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Conserved domains on  [gi|896156355|ref|WP_049172816|]
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MULTISPECIES: flavin reductase family protein [Corynebacterium]

Protein Classification

flavin reductase family protein( domain architecture ID 10937050)

flavin reductase family protein containing an N-terminal NAD(P) binding domain of flavin oxidoreductase-like proteins and a C-terminal 2Fe-2S iron-sulfur cluster binding domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FNR_like super family cl06868
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 19-262 1.59e-74

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).


The actual alignment was detected with superfamily member cd06216:

Pssm-ID: 447143 [Multi-domain]  Cd Length: 243  Bit Score: 230.57  E-value: 1.59e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  19 LPDDYTHLLNPLWSSRELRGQIEAINPTSPTSAELIIRPGWGmPTDFKPGQFIGLGVEVKGKYLWRSYSLTNAPRPHDGL 98
Cdd:cd06216    1 FVDFYLELINPLWSARELRARVVAVRPETADMVTLTLRPNRG-WPGHRAGQHVRLGVEIDGVRHWRSYSLSSSPTQEDGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  99 LTINIRALNDGYVSQHLVANVKPGTVVRLAAPAGDFHLPEPLPARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSY 178
Cdd:cd06216   80 ITLTVKAQPDGLVSNWLVNHLAPGDVVELSQPQGDFVLPDPLPPRLLLIAAGSGITPVMSMLRTLLARGPTADVVLLYYA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 179 RGEAEAVFVNELRELEQcsATSALKYRLHARNTETQPRIDAAAVTDIIADFgalaSSASAYACGPVELLKNLEPEF---- 254
Cdd:cd06216  160 RTREDVIFADELRALAA--QHPNLRLHLLYTREELDGRLSAAHLDAVVPDL----ADRQVYACGPPGFLDAAEELLeaag 233

                        250
                 ....*....|
gi 896156355 255 --PGLRTERF 262
Cdd:cd06216  234 laDRLHTERF 243
Fdx COG0633
Ferredoxin [Energy production and conversion];
278-354 1.76e-14

Ferredoxin [Energy production and conversion];


:

Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 67.95  E-value: 1.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 278 LGSRGDIDVDGATTILEAAESVGVDLPYGCRMGICATCVQQLSDGAARDIRTGA---TFVAGERVRTCVCAPAGHARIEL 354
Cdd:COG0633    7 IPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDAlsdEERAAGSRLACQARPTSDLVVEL 86
 
Name Accession Description Interval E-value
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 19-262 1.59e-74

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: 230.57  E-value: 1.59e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  19 LPDDYTHLLNPLWSSRELRGQIEAINPTSPTSAELIIRPGWGmPTDFKPGQFIGLGVEVKGKYLWRSYSLTNAPRPHDGL 98
Cdd:cd06216    1 FVDFYLELINPLWSARELRARVVAVRPETADMVTLTLRPNRG-WPGHRAGQHVRLGVEIDGVRHWRSYSLSSSPTQEDGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  99 LTINIRALNDGYVSQHLVANVKPGTVVRLAAPAGDFHLPEPLPARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSY 178
Cdd:cd06216   80 ITLTVKAQPDGLVSNWLVNHLAPGDVVELSQPQGDFVLPDPLPPRLLLIAAGSGITPVMSMLRTLLARGPTADVVLLYYA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 179 RGEAEAVFVNELRELEQcsATSALKYRLHARNTETQPRIDAAAVTDIIADFgalaSSASAYACGPVELLKNLEPEF---- 254
Cdd:cd06216  160 RTREDVIFADELRALAA--QHPNLRLHLLYTREELDGRLSAAHLDAVVPDL----ADRQVYACGPPGFLDAAEELLeaag 233

                        250
                 ....*....|
gi 896156355 255 --PGLRTERF 262
Cdd:cd06216  234 laDRLHTERF 243
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
33-229 2.44e-48

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 162.65  E-value: 2.44e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  33 SRELRGQIEAINPTSPTSAELIIRPGWGMPT-DFKPGQFIGLGVEVKGKYLWRSYSLTNAPrpHDGLLTINIRALNDGYV 111
Cdd:COG1018    1 AGFRPLRVVEVRRETPDVVSFTLEPPDGAPLpRFRPGQFVTLRLPIDGKPLRRAYSLSSAP--GDGRLEITVKRVPGGGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 112 SQHLVANVKPGTVVRLAAPAGDFHLPEPLPARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELR 191
Cdd:COG1018   79 SNWLHDHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGARSPADLAFRDELE 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 896156355 192 ELEQCSATSALKYRLHARNTETQPRIDAAAVTDIIADF 229
Cdd:COG1018  159 ALAARHPRLRLHPVLSREPAGLQGRLDAELLAALLPDP 196
PRK13289 PRK13289
NO-inducible flavohemoprotein;
64-193 1.61e-21

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 94.48  E-value: 1.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  64 DFKPGQFIGLGVEVKGKYL--WRSYSLTNAPRphDGLLTINIRALNDGYVSQHLVANVKPGTVVRLAAPAGDFHLPEPLP 141
Cdd:PRK13289 184 DFKPGQYLGVRLDPEGEEYqeIRQYSLSDAPN--GKYYRISVKREAGGKVSNYLHDHVNVGDVLELAAPAGDFFLDVASD 261

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 896156355 142 ARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELREL 193
Cdd:PRK13289 262 TPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIHAARNGGVHAFRDEVEAL 313
Fdx COG0633
Ferredoxin [Energy production and conversion];
278-354 1.76e-14

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 67.95  E-value: 1.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 278 LGSRGDIDVDGATTILEAAESVGVDLPYGCRMGICATCVQQLSDGAARDIRTGA---TFVAGERVRTCVCAPAGHARIEL 354
Cdd:COG0633    7 IPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDAlsdEERAAGSRLACQARPTSDLVVEL 86
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 284-353 1.64e-13

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: 65.11  E-value: 1.64e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896156355 284 IDVDGATTILEAAESVGVDLPYGCRMGICATCVQQLSDGAARDIRTGATF---VAGERVRTCVCAPAGHARIE 353
Cdd:cd00207   12 VEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDeeeAEGGYVLACQTRVTDGLVIE 84
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
286-346 1.02e-11

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 60.23  E-value: 1.02e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896156355  286 VDGATTILEAAESVGVDLPYGCRMGICATCVQQLSDGAARDIRT---GATFVAGERVRTCVCAP 346
Cdd:pfam00111  13 PDGETTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSfleDDELAAGYVVLACQTYP 76
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 279-353 2.03e-09

ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 54.00  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  279 GSRGDIDVDGATTILEAAESVGVDLPYGCRMGICATCVQQLSDGAARdiRTGATFVAGER-----VRTCVCAPAGHARIE 353
Cdd:TIGR02008  12 GGEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVD--QSDQSFLDDDQmeagyVLTCVAYPTSDCTIE 89
petF CHL00134
ferredoxin; Validated
 284-346 2.49e-09

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 53.96  E-value: 2.49e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896156355 284 IDVDGATTILEAAESVGVDLPYGCRMGICATCVQQLSDGAA--------RDIRTGATFVAgervrTCVCAP 346
Cdd:CHL00134  19 IDCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVdqsdqsflDDDQLEAGFVL-----TCVAYP 84
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
65-135 3.05e-07

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 47.96  E-value: 3.05e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896156355   65 FKPGQFIGLGVEVKGKYLWRSYSLTNAPRPhDGLLTINIRALNDGYVSQHLvANVKPGTVVRLAAPAGDFH 135
Cdd:pfam00970  30 LPVGQHLFLRLPIDGELVIRSYTPISSDDD-KGYLELLVKVYPGGKMSQYL-DELKIGDTIDFKGPLGRFE 98
 
Name Accession Description Interval E-value
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 19-262 1.59e-74

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: 230.57  E-value: 1.59e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  19 LPDDYTHLLNPLWSSRELRGQIEAINPTSPTSAELIIRPGWGmPTDFKPGQFIGLGVEVKGKYLWRSYSLTNAPRPHDGL 98
Cdd:cd06216    1 FVDFYLELINPLWSARELRARVVAVRPETADMVTLTLRPNRG-WPGHRAGQHVRLGVEIDGVRHWRSYSLSSSPTQEDGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  99 LTINIRALNDGYVSQHLVANVKPGTVVRLAAPAGDFHLPEPLPARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSY 178
Cdd:cd06216   80 ITLTVKAQPDGLVSNWLVNHLAPGDVVELSQPQGDFVLPDPLPPRLLLIAAGSGITPVMSMLRTLLARGPTADVVLLYYA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 179 RGEAEAVFVNELRELEQcsATSALKYRLHARNTETQPRIDAAAVTDIIADFgalaSSASAYACGPVELLKNLEPEF---- 254
Cdd:cd06216  160 RTREDVIFADELRALAA--QHPNLRLHLLYTREELDGRLSAAHLDAVVPDL----ADRQVYACGPPGFLDAAEELLeaag 233

                        250
                 ....*....|
gi 896156355 255 --PGLRTERF 262
Cdd:cd06216  234 laDRLHTERF 243
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
33-229 2.44e-48

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 162.65  E-value: 2.44e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  33 SRELRGQIEAINPTSPTSAELIIRPGWGMPT-DFKPGQFIGLGVEVKGKYLWRSYSLTNAPrpHDGLLTINIRALNDGYV 111
Cdd:COG1018    1 AGFRPLRVVEVRRETPDVVSFTLEPPDGAPLpRFRPGQFVTLRLPIDGKPLRRAYSLSSAP--GDGRLEITVKRVPGGGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 112 SQHLVANVKPGTVVRLAAPAGDFHLPEPLPARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELR 191
Cdd:COG1018   79 SNWLHDHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGARSPADLAFRDELE 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 896156355 192 ELEQCSATSALKYRLHARNTETQPRIDAAAVTDIIADF 229
Cdd:COG1018  159 ALAARHPRLRLHPVLSREPAGLQGRLDAELLAALLPDP 196
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 64-229 5.24e-37

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: 133.10  E-value: 5.24e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  64 DFKPGQFIGLGVEVKGKYLWRSYSLTNAP-RPHdgLLTINIRALNDGYVSQHLVANVKPGTVVRLAAPAGDFHLPEPLPA 142
Cdd:cd06215   27 AYKPGQFLTLELEIDGETVYRAYTLSSSPsRPD--SLSITVKRVPGGLVSNWLHDNLKVGDELWASGPAGEFTLIDHPAD 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 143 RIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELRELEQCSATSALKYRLHARNTET----QPRID 218
Cdd:cd06215  105 KLLLLSAGSGITPMMSMARWLLDTRPDADIVFIHSARSPADIIFADELEELARRHPNFRLHLILEQPAPGAwggyRGRLN 184

                        170
                 ....*....|.
gi 896156355 219 AAAVTDIIADF 229
Cdd:cd06215  185 AELLALLVPDL 195
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 64-263 1.15e-32

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: 121.88  E-value: 1.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  64 DFKPGQFIGLGVEVKGKYLWRSYSLTNAPrpHDGLLTINIRALNDGYVSQHLVANVKPGTVVRLAAPAGDFHLP-EPLPA 142
Cdd:cd06214   32 RYRPGQFLTLRVPIDGEEVRRSYSICSSP--GDDELRITVKRVPGGRFSNWANDELKAGDTLEVMPPAGRFTLPpLPGAR 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 143 RIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELRELEqcsatsaLKY--RLHARNTETQP----- 215
Cdd:cd06214  110 HYVLFAAGSGITPVLSILKTALAREPASRVTLVYGNRTEASVIFREELADLK-------ARYpdRLTVIHVLSREqgdpd 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 896156355 216 ----RIDAAAVTDIIADFGALASSASAYACGPVELLKNLEPEFPGL-------RTERFT 263
Cdd:cd06214  183 llrgRLDAAKLNALLKNLLDATEFDEAFLCGPEPMMDAVEAALLELgvpaeriHRELFT 241
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 60-250 3.33e-32

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: 120.74  E-value: 3.33e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  60 GMPTDFKPGQFIGLGVEVKGKYLW--RSYSLTNAPRphDGLLTINIRALNDGYVSQHLVANVKPGTVVRLAAPAGDFHLP 137
Cdd:cd06184   32 GPLPPFLPGQYLSVRVKLPGLGYRqiRQYSLSDAPN--GDYYRISVKREPGGLVSNYLHDNVKVGDVLEVSAPAGDFVLD 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 138 EPLPARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELRELEQcsATSALKYRLH---------A 208
Cdd:cd06184  110 EASDRPLVLISAGVGITPMLSMLEALAAEGPGRPVTFIHAARNSAVHAFRDELEELAA--RLPNLKLHVFysepeagdrE 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 896156355 209 RNTETQPRIDAAAVTDII----ADFgalassasaYACGPVELLKNL 250
Cdd:cd06184  188 EDYDHAGRIDLALLRELLlpadADF---------YLCGPVPFMQAV 224
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 38-262 1.21e-31

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: 118.78  E-value: 1.21e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  38 GQIEAINPTSPTSAELIIR-PGWgMPTDFKPGQFIGLGVEVKGKYLWRSYSLTNAPRPHDglLTINIRALNDGYVSQHLV 116
Cdd:cd06191    1 LRVAEVRSETPDAVTIVFAvPGP-LQYGFRPGQHVTLKLDFDGEELRRCYSLCSSPAPDE--ISITVKRVPGGRVSNYLR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 117 ANVKPGTVVRLAAPAGDFHLPEPLPARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELRELeqc 196
Cdd:cd06191   78 EHIQPGMTVEVMGPQGHFVYQPQPPGRYLLVAAGSGITPLMAMIRATLQTAPESDFTLIHSARTPADMIFAQELREL--- 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896156355 197 sATSALKYRLHARNTETQPRIDAAAVT-----DIIADFGALASSASAYACGPVELLKNLEP-------EFPGLRTERF 262
Cdd:cd06191  155 -ADKPQRLRLLCIFTRETLDSDLLHGRidgeqSLGAALIPDRLEREAFICGPAGMMDAVETalkelgmPPERIHTERF 231
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 62-248 1.78e-31

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: 118.32  E-value: 1.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  62 PTDFKPGQFIGLGVEVKGKYLWRSYSLTNAPRPHDgLLTINIRALNDGYVSQHLvANVKPGTVVRLAAPAGDFHLPEPLP 141
Cdd:cd00322   20 GFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEG-ELELTVKIVPGGPFSAWL-HDLKPGDEVEVSGPGGDFFLPLEES 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 142 ARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELRELEQCSAtsalKYRLHARNTETQPRIDAAA 221
Cdd:cd00322   98 GPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTPADLLFLDELEELAKEGP----NFRLVLALSRESEAKLGPG 173

                        170       180       190
                 ....*....|....*....|....*....|.
gi 896156355 222 VTDIIADFGALASSASAYA----CGPVELLK 248
Cdd:cd00322  174 GRIDREAEILALLPDDSGAlvyiCGPPAMAK 204
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 55-263 2.52e-25

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: 101.56  E-value: 2.52e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  55 IRPGWGMPtDFKPGQFigLGVEVKGKYLWRS--YSLTNAPRPhDGLLTINIRALNDGyvSQHLVANVKPGTVVRLAAPAG 132
Cdd:cd06198   14 LEPRGPAL-GHRAGQF--AFLRFDASGWEEPhpFTISSAPDP-DGRLRFTIKALGDY--TRRLAERLKPGTRVTVEGPYG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 133 DFHLPEPLPaRIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELRELEQcsatsALKYRLHARNTE 212
Cdd:cd06198   88 RFTFDDRRA-RQIWIAGGIGITPFLALLEALAARGDARPVTLFYCVRDPEDAVFLDELRALAA-----AAGVVLHVIDSP 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 896156355 213 TQPRIDAaavTDIIADFGALASSASAYACGPVELLKNLEPEFPGLR-------TERFT 263
Cdd:cd06198  162 SDGRLTL---EQLVRALVPDLADADVWFCGPPGMADALEKGLRALGvparrfhYERFE 216
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
23-262 6.69e-25

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 104.59  E-value: 6.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  23 YTHLLNPLWSSReLRGQIEAINPTSPTSAELIIRPGWGMPTDFKPGQFIGLGVEvKGKYLWRS--YSLTNAPRpHDGLLT 100
Cdd:COG4097  203 YSRLGRPLRSRR-HPYRVESVEPEAGDVVELTLRPEGGRWLGHRAGQFAFLRFD-GSPFWEEAhpFSISSAPG-GDGRLR 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 101 INIRALNDGyvSQHLvANVKPGTVVRLAAPAGDFHLPEPLPA-RIAFVTAGSGVTPVISMLRDLSARNAS-VEVEHIHSY 178
Cdd:COG4097  280 FTIKALGDF--TRRL-GRLKPGTRVYVEGPYGRFTFDRRDTApRQVWIAGGIGITPFLALLRALAARPGDqRPVDLFYCV 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 179 RGEAEAVFVNELRELeqcsATSALKYRLHARNTETQPRIDAAAVTDIIADfgalASSASAYACGPVELLKNLEPEFP--G 256
Cdd:COG4097  357 RDEEDAPFLEELRAL----AARLAGLRLHLVVSDEDGRLTAERLRRLVPD----LAEADVFFCGPPGMMDALRRDLRalG 428


                 ....*.
gi 896156355 257 LRTERF 262
Cdd:COG4097  429 VPARRI 434
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 41-262 4.64e-24

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: 98.49  E-value: 4.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  41 EAINPTSPTSAELIIRPGWGMPtDFKPGQFIGLGVEVK-GKYLWRSYSLTNAPRPHDGL-LTIniRALNDGYVSQHLVAN 118
Cdd:cd06217    8 EIIQETPTVKTFRLAVPDGVPP-PFLAGQHVDLRLTAIdGYTAQRSYSIASSPTQRGRVeLTV--KRVPGGEVSPYLHDE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 119 VKPGTVVRLAAPAGDFHLPEPLPARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELRELEqcsa 198
Cdd:cd06217   85 VKVGDLLEVRGPIGTFTWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVPFRLLYSARTAEDVIFRDELEQLA---- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 199 tsALKYRLHARNTETQP----------RIDAAAVTDIIADfgalASSASAYACGPVELLKNLEPEFPGL-------RTER 261
Cdd:cd06217  161 --RRHPNLHVTEALTRAapadwlgpagRITADLIAELVPP----LAGRRVYVCGPPAFVEAATRLLLELgvprdriRTEA 234


                 .
gi 896156355 262 F 262
Cdd:cd06217  235 F 235
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 40-266 2.55e-23

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: 96.51  E-value: 2.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  40 IEAINPTSPTSAELIIRPGWGMPtdFKPGQFIGLGVEvKGKYLWRSYSLTNAPRPhDGLLTINIRALNDGYVSQHLVANV 119
Cdd:cd06187    1 VVSVERLTHDIAVVRLQLDQPLP--FWAGQYVNVTVP-GRPRTWRAYSPANPPNE-DGEIEFHVRAVPGGRVSNALHDEL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 120 KPGTVVRLAAPAGDFHLPEPLPARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELRELEQcsat 199
Cdd:cd06187   77 KVGDRVRLSGPYGTFYLRRDHDRPVLCIAGGTGLAPLRAIVEDALRRGEPRPVHLFFGARTERDLYDLEGLLALAA---- 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896156355 200 salKYR-LHARNTETQPRIDAAA----VTDIIADFGALASSASAYACGP-------VELLKNLepefpGLRTERFTVDR 266
Cdd:cd06187  153 ---RHPwLRVVPVVSHEEGAWTGrrglVTDVVGRDGPDWADHDIYICGPpamvdatVDALLAR-----GAPPERIHFDK 223
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 38-195 1.12e-22

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: 94.72  E-value: 1.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  38 GQIEAINPTSPTSAELII--RPGWGMPT--DFKPGQFIGLgvEVKGKYLWRSYSLTNAPRPhDGLLTINIRALNDGYVSQ 113
Cdd:cd06210    4 AEIVAVDRVSSNVVRLRLqpDDAEGAGIaaEFVPGQFVEI--EIPGTDTRRSYSLANTPNW-DGRLEFLIRLLPGGAFST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 114 HLVANVKPGTVVRLAAPAGDFHLPEPLPARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELREL 193
Cdd:cd06210   81 YLETRAKVGQRLNLRGPLGAFGLRENGLRPRWFVAGGTGLAPLLSMLRRMAEWGEPQEARLFFGVNTEAELFYLDELKRL 160


                 ..
gi 896156355 194 EQ 195
Cdd:cd06210  161 AD 162
PRK13289 PRK13289
NO-inducible flavohemoprotein;
64-193 1.61e-21

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 94.48  E-value: 1.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  64 DFKPGQFIGLGVEVKGKYL--WRSYSLTNAPRphDGLLTINIRALNDGYVSQHLVANVKPGTVVRLAAPAGDFHLPEPLP 141
Cdd:PRK13289 184 DFKPGQYLGVRLDPEGEEYqeIRQYSLSDAPN--GKYYRISVKREAGGKVSNYLHDHVNVGDVLELAAPAGDFFLDVASD 261

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 896156355 142 ARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELREL 193
Cdd:PRK13289 262 TPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIHAARNGGVHAFRDEVEAL 313
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 39-265 1.74e-20

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: 1.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  39 QIEAINPTSPTSAELIIRPGwGMPTDFKPGQFIGlgVEVKGKYLWRSYSLTNAPRPhDGLLTINIRALndGYVSQHLvAN 118
Cdd:COG0543    1 KVVSVERLAPDVYLLRLEAP-LIALKFKPGQFVM--LRVPGDGLRRPFSIASAPRE-DGTIELHIRVV--GKGTRAL-AE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 119 VKPGTVVRLAAPAGDFHLPEPLPARIAFVTAGSGVTPVISMLRDLSARNASVEVehIHSYRGEAEAVFVNELRELEQCSA 198
Cdd:COG0543   74 LKPGDELDVRGPLGNGFPLEDSGRPVLLVAGGTGLAPLRSLAEALLARGRRVTL--YLGARTPEDLYLLDELEALADFRV 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896156355 199 TSAlkyrlharnTETQPRIDAAAVTDIIADFGALASSASAYACGPVELLKNLEPEFP--GLRTERFTVD 265
Cdd:COG0543  152 VVT---------TDDGWYGRKGFVTDALKELLAEDSGDDVYACGPPPMMKAVAELLLerGVPPERIYVS 211
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 65-348 1.82e-20

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 90.54  E-value: 1.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  65 FKPGQFIGLGVEVKGKYLwRSYSLTNAPrphdGL---LTINIRALNDGYVSQHLVANVKPGTVVRLAAPAGDFHLPEPLP 141
Cdd:PRK10684  37 YRAGQYALVSIRNSAETL-RAYTLSSTP----GVsefITLTVRRIDDGVGSQWLTRDVKRGDYLWLSDAMGEFTCDDKAE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 142 ARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELRELeqCSATSALKYRLHARNTET----QPRI 217
Cdd:PRK10684 112 DKYLLLAAGCGVTPIMSMRRWLLKNRPQADVQVIFNVRTPQDVIFADEWRQL--KQRYPQLNLTLVAENNATegfiAGRL 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 218 DAAAVTDIIADFgalaSSASAYACGPVELLKNLEPEFPGL-------RTERF--TVDRSAAGEVGGTVSLGSRgDIDVDG 288
Cdd:PRK10684 190 TRELLQQAVPDL----ASRTVMTCGPAPYMDWVEQEVKALgvtadrfFKEKFftPVAEAATSGLTFTKLQPAR-EFYAPV 264

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896156355 289 ATTILEAAESVGVDLPYGCRMGICATCVQQLSDGAARDIRTGaTFVAGE----RVRTCVCAPAG 348
Cdd:PRK10684 265 GTTLLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVSSTM-TLTPAEiaqgYVLACSCHPQG 327
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 38-266 6.28e-19

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: 84.30  E-value: 6.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  38 GQIEAINPTSPTSAELIIRPGWGMPTDFKPGQFIGlgVEVKGKYLWRSYSLTNAPRpHDGLLTINIRALNDGYVSQHLVA 117
Cdd:cd06212    3 GTVVAVEALTHDIRRLRLRLEEPEPIKFFAGQYVD--ITVPGTEETRSFSMANTPA-DPGRLEFIIKKYPGGLFSSFLDD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 118 NVKPGTVVRLAAPAGDFHLPEPLPARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELRELEQCS 197
Cdd:cd06212   80 GLAVGDPVTVTGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDMAASGSDRPVRFFYGARTARDLFYLEEIAALGEKI 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896156355 198 ATSALKYRLHARNTETQPRIDAAAVTDIIADFGALASSASAYACGPVELLKNLEP--EFPGLRTERFTVDR 266
Cdd:cd06212  160 PDFTFIPALSESPDDEGWSGETGLVTEVVQRNEATLAGCDVYLCGPPPMIDAALPvlEMSGVPPDQIFYDK 230
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 47-195 1.05e-18

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: 84.15  E-value: 1.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  47 SPTSAELIIRPGWGMPtdFKPGQFIGLGVEVK-GKYLWRSYSLTNAPrpHDGLLTINIRALNDGYVSQHLvANVKPGTVV 125
Cdd:cd06195    9 TDDLFSFRVTRDIPFR--FQAGQFTKLGLPNDdGKLVRRAYSIASAP--YEENLEFYIILVPDGPLTPRL-FKLKPGDTI 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896156355 126 RLAA-PAGDFHLPE-PLPARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELRELEQ 195
Cdd:cd06195   84 YVGKkPTGFLTLDEvPPGKRLWLLATGTGIAPFLSMLRDLEIWERFDKIVLVHGVRYAEELAYQDEIEALAK 155
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 35-166 4.49e-17

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: 79.17  E-value: 4.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  35 ELRGQIEAINPTSPTSAELIIRPGWGMPTDFKPGQFIGLgvEVKGKYLWRSYSLTNAPrpHDGLLTINIRALNDGYVSQH 114
Cdd:cd06209    1 TFEATVTEVERLSDSTIGLTLELDEAGALAFLPGQYVNL--QVPGTDETRSYSFSSAP--GDPRLEFLIRLLPGGAMSSY 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 896156355 115 LVANVKPGTVVRLAAPAGDFHLPEPlPARIAFVTAGSGVTPVISMLRDLSAR 166
Cdd:cd06209   77 LRDRAQPGDRLTLTGPLGSFYLREV-KRPLLMLAGGTGLAPFLSMLDVLAED 127
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 34-195 5.22e-16

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: 76.21  E-value: 5.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  34 RELRGQIEAINPTSPTSAELIIRPGWGMPTDFKPGQFIGLgvEVKGKYLWRSYSLTNAPRpHDGLLTINIRALNDG---- 109
Cdd:cd06211    5 KDFEGTVVEIEDLTPTIKGVRLKLDEPEEIEFQAGQYVNL--QAPGYEGTRAFSIASSPS-DAGEIELHIRLVPGGiatt 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 110 YVSQHLvanvKPGTVVRLAAPAGDFHLPEPLPARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNE 189
Cdd:cd06211   82 YVHKQL----KEGDELEISGPYGDFFVRDSDQRPIIFIAGGSGLSSPRSMILDLLERGDTRKITLFFGARTRAELYYLDE 157


                 ....*.
gi 896156355 190 LRELEQ 195
Cdd:cd06211  158 FEALEK 163
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 40-246 5.94e-16

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: 75.77  E-value: 5.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  40 IEAINPTSPTSAELIIRPGwgMPTDFKPGQFIGLgveVKGKYLWRSYSLTNAPRpHDGLLTINIRALNDGYVSQHLVANV 119
Cdd:cd06194    1 VVSLQRLSPDVLRVRLEPD--RPLPYLPGQYVNL---RRAGGLARSYSPTSLPD-GDNELEFHIRRKPNGAFSGWLGEEA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 120 KPGTVVRLAAPAGD-FHLPEPLPARIAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAEAVFVNELRELEQcsA 198
Cdd:cd06194   75 RPGHALRLQGPFGQaFYRPEYGEGPLLLVGAGTGLAPLWGIARAALRQGHQGEIRLVHGARDPDDLYLHPALLWLAR--E 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 896156355 199 TSALKYRLHArnTETQPRIDAAAVTDIIADFGALASSASAYACGPVEL 246
Cdd:cd06194  153 HPNFRYIPCV--SEGSQGDPRVRAGRIAAHLPPLTRDDVVYLCGAPSM 198
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 39-176 7.09e-16

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: 75.66  E-value: 7.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  39 QIEAINPTSPTSAELIIRPGwgMPTDFKPGQFigLGVEVKGKYlWRSYSLTNAPRpHDGLLTINIRALNDGYVSQHLVAN 118
Cdd:cd06189    2 KVESIEPLNDDVYRVRLKPP--APLDFLAGQY--LDLLLDDGD-KRPFSIASAPH-EDGEIELHIRAVPGGSFSDYVFEE 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 896156355 119 VKPGTVVRLAAPAGDFHLPEPLPARIAFVTAGSGVTPVISMLRDLSARNASVEVeHIH 176
Cdd:cd06189   76 LKENGLVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQGSKRPI-HLY 132
Fdx COG0633
Ferredoxin [Energy production and conversion];
278-354 1.76e-14

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 67.95  E-value: 1.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 278 LGSRGDIDVDGATTILEAAESVGVDLPYGCRMGICATCVQQLSDGAARDIRTGA---TFVAGERVRTCVCAPAGHARIEL 354
Cdd:COG0633    7 IPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDAlsdEERAAGSRLACQARPTSDLVVEL 86
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 34-195 1.63e-13

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: 71.05  E-value: 1.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  34 RELRGQIEAINPTSPTSAELIIRPGWGMPTDFKPGQFI------------GLGVEVKGKYLW---------RSYSLTNAP 92
Cdd:COG2871  130 KKWEATVVSNENVTTFIKELVLELPEGEEIDFKAGQYIqievppyevdfkDFDIPEEEKFGLfdkndeevtRAYSMANYP 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  93 RPhDGLLTINIR------ALNDGYVSQHlVANVKPGTVVRLAAPAGDFHLPEPlPARIAFVTAGSGVTPVISMLRDLSAR 166
Cdd:COG2871  210 AE-KGIIELNIRiatppmDVPPGIGSSY-IFSLKPGDKVTISGPYGEFFLRDS-DREMVFIGGGAGMAPLRSHIFDLLER 286

                        170       180       190
                 ....*....|....*....|....*....|....
gi 896156355 167 NAS-VEVehihSY----RGEAEAVFVNELRELEQ 195
Cdd:COG2871  287 GKTdRKI----TFwygaRSLRELFYLEEFRELEK 316
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 284-353 1.64e-13

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: 65.11  E-value: 1.64e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896156355 284 IDVDGATTILEAAESVGVDLPYGCRMGICATCVQQLSDGAARDIRTGATF---VAGERVRTCVCAPAGHARIE 353
Cdd:cd00207   12 VEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDeeeAEGGYVLACQTRVTDGLVIE 84
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
32-183 2.29e-13

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 70.16  E-value: 2.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  32 SSRELRGQIEAINPTSPTSAELIIRPGW-GMPTDFKPGQFIGLgvEVKGKYLWRSYSLTNAPRPHDGLLTInIRALNDGY 110
Cdd:PRK11872 103 DTLKISGVVTAVELVSETTAILHLDASAhGRQLDFLPGQYARL--QIPGTDDWRSYSFANRPNATNQLQFL-IRLLPDGV 179

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896156355 111 VSQHLVANVKPGTVVRLAAPAGDFHLPE---PLpariAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSYRGEAE 183
Cdd:PRK11872 180 MSNYLRERCQVGDEILFEAPLGAFYLREverPL----VFVAGGTGLSAFLGMLDELAEQGCSPPVHLYYGVRHAAD 251
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 37-166 4.73e-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: 67.72  E-value: 4.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  37 RGQIEAINPTSPTSAELIIRPGWGMPtdFKPGQFIGLGVEvkGKYLWRSYSLTNAPRPhDGLLTINIRALNDGYVSQHLV 116
Cdd:cd06213    2 RGTIVAQERLTHDIVRLTVQLDRPIA--YKAGQYAELTLP--GLPAARSYSFANAPQG-DGQLSFHIRKVPGGAFSGWLF 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 896156355 117 ANVKPGTVVRLAAPAGDFHLpEPLPARIAFVTAGSGVTPVISMLRDLSAR 166
Cdd:cd06213   77 GADRTGERLTVRGPFGDFWL-RPGDAPILCIAGGSGLAPILAILEQARAA 125
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 62-195 6.18e-13

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: 67.28  E-value: 6.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  62 PTDFKPGQFIGLGVEvkGKYLWRSYSLTNAPRPhDGLLTINIRALNDGYVSQHLVANVKPGTVVRLAAPAGDFHLPEPLP 141
Cdd:cd06190   21 PADFLPGQYALLALP--GVEGARAYSMANLANA-SGEWEFIIKRKPGGAASNALFDNLEPGDELELDGPYGLAYLRPDED 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 896156355 142 ARIAFVTAGSGVTPVISMLRDLSARNASVEvEHIHSY---RGEAEAVFVNELRELEQ 195
Cdd:cd06190   98 RDIVCIAGGSGLAPMLSILRGAARSPYLSD-RPVDLFyggRTPSDLCALDELSALVA 153
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 82-220 2.75e-12

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: 65.20  E-value: 2.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  82 LWRSYSLTNAPRpHDGLLTINI-RALNDGYVSQHLVANVKPGTVVRLAAPAGDFHLPEPLPaRIAFVTAGSGVTPVISML 160
Cdd:cd06185   40 LVRQYSLCGDPA-DRDRYRIAVlREPASRGGSRYMHELLRVGDELEVSAPRNLFPLDEAAR-RHLLIAGGIGITPILSMA 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 161 RDLSARNASVEVehIHSYRGEAEAVFVNELRELEqcsatsALKYRLHARNTETQPRIDAA 220
Cdd:cd06185  118 RALAARGADFEL--HYAGRSREDAAFLDELAALP------GDRVHLHFDDEGGRLDLAAL 169
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
286-346 1.02e-11

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 60.23  E-value: 1.02e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896156355  286 VDGATTILEAAESVGVDLPYGCRMGICATCVQQLSDGAARDIRT---GATFVAGERVRTCVCAP 346
Cdd:pfam00111  13 PDGETTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSfleDDELAAGYVVLACQTYP 76
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 59-195 2.53e-10

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: 59.89  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  59 WGMPtdfkPGQFIGLGVEVKGKYLWRSYSLTnaPRPHD-GLLTINIRALNDGYVSQHLvANVKPGTVVRLAAPAGDF-HL 136
Cdd:cd06183   27 LGLP----VGQHVELKAPDDGEQVVRPYTPI--SPDDDkGYFDLLIKIYPGGKMSQYL-HSLKPGDTVEIRGPFGKFeYK 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 137 PEPLPARIAFVTAGSGVTPVISMLRD-LSARNASVEVEHIHSYRGEAEAVFVNELRELEQ 195
Cdd:cd06183  100 PNGKVKHIGMIAGGTGITPMLQLIRAiLKDPEDKTKISLLYANRTEEDILLREELDELAK 159
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 64-167 1.96e-09

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 58.34  E-value: 1.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  64 DFKPGQFIGLGVEvKGKylWRSYSLTNAPRpHDGLLTINIRALNDGYVSQHLVANVKPGTVVRLAAPAGDFHLPEpLPAR 143
Cdd:PRK07609 131 QYLAGQYIEFILK-DGK--RRSYSIANAPH-SGGPLELHIRHMPGGVFTDHVFGALKERDILRIEGPLGTFFLRE-DSDK 205

                         90       100
                 ....*....|....*....|....*
gi 896156355 144 -IAFVTAGSGVTPVISMLRDLSARN 167
Cdd:PRK07609 206 pIVLLASGTGFAPIKSIVEHLRAKG 230
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 279-353 2.03e-09

ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 54.00  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  279 GSRGDIDVDGATTILEAAESVGVDLPYGCRMGICATCVQQLSDGAARdiRTGATFVAGER-----VRTCVCAPAGHARIE 353
Cdd:TIGR02008  12 GGEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVD--QSDQSFLDDDQmeagyVLTCVAYPTSDCTIE 89
petF CHL00134
ferredoxin; Validated
 284-346 2.49e-09

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 53.96  E-value: 2.49e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896156355 284 IDVDGATTILEAAESVGVDLPYGCRMGICATCVQQLSDGAA--------RDIRTGATFVAgervrTCVCAP 346
Cdd:CHL00134  19 IDCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVdqsdqsflDDDQLEAGFVL-----TCVAYP 84
PTZ00038 PTZ00038
ferredoxin; Provisional
 284-322 4.82e-09

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 55.23  E-value: 4.82e-09
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 896156355 284 IDVDGATTILEAAESVGVDLPYGCRMGICATCVQQLSDG 322
Cdd:PTZ00038 109 IECDEDEYILDAAERQGVELPYSCRGGSCSTCAAKLLEG 147
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 52-195 4.93e-09

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: 56.54  E-value: 4.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  52 ELIIRPGWGMPTDFKPGQFIGLGV----------EVKGKYL--W-----------------RSYSLTNapRPHD-GLLTI 101
Cdd:cd06188   26 ELVLKLPSGEEIAFKAGGYIQIEIpayeiayadfDVAEKYRadWdkfglwqlvfkhdepvsRAYSLAN--YPAEeGELKL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 102 NIR---------ALNDGYVSqHLVANVKPGTVVRLAAPAGDFHLPEPlPARIAFVTAGSGVTPVISMLRD-LSARNASVE 171
Cdd:cd06188  104 NVRiatpppgnsDIPPGIGS-SYIFNLKPGDKVTASGPFGEFFIKDT-DREMVFIGGGAGMAPLRSHIFHlLKTLKSKRK 181

                        170       180
                 ....*....|....*....|....
gi 896156355 172 VEHIHSYRGEAEAVFVNELRELEQ 195
Cdd:cd06188  182 ISFWYGARSLKELFYQEEFEALEK 205
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 64-325 8.25e-08

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: 52.71  E-value: 8.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  64 DFKPGQFIGLGVEVKGKYLWRSYSLTNApRPHDGLLTINIRALNdgyVSQHLVANVKPGTVVRLAAPAGDfhlPEPLPAR 143
Cdd:cd06192   24 LFRPGQFVFLRNFESPGLERIPLSLAGV-DPEEGTISLLVEIRG---PKTKLIAELKPGEKLDVMGPLGN---GFEGPKK 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 144 ---IAFVTAGSGVTPVISMLRDLSARNASVEVehIHSYRGEAEAVFVNELRELEQ--CSATSALKYRLHARNTETQPRID 218
Cdd:cd06192   97 ggtVLLVAGGIGLAPLLPIAKKLAANGNKVTV--LAGAKKAKEEFLDEYFELPADveIWTTDDGELGLEGKVTDSDKPIP 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 219 AAAVTDIIAdfgalassasayaCGPVELLKNLepefpglrterftvdRSAAGEVGGTVSLgsrgdidvdgattileaaeS 298
Cdd:cd06192  175 LEDVDRIIV-------------AGSDIMMKAV---------------VEALDEWLQLIKA-------------------S 207

                        250       260
                 ....*....|....*....|....*..
gi 896156355 299 VGVDLPYGCRMGICATCVQQLSDGAAR 325
Cdd:cd06192  208 VSNNSPMCCGIGICGACTIETKHGVKR 234
PRK10926 PRK10926
ferredoxin-NADP reductase; Provisional
 62-195 1.25e-07

ferredoxin-NADP reductase; Provisional


Pssm-ID: 182844  Cd Length: 248  Bit Score: 52.01  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  62 PTD-FKPGQFIGLGVEVKGKYLWRSYSLTNAPRPHDglLTINIRALNDGYVSQHLVAnVKPGTVVRLAAPAGDFHLPEPL 140
Cdd:PRK10926  27 PVDpFTAGQFTKLGLEIDGERVQRAYSYVNAPDNPD--LEFYLVTVPEGKLSPRLAA-LKPGDEVQVVSEAAGFFVLDEV 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 141 P--ARIAFVTAGSGVTPVISML---RDLSARNASVEVehiHSYRGEAEAVFVNELRELEQ 195
Cdd:PRK10926 104 PdcETLWMLATGTAIGPYLSILqegKDLERFKNLVLV---HAARYAADLSYLPLMQELEQ 160
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
65-135 3.05e-07

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 47.96  E-value: 3.05e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896156355   65 FKPGQFIGLGVEVKGKYLWRSYSLTNAPRPhDGLLTINIRALNDGYVSQHLvANVKPGTVVRLAAPAGDFH 135
Cdd:pfam00970  30 LPVGQHLFLRLPIDGELVIRSYTPISSDDD-KGYLELLVKVYPGGKMSQYL-DELKIGDTIDFKGPLGRFE 98
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 64-250 5.28e-07

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: 49.93  E-value: 5.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  64 DFKPGQfiglGVEVK-GKYLW----RSYSLTNapRPHDGLL--TINIRALNDGyVSQHLVAnVKPGTVVRLAAPAGDFHL 136
Cdd:cd06196   27 DFTPGQ----ATEVAiDKPGWrdekRPFTFTS--LPEDDVLefVIKSYPDHDG-VTEQLGR-LQPGDTLLIEDPWGAIEY 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 137 PEPLpariAFVTAGSGVTPVISMLRDLsARNASVEVEH-IHSYRGEAEAVFVNELRELEQ------CSATSALKYrlHAR 209
Cdd:cd06196   99 KGPG----VFIAGGAGITPFIAILRDL-AAKGKLEGNTlIFANKTEKDIILKDELEKMLGlkfinvVTDEKDPGY--AHG 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 896156355 210 ntetqpRIDAAAVTDIIADFGalassASAYACGP-------VELLKNL 250
Cdd:cd06196  172 ------RIDKAFLKQHVTDFN-----QHFYVCGPppmeeaiNGALKEL 208
PLN03136 PLN03136
Ferredoxin; Provisional
 283-353 6.99e-07

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 48.21  E-value: 6.99e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896156355 283 DIDVDGATTILEAAESVGVDLPYGCRMGICATCVQQLSDGAARdiRTGATFVAGER-----VRTCVCAPAGHARIE 353
Cdd:PLN03136  67 EVECEEDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSID--QSDQSFLDDEQisegyVLTCVAYPTSDVVIE 140
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 284-353 3.35e-05

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 45.25  E-value: 3.35e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896156355 284 IDVDGATTILEAAESVGVDLPYGCRMGICATCVQQLSDGAARDIRTGATFVAGERVR-----TCVCAPAGHARIE 353
Cdd:PRK07609  14 FTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQGPHQASALSGEERAagealTCCAKPLSDLVLE 88
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 84-181 6.47e-05

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: 43.53  E-value: 6.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  84 RSYSLTNAP--RPHDGLLTINIRalNDGYVSQHLVANVKPGTVVRLAAP----AGDFHLPEPLPA---RIAFVTAGSGVT 154
Cdd:cd06197   61 RTFTVSSAPphDPATDEFEITVR--KKGPVTGFLFQVARRLREQGLEVPvlgvGGEFTLSLPGEGaerKMVWIAGGVGIT 138

                         90       100
                 ....*....|....*....|....*...
gi 896156355 155 PVISMLRDL-SARNASVEVEHIHSYRGE 181
Cdd:cd06197  139 PFLAMLRAIlSSRNTTWDITLLWSLRED 166
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 40-193 1.55e-04

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 42.55  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  40 IEAINPTSPTSAELIIRpgWGMPTDFKPGQFIGLGVEVKGKYLWRSYSLTNaprPHDGLLTINIRALNDGyvsQHLVANV 119
Cdd:PRK00054   9 IVENKEIAPNIYTLVLD--GEKVFDMKPGQFVMVWVPGVEPLLERPISISD---IDKNEITILYRKVGEG---TKKLSKL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896156355 120 KPGTVVRLAAPAGD-FHLPEPLpARIAFVTAGSGVTPVISMLRDLSARNasVEVEHIHSYRGEAEAVFVNELREL 193
Cdd:PRK00054  81 KEGDELDIRGPLGNgFDLEEIG-GKVLLVGGGIGVAPLYELAKELKKKG--VEVTTVLGARTKDEVIFEEEFAKV 152
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 66-346 1.83e-04

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: 42.53  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  66 KPGQFIGLGV-EVKGKYLWRSYSLTNApRPHDGLLTINIRALNDGyvSQHLvANVKPGTVVRLAAPAGD-FHLPEPlPAR 143
Cdd:cd06218   26 KPGQFVMLRVpDGSDPLLRRPISIHDV-DPEEGTITLLYKVVGKG--TRLL-SELKAGDELDVLGPLGNgFDLPDD-DGK 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 144 IAFVTAGSGVTPVISMLRDLSARNasVEVEHIHSYRGEAEAVFVNELRELEQCSATSalkyrlharnTEtqpriDAAA-- 221
Cdd:cd06218  101 VLLVGGGIGIAPLLFLAKQLAERG--IKVTVLLGFRSADDLFLVEEFEALGAEVYVA----------TD-----DGSAgt 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 222 ---VTDIIADFGALASSASAYACGPVELLKNLepefpglrterftvdRSAAGEVG--GTVSLGSRgdidvdgattileaa 296
Cdd:cd06218  164 kgfVTDLLKELLAEARPDVVYACGPEPMLKAV---------------AELAAERGvpCQVSLEER--------------- 213

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 896156355 297 esvgvdlpYGCRMGICATCVQQLSDGaardirtgatfvAGERVRTCVCAP 346
Cdd:cd06218  214 --------MACGIGACLGCVVKTKDD------------EGGYKRVCKDGP 243
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
 84-160 2.16e-04

Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for the regeneration of methionine from homocysteine, as well as the coversion of methyltetrahydrofolate to tetrahydrofolate. In MSR, electrons are transferred from NADPH to FAD to FMN to cob(II)alamin. MSR resembles proteins of the cytochrome p450 family including nitric oxide synthase, the alpha subunit of sulfite reductase, but contains an extended hinge region. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPORs resemble ferredoxin reductase (FNR) but have a connecting subdomain inserted within the flavin binding region, which helps orient the FMN binding doamin with the FNR module. 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: 99800 [Multi-domain]  Cd Length: 398  Bit Score: 42.69  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  84 RSYSLTNAPRPHDGLLTINIRALNDGYV--------SQHLVANVKPGTVVRLAAPAGDFHLPEPLPAR-IAFVTAGSGVT 154
Cdd:cd06203  175 RPYSIASSPLEGPGKLRFIFSVVEFPAKglctswleSLCLSASSHGVKVPFYLRSSSRFRLPPDDLRRpIIMVGPGTGVA 254


                 ....*.
gi 896156355 155 PVISML 160
Cdd:cd06203  255 PFLGFL 260
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 106-163 2.59e-04

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: 42.31  E-value: 2.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 896156355 106 LNDGYVSQHLvANVKPGTVVRLAAPAGD-FHLPEPLPARIAFVTAGSGVTPVISMLRDL 163
Cdd:cd06208  100 TKKGVCSNYL-CDLKPGDDVQITGPVGKtMLLPEDPNATLIMIATGTGIAPFRSFLRRL 157
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
287-354 3.75e-04

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 38.94  E-value: 3.75e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896156355 287 DGATTILEAAESVGVDLPYGCRMGICATCVQQLSDGAARDIRTGATFVAGERVRTCVCAPAGHARIEL 354
Cdd:PRK10713  17 DEHPSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAEPLAFIQPGEILPCCCRAKGDIEIEM 84
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 40-199 4.34e-04

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: 41.44  E-value: 4.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  40 IEAINPTSPTSAE--LIIRPGWGMPTDFKPGQFIGLGV----EVkgkylwrSYSLTNAPrPHDGLLTINIRALndGYVSQ 113
Cdd:cd06221    1 IVEVVDETEDIKTftLRLEDDDEELFTFKPGQFVMLSLpgvgEA-------PISISSDP-TRRGPLELTIRRV--GRVTE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355 114 HLvANVKPGTVVRLAAPAGD-FHLPEPLPARIAFVTAGSGVTPVISMLRDLSARNASVE-VEHIHSYRGEAEAVFVNELR 191
Cdd:cd06221   71 AL-HELKPGDTVGLRGPFGNgFPVEEMKGKDLLLVAGGLGLAPLRSLINYILDNREDYGkVTLLYGARTPEDLLFKEELK 149


                 ....*...
gi 896156355 192 ELEQCSAT 199
Cdd:cd06221  150 EWAKRSDV 157
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 65-169 5.75e-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: 40.75  E-value: 5.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  65 FKPGQFIGLGV-EVKGKYLWRSYSLTNAPRPHDGLLTINIRALNdG---YVSQHLVANVKPGTVVRLAA--PAGdfHLPE 138
Cdd:cd06186   25 WKPGQHVYLNFpSLLSFWQSHPFTIASSPEDEQDTLSLIIRAKK-GfttRLLRKALKSPGGGVSLKVLVegPYG--SSSE 101

                         90       100       110
                 ....*....|....*....|....*....|...
gi 896156355 139 PLPA--RIAFVTAGSGVTPVISMLRDLSARNAS 169
Cdd:cd06186  102 DLLSydNVLLVAGGSGITFVLPILRDLLRRSSK 134
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 19-167 5.78e-04

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. 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: 99798 [Multi-domain]  Cd Length: 289  Bit Score: 41.16  E-value: 5.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896156355  19 LPDDYTHLLNPLWS----SRELRGqIEAINPTSPTSAELIIRPGWGMP-TDFKPGQFigLGVEVKGKYLWRSYSLTNAPR 93
Cdd:cd06201   34 LPLDHKKRLPRTKAlelvERKDYG-AAVQAPTAILRFKPAKRKLSGKGlPSFEAGDL--LGILPPGSDVPRFYSLASSSS 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896156355  94 phDGLLTINIRALNDGYVSQHLVAnVKPGTVVR-LAAPAGDFHLPEPLPARIAfVTAGSGVTPVISMLRDLSARN 167
Cdd:cd06201  111 --DGFLEICVRKHPGGLCSGYLHG-LKPGDTIKaFIRPNPSFRPAKGAAPVIL-IGAGTGIAPLAGFIRANAARR 181
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
144-194 8.79e-03

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 36.16  E-value: 8.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 896156355  144 IAFVTAGSGVTPVISMLRDLSARNASVEVEHIHSY---RGEAE-AVFVNELRELE 194
Cdd:pfam08030   4 VLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYwvvRDLSSlEWFKDVLNELE 58
 
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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