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Conserved domains on  [gi|15599527|ref|NP_253021|]
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hypothetical protein PA4331 [Pseudomonas aeruginosa PAO1]

Protein Classification

iron-sulfur-binding ferredoxin reductase( domain architecture ID 11481534)

iron-sulfur binding ferredoxin reductase (FNR) protein combines the FAD and NAD(P) binding regions of FNR with an N-terminal Iron-Sulfur binding cluster domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
1-308 0e+00

iron-sulfur-binding ferredoxin reductase;


:

Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 516.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527    1 MPDIRVGERRLAVAAGSNLLDALLAGGIAVPHSCRAGSCHACLVHCLQGEVDDTLPEALDPVRREAGWRLACQCRVLGDL 80
Cdd:PRK05713   1 MPELRVGERRWSVPAGSNLLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEDALPEALAAEKREQGWRLACQCRVVGDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   81 VLQPFDPERDGLPARVVACHWL-GDVLRLRLEPERPLRYRAGQHLLLWSDDGVARPYSLASLPHEDPWLEFHIDCSAPGA 159
Cdd:PRK05713  81 RVEVFDPQRDGLPARVVALDWLgGDVLRLRLEPERPLRYRAGQHLVLWTAGGVARPYSLASLPGEDPFLEFHIDCSRPGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  160 FCDRARRLAPGALLRLGELRGGALRYEPDWQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLARD---HYLASE 236
Cdd:PRK05713 161 FCDAARQLQVGDLLRLGELRGGALHYDPDWQERPLWLLAAGTGLAPLWGILREALRQGHQGPIRLLHLARDsagHYLAEP 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599527  237 LAELAGRHPQLRVNLVSAAQLPSALADLRLVPRRSMALLCGQPASVERFARHLYLAGVPRSQTLADLFLPHA 308
Cdd:PRK05713 241 LAALAGRHPQLSVELVTAAQLPAALAELRLVSRQTMALLCGSPASVERFARRLYLAGLPRNQLLADVFLPHA 312
 
Name Accession Description Interval E-value
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
1-308 0e+00

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 516.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527    1 MPDIRVGERRLAVAAGSNLLDALLAGGIAVPHSCRAGSCHACLVHCLQGEVDDTLPEALDPVRREAGWRLACQCRVLGDL 80
Cdd:PRK05713   1 MPELRVGERRWSVPAGSNLLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEDALPEALAAEKREQGWRLACQCRVVGDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   81 VLQPFDPERDGLPARVVACHWL-GDVLRLRLEPERPLRYRAGQHLLLWSDDGVARPYSLASLPHEDPWLEFHIDCSAPGA 159
Cdd:PRK05713  81 RVEVFDPQRDGLPARVVALDWLgGDVLRLRLEPERPLRYRAGQHLVLWTAGGVARPYSLASLPGEDPFLEFHIDCSRPGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  160 FCDRARRLAPGALLRLGELRGGALRYEPDWQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLARD---HYLASE 236
Cdd:PRK05713 161 FCDAARQLQVGDLLRLGELRGGALHYDPDWQERPLWLLAAGTGLAPLWGILREALRQGHQGPIRLLHLARDsagHYLAEP 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599527  237 LAELAGRHPQLRVNLVSAAQLPSALADLRLVPRRSMALLCGQPASVERFARHLYLAGVPRSQTLADLFLPHA 308
Cdd:PRK05713 241 LAALAGRHPQLSVELVTAAQLPAALAELRLVSRQTMALLCGSPASVERFARRLYLAGLPRNQLLADVFLPHA 312
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 96-305 5.78e-66

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: 206.35  E-value: 5.78e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  96 VVACHWLG-DVLRLRLEPERPLRYRAGQHLLLWSDDGVARPYSLASLPHEDPWLEFHIDCSAPGAFCDRARRLA-PGALL 173
Cdd:cd06194   1 VVSLQRLSpDVLRVRLEPDRPLPYLPGQYVNLRRAGGLARSYSPTSLPDGDNELEFHIRRKPNGAFSGWLGEEArPGHAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 174 RLGELRGGALrYEPDWQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLAR---DHYLASELAELAGRHPQLRVN 250
Cdd:cd06194  81 RLQGPFGQAF-YRPEYGEGPLLLVGAGTGLAPLWGIARAALRQGHQGEIRLVHGARdpdDLYLHPALLWLAREHPNFRYI 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599527 251 LVSAAQLPSA--------LADLRLVPRRSMALLCGQPASVERFARHLYLAGVPRSQTLADLFL 305
Cdd:cd06194 160 PCVSEGSQGDprvragriAAHLPPLTRDDVVYLCGAPSMVNAVRRRAFLAGAPMKRIYADPFE 222
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 3-245 1.21e-31

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


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 121.51  E-value: 1.21e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   3 DIRVGERRLAVAAGSNLLDALLAGGIAVPHSC-RAGSCHACLVHCLQGEVD--DTLPEALDPVRREAGWRLACQCRVLGD 79
Cdd:COG2871  38 TINGDGKEIEVEEGQTLLDALLRQGIFLPSACgGGGTCGQCKVKVLEGGGDilPTETFHLSDRERKEGYRLACQVKVKSD 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  80 LVLQpFDPERDGL---PARVVACHwlgDV------LRLRLEPERPLRYRAGQ----------------------HLLLW- 127
Cdd:COG2871 118 MEIE-VPEEVFGVkkwEATVVSNE---NVttfikeLVLELPEGEEIDFKAGQyiqievppyevdfkdfdipeeeKFGLFd 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 128 -SDDGVARPYSLASLPHEDPWLEFHI------DCSAPGAFCDRARRLAPGALLRL----GE--LRGGalryepdwqERPL 194
Cdd:COG2871 194 kNDEEVTRAYSMANYPAEKGIIELNIriatppMDVPPGIGSSYIFSLKPGDKVTIsgpyGEffLRDS---------DREM 264

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15599527 195 LLMAAGTGLAPLWGILREALRAEH-QAPIQLLHLAR---DHYLASELAELAGRHP 245
Cdd:COG2871 265 VFIGGGAGMAPLRSHIFDLLERGKtDRKITFWYGARslrELFYLEEFRELEKEHP 319
nqrF TIGR01941
NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit; This model represents the NqrF ...
 8-304 1.29e-14

NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit; This model represents the NqrF subunit of the six-protein, Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria. This oxidoreductase complex functions primarily as a sodium ion pump. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130996 [Multi-domain]  Cd Length: 405  Bit Score: 73.68  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527     8 ERRLAVAAGSNLLDALLAGGIAVPHSCRA-GSCHACLVHCLQGEvDDTLPEALDPV-RREA--GWRLACQCRVLGDLVLQ 83
Cdd:TIGR01941  41 EKSITVPAGGKLLNTLASNGIFISSACGGgGTCGQCRVRVVEGG-GEILPTELSHFsKREAkeGWRLSCQVKVKQDMSIE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527    84 pfdperdgLPARVV-ACHWLGDV------------LRLRLEPERPLRYRAG---------------------------QH 123
Cdd:TIGR01941 120 --------IPEEIFgVKKWECEVisndnvatfikeLVLKLPDGESVPFKAGgyiqieapphvvkyadfdippeyrgdwEK 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   124 LLLWS-----DDGVARPYSLASLPHEDPWLEFHIDCSAP---------GAFCDRARRLAPGALLRLGELRGGALRYEPDw 189
Cdd:TIGR01941 192 FNLFDlvskvDEETVRAYSMANYPAEKGIIKLNVRIATPpfinsdippGIMSSYIFSLKPGDKVTISGPFGEFFAKDTD- 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   190 qeRPLLLMAAGTGLAPLWG-ILREALRAEHQAPIQLLHLAR---DHYLASELAELAGRHPQLRVNLVSAAQLP------- 258
Cdd:TIGR01941 271 --AEMVFIGGGAGMAPMRShIFDQLKRLKSKRKISFWYGARslrEMFYQEDFDQLEAENPNFVWHVALSDPQPednwtgy 348

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15599527   259 -----SALADLRL----VPRRSMALLCGQP---ASVERFARHLylaGVPRSQTLADLF 304
Cdd:TIGR01941 349 tgfihNVLYENYLkdhdAPEDCEFYMCGPPmmnAAVIKMLEDL---GVERENILLDDF 403
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
12-76 1.18e-13

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 65.24  E-value: 1.18e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599527    12 AVAAGSNLLDALLAGGIAVPHSCRAGSCHACLVHCLQGEVDDTLPEALDPVRREAGWRLACQCRV 76
Cdd:pfam00111  12 VPDGETTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFLEDDELAAGYVVLACQTYP 76
 
Name Accession Description Interval E-value
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
1-308 0e+00

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 516.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527    1 MPDIRVGERRLAVAAGSNLLDALLAGGIAVPHSCRAGSCHACLVHCLQGEVDDTLPEALDPVRREAGWRLACQCRVLGDL 80
Cdd:PRK05713   1 MPELRVGERRWSVPAGSNLLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEDALPEALAAEKREQGWRLACQCRVVGDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   81 VLQPFDPERDGLPARVVACHWL-GDVLRLRLEPERPLRYRAGQHLLLWSDDGVARPYSLASLPHEDPWLEFHIDCSAPGA 159
Cdd:PRK05713  81 RVEVFDPQRDGLPARVVALDWLgGDVLRLRLEPERPLRYRAGQHLVLWTAGGVARPYSLASLPGEDPFLEFHIDCSRPGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  160 FCDRARRLAPGALLRLGELRGGALRYEPDWQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLARD---HYLASE 236
Cdd:PRK05713 161 FCDAARQLQVGDLLRLGELRGGALHYDPDWQERPLWLLAAGTGLAPLWGILREALRQGHQGPIRLLHLARDsagHYLAEP 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599527  237 LAELAGRHPQLRVNLVSAAQLPSALADLRLVPRRSMALLCGQPASVERFARHLYLAGVPRSQTLADLFLPHA 308
Cdd:PRK05713 241 LAALAGRHPQLSVELVTAAQLPAALAELRLVSRQTMALLCGSPASVERFARRLYLAGLPRNQLLADVFLPHA 312
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 96-305 5.78e-66

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: 206.35  E-value: 5.78e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  96 VVACHWLG-DVLRLRLEPERPLRYRAGQHLLLWSDDGVARPYSLASLPHEDPWLEFHIDCSAPGAFCDRARRLA-PGALL 173
Cdd:cd06194   1 VVSLQRLSpDVLRVRLEPDRPLPYLPGQYVNLRRAGGLARSYSPTSLPDGDNELEFHIRRKPNGAFSGWLGEEArPGHAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 174 RLGELRGGALrYEPDWQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLAR---DHYLASELAELAGRHPQLRVN 250
Cdd:cd06194  81 RLQGPFGQAF-YRPEYGEGPLLLVGAGTGLAPLWGIARAALRQGHQGEIRLVHGARdpdDLYLHPALLWLAREHPNFRYI 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599527 251 LVSAAQLPSA--------LADLRLVPRRSMALLCGQPASVERFARHLYLAGVPRSQTLADLFL 305
Cdd:cd06194 160 PCVSEGSQGDprvragriAAHLPPLTRDDVVYLCGAPSMVNAVRRRAFLAGAPMKRIYADPFE 222
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 9-248 5.68e-41

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 145.01  E-value: 5.68e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527    9 RRLAVAAGSNLLDALLAGGIAVPHSCRAGSCHACLVHCLQGEVD--DTLPEALDPVRREAGWRLACQCRVLGDLVLQ-PF 85
Cdd:PRK07609  12 RQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEqgPHQASALSGEERAAGEALTCCAKPLSDLVLEaRE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   86 DPERDG-----LPARVVACHWLGD---VLRLRLEPERPLRYRAGQHLLLWSDDGVARPYSLASLPHEDPWLEFHIDCSAP 157
Cdd:PRK07609  92 VPALGDipvkkLPCRVASLERVAGdvmRLKLRLPATERLQYLAGQYIEFILKDGKRRSYSIANAPHSGGPLELHIRHMPG 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  158 GAFCDRA-RRLAPGALLRLgELRGGA--LRYEPDwqeRPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLAR---DH 231
Cdd:PRK07609 172 GVFTDHVfGALKERDILRI-EGPLGTffLREDSD---KPIVLLASGTGFAPIKSIVEHLRAKGIQRPVTLYWGARrpeDL 247

                        250
                 ....*....|....*...
gi 15599527  232 YLaSELAEL-AGRHPQLR 248
Cdd:PRK07609 248 YL-SALAEQwAEELPNFR 264
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 94-252 2.95e-32

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: 119.19  E-value: 2.95e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  94 ARVVACHWL-GDVLRLRLEPERPLRYRAGQHLLLWSDDGVARPYSLASLPHEDPWLEFHIDCSAPGAFCDRAR-RLAPGA 171
Cdd:cd06189   1 CKVESIEPLnDDVYRVRLKPPAPLDFLAGQYLDLLLDDGDKRPFSIASAPHEDGEIELHIRAVPGGSFSDYVFeELKENG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 172 LLRLgELRGGA--LRYEPDwqeRPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLAR---DHYLASELAELAGRHPQ 246
Cdd:cd06189  81 LVRI-EGPLGDffLREDSD---RPLILIAGGTGFAPIKSILEHLLAQGSKRPIHLYWGARteeDLYLDELLEAWAEAHPN 156


                ....*.
gi 15599527 247 LRVNLV 252
Cdd:cd06189 157 FTYVPV 162
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 3-245 1.21e-31

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


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 121.51  E-value: 1.21e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   3 DIRVGERRLAVAAGSNLLDALLAGGIAVPHSC-RAGSCHACLVHCLQGEVD--DTLPEALDPVRREAGWRLACQCRVLGD 79
Cdd:COG2871  38 TINGDGKEIEVEEGQTLLDALLRQGIFLPSACgGGGTCGQCKVKVLEGGGDilPTETFHLSDRERKEGYRLACQVKVKSD 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  80 LVLQpFDPERDGL---PARVVACHwlgDV------LRLRLEPERPLRYRAGQ----------------------HLLLW- 127
Cdd:COG2871 118 MEIE-VPEEVFGVkkwEATVVSNE---NVttfikeLVLELPEGEEIDFKAGQyiqievppyevdfkdfdipeeeKFGLFd 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 128 -SDDGVARPYSLASLPHEDPWLEFHI------DCSAPGAFCDRARRLAPGALLRL----GE--LRGGalryepdwqERPL 194
Cdd:COG2871 194 kNDEEVTRAYSMANYPAEKGIIELNIriatppMDVPPGIGSSYIFSLKPGDKVTIsgpyGEffLRDS---------DREM 264

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15599527 195 LLMAAGTGLAPLWGILREALRAEH-QAPIQLLHLAR---DHYLASELAELAGRHP 245
Cdd:COG2871 265 VFIGGGAGMAPLRSHIFDLLERGKtDRKITFWYGARslrELFYLEEFRELEKEHP 319
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 104-298 6.59e-31

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


Pssm-ID: 99778 [Multi-domain]  Cd Length: 223  Bit Score: 115.62  E-value: 6.59e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 104 DVLRLRLEPERPLRYRAGQHLLLWSDD---GVARPYSLASLPHEDPWLEFHIDCSAPGAFCDRARRLAPGALLRLgELRG 180
Cdd:cd00322   9 DVRLFRLQLPNGFSFKPGQYVDLHLPGdgrGLRRAYSIASSPDEEGELELTVKIVPGGPFSAWLHDLKPGDEVEV-SGPG 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 181 GALRYEPDWqERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLAR---DHYLASELAELAGRHPQLRVNLVSAAQL 257
Cdd:cd00322  88 GDFFLPLEE-SGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARtpaDLLFLDELEELAKEGPNFRLVLALSRES 166

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15599527 258 PSALADLRLVPRRSMAL------------LCGQPASVERFARHLYLAGVPRSQ 298
Cdd:cd00322 167 EAKLGPGGRIDREAEILallpddsgalvyICGPPAMAKAVREALVSLGVPEER 219
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 95-303 6.70e-31

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 116.12  E-value: 6.70e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  95 RVVACHWL-GDVLRLRLE-PERPLRYRAGQHLLLW-SDDGVARPYSLASLPHEDPWLEFHIDcsAPGAFCDRARRLAPGA 171
Cdd:COG0543   1 KVVSVERLaPDVYLLRLEaPLIALKFKPGQFVMLRvPGDGLRRPFSIASAPREDGTIELHIR--VVGKGTRALAELKPGD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 172 LLRLGELRGGALRYEPDwqERPLLLMAAGTGLAPLWGILREALraEHQAPIQLLHLAR---DHYLASELAELAgrhpQLR 248
Cdd:COG0543  79 ELDVRGPLGNGFPLEDS--GRPVLLVAGGTGLAPLRSLAEALL--ARGRRVTLYLGARtpeDLYLLDELEALA----DFR 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599527 249 VNLVSAAQ-------LPSALADLRLVPRRSMALLCGQPASVERFARHLYLAGVPRSQTLADL 303
Cdd:COG0543 151 VVVTTDDGwygrkgfVTDALKELLAEDSGDDVYACGPPPMMKAVAELLLERGVPPERIYVSL 212
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
92-298 1.45e-29

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 112.19  E-value: 1.45e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  92 LPARVVACHWLG-DVLRLRLEPE---RPLRYRAGQHLLLWSD-DG--VARPYSLASLPHEDpWLEFHIDCSAPGAFCDRA 164
Cdd:COG1018   4 RPLRVVEVRRETpDVVSFTLEPPdgaPLPRFRPGQFVTLRLPiDGkpLRRAYSLSSAPGDG-RLEITVKRVPGGGGSNWL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 165 -RRLAPGALLRLGELRGG-ALRYEPDwqeRPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLAR---DHYLASELAE 239
Cdd:COG1018  83 hDHLKVGDTLEVSGPRGDfVLDPEPA---RPLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGARspaDLAFRDELEA 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599527 240 LAGRHPQLRVNLV------------SAAQLPSALADlrlvPRRSMALLCGQPASVERFARHLYLAGVPRSQ 298
Cdd:COG1018 160 LAARHPRLRLHPVlsrepaglqgrlDAELLAALLPD----PADAHVYLCGPPPMMEAVRAALAELGVPEER 226
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 96-304 1.86e-28

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: 109.22  E-value: 1.86e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  96 VVACHWLG-DVLRLRLEPERPLRYRAGQH--LLLWSDDGVARPYSLASLPHEDPWLEFHIDCSAPGAFCDR-ARRLAPGA 171
Cdd:cd06187   1 VVSVERLThDIAVVRLQLDQPLPFWAGQYvnVTVPGRPRTWRAYSPANPPNEDGEIEFHVRAVPGGRVSNAlHDELKVGD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 172 LLRLGELRGGAlrYEPDWQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLAR---DHYLASELAELAGRHPQLR 248
Cdd:cd06187  81 RVRLSGPYGTF--YLRRDHDRPVLCIAGGTGLAPLRAIVEDALRRGEPRPVHLFFGARterDLYDLEGLLALAARHPWLR 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599527 249 VNLVSAA----------QLPSALADLRLVPRRSMALLCGQPASVERFARHLYLAGVPRSQTLADLF 304
Cdd:cd06187 159 VVPVVSHeegawtgrrgLVTDVVGRDGPDWADHDIYICGPPAMVDATVDALLARGAPPERIHFDKF 224
Fdx COG0633
Ferredoxin [Energy production and conversion];
1-82 3.07e-26

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 99.15  E-value: 3.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   1 MPDIRV--GERRLAVAAGSNLLDALLAGGIAVPHSCRAGSCHACLVHCLQGEVDDTLPEALDPVRREAGWRLACQCRVLG 78
Cdd:COG0633   1 MPKVTFipEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARPTS 80


                ....
gi 15599527  79 DLVL 82
Cdd:COG0633  81 DLVV 84
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 77-297 4.20e-24

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap 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: 98.07  E-value: 4.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  77 LGDLVLQPFDP--ERDGLPARVVACHWL-GDVLRLRLEPER-PLRYRAGQHLLLWSD-DGV--ARPYSLASLPHEDPW-L 148
Cdd:cd06216   1 FVDFYLELINPlwSARELRARVVAVRPEtADMVTLTLRPNRgWPGHRAGQHVRLGVEiDGVrhWRSYSLSSSPTQEDGtI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 149 EFHIDCSAPGAFCDR-ARRLAPGALLRLGELRGGAlrYEPDWQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHL 227
Cdd:cd06216  81 TLTVKAQPDGLVSNWlVNHLAPGDVVELSQPQGDF--VLPDPLPPRLLLIAAGSGITPVMSMLRTLLARGPTADVVLLYY 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 228 AR---DHYLASELAELAGRHPQLRVNL----------VSAAQLPSALADLrlvpRRSMALLCGQPASVERFARHLYLAGV 294
Cdd:cd06216 159 ARtreDVIFADELRALAAQHPNLRLHLlytreeldgrLSAAHLDAVVPDL----ADRQVYACGPPGFLDAAEELLEAAGL 234


                ...
gi 15599527 295 PRS 297
Cdd:cd06216 235 ADR 237
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 4-83 6.59e-22

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: 87.45  E-value: 6.59e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   4 IRVGERRLAVAAGSNLLDALLAGGIAVPHSCRAGSCHACLVHCLQGEVDDTLPEALDPVRREAGWRLACQCRVLGDLVLQ 83
Cdd:cd00207   5 VPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTDGLVIE 84
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 100-289 1.02e-21

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: 91.47  E-value: 1.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 100 HWLGDVLRLRLEPERPLRYRAGQ----HLLLWSDDGVARPYSLASLPHEDpWLEFHIDCSAPGAFCDRARRLAPGALLRL 175
Cdd:cd06195   7 DWTDDLFSFRVTRDIPFRFQAGQftklGLPNDDGKLVRRAYSIASAPYEE-NLEFYIILVPDGPLTPRLFKLKPGDTIYV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 176 GELRGGALRYEPDWQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLARD-HYLA--SELAELAGRH-PQLR-VN 250
Cdd:cd06195  86 GKKPTGFLTLDEVPPGKRLWLLATGTGIAPFLSMLRDLEIWERFDKIVLVHGVRYaEELAyqDEIEALAKQYnGKFRyVP 165

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15599527 251 LVSAAQLPSAL----------------ADLRLVPRRSMALLCGQPASVERFARHL 289
Cdd:cd06195 166 IVSREKENGALtgripdliesgeleehAGLPLDPETSHVMLCGNPQMIDDTQELL 220
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 106-304 6.10e-19

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


Pssm-ID: 99808 [Multi-domain]  Cd Length: 232  Bit Score: 83.92  E-value: 6.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 106 LRLRLEPERPLRYRAGQHLLLW-SDDGVARPYSLASLPHEDPWLEFHIDCSAPGAFCDR-ARRLAPGALLRL-GELRGGA 182
Cdd:cd06212  18 LRLRLEEPEPIKFFAGQYVDITvPGTEETRSFSMANTPADPGRLEFIIKKYPGGLFSSFlDDGLAVGDPVTVtGPYGTCT 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 183 LRYEPDwqeRPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLAR---DHYLASELAELAGRHPQLR-VNLVSAAQ-- 256
Cdd:cd06212  98 LRESRD---RPIVLIGGGSGMAPLLSLLRDMAASGSDRPVRFFYGARtarDLFYLEEIAALGEKIPDFTfIPALSESPdd 174

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15599527 257 ---------LPSALADLRLVPRRSMALLCGQPASVERFARHLYLAGVPRSQTLADLF 304
Cdd:cd06212 175 egwsgetglVTEVVQRNEATLAGCDVYLCGPPPMIDAALPVLEMSGVPPDQIFYDKF 231
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 106-298 1.51e-18

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: 82.70  E-value: 1.51e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 106 LRLRLEPERPLRYRAGQH--LLLWSDDG--VARPYSLASLPHEDPWLEFHIDcSAPGAFCDR--ARRLAPGALLrlgELR 179
Cdd:cd06217  19 FRLAVPDGVPPPFLAGQHvdLRLTAIDGytAQRSYSIASSPTQRGRVELTVK-RVPGGEVSPylHDEVKVGDLL---EVR 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 180 G--GALRYEPDwQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLARDH---YLASELAELAGRHPQLRVNLVSA 254
Cdd:cd06217  95 GpiGTFTWNPL-HGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVPFRLLYSARTAedvIFRDELEQLARRHPNLHVTEALT 173

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15599527 255 AQLP----------SALADLRLVP--RRSMALLCGQPASVERFARHLYLAGVPRSQ 298
Cdd:cd06217 174 RAAPadwlgpagriTADLIAELVPplAGRRVYVCGPPAFVEAATRLLLELGVPRDR 229
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
93-304 1.49e-17

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 82.63  E-value: 1.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  93 PARVVACHWL-GDVLRLRLEPE--RPLRYRAGQHLLLWSDDGVAR----PYSLASLPHEDPWLEFHIdcSAPGAFCDRAR 165
Cdd:COG4097 216 PYRVESVEPEaGDVVELTLRPEggRWLGHRAGQFAFLRFDGSPFWeeahPFSISSAPGGDGRLRFTI--KALGDFTRRLG 293

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 166 RLAPGALLRlgeLRG--GALRYEPDWQERPLLLMAAGTGLAPLWGILRE-ALRAEHQAPIQLLHLARDH---YLASELAE 239
Cdd:COG4097 294 RLKPGTRVY---VEGpyGRFTFDRRDTAPRQVWIAGGIGITPFLALLRAlAARPGDQRPVDLFYCVRDEedaPFLEELRA 370

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599527 240 LAGRHPQLRVNLVSAAQLPSALADL--RLVP--RRSMALLCGQPASVERFARHLYLAGVPRSQTLADLF 304
Cdd:COG4097 371 LAARLAGLRLHLVVSDEDGRLTAERlrRLVPdlAEADVFFCGPPGMMDALRRDLRALGVPARRIHQERF 439
fre PRK08051
FMN reductase; Validated
 105-249 9.65e-17

FMN reductase; Validated


Pssm-ID: 236142 [Multi-domain]  Cd Length: 232  Bit Score: 77.59  E-value: 9.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  105 VLRLRLEPERPLRYRAGQHLLLWSDDGVARPYSLASLPHEDPWLEFHIDCSA----PGAFCDrarRLAPGALLRLGELRG 180
Cdd:PRK08051  17 VYRVRLVPEAPFSFRAGQYLMVVMGEKDKRPFSIASTPREKGFIELHIGASElnlyAMAVME---RILKDGEIEVDIPHG 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599527  181 GA-LRYEpdwQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLARDH---YLASELAELAGRHPQLRV 249
Cdd:PRK08051  94 DAwLREE---SERPLLLIAGGTGFSYARSILLTALAQGPNRPITLYWGGREEdhlYDLDELEALALKHPNLHF 163
COG3894 COG3894
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain ...
 1-81 2.94e-16

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


Pssm-ID: 443101 [Multi-domain]  Cd Length: 621  Bit Score: 79.08  E-value: 2.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   1 MPDIRV----GERRLAVAAGSNLLDALLAGGIAVPHSCR-AGSCHACLVHCLQGEVDDTLPEA---LDPVRREAGWRLAC 72
Cdd:COG3894   1 MPKVKVtflpSGKRVEVEAGTTLLDAAREAGVDIDAPCGgRGTCGKCKVKVEEGEFSPVTEEErrlLSPEELAEGYRLAC 80


                ....*....
gi 15599527  73 QCRVLGDLV 81
Cdd:COG3894  81 QARVLGDLV 89
nqrF TIGR01941
NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit; This model represents the NqrF ...
 8-304 1.29e-14

NADH:ubiquinone oxidoreductase, Na(+)-translocating, F subunit; This model represents the NqrF subunit of the six-protein, Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria. This oxidoreductase complex functions primarily as a sodium ion pump. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130996 [Multi-domain]  Cd Length: 405  Bit Score: 73.68  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527     8 ERRLAVAAGSNLLDALLAGGIAVPHSCRA-GSCHACLVHCLQGEvDDTLPEALDPV-RREA--GWRLACQCRVLGDLVLQ 83
Cdd:TIGR01941  41 EKSITVPAGGKLLNTLASNGIFISSACGGgGTCGQCRVRVVEGG-GEILPTELSHFsKREAkeGWRLSCQVKVKQDMSIE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527    84 pfdperdgLPARVV-ACHWLGDV------------LRLRLEPERPLRYRAG---------------------------QH 123
Cdd:TIGR01941 120 --------IPEEIFgVKKWECEVisndnvatfikeLVLKLPDGESVPFKAGgyiqieapphvvkyadfdippeyrgdwEK 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   124 LLLWS-----DDGVARPYSLASLPHEDPWLEFHIDCSAP---------GAFCDRARRLAPGALLRLGELRGGALRYEPDw 189
Cdd:TIGR01941 192 FNLFDlvskvDEETVRAYSMANYPAEKGIIKLNVRIATPpfinsdippGIMSSYIFSLKPGDKVTISGPFGEFFAKDTD- 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   190 qeRPLLLMAAGTGLAPLWG-ILREALRAEHQAPIQLLHLAR---DHYLASELAELAGRHPQLRVNLVSAAQLP------- 258
Cdd:TIGR01941 271 --AEMVFIGGGAGMAPMRShIFDQLKRLKSKRKISFWYGARslrEMFYQEDFDQLEAENPNFVWHVALSDPQPednwtgy 348

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15599527   259 -----SALADLRL----VPRRSMALLCGQP---ASVERFARHLylaGVPRSQTLADLF 304
Cdd:TIGR01941 349 tgfihNVLYENYLkdhdAPEDCEFYMCGPPmmnAAVIKMLEDL---GVERENILLDDF 403
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 94-305 2.47e-14

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


Pssm-ID: 99806  Cd Length: 236  Bit Score: 70.83  E-value: 2.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  94 ARVVACHWLG-DVLRLRLEPERP------LRYRAGQHL-LLWSDDGVARPYSLASLPHEDPWLEFHIDCSAPGAFCDRAR 165
Cdd:cd06210   4 AEIVAVDRVSsNVVRLRLQPDDAegagiaAEFVPGQFVeIEIPGTDTRRSYSLANTPNWDGRLEFLIRLLPGGAFSTYLE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 166 -RLAPGALLRL-GELRGGALRyepDWQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLARDH---YLASELAEL 240
Cdd:cd06210  84 tRAKVGQRLNLrGPLGAFGLR---ENGLRPRWFVAGGTGLAPLLSMLRRMAEWGEPQEARLFFGVNTEaelFYLDELKRL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599527 241 AGRHPQLRVNLV--------------SAAQLPSALADLRLVPRrsmALLCGQPASVERFARHLYLAGVPRSQTLADLFL 305
Cdd:cd06210 161 ADSLPNLTVRICvwrpggewegyrgtVVDALREDLASSDAKPD---IYLCGPPGMVDAAFAAAREAGVPDEQVYLEKFL 236
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
11-242 3.47e-14

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 72.08  E-value: 3.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   11 LAVAAGSNLLDALLAGGIAVPHSCRAGSCHACLVHCLQGE-----VDDtlpEALDPVRREAGWRLACQCRVLGDLVLQpF 85
Cdd:PRK11872  17 FPVGKDELLLDAALRNGINLPLDCREGVCGTCQGRCESGIysqdyVDE---DALSERDLAQRKMLACQTRVKSDAAFY-F 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   86 D--------PERDGLPARVVACHWLGD---VLRLRLEP-ERPLRYRAGQHLLLW-SDDGVARPYSLASLPHEDPWLEFHI 152
Cdd:PRK11872  93 DfdsslcnaGDTLKISGVVTAVELVSEttaILHLDASAhGRQLDFLPGQYARLQiPGTDDWRSYSFANRPNATNQLQFLI 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  153 DCSAPGAFCDRAR-RLAPGALLRLgELRGGA--LRYepdwQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLAR 229
Cdd:PRK11872 173 RLLPDGVMSNYLReRCQVGDEILF-EAPLGAfyLRE----VERPLVFVAGGTGLSAFLGMLDELAEQGCSPPVHLYYGVR 247

                        250
                 ....*....|...
gi 15599527  230 DHYLASELAELAG 242
Cdd:PRK11872 248 HAADLCELQRLAA 260
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 94-304 4.35e-14

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: 70.03  E-value: 4.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  94 ARVVA----CHwlgDVLRLRLEPERPLRYRAGQHLLLWSD-DGVARPYSLASLPHEDPWLEFHIDCSAPGAFCD---RAR 165
Cdd:cd06213   3 GTIVAqerlTH---DIVRLTVQLDRPIAYKAGQYAELTLPgLPAARSYSFANAPQGDGQLSFHIRKVPGGAFSGwlfGAD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 166 RlaPGALLrlgELRG--GALRYEPdwQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLAR---DHYLASELAEL 240
Cdd:cd06213  80 R--TGERL---TVRGpfGDFWLRP--GDAPILCIAGGSGLAPILAILEQARAAGTKRDVTLLFGARtqrDLYALDEIAAI 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599527 241 AGR-HPQLR-VNLVSAAQLPSALADLR---------LVPRRSMALLCGQPASVERFARHLYLAGVPRSQTLADLF 304
Cdd:cd06213 153 AARwRGRFRfIPVLSEEPADSSWKGARglvtehiaeVLLAATEAYLCGPPAMIDAAIAVLRALGIAREHIHADRF 227
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 106-298 4.69e-14

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: 70.33  E-value: 4.69e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 106 LRLRLEPERPLRYRAGQHLLLWSDdGVAR-PYSLASLPHEDPWLEFHIdcSAPGAFCDRARRLAPGAllRLGeLRG--GA 182
Cdd:cd06221  16 LRLEDDDEELFTFKPGQFVMLSLP-GVGEaPISISSDPTRRGPLELTI--RRVGRVTEALHELKPGD--TVG-LRGpfGN 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 183 LRYEPDWQERPLLLMAAGTGLAPLWGILREALRA-EHQAPIQLLHLAR---DHYLASELAELAGRhPQLRVNL-VSAAQ- 256
Cdd:cd06221  90 GFPVEEMKGKDLLLVAGGLGLAPLRSLINYILDNrEDYGKVTLLYGARtpeDLLFKEELKEWAKR-SDVEVILtVDRAEe 168

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15599527 257 --------LPSALADLRLVPRRSMALLCGQPASVERFARHLYLAGVPRSQ 298
Cdd:cd06221 169 gwtgnvglVTDLLPELTLDPDNTVAIVCGPPIMMRFVAKELLKLGVPEEQ 218
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
12-76 1.18e-13

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 65.24  E-value: 1.18e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599527    12 AVAAGSNLLDALLAGGIAVPHSCRAGSCHACLVHCLQGEVDDTLPEALDPVRREAGWRLACQCRV 76
Cdd:pfam00111  12 VPDGETTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSFLEDDELAAGYVVLACQTYP 76
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 106-248 3.08e-13

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: 68.12  E-value: 3.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 106 LRLRLEPERPLRYRAGQHLLLWSDDG-VARPYSLASLPHEDPWLEFHIdcsapgafcdrarRLAPGALL------RLGEl 178
Cdd:cd06211  24 VRLKLDEPEEIEFQAGQYVNLQAPGYeGTRAFSIASSPSDAGEIELHI-------------RLVPGGIAttyvhkQLKE- 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 179 rGGALR--------YEPDWQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLAR---DHYLASELAELAGRHPQL 247
Cdd:cd06211  90 -GDELEisgpygdfFVRDSDQRPIIFIAGGSGLSSPRSMILDLLERGDTRKITLFFGARtraELYYLDEFEALEKDHPNF 168


                .
gi 15599527 248 R 248
Cdd:cd06211 169 K 169
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 94-296 4.04e-13

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: 67.23  E-value: 4.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  94 ARVVACHWLGD---VLRLRLEPERPLRYRAGQHLLLW-SDDGVARPYSLASLPHeDPWLEFHIDCSAPGAFCDRARRLA- 168
Cdd:cd06209   4 ATVTEVERLSDstiGLTLELDEAGALAFLPGQYVNLQvPGTDETRSYSFSSAPG-DPRLEFLIRLLPGGAMSSYLRDRAq 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 169 PGALLRLGELRGG-ALRYEpdwqERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLH-LARDHYLAS--ELAELAGRH 244
Cdd:cd06209  83 PGDRLTLTGPLGSfYLREV----KRPLLMLAGGTGLAPFLSMLDVLAEDGSAHPVHLVYgVTRDADLVEldRLEALAERL 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599527 245 PQLRVNLVSAAQ---------LPSALADLRLVPRRSMALLCGQPASVERFARHLYLAGVPR 296
Cdd:cd06209 159 PGFSFRTVVADPdswhprkgyVTDHLEAEDLNDGDVDVYLCGPPPMVDAVRSWLDEQGIEP 219
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 116-298 3.05e-12

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: 65.26  E-value: 3.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 116 LRYRAGQHL-LLWSDDG--VARPYSLASLPHEDPwLEFHIDCSAPGAF----CDRarrLAPGALLRLGELRGgalR--YE 186
Cdd:cd06214  31 FRYRPGQFLtLRVPIDGeeVRRSYSICSSPGDDE-LRITVKRVPGGRFsnwaNDE---LKAGDTLEVMPPAG---RftLP 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 187 PDWQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLARDH---YLASELAELAGRHPQlRVNLV----------- 252
Cdd:cd06214 104 PLPGARHYVLFAAGSGITPVLSILKTALAREPASRVTLVYGNRTEasvIFREELADLKARYPD-RLTVIhvlsreqgdpd 182

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15599527 253 ------SAAQLPSALADLRLVPRRSMALLCGQPASVERFARHLYLAGVPRSQ 298
Cdd:cd06214 183 llrgrlDAAKLNALLKNLLDATEFDEAFLCGPEPMMDAVEAALLELGVPAER 234
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 104-252 6.01e-12

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: 64.15  E-value: 6.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 104 DV--LRLRLEPERPLRYRAGQHLLL---WSDDGVARPYSLASLPHEDPWLEFHIDCSAPGA----FCDRarrLAPGALLR 174
Cdd:cd06215  12 DVktFRFAAPDGSLFAYKPGQFLTLeleIDGETVYRAYTLSSSPSRPDSLSITVKRVPGGLvsnwLHDN---LKVGDELW 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 175 LGELRGgaLRYEPDWQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLAR---DHYLASELAELAGRHPQLRVNL 251
Cdd:cd06215  89 ASGPAG--EFTLIDHPADKLLLLSAGSGITPMMSMARWLLDTRPDADIVFIHSARspaDIIFADELEELARRHPNFRLHL 166


                .
gi 15599527 252 V 252
Cdd:cd06215 167 I 167
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 103-304 9.30e-12

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: 63.43  E-value: 9.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 103 GDVLRLRLEPERP-LRYRAGQHLLLWSDDGVAR---PYSLASLPHEDPWLEFHIdcSAPGAFCDR-ARRLAPGALLrlgE 177
Cdd:cd06198   7 RPTTTLTLEPRGPaLGHRAGQFAFLRFDASGWEephPFTISSAPDPDGRLRFTI--KALGDYTRRlAERLKPGTRV---T 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 178 LRGGALRYEPDWQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLARDH---YLASELAELAGRHpQLRVNLVSA 254
Cdd:cd06198  82 VEGPYGRFTFDDRRARQIWIAGGIGITPFLALLEALAARGDARPVTLFYCVRDPedaVFLDELRALAAAA-GVVLHVIDS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15599527 255 AQ-----LPSALADLRLVPRRSMALLCGQPASVERFARHLYLAGVPRSQTLADLF 304
Cdd:cd06198 161 PSdgrltLEQLVRALVPDLADADVWFCGPPGMADALEKGLRALGVPARRFHYERF 215
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 96-252 1.64e-11

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: 63.04  E-value: 1.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  96 VVACHWLG-DVLRLRLEPERPLRYRAGQHLLLWS-DDGVARPYSLASLPHEDPWLEFHIDCSAPGAFCDR-ARRLAPGAL 172
Cdd:cd06190   1 LVDVRELThDVAEFRFALDGPADFLPGQYALLALpGVEGARAYSMANLANASGEWEFIIKRKPGGAASNAlFDNLEPGDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 173 LRL-GELRGGALRYEPDwqeRPLLLMAAGTGLAPLWGILREALRAEHQA--PIQL---LHLARDHYLASELAELAGRHPQ 246
Cdd:cd06190  81 LELdGPYGLAYLRPDED---RDIVCIAGGSGLAPMLSILRGAARSPYLSdrPVDLfygGRTPSDLCALDELSALVALGAR 157


                ....*.
gi 15599527 247 LRVNLV 252
Cdd:cd06190 158 LRVTPA 163
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 104-307 6.69e-11

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: 61.42  E-value: 6.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 104 DVLRLRLEPE--RPL-RYRAGQHL-LLWSDDG----VARPYSLASLPHEDPW-----LEFHIDCSapGAFCDRarrLAPG 170
Cdd:cd06184  20 DITSFYLEPAdgGPLpPFLPGQYLsVRVKLPGlgyrQIRQYSLSDAPNGDYYrisvkREPGGLVS--NYLHDN---VKVG 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 171 ALLRL----GELrggalrYEPDWQERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLARD---HYLASELAELAGR 243
Cdd:cd06184  95 DVLEVsapaGDF------VLDEASDRPLVLISAGVGITPMLSMLEALAAEGPGRPVTFIHAARNsavHAFRDELEELAAR 168

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599527 244 HPQLRVNLVSAAQLPSA------------LADLR--LVPRRSMALLCGQPASVERFARHLYLAGVPRSQTLADLFLPH 307
Cdd:cd06184 169 LPNLKLHVFYSEPEAGDreedydhagridLALLRelLLPADADFYLCGPVPFMQAVREGLKALGVPAERIHYEVFGPG 246
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 104-280 7.50e-11

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


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 61.04  E-value: 7.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 104 DVLRLRLEPERP---LRYRAGQHLLL---WSDDGVARPYSLASLPHEDPWLEFHIDCSAPGAFCDRARRLAPGALLrlgE 177
Cdd:cd06183  12 DTRIFRFELPSPdqvLGLPVGQHVELkapDDGEQVVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYLHSLKPGDTV---E 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 178 LRG--GALRYEPDWQERPLLLMAAGTGLAPLWGILREALRAEHQAP-IQLLHLAR---DHYLASELAELAGRHP-QLRVN 250
Cdd:cd06183  89 IRGpfGKFEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKDPEDKTkISLLYANRteeDILLREELDELAKKHPdRFKVH 168

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15599527 251 L---------------VSAAQLPSALAdlRLVPRRSMALLCGQPA 280
Cdd:cd06183 169 YvlsrppegwkggvgfITKEMIKEHLP--PPPSEDTLVLVCGPPP 211
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 104-295 1.20e-10

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: 60.33  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 104 DVLRLRLEpeRP--LRYRAGQ--HLLL----WSDDGvaRPYSLASLPhEDPWLEFHIDC-SAPGAFCDRARRLAPGALLR 174
Cdd:cd06196  14 DVKRLRFD--KPegYDFTPGQatEVAIdkpgWRDEK--RPFTFTSLP-EDDVLEFVIKSyPDHDGVTEQLGRLQPGDTLL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 175 LGELrGGALRYEPdwqerPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLH---LARDHYLASELAELAGrhpqLRVNL 251
Cdd:cd06196  89 IEDP-WGAIEYKG-----PGVFIAGGAGITPFIAILRDLAAKGKLEGNTLIFankTEKDIILKDELEKMLG----LKFIN 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15599527 252 VSAAQLPSALADLRLvprrSMALLcgqPASVERFARHLYLAGVP 295
Cdd:cd06196 159 VVTDEKDPGYAHGRI----DKAFL---KQHVTDFNQHFYVCGPP 195
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 114-295 4.65e-10

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: 58.69  E-value: 4.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 114 RPLRYRAGQHLLLWSD-DGVA--RPYSLASLPHEDPwLEFHIDCSAPGAFCDRARR-LAPGALLrlgELRG--GALRYEP 187
Cdd:cd06191  24 LQYGFRPGQHVTLKLDfDGEElrRCYSLCSSPAPDE-ISITVKRVPGGRVSNYLREhIQPGMTV---EVMGpqGHFVYQP 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 188 DWQERpLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLAR---DHYLASELAELAGRHPQLRVN-LVSAAQLPSALAD 263
Cdd:cd06191 100 QPPGR-YLLVAAGSGITPLMAMIRATLQTAPESDFTLIHSARtpaDMIFAQELRELADKPQRLRLLcIFTRETLDSDLLH 178

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15599527 264 LR----------LVPRR--SMALLCGQPASVERFARHLYLAGVP 295
Cdd:cd06191 179 GRidgeqslgaaLIPDRleREAFICGPAGMMDAVETALKELGMP 222
PRK13289 PRK13289
NO-inducible flavohemoprotein;
191-308 4.52e-09

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 56.73  E-value: 4.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  191 ERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLARD---HYLASELAELAGRHPQLRV------------------ 249
Cdd:PRK13289 261 DTPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIHAARNggvHAFRDEVEALAARHPNLKAhtwyrepteqdragedfd 340

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599527  250 --NLVSAAQLPSALADlrlvpRRSMALLCGQPASVERFARHLYLAGVPRSQTLADLFLPHA 308
Cdd:PRK13289 341 seGLMDLEWLEAWLPD-----PDADFYFCGPVPFMQFVAKQLLELGVPEERIHYEFFGPAK 396
PTZ00038 PTZ00038
ferredoxin; Provisional
 7-74 1.43e-08

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 53.69  E-value: 1.43e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599527    7 GERRLAVAAGSNLLDALLAGGIAVPHSCRAGSCHACLVHCLQGEVDDTLPEALDPVRREAGWRLACQC 74
Cdd:PTZ00038 105 GEKVIECDEDEYILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKGYCLLCTC 172
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 4-82 5.34e-08

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 53.56  E-value: 5.34e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599527    4 IRVGERRLAVAAGSNLLDALLAGGIAVPHSCRAGSCHACLVHCLQGEVDDTLPEALDPVRREAGWRLACQCRVLGDLVL 82
Cdd:PRK10684 253 KLQPAREFYAPVGTTLLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVSSTMTLTPAEIAQGYVLACSCHPQGDLVL 331
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 196-245 1.29e-07

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: 49.18  E-value: 1.29e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15599527   196 LMAAGTGLAPLWGILREALR-AEHQAPIQLLHLAR---DHYLASELAELAGRHP 245
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEdPKDPTQVVLVFGNRnedDILYREELDELAEKHP 54
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 19-72 2.03e-07

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


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 48.22  E-value: 2.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15599527    19 LLDALLAGGIAVPHSCRAGSCHACLVHCLQGEVDDTLPEALDPVRREAGWRLAC 72
Cdd:TIGR02008  25 ILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTC 78
PLN03136 PLN03136
Ferredoxin; Provisional
 7-88 3.95e-07

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 48.59  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527    7 GERRLAVAAGSNLLDALLAGGIAVPHSCRAGSCHACLVHCLQGEVDDTLPEALDPVRREAGWRLACQCRVLGDLVLQPFD 86
Cdd:PLN03136  64 GEQEVECEEDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDEQISEGYVLTCVAYPTSDVVIETHK 143


                 ..
gi 15599527   87 PE 88
Cdd:PLN03136 144 EE 145
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 103-250 5.46e-07

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


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 49.23  E-value: 5.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 103 GDVLRLRLEPERPLRYRAGQHLLLWsddgVAR--------PYSLASLPHEDP-WLEFHIDCSApGAFCDRARRLA----P 169
Cdd:cd06186  10 SDVIRLTIPKPKPFKWKPGQHVYLN----FPSllsfwqshPFTIASSPEDEQdTLSLIIRAKK-GFTTRLLRKALkspgG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 170 GALLRL------GELRGGALRYepdwqERpLLLMAAGTGLAPLWGILREAL-RAEHQAPIQLLHL---ARDHYLASELAE 239
Cdd:cd06186  85 GVSLKVlvegpyGSSSEDLLSY-----DN-VLLVAGGSGITFVLPILRDLLrRSSKTSRTRRVKLvwvVRDREDLEWFLD 158

                       170
                ....*....|.
gi 15599527 240 LAGRHPQLRVN 250
Cdd:cd06186 159 ELRAAQELEVD 169
petF CHL00134
ferredoxin; Validated
 19-72 1.17e-06

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 46.25  E-value: 1.17e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15599527   19 LLDALLAGGIAVPHSCRAGSCHACLVHCLQGEVDDTLPEALDPVRREAGWRLAC 72
Cdd:CHL00134  27 ILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTC 80
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 106-239 2.92e-06

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. CYPOR has a C-terminal ferredoxin reducatase (FNR)- like FAD and NAD binding module, an FMN-binding domain, and an additional conecting domain (inserted within the FAD binding region) that orients the FNR and FMN binding domains. 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: 99779 [Multi-domain]  Cd Length: 267  Bit Score: 47.72  E-value: 2.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 106 LRLRLEPERPLRYRAGQHLLLW-SDDGVARPYSLASLPHEDPWlEFHIdCSAPGAFCDRARRLAPG------ALLRLG-- 176
Cdd:cd06182  20 LEFDLSGNSVLKYQPGDHLGVIpPNPLQPRYYSIASSPDVDPG-EVHL-CVRVVSYEAPAGRIRKGvcsnflAGLQLGak 97

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599527 177 ---ELRGGALRYEPDWQERPLLLMAAGTGLAPLWGILRE--ALRAEHQAPIQLL------HLARDHYLASELAE 239
Cdd:cd06182  98 vtvFIRPAPSFRLPKDPTTPIIMVGPGTGIAPFRGFLQEraALRANGKARGPAWlffgcrNFASDYLYREELQE 171
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 117-306 3.36e-06

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 47.78  E-value: 3.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  117 RYRAGQHLLLwSDDGVA---RPYSLASLPHEDPWLEFHIDCSAPGAFCD-RARRLAPGALLRLGELRGgalryE---PDW 189
Cdd:PRK10684  36 PYRAGQYALV-SIRNSAetlRAYTLSSTPGVSEFITLTVRRIDDGVGSQwLTRDVKRGDYLWLSDAMG-----EftcDDK 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  190 QERPLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLAR---DHYLASELAELAGRHPQLRVNLVSAAQLPSALADLRL 266
Cdd:PRK10684 110 AEDKYLLLAAGCGVTPIMSMRRWLLKNRPQADVQVIFNVRtpqDVIFADEWRQLKQRYPQLNLTLVAENNATEGFIAGRL 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15599527  267 --------VP----RRSMalLCGqPASVERFARHLYLA-GVPRSQTLADLFLP 306
Cdd:PRK10684 190 trellqqaVPdlasRTVM--TCG-PAPYMDWVEQEVKAlGVTADRFFKEKFFT 239
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
18-83 5.44e-05

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 40.87  E-value: 5.44e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599527   18 NLLDALLAGGIAVPHSCRAGSCHACLVHCLQGEVdDTLPEALDPVRReaGWRLACQCRVLGDLVLQ 83
Cdd:PRK10713  21 SLLAALESHNVAVEYQCREGYCGSCRTRLVAGQV-DWIAEPLAFIQP--GEILPCCCRAKGDIEIE 83
PRK10926 PRK10926
ferredoxin-NADP reductase; Provisional
 100-282 6.08e-05

ferredoxin-NADP reductase; Provisional


Pssm-ID: 182844  Cd Length: 248  Bit Score: 43.53  E-value: 6.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  100 HWLGDVLRLRLE-PERPlrYRAGQHLLLWSD-DG--VARPYSLASLPhEDPWLEFHIDCSAPGAFCDRARRLAPGALLRL 175
Cdd:PRK10926  14 NWTDALFSLTVHaPVDP--FTAGQFTKLGLEiDGerVQRAYSYVNAP-DNPDLEFYLVTVPEGKLSPRLAALKPGDEVQV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527  176 GELRGG--ALRYEPDWQErpLLLMAAGTGLAPLWGILREALRAEHQAPIQLLHLARdhyLASELA------ELAGR-HPQ 246
Cdd:PRK10926  91 VSEAAGffVLDEVPDCET--LWMLATGTAIGPYLSILQEGKDLERFKNLVLVHAAR---YAADLSylplmqELEQRyEGK 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15599527  247 LRVN-LVSAAQLPSAL----------------ADLRLVPRRSMALLCGQPASV 282
Cdd:PRK10926 166 LRIQtVVSRETAPGSLtgrvpaliesgeleaaVGLPMDAETSHVMLCGNPQMV 218
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
 133-220 1.23e-03

Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for the regeneration of methionine from homocysteine, as well as the coversion of methyltetrahydrofolate to tetrahydrofolate. In MSR, electrons are transferred from NADPH to FAD to FMN to cob(II)alamin. MSR resembles proteins of the cytochrome p450 family including nitric oxide synthase, the alpha subunit of sulfite reductase, but contains an extended hinge region. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPORs resemble ferredoxin reductase (FNR) but have a connecting subdomain inserted within the flavin binding region, which helps orient the FMN binding doamin with the FNR module. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99800 [Multi-domain]  Cd Length: 398  Bit Score: 40.00  E-value: 1.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527 133 ARPYSLASLPHEDPW-LEF---HIDCSAPG-------AFCDRARRLAPGALLRLGElrGGALRYEPDWQERPLLLMAAGT 201
Cdd:cd06203 174 PRPYSIASSPLEGPGkLRFifsVVEFPAKGlctswleSLCLSASSHGVKVPFYLRS--SSRFRLPPDDLRRPIIMVGPGT 251

                        90       100
                ....*....|....*....|.
gi 15599527 202 GLAPLWGIL--REALRAEHQA 220
Cdd:cd06203 252 GVAPFLGFLqhREKLKESHTE 272
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
105-185 2.45e-03

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 36.79  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599527   105 VLRLRLE-PERPLRYRAGQHLLL---WSDDGVARPYSLASLPHEDPWLEFHIDCSAPGAFCDRARRLAPGALLrlgELRG 180
Cdd:pfam00970  16 IFRFALPhPDQVLGLPVGQHLFLrlpIDGELVIRSYTPISSDDDKGYLELLVKVYPGGKMSQYLDELKIGDTI---DFKG 92


                  ....*..
gi 15599527   181 --GALRY 185
Cdd:pfam00970  93 plGRFEY 99
Fer2_4 pfam13510
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 9-45 7.26e-03

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.


Pssm-ID: 433268 [Multi-domain]  Cd Length: 82  Bit Score: 34.82  E-value: 7.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 15599527     9 RRLAVAAGSNLLDALLAGGIAVPHSCR----------AGSCHACLVH 45
Cdd:pfam13510  11 RPVTAPEGDTIAAALLANGVRVPRSCKygrprgifcaMGECRNCLVE 57
NuoG COG1034
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ...
 1-52 8.47e-03

NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440657 [Multi-domain]  Cd Length: 453  Bit Score: 37.51  E-value: 8.47e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15599527   1 MPDIRVGERRLAVAAGSNLLDALLAGGIAVPHSC------RAGSCHACLVhclqgEVD 52
Cdd:COG1034   1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCyhpklsIAGACRMCLV-----EVE 53
 
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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