQG 216
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 97-295 2.75e-16

Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with a C-terminal iron-sulfur binding cluster domain. FNR was intially identified as a chloroplast reductase activity catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methnae assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99788 [Multi-domain]  Cd Length: 231  Bit Score: 76.41  E-value: 2.75e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   97 PFERLHIPmGYHLAVRVTINGERLVRYYTpVNVPNTEGHLELVVKTYKHGVVSKYF-DKLKIRQYVEFKGPLGELEYDQD 175
Cdd:cd06191  23 PLQYGFRP-GQHVTLKLDFDGEELRRCYS-LCSSPAPDEISITVKRVPGGRVSNYLrEHIQPGMTVEVMGPQGHFVYQPQ 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  176 TATELGIIAGGSGITPVLQVLQEIIPSPEDlTHISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHK--PNGKWNGD 253
Cdd:cd06191 101 PPGRYLLVAAGSGITPLMAMIRATLQTAPE-SDFTLIHSARTPADMIFAQELRELADKPQRLRLLCIFTRetLDSDLLHG 179

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6323552  254 VGYVTLEEMKRYLPKQAEDhRLLICGPPKMNEMVLNYAKELG 295
Cdd:cd06191 180 RIDGEQSLGAALIPDRLER-EAFICGPAGMMDAVETALKELG 220
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 124-295 1.73e-14

NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 71.13  E-value: 1.73e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  124 YTPVNVPNTEGHLELVVKT---YKHGVVskyfDKLKIRQYVEFKGPLGELEYDQDTATELgIIAGGSGITPVLQVLQEII 200
Cdd:cd06198  44 FTISSAPDPDGRLRFTIKAlgdYTRRLA----ERLKPGTRVTVEGPYGRFTFDDRRARQI-WIAGGIGITPFLALLEALA 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  201 PSPeDLTHISLIYANETEDDILMKSQLDHMAKEYpHFKVHYVIHKPNGkwngdvgYVTLEEMKRYLPKQAEDHRLLICGP 280
Cdd:cd06198 119 ARG-DARPVTLFYCVRDPEDAVFLDELRALAAAA-GVVLHVIDSPSDG-------RLTLEQLVRALVPDLADADVWFCGP 189

                       170
                ....*....|....*
gi 6323552  281 PKMNEMVLNYAKELG 295
Cdd:cd06198 190 PGMADALEKGLRALG 204
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 113-283 2.11e-13

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate while mono-oxygenases add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99809  Cd Length: 227  Bit Score: 68.11  E-value: 2.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  113 VTINGERLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKY-FDKLKIRQYVEFKGPLGELEYDQDTATELgIIAGGSGITP 191
Cdd:cd06213  36 LTLPGLPAARSYSFANAPQGDGQLSFHIRKVPGGAFSGWlFGADRTGERLTVRGPFGDFWLRPGDAPIL-CIAGGSGLAP 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  192 VLQVLQEIIPS--PEDLThisLIYANETEDDILMKSQLDHMAKEY-PHFKVHYVI-HKP-NGKWNGDVGYVTlEEMKRYL 266
Cdd:cd06213 115 ILAILEQARAAgtKRDVT---LLFGARTQRDLYALDEIAAIAARWrGRFRFIPVLsEEPaDSSWKGARGLVT-EHIAEVL 190

                       170
                ....*....|....*..
gi 6323552  267 PKQAEDHrllICGPPKM 283
Cdd:cd06213 191 LAATEAY---LCGPPAM 204
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 111-304 5.61e-13

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an N-terminal Iron-Sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99791 [Multi-domain]  Cd Length: 222  Bit Score: 66.91  E-value: 5.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  111 VRVTINGERLVRY-----------------YTPVNVPNTEGHLELVVKTYKHGVVS-KYFDKLKIRQYVEFKGPLGELEY 172
Cdd:cd06194  12 LRVRLEPDRPLPYlpgqyvnlrragglarsYSPTSLPDGDNELEFHIRRKPNGAFSgWLGEEARPGHALRLQGPFGQAFY 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  173 DQDTAT-ELGIIAGGSGITPVLQVLQEII---PSPEdlthISLIYANETEDDILMKSQLDHMAKEYPHFkvHY---VIHK 245
Cdd:cd06194  92 RPEYGEgPLLLVGAGTGLAPLWGIARAALrqgHQGE----IRLVHGARDPDDLYLHPALLWLAREHPNF--RYipcVSEG 165

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6323552  246 PNGKWNGDVGYVTLEemkryLPKQAEDHRLLICGPPkmnEMVlNYAKELGWSNGFHKGN 304
Cdd:cd06194 166 SQGDPRVRAGRIAAH-----LPPLTRDDVVYLCGAP---SMV-NAVRRRAFLAGAPMKR 215
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 130-294 4.78e-10

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 59.43  E-value: 4.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   130 PNTEGHLELVVKtyKHGVVSKYFDKLKIRQYVEFKGPLGE-LEYDQDTATELGIIAGGSGITPVLQVLQEIIPSPEDLTH 208
Cdd:PRK08345  62 PTRKGFFELCIR--RAGRVTTVIHRLKEGDIVGVRGPYGNgFPVDEMEGMDLLLIAGGLGMAPLRSVLLYAMDNRWKYGN 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   209 ISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHKpNGKWNGDVGYvtleeMKRYLPK---------------QAEDH 273
Cdd:PRK08345 140 ITLIYGAKYYEDLLFYDELIKDLAEAENVKIIQSVTR-DPEWPGCHGL-----PQGFIERvckgvvtdlfreantDPKNT 213

                        170       180
                 ....*....|....*....|.
gi 6323552   274 RLLICGPPKMNEMVLnyaKEL 294
Cdd:PRK08345 214 YAAICGPPVMYKFVF---KEL 231
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 116-283 9.59e-10

CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 58.73  E-value: 9.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   116 NGERlvRYYTPVNVPNTEGHLELVVKTYKHGVVSKY-FDKLKIRQYVEFKGPLGELEYDQDTATELGIIAGGSGITPVlq 194
Cdd:PRK07609 144 DGKR--RSYSIANAPHSGGPLELHIRHMPGGVFTDHvFGALKERDILRIEGPLGTFFLREDSDKPIVLLASGTGFAPI-- 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   195 vlQEIIpspEDLTH------ISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHKPNGK--WNGDVGYVtleemkryl 266
Cdd:PRK07609 220 --KSIV---EHLRAkgiqrpVTLYWGARRPEDLYLSALAEQWAEELPNFRYVPVVSDALDDdaWTGRTGFV--------- 285

                        170       180
                 ....*....|....*....|....*
gi 6323552   267 pKQA--EDHRLL------ICGPPKM 283
Cdd:PRK07609 286 -HQAvlEDFPDLsghqvyACGSPVM 309
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 116-297 1.68e-09

Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99792 [Multi-domain]  Cd Length: 241  Bit Score: 57.19  E-value: 1.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  116 NGERLVRYYTPVNvPNTEGHLELVVKTYKHGVVSKYFDKLKI--RQYVEfKGPLGELEYDQDTATE-LGIIAGGSGITPV 192
Cdd:cd06195  39 DGKLVRRAYSIAS-APYEENLEFYIILVPDGPLTPRLFKLKPgdTIYVG-KKPTGFLTLDEVPPGKrLWLLATGTGIAPF 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  193 LQVLQEIIPSpEDLTHISLIYANETEDDILMKSQLDHMAKEYPHfKVHYV--IHKPNGKWNGDvGYVT-------LEEMK 263
Cdd:cd06195 117 LSMLRDLEIW-ERFDKIVLVHGVRYAEELAYQDEIEALAKQYNG-KFRYVpiVSREKENGALT-GRIPdliesgeLEEHA 193

                       170       180       190
                ....*....|....*....|....*....|....
gi 6323552  264 RyLPKQAEDHRLLICGPPKMNEMVLNYAKELGWS 297
Cdd:cd06195 194 G-LPLDPETSHVMLCGNPQMIDDTQELLKEKGFS 226
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 96-302 1.64e-07

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 52.02  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552    96 YPFErlhiPMGYHLavrVTI-NGERLVRYYTPVNVPNTEGHLELVVKTYKHGVVSKYF-DKLKIRQYVEFKGPLGELEYD 173
Cdd:PRK10684  35 YPYR----AGQYAL---VSIrNSAETLRAYTLSSTPGVSEFITLTVRRIDDGVGSQWLtRDVKRGDYLWLSDAMGEFTCD 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   174 QDTATELGIIAGGSGITPVLQVLQEIIP-SPEdlTHISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVihkpnGKWNG 252
Cdd:PRK10684 108 DKAEDKYLLLAAGCGVTPIMSMRRWLLKnRPQ--ADVQVIFNVRTPQDVIFADEWRQLKQRYPQLNLTLV-----AENNA 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6323552   253 DVGYV----TLEEMKRYLPKQAeDHRLLICGP-PKMNeMVLNYAKELGWSNG-FHK 302
Cdd:PRK10684 181 TEGFIagrlTRELLQQAVPDLA-SRTVMTCGPaPYMD-WVEQEVKALGVTADrFFK 234
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 124-295 3.06e-07

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 50.00  E-value: 3.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  124 YTPVNVPNTE-GHLELVVKTYK-------HGVVSKYFDKLKIRQYVEfkGPLGELEYDQDTATELGIIAGGSGITPVLQV 195
Cdd:cd06186  47 FTIASSPEDEqDTLSLIIRAKKgfttrllRKALKSPGGGVSLKVLVE--GPYGSSSEDLLSYDNVLLVAGGSGITFVLPI 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  196 LQEII---PSPEDLTHISLIYANETEDDIL-MKSQLDHMAKEYPHFKVHYvihkpngkwngdvgYVTleemkrylpkqae 271
Cdd:cd06186 125 LRDLLrrsSKTSRTRRVKLVWVVRDREDLEwFLDELRAAQELEVDGEIEI--------------YVT------------- 177

                       170       180
                ....*....|....*....|....
gi 6323552  272 dhRLLICGPPKMNEMVLNYAKELG 295
Cdd:cd06186 178 --RVVVCGPPGLVDDVRNAVAKKG 199
fre PRK08051
FMN reductase; Validated
 117-283 8.61e-07

FMN reductase; Validated


Pssm-ID: 236142 [Multi-domain]  Cd Length: 232  Bit Score: 49.08  E-value: 8.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   117 GERLVRYYTPVNVPNTEGHLEL-----VVKTYKHGVVskyfDKLKIRQYVEFKGPLGELEYDQDTATELGIIAGGSGITP 191
Cdd:PRK08051  41 GEKDKRPFSIASTPREKGFIELhigasELNLYAMAVM----ERILKDGEIEVDIPHGDAWLREESERPLLLIAGGTGFSY 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   192 VLQVLQEIIP-SPEDltHISLIYANETEDDILMKSQLDHMAKEYPHFKVHYVIHKPNGKWNGDVGYVtLEEMKrylpkqa 270
Cdd:PRK08051 117 ARSILLTALAqGPNR--PITLYWGGREEDHLYDLDELEALALKHPNLHFVPVVEQPEEGWQGKTGTV-LTAVM------- 186

                        170
                 ....*....|....*....
gi 6323552   271 EDHRLL------ICGPPKM 283
Cdd:PRK08051 187 QDFGSLaeydiyIAGRFEM 205
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 78-222 7.87e-06

FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and have a variety of physiological functions in a variety of organisms including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99794  Cd Length: 220  Bit Score: 46.23  E-value: 7.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   78 SKKTRISRNTSLYCFKLKYPFERLHI--------------PMGY-HLAVR--VTINGERlVRYYTPVNVPN-TEGHLELV 139
Cdd:cd06197   1 IKSEVITPTLTRFTFELSPPDVVGKWtpgqyitldfsselDSGYsHMADDdpQSLNDDF-VRTFTVSSAPPhDPATDEFE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  140 VKTYKHGVVSKYFDKLKIRQY-----VEFKGPLGELEYD---QDTATELGIIAGGSGITPVLQVLQEIIPSPEDLTHISL 211
Cdd:cd06197  80 ITVRKKGPVTGFLFQVARRLReqgleVPVLGVGGEFTLSlpgEGAERKMVWIAGGVGITPFLAMLRAILSSRNTTWDITL 159

                       170
                ....*....|.
gi 6323552  212 IYANETEDDIL 222
Cdd:cd06197 160 LWSLREDDLPL 170
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 77-295 3.33e-05

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 45.50  E-value: 3.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552    77 LSKKTRISRNtsLYCFKLKYPFERLHIPMGYHLAVRVTINGERLVryYTPVNVPNTEGHLELVVKTYkhGVVSKYFDKLK 156
Cdd:PRK12778   4 IVEKEIFSEK--VFLLEIEAPLIAKSRKPGQFVIVRVGEKGERIP--LTIADADPEKGTITLVIQEV--GLSTTKLCELN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   157 IRQYVE-FKGPLGELEYDQDTATELgIIAGGSGITPVLQVLQEIIPSPEDLThisLIYANETEDDILMKSQLDHMAKEyp 235
Cdd:PRK12778  78 EGDYITdVVGPLGNPSEIENYGTVV-CAGGGVGVAPMLPIVKALKAAGNRVI---TILGGRSKELIILEDEMRESSDE-- 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   236 hfkvhYVIHKPNGKWnGDVGYVTlEEMKRYLPKQAEDHRLLICGPPKMNEMVLNYAKELG 295
Cdd:PRK12778 152 -----VIIMTDDGSY-GRKGLVT-DGLEEVIKRETKVDKVFAIGPAIMMKFVCLLTKKYG 204
PRK10926 PRK10926
ferredoxin-NADP reductase; Provisional
 115-283 3.90e-05

ferredoxin-NADP reductase; Provisional


Pssm-ID: 182844  Cd Length: 248  Bit Score: 44.30  E-value: 3.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   115 INGERLVRYYTPVNVPNtEGHLELVVKTYKHGVVSKYFDKLKIRQYV----EFKG--PLGELEyDQDTateLGIIAGGSG 188
Cdd:PRK10926  43 IDGERVQRAYSYVNAPD-NPDLEFYLVTVPEGKLSPRLAALKPGDEVqvvsEAAGffVLDEVP-DCET---LWMLATGTA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552   189 ITPVLQVLQEiipsPEDL---THISLIYANETEDDILMKSQLDHMAKEYP-HFKVHYVIHKPN--GKWNGDVGYV----T 258
Cdd:PRK10926 118 IGPYLSILQE----GKDLerfKNLVLVHAARYAADLSYLPLMQELEQRYEgKLRIQTVVSRETapGSLTGRVPALiesgE 193

                        170       180
                 ....*....|....*....|....*
gi 6323552   259 LEEMKRyLPKQAEDHRLLICGPPKM 283
Cdd:PRK10926 194 LEAAVG-LPMDAETSHVMLCGNPQM 217
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 136-283 5.00e-05

These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but lack the FAD-binding region connecting sub-domain. Ferredoxin-NADP+ reductase (FNR) is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins, such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2, which then transfers two electrons and a proton to NADP+ to form NADPH. CYPOR serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases, sulfite reducatase, and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal FNR-like FAD and NAD binding module, an FMN-binding domain, and an additional connecting domain (inserted within the FAD binding region) that orients the FNR and FMN -binding domains. The C-terminal domain contains most of the NADP(H) binding residues, and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule, which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99804 [Multi-domain]  Cd Length: 286  Bit Score: 44.23  E-value: 5.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  136 LELVVK--TYKH--------GVVSKYFDKLKIRQYVEFKGPLG-ELEYDQDTATELGIIAGGSGITPVLQVLQ----EII 200
Cdd:cd06208  83 LSLCVKrlVYTDpetdetkkGVCSNYLCDLKPGDDVQITGPVGkTMLLPEDPNATLIMIATGTGIAPFRSFLRrlfrEKH 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  201 PSPEDLTHISLIYANETEDDILMKSQLDHMAKEYP-HFKVHYVIHKPNGKWNGDVGYVTlEEMKRYLPK-----QAEDHR 274
Cdd:cd06208 163 ADYKFTGLAWLFFGVPNSDSLLYDDELEKYPKQYPdNFRIDYAFSREQKNADGGKMYVQ-DRIAEYAEEiwnllDKDNTH 241


                ....*....
gi 6323552  275 LLICGPPKM 283
Cdd:cd06208 242 VYICGLKGM 250
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 126-295 5.33e-04

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 40.69  E-value: 5.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  126 PVNVPNTEGHLELVVKtyKHGVVSKYFDKLKIRQYVEFKGPLG---ELEYDQdtateLGIIAGGSGITPvlqvlqeIIPS 202
Cdd:cd06220  41 PMSLSYIDGPNSITVK--KVGEATSALHDLKEGDKLGIRGPYGngfELVGGK-----VLLIGGGIGIAP-------LAPL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323552  203 PEDLT---HISLIYANETEDDILMKSQLDhmakeyphfKVHYVIHKPNGKWNGDVGYVT--LEEMkrylpKQAEDHRLLI 277
Cdd:cd06220 107 AERLKkaaDVTVLLGARTKEELLFLDRLR---------KSDELIVTTDDGSYGFKGFVTdlLKEL-----DLEEYDAIYV 172

                       170
                ....*....|....*...
gi 6323552  278 CGPPKMNEMVLNYAKELG 295
Cdd:cd06220 173 CGPEIMMYKVLEILDERG 190
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 161-223 2.00e-03

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 39.83  E-value: 2.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323552   161 VEFKGPLGELEYDQDTATELGIIAGGSGITPVLQVLQEIIPSPEDL----THISLIYANETEDDILM 223
Cdd:PLN02844 407 VAIEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSRyrfpKRVQLIYVVKKSQDICL 473
 
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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