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Conserved domains on  [gi|1126528355|ref|WP_075166613|]
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ferredoxin reductase [Acinetobacter indicus]

Protein Classification

ferredoxin reductase( domain architecture ID 10865445)

ferredoxin reductase, similar to stearoyl-CoA 9-desaturase electron transfer protein that is part of an acyl-CoA desaturase complex involved in the production of oleic acid

Graphical summary

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List of domain hits

 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 ...
 16-249 3.72e-82

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: 249.45  E-value: 3.72e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  16 FIDFIAEKINPVWALKKVKACVVEIQALSPDFYKIHLRPNQNFQAqrFQAGQSILVTLAMNGVRQQRSYSI--VTLLDNG 93
Cdd:cd06216     1 FVDFYLELINPLWSARELRARVVAVRPETADMVTLTLRPNRGWPG--HRAGQHVRLGVEIDGVRHWRSYSLssSPTQEDG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  94 DVILAIKRQ--GKMSNALTR-LPAGAVVELSQPQGNFVLPAPVPS-LCFIASGSGITAIYSLLQKAVVSS-TQPIDLLYF 168
Cdd:cd06216    79 TITLTVKAQpdGLVSNWLVNhLAPGDVVELSQPQGDFVLPDPLPPrLLLIAAGSGITPVMSMLRTLLARGpTADVVLLYY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 169 TR---DDAFHAEIKTLALMYPHFKYHHFNT-VEQHQHLSLSLLQNTVEQLGERHIYACGSASMMQAAQQICQQLDLSEQF 244
Cdd:cd06216   159 ARtreDVIFADELRALAAQHPNLRLHLLYTrEELDGRLSAAHLDAVVPDLADRQVYACGPPGFLDAAEELLEAAGLADRL 238


                  ....*
gi 1126528355 245 HSEYF 249
Cdd:cd06216   239 HTERF 243
Fdx COG0633
Ferredoxin [Energy production and conversion];
262-340 1.37e-13

Ferredoxin [Energy production and conversion];


:

Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 65.64  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 262 VQFLRSQQDFQA--NSNLLDSAEAAGLRPAHGCRMGICNTCSCTKVSGSVRN-----LLTGEIDHNHntqIKLCVTQAIS 334
Cdd:COG0633     4 VTFIPEGHTVEVpaGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHreedaLSDEERAAGS---RLACQARPTS 80


                  ....*.
gi 1126528355 335 PVVINL 340
Cdd:COG0633    81 DLVVEL 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 ...
 16-249 3.72e-82

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: 249.45  E-value: 3.72e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  16 FIDFIAEKINPVWALKKVKACVVEIQALSPDFYKIHLRPNQNFQAqrFQAGQSILVTLAMNGVRQQRSYSI--VTLLDNG 93
Cdd:cd06216     1 FVDFYLELINPLWSARELRARVVAVRPETADMVTLTLRPNRGWPG--HRAGQHVRLGVEIDGVRHWRSYSLssSPTQEDG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  94 DVILAIKRQ--GKMSNALTR-LPAGAVVELSQPQGNFVLPAPVPS-LCFIASGSGITAIYSLLQKAVVSS-TQPIDLLYF 168
Cdd:cd06216    79 TITLTVKAQpdGLVSNWLVNhLAPGDVVELSQPQGDFVLPDPLPPrLLLIAAGSGITPVMSMLRTLLARGpTADVVLLYY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 169 TR---DDAFHAEIKTLALMYPHFKYHHFNT-VEQHQHLSLSLLQNTVEQLGERHIYACGSASMMQAAQQICQQLDLSEQF 244
Cdd:cd06216   159 ARtreDVIFADELRALAAQHPNLRLHLLYTrEELDGRLSAAHLDAVVPDLADRQVYACGPPGFLDAAEELLEAAGLADRL 238


                  ....*
gi 1126528355 245 HSEYF 249
Cdd:cd06216   239 HTERF 243
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
37-248 3.11e-51

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 169.58  E-value: 3.11e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYKIHLRPNQNFQAQRFQAGQSILVTLAMNGVRQQRSYSIVTLLDNGDVILAIKRQ--GKMSNAL-TRLP 113
Cdd:COG1018     8 VVEVRRETPDVVSFTLEPPDGAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKRVpgGGGSNWLhDHLK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 114 AGAVVELSQPQGNFVLPAPVP-SLCFIASGSGITAIYSLLQKAVVS-STQPIDLLYFTRDD---AFHAEIKTLALMYPHF 188
Cdd:COG1018    88 VGDTLEVSGPRGDFVLDPEPArPLLLIAGGIGITPFLSMLRTLLARgPFRPVTLVYGARSPadlAFRDELEALAARHPRL 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1126528355 189 KYHHFNTVEQ---HQHLSLSLLQNTVEQLGERHIYACGSASMMQAAQQICQQLDLSE-QFHSEY 248
Cdd:COG1018   168 RLHPVLSREPaglQGRLDAELLAALLPDPADAHVYLCGPPPMMEAVRAALAELGVPEeRIHFER 231
PRK13289 PRK13289
NO-inducible flavohemoprotein;
62-249 2.92e-18

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 84.85  E-value: 2.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  62 RFQAGQ--SILVTLAMNGVRQQRSYSIVTLLDNGDVILAIKR--QGKMSNAL-TRLPAGAVVELSQPQGNFVLPA----P 132
Cdd:PRK13289  184 DFKPGQylGVRLDPEGEEYQEIRQYSLSDAPNGKYYRISVKReaGGKVSNYLhDHVNVGDVLELAAPAGDFFLDVasdtP 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 133 VpslCFIASGSGITAIYSLLQKAVVSSTQ-PIDLLYFTRDDAFHA---EIKTLALMYPHFKYHHF-------NTVEQHQH 201
Cdd:PRK13289  264 V---VLISGGVGITPMLSMLETLAAQQPKrPVHFIHAARNGGVHAfrdEVEALAARHPNLKAHTWyrepteqDRAGEDFD 340

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1126528355 202 ----LSLSLLQNTVEqLGERHIYACGSASMMQAAQQICQQLDL-SEQFHSEYF 249
Cdd:PRK13289  341 seglMDLEWLEAWLP-DPDADFYFCGPVPFMQFVAKQLLELGVpEERIHYEFF 392
Fdx COG0633
Ferredoxin [Energy production and conversion];
262-340 1.37e-13

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 65.64  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 262 VQFLRSQQDFQA--NSNLLDSAEAAGLRPAHGCRMGICNTCSCTKVSGSVRN-----LLTGEIDHNHntqIKLCVTQAIS 334
Cdd:COG0633     4 VTFIPEGHTVEVpaGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHreedaLSDEERAAGS---RLACQARPTS 80


                  ....*.
gi 1126528355 335 PVVINL 340
Cdd:COG0633    81 DLVVEL 86
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
37-128 1.35e-10

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 57.59  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYKIHLRPNQNFQAQRFQAGQSILVTLAMNGVRQQRSYSIVTLLD-NGDVILAIKR--QGKMSNALTRLP 113
Cdd:pfam00970   4 LVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDdKGYLELLVKVypGGKMSQYLDELK 83

                          90
                  ....*....|....*
gi 1126528355 114 AGAVVELSQPQGNFV 128
Cdd:pfam00970  84 IGDTIDFKGPLGRFE 98
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 262-338 1.80e-07

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: 48.16  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 262 VQFLRSQQDF----QANSNLLDSAEAAGLRPAHGCRMGICNTCSCTKVSGSVRNL---LTGEIDHNHNtQIKLCVTQAIS 334
Cdd:cd00207     1 VTINVPGSGVevevPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSdpsLLDEEEAEGG-YVLACQTRVTD 79


                  ....
gi 1126528355 335 PVVI 338
Cdd:cd00207    80 GLVI 83
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 262-338 3.12e-06

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 48.33  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 262 VQFLRSQQDFQANS--NLLDSAEAAGLRPAHGCRMGICNTCSCTKVSGSVRN------LLTGEiDHNHNTqIKLCVTQAI 333
Cdd:PRK07609    5 VTLQPSGRQFTAEPdeTILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQgphqasALSGE-ERAAGE-ALTCCAKPL 82


                  ....*
gi 1126528355 334 SPVVI 338
Cdd:PRK07609   83 SDLVL 87
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
275-332 4.25e-04

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 38.66  E-value: 4.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 275 SNLLDSAEAAGLRPAHGCRMGICNTCSCTKVSGSVRNLLTG-EIDHNHNTQIKL-CVTQA 332
Cdd:pfam00111  17 TTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFlEDDELAAGYVVLaCQTYP 76
 
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 ...
 16-249 3.72e-82

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: 249.45  E-value: 3.72e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  16 FIDFIAEKINPVWALKKVKACVVEIQALSPDFYKIHLRPNQNFQAqrFQAGQSILVTLAMNGVRQQRSYSI--VTLLDNG 93
Cdd:cd06216     1 FVDFYLELINPLWSARELRARVVAVRPETADMVTLTLRPNRGWPG--HRAGQHVRLGVEIDGVRHWRSYSLssSPTQEDG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  94 DVILAIKRQ--GKMSNALTR-LPAGAVVELSQPQGNFVLPAPVPS-LCFIASGSGITAIYSLLQKAVVSS-TQPIDLLYF 168
Cdd:cd06216    79 TITLTVKAQpdGLVSNWLVNhLAPGDVVELSQPQGDFVLPDPLPPrLLLIAAGSGITPVMSMLRTLLARGpTADVVLLYY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 169 TR---DDAFHAEIKTLALMYPHFKYHHFNT-VEQHQHLSLSLLQNTVEQLGERHIYACGSASMMQAAQQICQQLDLSEQF 244
Cdd:cd06216   159 ARtreDVIFADELRALAAQHPNLRLHLLYTrEELDGRLSAAHLDAVVPDLADRQVYACGPPGFLDAAEELLEAAGLADRL 238


                  ....*
gi 1126528355 245 HSEYF 249
Cdd:cd06216   239 HTERF 243
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
37-248 3.11e-51

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 169.58  E-value: 3.11e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYKIHLRPNQNFQAQRFQAGQSILVTLAMNGVRQQRSYSIVTLLDNGDVILAIKRQ--GKMSNAL-TRLP 113
Cdd:COG1018     8 VVEVRRETPDVVSFTLEPPDGAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKRVpgGGGSNWLhDHLK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 114 AGAVVELSQPQGNFVLPAPVP-SLCFIASGSGITAIYSLLQKAVVS-STQPIDLLYFTRDD---AFHAEIKTLALMYPHF 188
Cdd:COG1018    88 VGDTLEVSGPRGDFVLDPEPArPLLLIAGGIGITPFLSMLRTLLARgPFRPVTLVYGARSPadlAFRDELEALAARHPRL 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1126528355 189 KYHHFNTVEQ---HQHLSLSLLQNTVEQLGERHIYACGSASMMQAAQQICQQLDLSE-QFHSEY 248
Cdd:COG1018   168 RLHPVLSREPaglQGRLDAELLAALLPDPADAHVYLCGPPPMMEAVRAALAELGVPEeRIHFER 231
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 38-247 4.78e-33

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: 122.17  E-value: 4.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  38 VEIQALSPDFYKIHLRPNQNFqaqRFQAGQSILVTLAMNGVRQQRSYSIVTLLDNGDVI-LAIKR--QGKMSNALTRLPA 114
Cdd:cd00322     1 VATEDVTDDVRLFRLQLPNGF---SFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGELeLTVKIvpGGPFSAWLHDLKP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 115 GAVVELSQPQGNFVLPA-PVPSLCFIASGSGITAIYSLLQKAVVSSTQ-PIDLLYFTR---DDAFHAEIKTLALMYPHFK 189
Cdd:cd00322    78 GDEVEVSGPGGDFFLPLeESGPVVLIAGGIGITPFRSMLRHLAADKPGgEITLLYGARtpaDLLFLDELEELAKEGPNFR 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126528355 190 YHHFNTVEQHQH---LSLSLLQNTVEQL----GERHIYACGSASMMQAAQQICQQLDL-SEQFHSE 247
Cdd:cd00322   158 LVLALSRESEAKlgpGGRIDREAEILALlpddSGALVYICGPPAMAKAVREALVSLGVpEERIHTE 223
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 36-249 1.03e-30

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: 116.15  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  36 CVVEIQALSPDFYKIHLRPnQNFQAQRFQAGQSILVTLAMNGVRQQRSYSIV-TLLDNGDVILAIKRQ--GKMSNALTR- 111
Cdd:cd06215     2 RCVKIIQETPDVKTFRFAA-PDGSLFAYKPGQFLTLELEIDGETVYRAYTLSsSPSRPDSLSITVKRVpgGLVSNWLHDn 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 112 LPAGAVVELSQPQGNFVLP-APVPSLCFIASGSGITAIYSLLQKAVvsSTQP---IDLLYFTRDDA---FHAEIKTLALM 184
Cdd:cd06215    81 LKVGDELWASGPAGEFTLIdHPADKLLLLSAGSGITPMMSMARWLL--DTRPdadIVFIHSARSPAdiiFADELEELARR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126528355 185 YPHFKYHhfNTVEQHQH---------LSLSLLQNTVEQLGERHIYACGSASMMQAAQQICQQLDLS-EQFHSEYF 249
Cdd:cd06215   159 HPNFRLH--LILEQPAPgawggyrgrLNAELLALLVPDLKERTVFVCGPAGFMKAVKSLLAELGFPmSRFHQESF 231
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
27-251 2.06e-29

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 116.92  E-value: 2.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  27 VWALKKVKACVVEIQALSPDFYKIHLRPNQNfQAQRFQAGQSILVTL-AMNGVRQQRSYSIVTLLDNGDVI-LAIKRQGK 104
Cdd:COG4097   209 PLRSRRHPYRVESVEPEAGDVVELTLRPEGG-RWLGHRAGQFAFLRFdGSPFWEEAHPFSISSAPGGDGRLrFTIKALGD 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 105 MSNALTRLPAGAVVELSQPQGNFVLPA--PVPSLCFIASGSGITAIYSLLQ--KAVVSSTQPIDLLYFTR---DDAFHAE 177
Cdd:COG4097   288 FTRRLGRLKPGTRVYVEGPYGRFTFDRrdTAPRQVWIAGGIGITPFLALLRalAARPGDQRPVDLFYCVRdeeDAPFLEE 367

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126528355 178 IKTLALMYPHFKYHHFNTVEQHqHLSLSLLQNTVEQLGERHIYACGSASMMQAAQQICQQLDL-SEQFHSEYFQM 251
Cdd:COG4097   368 LRALAARLAGLRLHLVVSDEDG-RLTAERLRRLVPDLAEADVFFCGPPGMMDALRRDLRALGVpARRIHQERFEF 441
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 37-249 4.68e-28

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: 109.17  E-value: 4.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYKIHLRPNQNFQAQ-RFQAGQSILVTLAMNGVRQQRSYSIVTLLDNGDVILAIKR--QGKMSN-ALTRL 112
Cdd:cd06214     6 VAEVVRETADAVSITFDVPEELRDAfRYRPGQFLTLRVPIDGEEVRRSYSICSSPGDDELRITVKRvpGGRFSNwANDEL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 113 PAGAVVELSQPQGNFVLPAPVPS--LCFIASGSGITAIYSLLQKAVvsSTQP---IDLLYFTRDDA---FHAEIKTLALM 184
Cdd:cd06214    86 KAGDTLEVMPPAGRFTLPPLPGArhYVLFAAGSGITPVLSILKTAL--AREPasrVTLVYGNRTEAsviFREELADLKAR 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126528355 185 YP-HFK-YHHFNTVEQH---------QHLSLSLLQNTVEQLGERHIYACGSASMMQAAQQICQQLDL-SEQFHSEYF 249
Cdd:cd06214   164 YPdRLTvIHVLSREQGDpdllrgrldAAKLNALLKNLLDATEFDEAFLCGPEPMMDAVEAALLELGVpAERIHRELF 240
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 37-249 5.42e-28

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: 109.18  E-value: 5.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYKIHLRPNQNFQAQRFQAGQ--SILVTLAMNGVRQQRSYSIVTLLDNGDVILAIKRQ--GKMSNAL-TR 111
Cdd:cd06184    11 VARKVAESEDITSFYLEPADGGPLPPFLPGQylSVRVKLPGLGYRQIRQYSLSDAPNGDYYRISVKREpgGLVSNYLhDN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 112 LPAGAVVELSQPQGNFVLP--APVPsLCFIASGSGITAIYSLLQKAV-VSSTQPIDLLYFTRDD---AFHAEIKTLALMY 185
Cdd:cd06184    91 VKVGDVLEVSAPAGDFVLDeaSDRP-LVLISAGVGITPMLSMLEALAaEGPGRPVTFIHAARNSavhAFRDELEELAARL 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126528355 186 PHFKYHHFNTVEQHQ----------HLSLSLLQNTVeQLGERHIYACGSASMMQAAQQICQQLDLS-EQFHSEYF 249
Cdd:cd06184   170 PNLKLHVFYSEPEAGdreedydhagRIDLALLRELL-LPADADFYLCGPVPFMQAVREGLKALGVPaERIHYEVF 243
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 37-249 2.11e-26

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: 104.55  E-value: 2.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYKIHLRPNQNFQaqrFQAGQSILVTLamnGVRQQRSYSIVTLLDNGDVI-LAIKRQ--GKMSNA-LTRL 112
Cdd:cd06189     3 VESIEPLNDDVYRVRLKPPAPLD---FLAGQYLDLLL---DDGDKRPFSIASAPHEDGEIeLHIRAVpgGSFSDYvFEEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 113 PAGAVVELSQPQGNFVL-PAPVPSLCFIASGSGITAIYSLLQKAV-VSSTQPIDLLYFTRDDA---FHAEIKTLALMYPH 187
Cdd:cd06189    77 KENGLVRIEGPLGDFFLrEDSDRPLILIAGGTGFAPIKSILEHLLaQGSKRPIHLYWGARTEEdlyLDELLEAWAEAHPN 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1126528355 188 FKYH-----HFNTVEQHQHLSLSLLQNTVEQLGERHIYACGSASMMQAAQQICQQLDLS-EQFHSEYF 249
Cdd:cd06189   157 FTYVpvlsePEEGWQGRTGLVHEAVLEDFPDLSDFDVYACGSPEMVYAARDDFVEKGLPeENFFSDAF 224
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 37-256 5.02e-25

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 101.09  E-value: 5.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYKIHLRPNQnfQAQRFQAGQSILVTLAMNGVRqqRSYSIVTL-LDNGDVILAIKRQGKMSNALTRLPAG 115
Cdd:COG0543     2 VVSVERLAPDVYLLRLEAPL--IALKFKPGQFVMLRVPGDGLR--RPFSIASApREDGTIELHIRVVGKGTRALAELKPG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 116 AVVELSQPQGN-FVLPAPVPSLCFIASGSGITAIYSLLqKAVVSSTQPIDLLY-F-TRDD-AFHAEIKTLAlmypHFKYH 191
Cdd:COG0543    78 DELDVRGPLGNgFPLEDSGRPVLLVAGGTGLAPLRSLA-EALLARGRRVTLYLgArTPEDlYLLDELEALA----DFRVV 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 192 HfnTVEQ----HQHLSLSLLQNTVEQLGERHIYACGSASMMQAAQQICQQLDLS-EQFHSEYFQMTADAT 256
Cdd:COG0543   153 V--TTDDgwygRKGFVTDALKELLAEDSGDDVYACGPPPMMKAVAELLLERGVPpERIYVSLERRMACGI 220
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 37-242 1.23e-23

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: 97.25  E-value: 1.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYKIHLRPNQNFQAQRFQAGQSILVTLAMNGVRQQRSYSIVTLLDN-GDVILAIKR--QGKMSNALTRLP 113
Cdd:cd06183     3 LVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDkGYFDLLIKIypGGKMSQYLHSLK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 114 AGAVVELSQPQGNFVLPA--PVPSLCFIASGSGITAIYSLLQKAV--VSSTQPIDLLYF--TRDD-AFHAEIKTLALMYP 186
Cdd:cd06183    83 PGDTVEIRGPFGKFEYKPngKVKHIGMIAGGTGITPMLQLIRAILkdPEDKTKISLLYAnrTEEDiLLREELDELAKKHP 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126528355 187 -HFKYHHFNTVEQHQ------HLSLSLLQNTVEQL--GERHIYACGSASMMQ-AAQQICQQLDLSE 242
Cdd:cd06183   163 dRFKVHYVLSRPPEGwkggvgFITKEMIKEHLPPPpsEDTLVLVCGPPPMIEgAVKGLLKELGYKK 228
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 37-249 5.05e-21

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: 89.89  E-value: 5.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYKIHLRPNQNFQaQRFQAGQSILVTLAMNGVRQQRSYSIVTLLDNGDVILAIKR--QGKMSNALTR-LP 113
Cdd:cd06191     3 VAEVRSETPDAVTIVFAVPGPLQ-YGFRPGQHVTLKLDFDGEELRRCYSLCSSPAPDEISITVKRvpGGRVSNYLREhIQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 114 AGAVVELSQPQGNFVL-PAPVPSLCFIASGSGITAIYSLLQ-KAVVSSTQPIDLLYFTRDDA---FHAEIKTLALMYPHF 188
Cdd:cd06191    82 PGMTVEVMGPQGHFVYqPQPPGRYLLVAAGSGITPLMAMIRaTLQTAPESDFTLIHSARTPAdmiFAQELRELADKPQRL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 189 KYHHFNTVEQHQH--------LSLSLLQNTVEQLGERHIYACGSASMMQAAQQICQQLDL-SEQFHSEYF 249
Cdd:cd06191   162 RLLCIFTRETLDSdllhgridGEQSLGAALIPDRLEREAFICGPAGMMDAVETALKELGMpPERIHTERF 231
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 63-249 2.08e-20

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: 88.48  E-value: 2.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  63 FQAGQSILVTL-AMNGVRQQRSYSIV-TLLDNGDVILAIKR--QGKMSNALTR-LPAGAVVELSQPQGNFVL-PAPVPSL 136
Cdd:cd06217    31 FLAGQHVDLRLtAIDGYTAQRSYSIAsSPTQRGRVELTVKRvpGGEVSPYLHDeVKVGDLLEVRGPIGTFTWnPLHGDPV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 137 CFIASGSGITAIYSLL-QKAVVSSTQPIDLLYFTRDDA---FHAEIKTLALMYPHFKYHHFNTVEQHQH-------LSLS 205
Cdd:cd06217   111 VLLAGGSGIVPLMSMIrYRRDLGWPVPFRLLYSARTAEdviFRDELEQLARRHPNLHVTEALTRAAPADwlgpagrITAD 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1126528355 206 LLQNTVEQLGERHIYACGSASMMQAAQQICQQLDLS-EQFHSEYF 249
Cdd:cd06217   191 LIAELVPPLAGRRVYVCGPPAFVEAATRLLLELGVPrDRIRTEAF 235
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 37-249 6.91e-19

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: 83.80  E-value: 6.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYKIHLRPNQnfqAQRFQAGQSilVTLAMNGVRQQ-RSYSIVTLLDNGDVI-LAIKR--QGKMSNAL-TR 111
Cdd:cd06187     1 VVSVERLTHDIAVVRLQLDQ---PLPFWAGQY--VNVTVPGRPRTwRAYSPANPPNEDGEIeFHVRAvpGGRVSNALhDE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 112 LPAGAVVELSQPQGNFVLPAPV--PSLCfIASGSGITAIYSLLQKAVVSSTQPIDLLYF---TRDDAF-HAEIKTLALMY 185
Cdd:cd06187    76 LKVGDRVRLSGPYGTFYLRRDHdrPVLC-IAGGTGLAPLRAIVEDALRRGEPRPVHLFFgarTERDLYdLEGLLALAARH 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126528355 186 PHFKYHhfNTVEQ---HQHLSLSLLQNTVEQLG----ERHIYACGSASMMQAAQQICQQLDLS-EQFHSEYF 249
Cdd:cd06187   155 PWLRVV--PVVSHeegAWTGRRGLVTDVVGRDGpdwaDHDIYICGPPAMVDATVDALLARGAPpERIHFDKF 224
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 38-250 8.35e-19

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: 83.30  E-value: 8.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  38 VEIQALSPDFYKIHLRPNQNFQAQRFQAGQSILVTLAmNGVRqqRSYSIVTLLDNGD--VIlAIKRQ-----GkmSNAL- 109
Cdd:cd06185     1 VRIRDEAPDIRSFELEAPDGAPLPAFEPGAHIDVHLP-NGLV--RQYSLCGDPADRDryRI-AVLREpasrgG--SRYMh 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 110 TRLPAGAVVELSQPQGNFVLPAPVPSLCFIASGSGITAIYSLLQkAVVSSTQPIDLLYFTR---DDAFHAEIKTLAlmYP 186
Cdd:cd06185    75 ELLRVGDELEVSAPRNLFPLDEAARRHLLIAGGIGITPILSMAR-ALAARGADFELHYAGRsreDAAFLDELAALP--GD 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126528355 187 HFKYHHfntVEQHQHLSLS-LLQNtveQLGERHIYACGSASMMQAAQQICQQLDL-SEQFHSEYFQ 250
Cdd:cd06185   152 RVHLHF---DDEGGRLDLAaLLAA---PPAGTHVYVCGPEGMMDAVRAAAAALGWpEARLHFERFA 211
PRK13289 PRK13289
NO-inducible flavohemoprotein;
62-249 2.92e-18

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 84.85  E-value: 2.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  62 RFQAGQ--SILVTLAMNGVRQQRSYSIVTLLDNGDVILAIKR--QGKMSNAL-TRLPAGAVVELSQPQGNFVLPA----P 132
Cdd:PRK13289  184 DFKPGQylGVRLDPEGEEYQEIRQYSLSDAPNGKYYRISVKReaGGKVSNYLhDHVNVGDVLELAAPAGDFFLDVasdtP 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 133 VpslCFIASGSGITAIYSLLQKAVVSSTQ-PIDLLYFTRDDAFHA---EIKTLALMYPHFKYHHF-------NTVEQHQH 201
Cdd:PRK13289  264 V---VLISGGVGITPMLSMLETLAAQQPKrPVHFIHAARNGGVHAfrdEVEALAARHPNLKAHTWyrepteqDRAGEDFD 340

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1126528355 202 ----LSLSLLQNTVEqLGERHIYACGSASMMQAAQQICQQLDL-SEQFHSEYF 249
Cdd:PRK13289  341 seglMDLEWLEAWLP-DPDADFYFCGPVPFMQFVAKQLLELGVpEERIHYEFF 392
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 50-249 1.70e-16

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: 76.91  E-value: 1.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  50 IHLRPNQNfqAQRFQAGQSILVTLAMNGVRQQRSYSIVTL-LDNGDVILAIKRQGKMSNAL-TRLPAGAVVELSQPQGNF 127
Cdd:cd06198    12 LTLEPRGP--ALGHRAGQFAFLRFDASGWEEPHPFTISSApDPDGRLRFTIKALGDYTRRLaERLKPGTRVTVEGPYGRF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 128 VLPAPVPSLCFIASGSGITAIYSLLQKAVVSSTQ-PIDLLYFTR---DDAFHAEIKTLA-LMYPHFkyhHFNTVEQHQHL 202
Cdd:cd06198    90 TFDDRRARQIWIAGGIGITPFLALLEALAARGDArPVTLFYCVRdpeDAVFLDELRALAaAAGVVL---HVIDSPSDGRL 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1126528355 203 SLSLLQNT-VEQLGERHIYACGSASMMQA-AQQICQQLDLSEQFHSEYF 249
Cdd:cd06198   167 TLEQLVRAlVPDLADADVWFCGPPGMADAlEKGLRALGVPARRFHYERF 215
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 37-307 5.02e-15

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 74.75  E-value: 5.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYkihlrpnqnfqaqRFQAGQSILVTLAmNGVRQQRSYSI---------VTL----LDNGdvilaikrQG 103
Cdd:PRK10684   24 VWTISLICHDFY-------------PYRAGQYALVSIR-NSAETLRAYTLsstpgvsefITLtvrrIDDG--------VG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 104 kmSNALTR-LPAGAVVELSQPQGNFVLP-APVPSLCFIASGSGITAIYSLLQKAVVSSTQP-IDLLYFTRDDA---FHAE 177
Cdd:PRK10684   82 --SQWLTRdVKRGDYLWLSDAMGEFTCDdKAEDKYLLLAAGCGVTPIMSMRRWLLKNRPQAdVQVIFNVRTPQdviFADE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 178 IKTLALMYPhfkYHHFNTVEQHQ--------HLSLSLLQNTVEQLGERHIYACGSASMMQAAQQICQQLDLSEQ-FHSEY 248
Cdd:PRK10684  160 WRQLKQRYP---QLNLTLVAENNategfiagRLTRELLQQAVPDLASRTVMTCGPAPYMDWVEQEVKALGVTADrFFKEK 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1126528355 249 FQMTADATlEAQPVQFLRSQ--QDFQA--NSNLLDSAEAAGLRPAHGCRMGICNTCSCTKVSG 307
Cdd:PRK10684  237 FFTPVAEA-ATSGLTFTKLQpaREFYApvGTTLLEALESNKVPVVAACRAGVCGCCKTKVVSG 298
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 32-249 2.65e-14

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: 71.09  E-value: 2.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  32 KVKACVVEIQALSPDFYKIHLRPNqNFQAQRFQAGQSILVTLAmnGVRQQRSYSIVTLLDNGDVILAIKR--QGKMSNAL 109
Cdd:cd06209     1 TFEATVTEVERLSDSTIGLTLELD-EAGALAFLPGQYVNLQVP--GTDETRSYSFSSAPGDPRLEFLIRLlpGGAMSSYL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 110 TRLPA-GAVVELSQPQGNFVLPAPVPSLCFIASGSGITAIYSLLQK-AVVSSTQPIDLLY-FTRD-DAFHAE-IKTLALM 184
Cdd:cd06209    78 RDRAQpGDRLTLTGPLGSFYLREVKRPLLMLAGGTGLAPFLSMLDVlAEDGSAHPVHLVYgVTRDaDLVELDrLEALAER 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1126528355 185 YPHFKYHhfnTVEQHQHlSLSLLQNTVEQL--------GERHIYACGSASMMQAAQQICQQLDLS-EQFHSEYF 249
Cdd:cd06209   158 LPGFSFR---TVVADPD-SWHPRKGYVTDHleaedlndGDVDVYLCGPPPMVDAVRSWLDEQGIEpANFYYEKF 227
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 37-234 2.94e-14

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: 70.76  E-value: 2.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYKIHLRPNQNFqaqRFQAGQSILVTLAmNGVrqQRSYSIVTLLDNGDVI-LAIKRQ--GKMSNALTRLP 113
Cdd:cd06194     1 VVSLQRLSPDVLRVRLEPDRPL---PYLPGQYVNLRRA-GGL--ARSYSPTSLPDGDNELeFHIRRKpnGAFSGWLGEEA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 114 A-GAVVELSQPQGN-FVLPAPVPS-LCFIASGSGITAIYSLLQKAVVSSTQ-PIDLLYFTRDDA---FHAEIKTLALMYP 186
Cdd:cd06194    75 RpGHALRLQGPFGQaFYRPEYGEGpLLLVGAGTGLAPLWGIARAALRQGHQgEIRLVHGARDPDdlyLHPALLWLAREHP 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1126528355 187 HFKYhhFNTVEQHQHLSLSLlqNTVEQLGERH-------IYACGSASMMQAAQQI 234
Cdd:cd06194   155 NFRY--IPCVSEGSQGDPRV--RAGRIAAHLPpltrddvVYLCGAPSMVNAVRRR 205
Fdx COG0633
Ferredoxin [Energy production and conversion];
262-340 1.37e-13

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 65.64  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 262 VQFLRSQQDFQA--NSNLLDSAEAAGLRPAHGCRMGICNTCSCTKVSGSVRN-----LLTGEIDHNHntqIKLCVTQAIS 334
Cdd:COG0633     4 VTFIPEGHTVEVpaGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHreedaLSDEERAAGS---RLACQARPTS 80


                  ....*.
gi 1126528355 335 PVVINL 340
Cdd:COG0633    81 DLVVEL 86
fre PRK08051
FMN reductase; Validated
 36-255 1.23e-12

FMN reductase; Validated


Pssm-ID: 236142 [Multi-domain]  Cd Length: 232  Bit Score: 66.42  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  36 CVVE-IQALSPDFYKIHLRPNQNFQaqrFQAGQSILVTLamnGVRQQRSYSIVTLLDNGDVI-LAIkrqgkmSNALTRLP 113
Cdd:PRK08051    5 CKVTsVEAITDTVYRVRLVPEAPFS---FRAGQYLMVVM---GEKDKRPFSIASTPREKGFIeLHI------GASELNLY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 114 AGAVVELSQPQGNFVLPAP----------VPSLCFIASGSGITAIYSLLQKAV-VSSTQPIDLLYFTRDDAF---HAEIK 179
Cdd:PRK08051   73 AMAVMERILKDGEIEVDIPhgdawlreesERPLLLIAGGTGFSYARSILLTALaQGPNRPITLYWGGREEDHlydLDELE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 180 TLALMYPHFKYHhfNTVEQ-------HQHLSLSLLQNTVEQLGERHIYACGSASMMQAA-QQICQQLDLSEQfhseyfQM 251
Cdd:PRK08051  153 ALALKHPNLHFV--PVVEQpeegwqgKTGTVLTAVMQDFGSLAEYDIYIAGRFEMAKIArELFCRERGAREE------HL 224


                  ....
gi 1126528355 252 TADA 255
Cdd:PRK08051  225 FGDA 228
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 30-249 1.49e-12

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: 66.19  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  30 LKKVKACVVEIQALSPDFYKIHLRPNQNFQAqRFQAGQSILVTLAmnGVRQQRSYSIVTLLDNGDVILAIKRQGKMSNAL 109
Cdd:cd06211     4 VKDFEGTVVEIEDLTPTIKGVRLKLDEPEEI-EFQAGQYVNLQAP--GYEGTRAFSIASSPSDAGEIELHIRLVPGGIAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 110 T----RLPAGAVVELSQPQGNFVL--PAPVPsLCFIASGSGITAIYSLLQKAVVSS-TQPIDLLY--FTRDDAF-HAEIK 179
Cdd:cd06211    81 TyvhkQLKEGDELEISGPYGDFFVrdSDQRP-IIFIAGGSGLSSPRSMILDLLERGdTRKITLFFgaRTRAELYyLDEFE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1126528355 180 TLALMYPHFKYHHFNTVEQHQ--------HLSLSLLQNTVEQLGERHIYACGSASMMQAAQQICQQLDLSEQ-FHSEYF 249
Cdd:cd06211   160 ALEKDHPNFKYVPALSREPPEsnwkgftgFVHDAAKKHFKNDFRGHKAYLCGPPPMIDACIKTLMQGRLFERdIYYEKF 238
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 37-247 2.51e-12

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: 65.66  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYKIHLRPNQNFqaqRFQAGQSIlvTLAM---NGVRQQRSYSIVTLLDNGDV-ILAIK-RQGKMSNALTR 111
Cdd:cd06195     2 VLKRRDWTDDLFSFRVTRDIPF---RFQAGQFT--KLGLpndDGKLVRRAYSIASAPYEENLeFYIILvPDGPLTPRLFK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 112 LPAGAVVELS-QPQGNFVLpAPVPS---LCFIASGSGITAIYSLLQK-AVVSSTQPIDLLYFTR---DDAFHAEIKTLAL 183
Cdd:cd06195    77 LKPGDTIYVGkKPTGFLTL-DEVPPgkrLWLLATGTGIAPFLSMLRDlEIWERFDKIVLVHGVRyaeELAYQDEIEALAK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 184 MYPH-FKYHHFNTVEQH---------QHLSLSLLQNTVEQ--LGER-HIYACGSASMMQAAQQICQQLDLSE-------Q 243
Cdd:cd06195   156 QYNGkFRYVPIVSREKEngaltgripDLIESGELEEHAGLplDPETsHVMLCGNPQMIDDTQELLKEKGFSKnhrrkpgN 235


                  ....
gi 1126528355 244 FHSE 247
Cdd:cd06195   236 ITVE 239
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 37-249 2.60e-11

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: 62.73  E-value: 2.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYKIHLRPNQNfQAQRFQAGQSILVTLAmnGVRQQRSYSIVTL-LDNGDVILAIKR--QGKMSNAL-TRL 112
Cdd:cd06212     5 VVAVEALTHDIRRLRLRLEEP-EPIKFFAGQYVDITVP--GTEETRSFSMANTpADPGRLEFIIKKypGGLFSSFLdDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 113 PAGAVVELSQPQGNFVLPAPVPS-LCFIASGSGITAIYSLLQKAVVSSTQ-PIDLLY--FTRDDAFHA-EIKTLALMYPH 187
Cdd:cd06212    82 AVGDPVTVTGPYGTCTLRESRDRpIVLIGGGSGMAPLLSLLRDMAASGSDrPVRFFYgaRTARDLFYLeEIAALGEKIPD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126528355 188 FKY---------HHFNTVEqhQHLSLSLLQNTVEQLGERHIYACGSASMMQAAQQICQQLDL-SEQFHSEYF 249
Cdd:cd06212   162 FTFipalsespdDEGWSGE--TGLVTEVVQRNEATLAGCDVYLCGPPPMIDAALPVLEMSGVpPDQIFYDKF 231
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
37-128 1.35e-10

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 57.59  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYKIHLRPNQNFQAQRFQAGQSILVTLAMNGVRQQRSYSIVTLLD-NGDVILAIKR--QGKMSNALTRLP 113
Cdd:pfam00970   4 LVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDdKGYLELLVKVypGGKMSQYLDELK 83

                          90
                  ....*....|....*
gi 1126528355 114 AGAVVELSQPQGNFV 128
Cdd:pfam00970  84 IGDTIDFKGPLGRFE 98
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 62-232 3.65e-10

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: 59.19  E-value: 3.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  62 RFQAGQSILVTLAmnGVRQQRSYSIVTLLDNGDVI-LAIKR--QGKMSNAL-TRLPAGAVVELSQPQGNFVL--PAPVPS 135
Cdd:cd06190    23 DFLPGQYALLALP--GVEGARAYSMANLANASGEWeFIIKRkpGGAASNALfDNLEPGDELELDGPYGLAYLrpDEDRDI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 136 LCfIASGSGITAIYSLLQKAVVS---STQPIDLLYFTR---DDAFHAEIKTLALMYPHFKYH--------------HFNT 195
Cdd:cd06190   101 VC-IAGGSGLAPMLSILRGAARSpylSDRPVDLFYGGRtpsDLCALDELSALVALGARLRVTpavsdagsgsaagwDGPT 179

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1126528355 196 VEQHQHLSlsllQNTVEQLGERHIYACGSASMMQAAQ 232
Cdd:cd06190   180 GFVHEVVE----ATLGDRLAEFEFYFAGPPPMVDAVQ 212
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 138-233 8.69e-10

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


Pssm-ID: 425503 [Multi-domain]  Cd Length: 109  Bit Score: 55.34  E-value: 8.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 138 FIASGSGITAIYSLLQKAV--VSSTQPIDLLYFTR---DDAFHAEIKTLALMYPHfKYHHFNTVEQHQ--------HLSL 204
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILedPKDPTQVVLVFGNRnedDILYREELDELAEKHPG-RLTVVYVVSRPEagwtggkgRVQD 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1126528355 205 SLLQNTVE-QLGERHIYACGSASMMQAAQQ 233
Cdd:pfam00175  80 ALLEDHLSlPDEETHVYVCGPPGMIKAVRK 109
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 31-254 8.54e-09

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 56.03  E-value: 8.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  31 KKVKACVVEIQALSPDFYKIHLR--PNQNFQaqrFQAGQSILVTLAmNGVRqqRSYSIVTL-LDNGDVILAIKRQ--GKM 105
Cdd:PRK07609  101 KKLPCRVASLERVAGDVMRLKLRlpATERLQ---YLAGQYIEFILK-DGKR--RSYSIANApHSGGPLELHIRHMpgGVF 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 106 SNAL-TRLPAGAVVELSQPQGNFVLpAPVPS--LCFIASGSGITAIYSLLQKAVVSSTQ-PIDLLYFTRDdafHAEIKTL 181
Cdd:PRK07609  175 TDHVfGALKERDILRIEGPLGTFFL-REDSDkpIVLLASGTGFAPIKSIVEHLRAKGIQrPVTLYWGARR---PEDLYLS 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 182 ALM------YPHFKYH-------------------HFNTVEQHQHLSLSllqntveqlgerHIYACGSASMMQAAQQICQ 236
Cdd:PRK07609  251 ALAeqwaeeLPNFRYVpvvsdaldddawtgrtgfvHQAVLEDFPDLSGH------------QVYACGSPVMVYAARDDFV 318

                         250
                  ....*....|....*....
gi 1126528355 237 QLDL-SEQFHSEYFQMTAD 254
Cdd:PRK07609  319 AAGLpAEEFFADAFTYAAD 337
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 82-230 1.13e-08

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: 55.39  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  82 RSYSIVTLLDNGDVILAIKRQ------------GKMSNALTRLPAGAVVELSQPQGNFVLPAPVPSLCFIASGSGI---- 145
Cdd:cd06188    87 RAYSLANYPAEEGELKLNVRIatpppgnsdippGIGSSYIFNLKPGDKVTASGPFGEFFIKDTDREMVFIGGGAGMaplr 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 146 TAIYSLLQKavVSSTQPIDLLYFTR---DDAFHAEIKTLALMYPHFKYhhfntveqhqHLSLS-------------LLQN 209
Cdd:cd06188   167 SHIFHLLKT--LKSKRKISFWYGARslkELFYQEEFEALEKEFPNFKY----------HPVLSepqpednwdgytgFIHQ 234

                         170       180
                  ....*....|....*....|....*....
gi 1126528355 210 TV-EQLGERH-------IYACGSASMMQA 230
Cdd:cd06188   235 VLlENYLKKHpapedieFYLCGPPPMNSA 263
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 33-170 3.41e-08

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: 53.47  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  33 VKACVVEIQALSPDFYKIHLrpnQNFQAQRFQAGQSILVTLAmnGVRQQRSYSIVTlldngdvilAIKRQGKMSNALTRL 112
Cdd:cd06213     1 IRGTIVAQERLTHDIVRLTV---QLDRPIAYKAGQYAELTLP--GLPAARSYSFAN---------APQGDGQLSFHIRKV 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1126528355 113 PAGAV-------------VELSQPQGNFVL-PAPVPSLCfIASGSGITAIYSLLQKAVVS-STQPIDLLYFTR 170
Cdd:cd06213    67 PGGAFsgwlfgadrtgerLTVRGPFGDFWLrPGDAPILC-IAGGSGLAPILAILEQARAAgTKRDVTLLFGAR 138
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
32-249 4.19e-08

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 53.98  E-value: 4.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  32 KVKACVVEIQALSPDFYKIHLRPNQNFQAQRFQAGQsiLVTLAMNGVRQQRSYSIVTLLDNGDVILAIKR---QGKMSNA 108
Cdd:PRK11872  106 KISGVVTAVELVSETTAILHLDASAHGRQLDFLPGQ--YARLQIPGTDDWRSYSFANRPNATNQLQFLIRllpDGVMSNY 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 109 L-TRLPAGAVVELSQPQGNFVLPAPVPSLCFIASGSGITAIYSLLQKAVVSS-TQPIDLLYFTRDDAFHAEIKTL---AL 183
Cdd:PRK11872  184 LrERCQVGDEILFEAPLGAFYLREVERPLVFVAGGTGLSAFLGMLDELAEQGcSPPVHLYYGVRHAADLCELQRLaayAE 263

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126528355 184 MYPHFKYHHF--NTVEQ--------HQHLSLSLLQNTVEQLgerhiYACGSASMMQAAQQICQQLDLSE-QFHSEYF 249
Cdd:PRK11872  264 RLPNFRYHPVvsKASADwqgkrgyiHEHFDKAQLRDQAFDM-----YLCGPPPMVEAVKQWLDEQALENyRLYYEKF 335
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 37-243 1.11e-07

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: 52.22  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALSPDFYKIHLRP-NQNFQAQRFQAGQSILVTLAMNGvrqQRSYSIVTLLDNGDVI-LAIKRQGKMSNALTRLPA 114
Cdd:cd06221     1 IVEVVDETEDIKTFTLRLeDDDEELFTFKPGQFVMLSLPGVG---EAPISISSDPTRRGPLeLTIRRVGRVTEALHELKP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 115 GAVVELSQPQGNfvlPAPVPS-----LCFIASGSGITAIYSLLQKAVvssTQP-----IDLLYFTR---DDAFHAEIKTL 181
Cdd:cd06221    78 GDTVGLRGPFGN---GFPVEEmkgkdLLLVAGGLGLAPLRSLINYIL---DNRedygkVTLLYGARtpeDLLFKEELKEW 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126528355 182 AlMYPHFKYHhfNTVEQ-------HQHLSLSLL-------QNTVeqlgerhIYACGSASMMQAAQQICQQLDLSEQ 243
Cdd:cd06221   152 A-KRSDVEVI--LTVDRaeegwtgNVGLVTDLLpeltldpDNTV-------AIVCGPPIMMRFVAKELLKLGVPEE 217
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 262-338 1.80e-07

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: 48.16  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 262 VQFLRSQQDF----QANSNLLDSAEAAGLRPAHGCRMGICNTCSCTKVSGSVRNL---LTGEIDHNHNtQIKLCVTQAIS 334
Cdd:cd00207     1 VTINVPGSGVevevPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSdpsLLDEEEAEGG-YVLACQTRVTD 79


                  ....
gi 1126528355 335 PVVI 338
Cdd:cd00207    80 GLVI 83
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 37-249 1.21e-06

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: 48.45  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  37 VVEIQALS-PDFYKIHLRPNQNFqaqRFQAGQSILVT-LAMNGVRQQRSYSIVTLLDNGD---VILAIKRQGKMSNALTR 111
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPKPF---KWKPGQHVYLNfPSLLSFWQSHPFTIASSPEDEQdtlSLIIRAKKGFTTRLLRK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 112 LpagavveLSQPQGNFVLPAPV--P------------SLCFIASGSGITAIYSLLQKAV-----VSSTQPIDLLYFTRDd 172
Cdd:cd06186    78 A-------LKSPGGGVSLKVLVegPygsssedllsydNVLLVAGGSGITFVLPILRDLLrrsskTSRTRRVKLVWVVRD- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 173 afhaeiktlalmyphfkYHHFNTVEQHqhlsLSLLQNtVEQLGERHIY-----ACGSASMMQAAQQICQQLDLSEQ-FHS 246
Cdd:cd06186   150 -----------------REDLEWFLDE----LRAAQE-LEVDGEIEIYvtrvvVCGPPGLVDDVRNAVAKKGGTGVeFHE 207


                  ...
gi 1126528355 247 EYF 249
Cdd:cd06186   208 ESF 210
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 262-338 3.12e-06

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 48.33  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 262 VQFLRSQQDFQANS--NLLDSAEAAGLRPAHGCRMGICNTCSCTKVSGSVRN------LLTGEiDHNHNTqIKLCVTQAI 333
Cdd:PRK07609    5 VTLQPSGRQFTAEPdeTILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQgphqasALSGE-ERAAGE-ALTCCAKPL 82


                  ....*
gi 1126528355 334 SPVVI 338
Cdd:PRK07609   83 SDLVL 87
PRK10926 PRK10926
ferredoxin-NADP reductase; Provisional
 63-153 3.57e-06

ferredoxin-NADP reductase; Provisional


Pssm-ID: 182844  Cd Length: 248  Bit Score: 47.39  E-value: 3.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  63 FQAGQSILVTLAMNGVRQQRSYSIVTLLDNGDV--ILAIKRQGKMSNALTRL-PAGAVVELSQPQGNFVLPApVP---SL 136
Cdd:PRK10926   31 FTAGQFTKLGLEIDGERVQRAYSYVNAPDNPDLefYLVTVPEGKLSPRLAALkPGDEVQVVSEAAGFFVLDE-VPdceTL 109

                          90
                  ....*....|....*..
gi 1126528355 137 CFIASGSGITAIYSLLQ 153
Cdd:PRK10926  110 WMLATGTAIGPYLSILQ 126
SiR_like1 cd06200
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 48-177 3.15e-05

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: 99797  Cd Length: 245  Bit Score: 44.58  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  48 YKIHLRPNQnfQAQRFQAGQsilvtLAMNGVRQQ---RSYSIVTLLDNGDVILAIKRQ-------GKMSNALTR-LPAGA 116
Cdd:cd06200    19 WRLRLTPPD--AGAQWQAGD-----IAEIGPRHPlphREYSIASLPADGALELLVRQVrhadgglGLGSGWLTRhAPIGA 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126528355 117 VVELS-QPQGNFVLPAPVPSLCFIASGSGITAIYSLLQKAVVSSTQPIDLLYFTRD---DAFHAE 177
Cdd:cd06200    92 SVALRlRENPGFHLPDDGRPLILIGNGTGLAGLRSHLRARARAGRHRNWLLFGERQaahDFFCRE 156
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 31-244 6.40e-05

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 43.71  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  31 KKVKACVVEIQALSPDFYKIHLRPNQNFQaqrFQAGQSILVTLAMNGVRQQRSYSIvTLLDNGDVILAIKRQGKMSNALT 110
Cdd:PRK00054    3 KPENMKIVENKEIAPNIYTLVLDGEKVFD---MKPGQFVMVWVPGVEPLLERPISI-SDIDKNEITILYRKVGEGTKKLS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 111 RLPAGAVVELSQPQGN-FVLPAPVPSLCFIASGSGITAIYSLLQKAVVSSTQPIDLLYF-TRDD-AFHAEIKTLALMYP- 186
Cdd:PRK00054   79 KLKEGDELDIRGPLGNgFDLEEIGGKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGArTKDEvIFEEEFAKVGDVYVt 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1126528355 187 ----HFKYHHFNTveqhqhlslsllqNTVEQLGERH--IYACGSASMMQAAQQICQQLDLSEQF 244
Cdd:PRK00054  159 tddgSYGFKGFVT-------------DVLDELDSEYdaIYSCGPEIMMKKVVEILKEKKVPAYV 209
PTZ00038 PTZ00038
ferredoxin; Provisional
 277-338 1.02e-04

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 42.52  E-value: 1.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126528355 277 LLDSAEAAGLRPAHGCRMGICNTCSCTKVSGSVRNLLTGEIDhnhNTQIK-----LCVTQAISPVVI 338
Cdd:PTZ00038  117 ILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLD---DEQLKkgyclLCTCYPKSDCTI 180
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
275-332 4.25e-04

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 38.66  E-value: 4.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 275 SNLLDSAEAAGLRPAHGCRMGICNTCSCTKVSGSVRNLLTG-EIDHNHNTQIKL-CVTQA 332
Cdd:pfam00111  17 TTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFlEDDELAAGYVVLaCQTYP 76
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 39-242 5.33e-04

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


Pssm-ID: 99793 [Multi-domain]  Cd Length: 218  Bit Score: 40.69  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  39 EIQALSPDFYKIHL-RPnqnfQAQRFQAGQSILVTLAMNGVRQQ-RSYSIVTLLDNGDVILAIKR---QGKMSNALTRLP 113
Cdd:cd06196     7 SIEPVTHDVKRLRFdKP----EGYDFTPGQATEVAIDKPGWRDEkRPFTFTSLPEDDVLEFVIKSypdHDGVTEQLGRLQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 114 AGAVVELSQPQGNFVLPAP-VpslcFIASGSGIT---AIYSLLQKA--------VVSSTQPIDLLYftrDDAFhAEIKTL 181
Cdd:cd06196    83 PGDTLLIEDPWGAIEYKGPgV----FIAGGAGITpfiAILRDLAAKgklegntlIFANKTEKDIIL---KDEL-EKMLGL 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126528355 182 ALMY-----PHFKYHhfntveqHQHLSLSLLQNTVEQLGErHIYACGSASMMQAAQQICQQLDLSE 242
Cdd:cd06196   155 KFINvvtdeKDPGYA-------HGRIDKAFLKQHVTDFNQ-HFYVCGPPPMEEAINGALKELGVPE 212
PLN03136 PLN03136
Ferredoxin; Provisional
 250-338 7.02e-04

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 39.35  E-value: 7.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 250 QMTADATLEaqpVQFLRSQQDFQANSN----LLDSAEAAGLRPAHGCRMGICNTCSCTKVSGSVRNLLTGEIDHNHNTQ- 324
Cdd:PLN03136   48 RVTAMATYK---VKFITPEGEQEVECEedvyVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDEQISEg 124

                          90
                  ....*....|....*
gi 1126528355 325 -IKLCVTQAISPVVI 338
Cdd:PLN03136  125 yVLTCVAYPTSDVVI 139
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 66-234 2.07e-03

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: 39.23  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  66 GQSILV----TLAMNGVRQQ-RSYSIVT--LLDNGD---VILAIKR------------QGKMSNALTRLPAGAVVELSQP 123
Cdd:cd06208    44 GQSIGIippgTDAKNGKPHKlRLYSIASsrYGDDGDgktLSLCVKRlvytdpetdetkKGVCSNYLCDLKPGDDVQITGP 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355 124 QGNFVLP--APVPSLCFIASGSGITAIYSLLQKAVVSST-----QPIDLLYF--TRDDA--FHAEIKTLALMYPHFKYHH 192
Cdd:cd06208   124 VGKTMLLpeDPNATLIMIATGTGIAPFRSFLRRLFREKHadykfTGLAWLFFgvPNSDSllYDDELEKYPKQYPDNFRID 203

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1126528355 193 F-----------------NTVEQHQHLSLSLLQNtveqlGERHIYACGSASMMQAAQQI 234
Cdd:cd06208   204 YafsreqknadggkmyvqDRIAEYAEEIWNLLDK-----DNTHVYICGLKGMEPGVDDA 257
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 92-172 2.40e-03

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: 38.91  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126528355  92 NGDVILAIKRQGKMSNAL-----TRLPAGAVVELSQPQGNFVLPAPVPS----LCFIASGSGITAIYSLLqKAVVSS--- 159
Cdd:cd06197    75 TDEFEITVRKKGPVTGFLfqvarRLREQGLEVPVLGVGGEFTLSLPGEGaerkMVWIAGGVGITPFLAML-RAILSSrnt 153

                          90
                  ....*....|...
gi 1126528355 160 TQPIDLLYFTRDD 172
Cdd:cd06197   154 TWDITLLWSLRED 166
petF CHL00134
ferredoxin; Validated
 277-309 2.61e-03

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 36.62  E-value: 2.61e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1126528355 277 LLDSAEAAGLRPAHGCRMGICNTCSCTKVSGSV 309
Cdd:CHL00134   27 ILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTV 59
 
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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