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Conserved domains on  [gi|446304674|ref|WP_000382529|]
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MULTISPECIES: PDR/VanB family oxidoreductase [Acinetobacter]

Protein Classification

PDR/VanB family oxidoreductase( domain architecture ID 18977663)

PDR/VanB family oxidoreductase containing a 2Fe-2S iron-sulfur cluster binding domain, similar to phthalate dioxygenase reductase (PDR), which is involved in the pyridine nucleotide-dependent dihydroxylation of phthalate, and to vanillate O-demethylase oxidoreductase, which plays a role in the degradation of aromatic compounds

CATH:  3.10.20.30|3.40.50.80|2.40.30.10
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0051537|GO:0046872|GO:0010181
PubMed:  11192725|11734195
SCOP:  4000241|4003789|4002840

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 8-216 1.04e-105

Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal.


:

Pssm-ID: 99782 [Multi-domain]  Cd Length: 211  Bit Score: 307.10  E-value: 1.04e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   8 IHQLTPTIRAFELVAANGKALPSFEAGAHIDVHLKNGLTRQYSLSNCCTEKHRYVIGVLHDANSRGGSRCIHTEYREGDH 87
Cdd:cd06185    3 IRDEAPDIRSFELEAPDGAPLPAFEPGAHIDVHLPNGLVRQYSLCGDPADRDRYRIAVLREPASRGGSRYMHELLRVGDE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  88 LKIGEPRNLFEIHSQTKQAVLFAGGIGITPILSMAYRLKSANIPFELHYFVRSHEMIAFYGNLTEHFGDQVHFHIQDQpD 167
Cdd:cd06185   83 LEVSAPRNLFPLDEAARRHLLIAGGIGITPILSMARALAARGADFELHYAGRSREDAAFLDELAALPGDRVHLHFDDE-G 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446304674 168 TECNMAEALGQSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHF 216
Cdd:cd06185  162 GRLDLAALLAAPPAGTHVYVCGPEGMMDAVRAAAAALGWPEARLHFERF 210
Fdx COG0633
Ferredoxin [Energy production and conversion];
230-314 1.04e-21

Ferredoxin [Energy production and conversion];


:

Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 87.21  E-value: 1.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 230 TIEVKGTGRRIEVLPEQTATEALIANGFDIPVSCEQGICGTCITRVVEGSPDHRDMFMTDEEHALNDQFTPCCSRAKTkH 309
Cdd:COG0633    3 KVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARPTS-D 81


                 ....*
gi 446304674 310 LVIEL 314
Cdd:COG0633   82 LVVEL 86
 
Name Accession Description Interval E-value
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 8-216 1.04e-105

Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal.


Pssm-ID: 99782 [Multi-domain]  Cd Length: 211  Bit Score: 307.10  E-value: 1.04e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   8 IHQLTPTIRAFELVAANGKALPSFEAGAHIDVHLKNGLTRQYSLSNCCTEKHRYVIGVLHDANSRGGSRCIHTEYREGDH 87
Cdd:cd06185    3 IRDEAPDIRSFELEAPDGAPLPAFEPGAHIDVHLPNGLVRQYSLCGDPADRDRYRIAVLREPASRGGSRYMHELLRVGDE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  88 LKIGEPRNLFEIHSQTKQAVLFAGGIGITPILSMAYRLKSANIPFELHYFVRSHEMIAFYGNLTEHFGDQVHFHIQDQpD 167
Cdd:cd06185   83 LEVSAPRNLFPLDEAARRHLLIAGGIGITPILSMARALAARGADFELHYAGRSREDAAFLDELAALPGDRVHLHFDDE-G 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446304674 168 TECNMAEALGQSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHF 216
Cdd:cd06185  162 GRLDLAALLAAPPAGTHVYVCGPEGMMDAVRAAAAALGWPEARLHFERF 210
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
1-215 7.20e-58

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 185.76  E-value: 7.20e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   1 MDVIIQKIHQLTPTIRAFELVAANGKALPSFEAGAHIDVHLKNG---LTRQYSLSNCCTEkHRYVIGVLHDANsRGGSRC 77
Cdd:COG1018    4 RPLRVVEVRRETPDVVSFTLEPPDGAPLPRFRPGQFVTLRLPIDgkpLRRAYSLSSAPGD-GRLEITVKRVPG-GGGSNW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  78 IHTEYREGDHLKIGEPRNLFEIH-SQTKQAVLFAGGIGITPILSMAYRLKSAN--IPFELHYFVRSHEMIAFYGNLTEHF 154
Cdd:COG1018   82 LHDHLKVGDTLEVSGPRGDFVLDpEPARPLLLIAGGIGITPFLSMLRTLLARGpfRPVTLVYGARSPADLAFRDELEALA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 155 G--DQVHFHIQ-DQPDTECN------MAEALGQSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEH 215
Cdd:COG1018  162 ArhPRLRLHPVlSREPAGLQgrldaeLLAALLPDPADAHVYLCGPPPMMEAVRAALAELGVPEERIHFER 231
PRK13289 PRK13289
NO-inducible flavohemoprotein;
14-216 1.29e-23

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 99.49  E-value: 1.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  14 TIRAFELVAANGKALPSFEAGAHIDVHLK-NGLT----RQYSLSNCCTEKHrYVIGVLHDAnsrGG--SRCIHTEYREGD 86
Cdd:PRK13289 168 VITSFYLEPVDGGPVADFKPGQYLGVRLDpEGEEyqeiRQYSLSDAPNGKY-YRISVKREA---GGkvSNYLHDHVNVGD 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  87 HLKIGEPRNLFEI-HSQTKQAVLFAGGIGITPILSMAYRLKSANIPFELHYF-----VRSHEM-------IAFYGNLTEH 153
Cdd:PRK13289 244 VLELAAPAGDFFLdVASDTPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIhaarnGGVHAFrdevealAARHPNLKAH 323

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446304674 154 F-------GDQ--VHFHIQDQPDTEcNMAEALgqSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHF 216
Cdd:PRK13289 324 TwyrepteQDRagEDFDSEGLMDLE-WLEAWL--PDPDADFYFCGPVPFMQFVAKQLLELGVPEERIHYEFF 392
Fdx COG0633
Ferredoxin [Energy production and conversion];
230-314 1.04e-21

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 87.21  E-value: 1.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 230 TIEVKGTGRRIEVLPEQTATEALIANGFDIPVSCEQGICGTCITRVVEGSPDHRDMFMTDEEHALNDQFTPCCSRAKTkH 309
Cdd:COG0633    3 KVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARPTS-D 81


                 ....*
gi 446304674 310 LVIEL 314
Cdd:COG0633   82 LVVEL 86
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 230-313 5.94e-20

2Fe-2S iron-sulfur cluster 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). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 82.44  E-value: 5.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 230 TIEVKGTGRRIEVLPEQTATEALIANGFDIPVSCEQGICGTCITRVVEGSPDHRDMFMTDEEHALNDQFTPCCSRAKTkH 309
Cdd:cd00207    2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTD-G 80


                 ....
gi 446304674 310 LVIE 313
Cdd:cd00207   81 LVIE 84
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
231-306 3.74e-14

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 66.39  E-value: 3.74e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446304674  231 IEVKGTGRRIEVLPEQTA-TEALIANGFDIPVSCEQGICGTCITRVVEGSPDHRDMFMTDEEHALNDQFTPCCSRAK 306
Cdd:pfam00111   1 VTINGKGVTIEVPDGETTlLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFLEDDELAAGYVVLACQTYPK 77
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 228-313 6.34e-10

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 59.50  E-value: 6.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 228 AFTIEVKGTGRRIEVLPEQTATEALIANGFDIPVSCEQGICGTCITRVVEGS---PDHRDMFMTDEEHALNDQFTpCCSR 304
Cdd:PRK07609   2 SFQVTLQPSGRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEveqGPHQASALSGEERAAGEALT-CCAK 80


                 ....*....
gi 446304674 305 AKTKhLVIE 313
Cdd:PRK07609  81 PLSD-LVLE 88
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 108-197 1.27e-05

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: 43.40  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  108 LFAGGIGITPILSMA-YRLKSANIPfelhyfvrsHEMIAFYGNLTEH--------------FGDQVH-FHIQDQPDTECN 171
Cdd:pfam00175   1 MIAGGTGIAPVRSMLrAILEDPKDP---------TQVVLVFGNRNEDdilyreeldelaekHPGRLTvVYVVSRPEAGWT 71

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 446304674  172 ----------MAEALGQSSPDKHLYVCGPTGFMQFV 197
Cdd:pfam00175  72 ggkgrvqdalLEDHLSLPDEETHVYVCGPPGMIKAV 107
 
Name Accession Description Interval E-value
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 8-216 1.04e-105

Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal.


Pssm-ID: 99782 [Multi-domain]  Cd Length: 211  Bit Score: 307.10  E-value: 1.04e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   8 IHQLTPTIRAFELVAANGKALPSFEAGAHIDVHLKNGLTRQYSLSNCCTEKHRYVIGVLHDANSRGGSRCIHTEYREGDH 87
Cdd:cd06185    3 IRDEAPDIRSFELEAPDGAPLPAFEPGAHIDVHLPNGLVRQYSLCGDPADRDRYRIAVLREPASRGGSRYMHELLRVGDE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  88 LKIGEPRNLFEIHSQTKQAVLFAGGIGITPILSMAYRLKSANIPFELHYFVRSHEMIAFYGNLTEHFGDQVHFHIQDQpD 167
Cdd:cd06185   83 LEVSAPRNLFPLDEAARRHLLIAGGIGITPILSMARALAARGADFELHYAGRSREDAAFLDELAALPGDRVHLHFDDE-G 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446304674 168 TECNMAEALGQSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHF 216
Cdd:cd06185  162 GRLDLAALLAAPPAGTHVYVCGPEGMMDAVRAAAAALGWPEARLHFERF 210
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
1-215 7.20e-58

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 185.76  E-value: 7.20e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   1 MDVIIQKIHQLTPTIRAFELVAANGKALPSFEAGAHIDVHLKNG---LTRQYSLSNCCTEkHRYVIGVLHDANsRGGSRC 77
Cdd:COG1018    4 RPLRVVEVRRETPDVVSFTLEPPDGAPLPRFRPGQFVTLRLPIDgkpLRRAYSLSSAPGD-GRLEITVKRVPG-GGGSNW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  78 IHTEYREGDHLKIGEPRNLFEIH-SQTKQAVLFAGGIGITPILSMAYRLKSAN--IPFELHYFVRSHEMIAFYGNLTEHF 154
Cdd:COG1018   82 LHDHLKVGDTLEVSGPRGDFVLDpEPARPLLLIAGGIGITPFLSMLRTLLARGpfRPVTLVYGARSPADLAFRDELEALA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 155 G--DQVHFHIQ-DQPDTECN------MAEALGQSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEH 215
Cdd:COG1018  162 ArhPRLRLHPVlSREPAGLQgrldaeLLAALLPDPADAHVYLCGPPPMMEAVRAALAELGVPEERIHFER 231
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 5-216 3.60e-31

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: 117.27  E-value: 3.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   5 IQKIHQLTPTIRAFELVAANGKALPSFEAGAHIDVHLK-----NGLTRQYSLSNCCTEKHrYVIGVLHDAnsrGG--SRC 77
Cdd:cd06184   11 VARKVAESEDITSFYLEPADGGPLPPFLPGQYLSVRVKlpglgYRQIRQYSLSDAPNGDY-YRISVKREP---GGlvSNY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  78 IHTEYREGDHLKIGEPRNLFEIHSQTKQ-AVLFAGGIGITPILSMAYRLKSANIPFELHYF--VRSHEMIAF-------- 146
Cdd:cd06184   87 LHDNVKVGDVLEVSAPAGDFVLDEASDRpLVLISAGVGITPMLSMLEALAAEGPGRPVTFIhaARNSAVHAFrdeleela 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 147 --YGNLTEHF--------GDQVHFHIQDQPDtecnmAEALGQS--SPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQE 214
Cdd:cd06184  167 arLPNLKLHVfysepeagDREEDYDHAGRID-----LALLRELllPADADFYLCGPVPFMQAVREGLKALGVPAERIHYE 241


                 ..
gi 446304674 215 HF 216
Cdd:cd06184  242 VF 243
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 7-216 7.23e-28

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: 108.06  E-value: 7.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   7 KIHQLTPTIRAFELVAANGkALPSFEAGAHIDVHLKNG---LTRQYSLSNCCTEKHRYVIGVLHDANSRGgSRCIHTEYR 83
Cdd:cd06215    5 KIIQETPDVKTFRFAAPDG-SLFAYKPGQFLTLELEIDgetVYRAYTLSSSPSRPDSLSITVKRVPGGLV-SNWLHDNLK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  84 EGDHLKIGEPRNLF-EIHSQTKQAVLFAGGIGITPILSMAYRLKS----ANIPFeLHyFVRS----------HEMIAFYG 148
Cdd:cd06215   83 VGDELWASGPAGEFtLIDHPADKLLLLSAGSGITPMMSMARWLLDtrpdADIVF-IH-SARSpadiifadelEELARRHP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446304674 149 NLTEHF-----GDQVHFHIQDQPDTEcnMAEALGQSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHF 216
Cdd:cd06215  161 NFRLHLileqpAPGAWGGYRGRLNAE--LLALLVPDLKERTVFVCGPAGFMKAVKSLLAELGFPMSRFHQESF 231
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 7-214 2.59e-26

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: 103.68  E-value: 2.59e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   7 KIHQLTPTIRAFELVAANGkalPSFEAGAHIDVHLKN---GLTRQYSLSNCCTEKHRYVIGVLHDANSRGgSRCIHTEyR 83
Cdd:cd00322    2 ATEDVTDDVRLFRLQLPNG---FSFKPGQYVDLHLPGdgrGLRRAYSIASSPDEEGELELTVKIVPGGPF-SAWLHDL-K 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  84 EGDHLKIGEPRNLFEIHSQTKQ-AVLFAGGIGITPILSMAYRLKSANIPFELH--YFVRSHEMIAFYGNLTEHFGDQVHF 160
Cdd:cd00322   77 PGDEVEVSGPGGDFFLPLEESGpVVLIAGGIGITPFRSMLRHLAADKPGGEITllYGARTPADLLFLDELEELAKEGPNF 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446304674 161 HI-----QDQPDT--------ECNMAEALGQSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQE 214
Cdd:cd00322  157 RLvlalsRESEAKlgpggridREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
PRK13289 PRK13289
NO-inducible flavohemoprotein;
14-216 1.29e-23

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 99.49  E-value: 1.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  14 TIRAFELVAANGKALPSFEAGAHIDVHLK-NGLT----RQYSLSNCCTEKHrYVIGVLHDAnsrGG--SRCIHTEYREGD 86
Cdd:PRK13289 168 VITSFYLEPVDGGPVADFKPGQYLGVRLDpEGEEyqeiRQYSLSDAPNGKY-YRISVKREA---GGkvSNYLHDHVNVGD 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  87 HLKIGEPRNLFEI-HSQTKQAVLFAGGIGITPILSMAYRLKSANIPFELHYF-----VRSHEM-------IAFYGNLTEH 153
Cdd:PRK13289 244 VLELAAPAGDFFLdVASDTPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIhaarnGGVHAFrdevealAARHPNLKAH 323

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446304674 154 F-------GDQ--VHFHIQDQPDTEcNMAEALgqSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHF 216
Cdd:PRK13289 324 TwyrepteQDRagEDFDSEGLMDLE-WLEAWL--PDPDADFYFCGPVPFMQFVAKQLLELGVPEERIHYEFF 392
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 5-216 5.41e-23

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: 95.03  E-value: 5.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   5 IQKIHQLTPTIRAFELvAANGKALPSFEAGAHIDVHLK--NGLT--RQYSLSNCCTEKHRYVIGVLHDAnsrGG--SRCI 78
Cdd:cd06217    6 VTEIIQETPTVKTFRL-AVPDGVPPPFLAGQHVDLRLTaiDGYTaqRSYSIASSPTQRGRVELTVKRVP---GGevSPYL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  79 HTEYREGDHLKIGEPRNLFeIHS--QTKQAVLFAGGIGITPILSMA-YRLKSA-NIPFELHYFVRSHEMIAFYGNL---- 150
Cdd:cd06217   82 HDEVKVGDLLEVRGPIGTF-TWNplHGDPVVLLAGGSGIVPLMSMIrYRRDLGwPVPFRLLYSARTAEDVIFRDELeqla 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446304674 151 TEHFGDQVHFHIQDQPDT---------ECNMAEALGQSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHF 216
Cdd:cd06217  161 RRHPNLHVTEALTRAAPAdwlgpagriTADLIAELVPPLAGRRVYVCGPPAFVEAATRLLLELGVPRDRIRTEAF 235
Fdx COG0633
Ferredoxin [Energy production and conversion];
230-314 1.04e-21

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 87.21  E-value: 1.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 230 TIEVKGTGRRIEVLPEQTATEALIANGFDIPVSCEQGICGTCITRVVEGSPDHRDMFMTDEEHALNDQFTPCCSRAKTkH 309
Cdd:COG0633    3 KVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARPTS-D 81


                 ....*
gi 446304674 310 LVIEL 314
Cdd:COG0633   82 LVVEL 86
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 5-212 9.64e-21

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 89.15  E-value: 9.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   5 IQKIHQLTPTIRAFELVAAngKALPSFEAGAHIDVHLKN-GLTRQYSLSNCCTEKHRYVIGVLHdansRG-GSRCIHtEY 82
Cdd:COG0543    2 VVSVERLAPDVYLLRLEAP--LIALKFKPGQFVMLRVPGdGLRRPFSIASAPREDGTIELHIRV----VGkGTRALA-EL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  83 REGDHLKIGEPR-NLFEIHSQTKQAVLFAGGIGITPILSMAYRLKSANIPFELHYFVRSHEMIaFYGNLTEHFGDqVHFH 161
Cdd:COG0543   75 KPGDELDVRGPLgNGFPLEDSGRPVLLVAGGTGLAPLRSLAEALLARGRRVTLYLGARTPEDL-YLLDELEALAD-FRVV 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446304674 162 I--QDQPDTEC----NMAEALGQSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLH 212
Cdd:COG0543  153 VttDDGWYGRKgfvtDALKELLAEDSGDDVYACGPPPMMKAVAELLLERGVPPERIY 209
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 230-313 5.94e-20

2Fe-2S iron-sulfur cluster 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). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 82.44  E-value: 5.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 230 TIEVKGTGRRIEVLPEQTATEALIANGFDIPVSCEQGICGTCITRVVEGSPDHRDMFMTDEEHALNDQFTPCCSRAKTkH 309
Cdd:cd00207    2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTD-G 80


                 ....
gi 446304674 310 LVIE 313
Cdd:cd00207   81 LVIE 84
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 29-216 3.80e-19

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: 84.58  E-value: 3.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  29 PSFEAGAHIDVHLK-NG--LTRQYSLSNCCTEKHRYV-IGVLHDANSRGgSRCIHTEYREGDHLKIGEPRNLFEIHSQTK 104
Cdd:cd06216   44 PGHRAGQHVRLGVEiDGvrHWRSYSLSSSPTQEDGTItLTVKAQPDGLV-SNWLVNHLAPGDVVELSQPQGDFVLPDPLP 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 105 QAVLF-AGGIGITPILSMAYRLKSAN--IPFELHYFVRS----------HEMIAFYGNLTEHfgdqvHFHIQDQPDTECN 171
Cdd:cd06216  123 PRLLLiAAGSGITPVMSMLRTLLARGptADVVLLYYARTredvifadelRALAAQHPNLRLH-----LLYTREELDGRLS 197

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446304674 172 mAEALGQSSPD---KHLYVCGPTGFMQFVMSSAEQAGwHSEQLHQEHF 216
Cdd:cd06216  198 -AAHLDAVVPDladRQVYACGPPGFLDAAEELLEAAG-LADRLHTERF 243
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 5-217 3.53e-18

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: 81.82  E-value: 3.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   5 IQKIHQLTPTIRAFEL-VAANGKALPSFEAGAHIDV-HLKNG--LTRQYSLSNCCTEkHRYVIGVLHDANSRGgSRCIHT 80
Cdd:cd06214    6 VAEVVRETADAVSITFdVPEELRDAFRYRPGQFLTLrVPIDGeeVRRSYSICSSPGD-DELRITVKRVPGGRF-SNWAND 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  81 EYREGDHLKIGEPRNLF--EIHSQTKQAVLFAGGIGITPILSMAyrlKSA--NIP---FELHYFVRSHEMIAFY---GNL 150
Cdd:cd06214   84 ELKAGDTLEVMPPAGRFtlPPLPGARHYVLFAAGSGITPVLSIL---KTAlaREPasrVTLVYGNRTEASVIFReelADL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 151 TEHFGD--QVHFHI-QDQPDTECNM----AEALGQSSPDK-------HLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHF 216
Cdd:cd06214  161 KARYPDrlTVIHVLsREQGDPDLLRgrldAAKLNALLKNLldatefdEAFLCGPEPMMDAVEAALLELGVPAERIHRELF 240


                 .
gi 446304674 217 V 217
Cdd:cd06214  241 T 241
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
97-216 2.40e-16

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 79.17  E-value: 2.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  97 FEIHSQTKQAVLFAGGIGITPILSMAYRL---KSANIPFELHYFVRSHEMIAFYGNLTE--HFGDQVHFHIQDQPDTECN 171
Cdd:COG4097  312 FDRRDTAPRQVWIAGGIGITPFLALLRALaarPGDQRPVDLFYCVRDEEDAPFLEELRAlaARLAGLRLHLVVSDEDGRL 391

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446304674 172 MAEALGQSSPD---KHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHF 216
Cdd:COG4097  392 TAERLRRLVPDlaeADVFFCGPPGMMDALRRDLRALGVPARRIHQERF 439
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 8-293 3.39e-15

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 74.75  E-value: 3.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   8 IHQLTPTIRAFELVAANgkaLPSFEAGAHIDVHLKNG--LTRQYSLSNCCTEKhRYVIGVLHDANSRGGSRCIHTEYREG 85
Cdd:PRK10684  17 IVQETPDVWTISLICHD---FYPYRAGQYALVSIRNSaeTLRAYTLSSTPGVS-EFITLTVRRIDDGVGSQWLTRDVKRG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  86 DHLKIGEPRNLFEI-HSQTKQAVLFAGGIGITPILSMAyRLKSANIP---FELHYFVRSHEMIAF---YGNLTEHFGDQV 158
Cdd:PRK10684  93 DYLWLSDAMGEFTCdDKAEDKYLLLAAGCGVTPIMSMR-RWLLKNRPqadVQVIFNVRTPQDVIFadeWRQLKQRYPQLN 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 159 HFHIQDQPDTECNMA-----EALGQSSPD---KHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHFVAQKVDTSNDEaFT 230
Cdd:PRK10684 172 LTLVAENNATEGFIAgrltrELLQQAVPDlasRTVMTCGPAPYMDWVEQEVKALGVTADRFFKEKFFTPVAEAATSG-LT 250

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446304674 231 IEVKGTGRRIEVLPEQTATEALIANGFDIPVSCEQGICGTCITRVVEGspDHR---DMFMTDEEHA 293
Cdd:PRK10684 251 FTKLQPAREFYAPVGTTLLEALESNKVPVVAACRAGVCGCCKTKVVSG--EYTvssTMTLTPAEIA 314
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 85-217 4.80e-15

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: 72.67  E-value: 4.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  85 GDHLKIGEPRNL------FEIHSQTKQAVLFAGGIGITPILSMAYRLKSANI--PFELHYFVRSHEMIAFYG---NLTEH 153
Cdd:cd06198   71 AERLKPGTRVTVegpygrFTFDDRRARQIWIAGGIGITPFLALLEALAARGDarPVTLFYCVRDPEDAVFLDelrALAAA 150

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446304674 154 FGdqVHFHI----QDQPDTECNMAEALGQSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHFV 217
Cdd:cd06198  151 AG--VVLHVidspSDGRLTLEQLVRALVPDLADADVWFCGPPGMADALEKGLRALGVPARRFHYERFE 216
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 5-216 1.28e-14

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: 71.79  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   5 IQKIHQLTPTIRAFeLVAANGKALPSFEAGAHIDVHLK-NGLT--RQYSLSNCcTEKHRYVIGVlhdANSRGG--SRCIH 79
Cdd:cd06191    3 VAEVRSETPDAVTI-VFAVPGPLQYGFRPGQHVTLKLDfDGEElrRCYSLCSS-PAPDEISITV---KRVPGGrvSNYLR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  80 TEYREGDHLKIGEPRNLFEIHSQTKQAVLF-AGGIGITPILSM--AYRLKSANIPFELHYFVRSHEMIAFYGNLTE---- 152
Cdd:cd06191   78 EHIQPGMTVEVMGPQGHFVYQPQPPGRYLLvAAGSGITPLMAMirATLQTAPESDFTLIHSARTPADMIFAQELREladk 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446304674 153 HFGDQVHF-HIQDQPDT---------ECNMAEALGQSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHF 216
Cdd:cd06191  158 PQRLRLLCiFTRETLDSdllhgridgEQSLGAALIPDRLEREAFICGPAGMMDAVETALKELGMPPERIHTERF 231
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
231-306 3.74e-14

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 66.39  E-value: 3.74e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446304674  231 IEVKGTGRRIEVLPEQTA-TEALIANGFDIPVSCEQGICGTCITRVVEGSPDHRDMFMTDEEHALNDQFTPCCSRAK 306
Cdd:pfam00111   1 VTINGKGVTIEVPDGETTlLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFLEDDELAAGYVVLACQTYPK 77
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 5-212 1.30e-11

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: 63.35  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   5 IQKIHQLTPTIRAFELVAANGKALPSFEAGAHIDVHLKNG---LTRQYS-LSNCCTEKH------RYVIGVLhdansrgg 74
Cdd:cd06183    3 LVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDgeqVVRPYTpISPDDDKGYfdllikIYPGGKM-------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  75 SRCIHTeYREGDHLKIGEPRNLFEIHSQT--KQAVLFAGGIGITPILSMA-YRLKSANIPFE--LHYFVRSHEMIAFYGN 149
Cdd:cd06183   75 SQYLHS-LKPGDTVEIRGPFGKFEYKPNGkvKHIGMIAGGTGITPMLQLIrAILKDPEDKTKisLLYANRTEEDILLREE 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446304674 150 LTE---HFGDQVH-FHIQDQPDTECN----------MAEALGQSSPDKHL-YVCGPTGFMQFVM-SSAEQAGWHSEQLH 212
Cdd:cd06183  154 LDElakKHPDRFKvHYVLSRPPEGWKggvgfitkemIKEHLPPPPSEDTLvLVCGPPPMIEGAVkGLLKELGYKKDNVF 232
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 228-313 6.34e-10

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 59.50  E-value: 6.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 228 AFTIEVKGTGRRIEVLPEQTATEALIANGFDIPVSCEQGICGTCITRVVEGS---PDHRDMFMTDEEHALNDQFTpCCSR 304
Cdd:PRK07609   2 SFQVTLQPSGRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEveqGPHQASALSGEERAAGEALT-CCAK 80


                 ....*....
gi 446304674 305 AKTKhLVIE 313
Cdd:PRK07609  81 PLSD-LVLE 88
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 4-137 8.74e-10

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: 58.10  E-value: 8.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   4 IIQKIHQLTPTIRA--FELVAANGKAlpsFEAGAHIDVHLKNG-LTRQYSLSNCCTEKH------RYVIGVLhdansrgG 74
Cdd:cd06211   10 TVVEIEDLTPTIKGvrLKLDEPEEIE---FQAGQYVNLQAPGYeGTRAFSIASSPSDAGeielhiRLVPGGI-------A 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446304674  75 SRCIHTEYREGDHLKIGEPRNLFEIH-SQTKQAVLFAGGIGITPILSMAYRLKSANIPFELHYF 137
Cdd:cd06211   80 TTYVHKQLKEGDELEISGPYGDFFVRdSDQRPIIFIAGGSGLSSPRSMILDLLERGDTRKITLF 143
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 31-217 2.80e-08

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: 53.50  E-value: 2.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  31 FEAGAHIDVHLK-NGLTRQYSLSNCCTEKHR--YVIGVLhdansRGG--SRCIHTEYREGDHLKIGEPRNLFEIHSQTKQ 105
Cdd:cd06210   35 FVPGQFVEIEIPgTDTRRSYSLANTPNWDGRleFLIRLL-----PGGafSTYLETRAKVGQRLNLRGPLGAFGLRENGLR 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 106 AVLF-AGGIGITPILSMAYRLKSANIPFELH-YFVRSHEMIAFYGNLTEHFGDQ-----VHFHIQdQPDTECN------- 171
Cdd:cd06210  110 PRWFvAGGTGLAPLLSMLRRMAEWGEPQEARlFFGVNTEAELFYLDELKRLADSlpnltVRICVW-RPGGEWEgyrgtvv 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446304674 172 --MAEALGQSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHFV 217
Cdd:cd06210  189 daLREDLASSDAKPDIYLCGPPGMVDAAFAAAREAGVPDEQVYLEKFL 236
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 8-142 6.86e-08

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: 52.21  E-value: 6.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   8 IHQLTPTIRAFELVAAngKALPsFEAGAHIDVHL--KNGLTRQYSLSNCCTEKHRYVigvLHDANSRGG--SRCIHTEYR 83
Cdd:cd06187    4 VERLTHDIAVVRLQLD--QPLP-FWAGQYVNVTVpgRPRTWRAYSPANPPNEDGEIE---FHVRAVPGGrvSNALHDELK 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446304674  84 EGDHLKIGEPRNLFEIHSQTKQAVLF-AGGIGITPILSMAYRLKSANIPFELHYF--VRSHE 142
Cdd:cd06187   78 VGDRVRLSGPYGTFYLRRDHDRPVLCiAGGTGLAPLRAIVEDALRRGEPRPVHLFfgARTER 139
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 5-121 6.93e-07

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: 49.08  E-value: 6.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   5 IQKIHQLTPTIRAFELVAAngkALPSFEAGAHIDVHLKNGLTRQYSLSNCCTEKHRYVIGVLHDANSRGGSRcIHTEYRE 84
Cdd:cd06189    3 VESIEPLNDDVYRVRLKPP---APLDFLAGQYLDLLLDDGDKRPFSIASAPHEDGEIELHIRAVPGGSFSDY-VFEELKE 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446304674  85 GDHLKIGEPRNLFEIHSQ-TKQAVLFAGGIGITPILSM 121
Cdd:cd06189   79 NGLVRIEGPLGDFFLREDsDRPLILIAGGTGFAPIKSI 116
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 5-217 8.94e-07

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: 48.80  E-value: 8.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   5 IQKIHQLTPTIRafELVAANGKALPsFEAGAHIDVHLKNGLTRQYSLSNCCTEKHryVIgVLHDANSRGG--SRCIHTEY 82
Cdd:cd06194    1 VVSLQRLSPDVL--RVRLEPDRPLP-YLPGQYVNLRRAGGLARSYSPTSLPDGDN--EL-EFHIRRKPNGafSGWLGEEA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  83 REGDHLKIGEPRN--LFEIHSQTKQAVLFAGGIGITPILSMAYRLKSANIPFELHYFVRSHEMIAFY-----GNLTEHFG 155
Cdd:cd06194   75 RPGHALRLQGPFGqaFYRPEYGEGPLLLVGAGTGLAPLWGIARAALRQGHQGEIRLVHGARDPDDLYlhpalLWLAREHP 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446304674 156 DqvhFHIQ------DQPDTECN---MAEALGQSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHFV 217
Cdd:cd06194  155 N---FRYIpcvsegSQGDPRVRagrIAAHLPPLTRDDVVYLCGAPSMVNAVRRRAFLAGAPMKRIYADPFE 222
PLN03136 PLN03136
Ferredoxin; Provisional
 256-313 4.28e-06

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 45.90  E-value: 4.28e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446304674 256 GFDIPVSCEQGICGTCITRVVEGSPDHRDMFMTDEEHaLNDQFTPCCSRAKTKHLVIE 313
Cdd:PLN03136  84 GIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDEQ-ISEGYVLTCVAYPTSDVVIE 140
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 5-278 5.94e-06

FAD/NAD binding domain (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 NAD binding. 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 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: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 46.55  E-value: 5.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   5 IQKIHQLTPTIraFELVAANGKALPSFEAG--AHIDVHLKNGLTRQySLSNCCTEKHRYVIGVLHDAnsRGGS--RCIht 80
Cdd:cd06192    1 IVKKEQLEPNL--VLLTIKAPLAARLFRPGqfVFLRNFESPGLERI-PLSLAGVDPEEGTISLLVEI--RGPKtkLIA-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  81 EYREGDHLKI----GEPrnlFEIHSQTKQAVLFAGGIGITPILSMAYRLKSANipFELHYFvrshemiAFYGNLTEHFGD 156
Cdd:cd06192   74 ELKPGEKLDVmgplGNG---FEGPKKGGTVLLVAGGIGLAPLLPIAKKLAANG--NKVTVL-------AGAKKAKEEFLD 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 157 -------QVHFHIQDqpDTECNMAEALGQSSPDKHL------YVCGPTGFMQFVMSSAEQAGwhseqlhQEHFVAqkvdT 223
Cdd:cd06192  142 eyfelpaDVEIWTTD--DGELGLEGKVTDSDKPIPLedvdriIVAGSDIMMKAVVEALDEWL-------QLIKAS----V 208

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446304674 224 SNDEaftievkgtgrrievlpeqtatealiangfdiPVSCEQGICGTCITRVVEG 278
Cdd:cd06192  209 SNNS--------------------------------PMCCGIGICGACTIETKHG 231
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 80-206 6.61e-06

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. 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: 99814 [Multi-domain]  Cd Length: 246  Bit Score: 46.38  E-value: 6.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  80 TEYREGDHLKIGEPR-NLFEIHSQTKQAVLFAGGIGITPILSMAYRLKSANIPFELHYFVRSHEMIAfygnLTEHF---G 155
Cdd:cd06218   74 SELKAGDELDVLGPLgNGFDLPDDDGKVLLVGGGIGIAPLLFLAKQLAERGIKVTVLLGFRSADDLF----LVEEFealG 149

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446304674 156 DQVHF-----------HIQDqpdtecNMAEALGQSSPDKhLYVCGPTGFMQFVMSSAEQAGW 206
Cdd:cd06218  150 AEVYVatddgsagtkgFVTD------LLKELLAEARPDV-VYACGPEPMLKAVAELAAERGV 204
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 108-197 1.27e-05

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: 43.40  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  108 LFAGGIGITPILSMA-YRLKSANIPfelhyfvrsHEMIAFYGNLTEH--------------FGDQVH-FHIQDQPDTECN 171
Cdd:pfam00175   1 MIAGGTGIAPVRSMLrAILEDPKDP---------TQVVLVFGNRNEDdilyreeldelaekHPGRLTvVYVVSRPEAGWT 71

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 446304674  172 ----------MAEALGQSSPDKHLYVCGPTGFMQFV 197
Cdd:pfam00175  72 ggkgrvqdalLEDHLSLPDEETHVYVCGPPGMIKAV 107
COG3894 COG3894
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain ...
 229-297 1.92e-05

Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain [Function unknown];


Pssm-ID: 443101 [Multi-domain]  Cd Length: 621  Bit Score: 45.95  E-value: 1.92e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 229 FTIEVKGTGRRIEVLPEQTATEALIANGFDIPVSC-EQGICGTCITRVVEGSPDHRDmfmTDEEHALNDQ 297
Cdd:COG3894    4 VKVTFLPSGKRVEVEAGTTLLDAAREAGVDIDAPCgGRGTCGKCKVKVEEGEFSPVT---EEERRLLSPE 70
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 3-209 1.95e-05

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 45.25  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   3 VIIQKIHQLTPTIRAFELvaaNGKALPSFEAG--AHIDV-HLKNGLTRQYSLSNccteKHRYVIGVLHDANSRGGSRCih 79
Cdd:PRK00054   7 MKIVENKEIAPNIYTLVL---DGEKVFDMKPGqfVMVWVpGVEPLLERPISISD----IDKNEITILYRKVGEGTKKL-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  80 TEYREGDHLKIGEPR-NLFEIHSQTKQAVLFAGGIGITPILSMAYRLKSANIPFELHYFVRSHEMIAFYGNLTEhfGDQV 158
Cdd:PRK00054  78 SKLKEGDELDIRGPLgNGFDLEEIGGKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTKDEVIFEEEFAK--VGDV 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446304674 159 HFHIQDQPD------TECnMAEALgqSSPDkHLYVCGPTGFMQFVMSSAEQAGWHSE 209
Cdd:PRK00054 156 YVTTDDGSYgfkgfvTDV-LDELD--SEYD-AIYSCGPEIMMKKVVEILKEKKVPAY 208
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 5-217 2.61e-05

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: 44.51  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   5 IQKIHQLTPTIRAFELVAANGKALpSFEAGAHIDVHLKN-GLTRQYSLSNCCTEKH-RYVIGVLHDA--NSRGGSRCiht 80
Cdd:cd06209    6 VTEVERLSDSTIGLTLELDEAGAL-AFLPGQYVNLQVPGtDETRSYSFSSAPGDPRlEFLIRLLPGGamSSYLRDRA--- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  81 eyREGDHLKIGEPRNLFEIHSQTKQAVLFAGGIGITPILSMAYRLKSA--NIPFELHYFVRS-------HEMIAFYGNLT 151
Cdd:cd06209   82 --QPGDRLTLTGPLGSFYLREVKRPLLMLAGGTGLAPFLSMLDVLAEDgsAHPVHLVYGVTRdadlvelDRLEALAERLP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446304674 152 ehfGDQVHFHIQDQPDTECN-------MAEALGqSSPDKHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHFV 217
Cdd:cd06209  160 ---GFSFRTVVADPDSWHPRkgyvtdhLEAEDL-NDGDVDVYLCGPPPMVDAVRSWLDEQGIEPANFYYEKFT 228
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 8-217 9.62e-05

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: 43.09  E-value: 9.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   8 IHQLTPTIRAFELVAANGKALPsFEAGAHIDVHLKN-GLTRQYSLSNCCTEKHR--YVIGVLhdansRGG--SRCIHTEY 82
Cdd:cd06212    8 VEALTHDIRRLRLRLEEPEPIK-FFAGQYVDITVPGtEETRSFSMANTPADPGRleFIIKKY-----PGGlfSSFLDDGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  83 REGDHLKIGEPRNLFEIH-SQTKQAVLFAGGIGITPILSMAYRLKSANIPFELHYfvrshemiaFYGN-------LTEHF 154
Cdd:cd06212   82 AVGDPVTVTGPYGTCTLReSRDRPIVLIGGGSGMAPLLSLLRDMAASGSDRPVRF---------FYGArtardlfYLEEI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 155 G------DQVHF--HIQDQPDTEC------NMAEALGQSSPDK---HLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHFV 217
Cdd:cd06212  153 AalgekiPDFTFipALSESPDDEGwsgetgLVTEVVQRNEATLagcDVYLCGPPPMIDAALPVLEMSGVPPDQIFYDKFT 232
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 103-217 1.08e-04

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: 42.76  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 103 TKQAVLFAGGIGITPILSMAYRLKSAN---IPFELHYFVRSHEMIafygnltehfgdQVHFHIQDQPDTECNMAEALgqs 179
Cdd:cd06197  125 ERKMVWIAGGVGITPFLAMLRAILSSRnttWDITLLWSLREDDLP------------LVMDTLVRFPGLPVSTTLFI--- 189

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446304674 180 spDKHLYVCGPTGFMQFVMSSAEqagwhSEQLHQEHFV 217
Cdd:cd06197  190 --TSEVYLCGPPALEKAVLEWLE-----GKKVHRESFA 220
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 106-216 2.38e-04

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: 41.52  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 106 AVLFAGGIGITPILSMA------YRLKSANIPFELHYFVRSHEMIAFYGNLTEHF-----GDQVHFHIqdqpdTecnmae 174
Cdd:cd06186  109 VLLVAGGSGITFVLPILrdllrrSSKTSRTRRVKLVWVVRDREDLEWFLDELRAAqelevDGEIEIYV-----T------ 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446304674 175 algqsspdkHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQEHF 216
Cdd:cd06186  178 ---------RVVVCGPPGLVDDVRNAVAKKGGTGVEFHEESF 210
petF CHL00134
ferredoxin; Validated
 255-291 3.13e-04

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 39.32  E-value: 3.13e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446304674 255 NGFDIPVSCEQGICGTCITRVVEGSPDHRDM-FMTDEE 291
Cdd:CHL00134  34 QGIDLPYSCRAGACSTCAGKVTEGTVDQSDQsFLDDDQ 71
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 3-214 7.33e-04

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: 40.30  E-value: 7.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674   3 VIIQKIHQLTPTIRAFELVAANGKalpSFEAGAHIDVHL-KNGL---TRQYSLSNCCTEKH-RYVIGVL--HDansrGGS 75
Cdd:cd06196    3 VTLLSIEPVTHDVKRLRFDKPEGY---DFTPGQATEVAIdKPGWrdeKRPFTFTSLPEDDVlEFVIKSYpdHD----GVT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  76 RCIHTeYREGDHLKIGEPrnlFEIHSQTKQAVLFAGGIGITPILSMaYRLKSANIPFELHYFVRSHEM---IAFYGNLTE 152
Cdd:cd06196   76 EQLGR-LQPGDTLLIEDP---WGAIEYKGPGVFIAGGAGITPFIAI-LRDLAAKGKLEGNTLIFANKTekdIILKDELEK 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446304674 153 HFGDQVHFHIQDQPDTECNM----AEALGQSSPD--KHLYVCGPTGFMQFVMSSAEQAGWHSEQLHQE 214
Cdd:cd06196  151 MLGLKFINVVTDEKDPGYAHgridKAFLKQHVTDfnQHFYVCGPPPMEEAINGALKELGVPEDSIVFE 218
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
230-314 8.47e-04

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 37.79  E-value: 8.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674 230 TIEVKGTGRRIEVLPEQTAT-EALIANGFDIPVSCEQGICGTCITRVVEGSPDHRD---MFMTDEEhalndqFTPCCSRA 305
Cdd:PRK10713   3 RVTLRITGTQLLCQDEHPSLlAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAeplAFIQPGE------ILPCCCRA 76


                 ....*....
gi 446304674 306 KTKhlvIEL 314
Cdd:PRK10713  77 KGD---IEI 82
PTZ00038 PTZ00038
ferredoxin; Provisional
 250-291 1.45e-03

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 39.05  E-value: 1.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446304674 250 EALIANGFDIPVSCEQGICGTCITRVVEGSPDHRDMFMTDEE 291
Cdd:PTZ00038 119 DAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDE 160
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 11-190 4.44e-03

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: 38.00  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  11 LTPTIRAFELvAANGKAlpSFEAGAHIDVHLKNG-LTRQYSLSNCCTEkhryvIGVLH---DANSRG-GSRCIHTEYREG 85
Cdd:cd06190    7 LTHDVAEFRF-ALDGPA--DFLPGQYALLALPGVeGARAYSMANLANA-----SGEWEfiiKRKPGGaASNALFDNLEPG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446304674  86 DHLKIGEPRNLFEIHSQT-KQAVLFAGGIGITPILSMAYRLKSANIPFE--LHYF--VRSHEMIAFYGNLTE--HFGDQV 158
Cdd:cd06190   79 DELELDGPYGLAYLRPDEdRDIVCIAGGSGLAPMLSILRGAARSPYLSDrpVDLFygGRTPSDLCALDELSAlvALGARL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446304674 159 HFHI-----QDQPDTECN---------MAEALGQSSPDKHLYVCGP 190
Cdd:cd06190  159 RVTPavsdaGSGSAAGWDgptgfvhevVEATLGDRLAEFEFYFAGP 204
 
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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