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Conserved domains on  [gi|1720423028|ref|XP_030098539|]
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NADH-cytochrome b5 reductase 2 isoform X5 [Mus musculus]

Protein Classification

cytochrome b5 reductase family protein( domain architecture ID 10153046)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 1-175 3.57e-79

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: 234.77  E-value: 3.57e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYLENMKIGDTILFRGPTGRLFYnepgtlliKANKTSEpekklvhHLGMIAGGTGITPMLQLIRHITKDTSDETRMSL 80
Cdd:cd06183    74 MSQYLHSLKPGDTVEIRGPFGKFEY--------KPNGKVK-------HIGMIAGGTGITPMLQLIRAILKDPEDKTKISL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  81 LFANQTEEDILLRKELEEVATTHHKQFNLWYTLDRPPSDWKYSSGFVSADMIKEHLPP-PGEDTLILVCGPPPLIQAAAH 159
Cdd:cd06183   139 LYANRTEEDILLREELDELAKKHPDRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPPpPSEDTLVLVCGPPPMIEGAVK 218

                         170
                  ....*....|....*.
gi 1720423028 160 PSLEQLSYTKDMIFIY 175
Cdd:cd06183   219 GLLKELGYKKDNVFKF 234
 
Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 1-175 3.57e-79

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: 234.77  E-value: 3.57e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYLENMKIGDTILFRGPTGRLFYnepgtlliKANKTSEpekklvhHLGMIAGGTGITPMLQLIRHITKDTSDETRMSL 80
Cdd:cd06183    74 MSQYLHSLKPGDTVEIRGPFGKFEY--------KPNGKVK-------HIGMIAGGTGITPMLQLIRAILKDPEDKTKISL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  81 LFANQTEEDILLRKELEEVATTHHKQFNLWYTLDRPPSDWKYSSGFVSADMIKEHLPP-PGEDTLILVCGPPPLIQAAAH 159
Cdd:cd06183   139 LYANRTEEDILLREELDELAKKHPDRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPPpPSEDTLVLVCGPPPMIEGAVK 218

                         170
                  ....*....|....*.
gi 1720423028 160 PSLEQLSYTKDMIFIY 175
Cdd:cd06183   219 GLLKELGYKKDNVFKF 234
PLN02252 PLN02252
nitrate reductase [NADPH]
 1-175 3.66e-67

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 219.55  E-value: 3.66e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYLENMKIGDTILFRGPTGRLFYNEPGTLLIKAnktsepEKKLVHHLGMIAGGTGITPMLQLIRHITKDTSDETRMSL 80
Cdd:PLN02252  719 MSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLVNG------KPKFAKKLAMLAGGTGITPMYQVIQAILRDPEDKTEMSL 792

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  81 LFANQTEEDILLRKELEEVATTHHKQFNLWYTLDRP-PSDWKYSSGFVSADMIKEHLPPPGEDTLILVCGPPPLIQAAAH 159
Cdd:PLN02252  793 VYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQVkREGWKYSVGRVTEAMLREHLPEGGDETLALMCGPPPMIEFACQ 872

                         170
                  ....*....|....*.
gi 1720423028 160 PSLEQLSYTKDMIFIY 175
Cdd:PLN02252  873 PNLEKMGYDKDSILVF 888
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 51-159 1.75e-45

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: 145.10  E-value: 1.75e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  51 MIAGGTGITPMLQLIRHITKDTSDETRMSLLFANQTEEDILLRKELEEVATTHHKQFNLWYTLDRPPSDWKYSSGFVSAD 130
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKDPTQVVLVFGNRNEDDILYREELDELAEKHPGRLTVVYVVSRPEAGWTGGKGRVQDA 80

                          90       100
                  ....*....|....*....|....*....
gi 1720423028 131 MIKEHLPPPGEDTLILVCGPPPLIQAAAH 159
Cdd:pfam00175  81 LLEDHLSLPDEETHVYVCGPPGMIKAVRK 109
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
1-174 5.01e-32

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 114.50  E-value: 5.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYL-ENMKIGDTILFRGPTGRLFYNEPgtllikanktsePEKKLVhhlgMIAGGTGITPMLQLIRHItKDTSDETRMS 79
Cdd:COG1018    78 GSNWLhDHLKVGDTLEVSGPRGDFVLDPE------------PARPLL----LIAGGIGITPFLSMLRTL-LARGPFRPVT 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  80 LLFANQTEEDILLRKELEEVAtTHHKQFNLWYTLDRPPSDWkysSGFVSADMIKEHLPPPgEDTLILVCGPPPLIQAAAH 159
Cdd:COG1018   141 LVYGARSPADLAFRDELEALA-ARHPRLRLHPVLSREPAGL---QGRLDAELLAALLPDP-ADAHVYLCGPPPMMEAVRA 215

                         170
                  ....*....|....*
gi 1720423028 160 pSLEQLSYTKDMIFI 174
Cdd:COG1018   216 -ALAELGVPEERIHF 229
 
Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 1-175 3.57e-79

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: 234.77  E-value: 3.57e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYLENMKIGDTILFRGPTGRLFYnepgtlliKANKTSEpekklvhHLGMIAGGTGITPMLQLIRHITKDTSDETRMSL 80
Cdd:cd06183    74 MSQYLHSLKPGDTVEIRGPFGKFEY--------KPNGKVK-------HIGMIAGGTGITPMLQLIRAILKDPEDKTKISL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  81 LFANQTEEDILLRKELEEVATTHHKQFNLWYTLDRPPSDWKYSSGFVSADMIKEHLPP-PGEDTLILVCGPPPLIQAAAH 159
Cdd:cd06183   139 LYANRTEEDILLREELDELAKKHPDRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPPpPSEDTLVLVCGPPPMIEGAVK 218

                         170
                  ....*....|....*.
gi 1720423028 160 PSLEQLSYTKDMIFIY 175
Cdd:cd06183   219 GLLKELGYKKDNVFKF 234
PLN02252 PLN02252
nitrate reductase [NADPH]
 1-175 3.66e-67

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 219.55  E-value: 3.66e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYLENMKIGDTILFRGPTGRLFYNEPGTLLIKAnktsepEKKLVHHLGMIAGGTGITPMLQLIRHITKDTSDETRMSL 80
Cdd:PLN02252  719 MSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLVNG------KPKFAKKLAMLAGGTGITPMYQVIQAILRDPEDKTEMSL 792

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  81 LFANQTEEDILLRKELEEVATTHHKQFNLWYTLDRP-PSDWKYSSGFVSADMIKEHLPPPGEDTLILVCGPPPLIQAAAH 159
Cdd:PLN02252  793 VYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQVkREGWKYSVGRVTEAMLREHLPEGGDETLALMCGPPPMIEFACQ 872

                         170
                  ....*....|....*.
gi 1720423028 160 PSLEQLSYTKDMIFIY 175
Cdd:PLN02252  873 PNLEKMGYDKDSILVF 888
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 1-175 1.18e-62

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 195.05  E-value: 1.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYLENMKIGDTILFRGPTGRLFYNEPGTLLIKANKTSEPEKKlVHHLGMIAGGTGITPMLQLIRHITKDTSDETRMSL 80
Cdd:PTZ00319  122 LSQHLYHMKLGDKIEMRGPVGKFEYLGNGTYTVHKGKGGLKTMH-VDAFAMIAGGTGITPMLQIIHAIKKNKEDRTKVFL 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  81 LFANQTEEDILLRKELEEVAttHHKQFNLWYTLDRP-PSDWKYSSGFVSADMIKEHLPPPG------EDTLILVCGPPPL 153
Cdd:PTZ00319  201 VYANQTEDDILLRKELDEAA--KDPRFHVWYTLDREaTPEWKYGTGYVDEEMLRAHLPVPDpqnsgiKKVMALMCGPPPM 278

                         170       180
                  ....*....|....*....|..
gi 1720423028 154 IQAAAHPSLEQLSYTKDMIFIY 175
Cdd:PTZ00319  279 LQMAVKPNLEKIGYTADNMFTF 300
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 51-159 1.75e-45

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: 145.10  E-value: 1.75e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  51 MIAGGTGITPMLQLIRHITKDTSDETRMSLLFANQTEEDILLRKELEEVATTHHKQFNLWYTLDRPPSDWKYSSGFVSAD 130
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKDPTQVVLVFGNRNEDDILYREELDELAEKHPGRLTVVYVVSRPEAGWTGGKGRVQDA 80

                          90       100
                  ....*....|....*....|....*....
gi 1720423028 131 MIKEHLPPPGEDTLILVCGPPPLIQAAAH 159
Cdd:pfam00175  81 LLEDHLSLPDEETHVYVCGPPGMIKAVRK 109
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
 1-158 1.39e-35

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 126.19  E-value: 1.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYLENMKIGDTILFRGPTGRLFYnepgtlliKANKTSepekklvhHLGMIAGGTGITPMLQLIRHITKD-----TSDE 75
Cdd:PTZ00274  130 MTNHLFGMHVGDKLLFRSVTFKIQY--------RPNRWK--------HVGMIAGGTGFTPMLQIIRHSLTEpwdsgEVDR 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  76 TRMSLLFANQTEEDILLRKELEEVATTHHKQFNLWYTLDRP--PSDWKYSSGFVSADMIKEHLPPPGEDT-LILVCGPPP 152
Cdd:PTZ00274  194 TKLSFLFCNRTERHILLKGLFDDLARRYSNRFKVYYTIDQAvePDKWNHFLGYVTKEMVRRTMPAPEEKKkIIMLCGPDQ 273


                  ....*.
gi 1720423028 153 LIQAAA 158
Cdd:PTZ00274  274 LLNHVA 279
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
1-174 5.01e-32

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 114.50  E-value: 5.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYL-ENMKIGDTILFRGPTGRLFYNEPgtllikanktsePEKKLVhhlgMIAGGTGITPMLQLIRHItKDTSDETRMS 79
Cdd:COG1018    78 GSNWLhDHLKVGDTLEVSGPRGDFVLDPE------------PARPLL----LIAGGIGITPFLSMLRTL-LARGPFRPVT 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  80 LLFANQTEEDILLRKELEEVAtTHHKQFNLWYTLDRPPSDWkysSGFVSADMIKEHLPPPgEDTLILVCGPPPLIQAAAH 159
Cdd:COG1018   141 LVYGARSPADLAFRDELEALA-ARHPRLRLHPVLSREPAGL---QGRLDAELLAALLPDP-ADAHVYLCGPPPMMEAVRA 215

                         170
                  ....*....|....*
gi 1720423028 160 pSLEQLSYTKDMIFI 174
Cdd:COG1018   216 -ALAELGVPEERIHF 229
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 1-158 1.89e-28

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: 105.22  E-value: 1.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYLENMKIGDTILFRGPTGRLFynepgtllikanKTSEPEKKLVhhlgMIAGGTGITPMLQLIRHITKDtSDETRMSL 80
Cdd:cd00322    68 FSAWLHDLKPGDEVEVSGPGGDFF------------LPLEESGPVV----LIAGGIGITPFRSMLRHLAAD-KPGGEITL 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720423028  81 LFANQTEEDILLRKELEEVATTHHKQFnLWYTLDRPPSDWKYSSGFVSADMIKEHLPPPGEDTLILVCGPPPLIQAAA 158
Cdd:cd00322   131 LYGARTPADLLFLDELEELAKEGPNFR-LVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVR 207
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 1-173 3.55e-27

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: 102.69  E-value: 3.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYLENMKIGDTILFRGPTGRLFynepgtllikanktsePEKKLVHH-LGMIAGGTGITPMLQLIRHITKDTSDETRMS 79
Cdd:cd06221    68 VTEALHELKPGDTVGLRGPFGNGF----------------PVEEMKGKdLLLVAGGLGLAPLRSLINYILDNREDYGKVT 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  80 LLFANQTEEDILLRKELEEVATTHHkqFNLWYTLDRPPSDWKYSSGFVSaDMIKEHLPPPgEDTLILVCGPPPLIQAAAh 159
Cdd:cd06221   132 LLYGARTPEDLLFKEELKEWAKRSD--VEVILTVDRAEEGWTGNVGLVT-DLLPELTLDP-DNTVAIVCGPPIMMRFVA- 206

                         170
                  ....*....|....
gi 1720423028 160 PSLEQLSYTKDMIF 173
Cdd:cd06221   207 KELLKLGVPEEQIW 220
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 9-158 5.62e-27

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


Pssm-ID: 99813 [Multi-domain]  Cd Length: 235  Bit Score: 101.57  E-value: 5.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   9 KIGDTILFRGPTGRLFYNEPGtllikanktSEPekkLVhhlgMIAGGTGITPMLQLIRHITkDTSDETRMSLLFANQTEE 88
Cdd:cd06217    86 KVGDLLEVRGPIGTFTWNPLH---------GDP---VV----LLAGGSGIVPLMSMIRYRR-DLGWPVPFRLLYSARTAE 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720423028  89 DILLRKELEEVATTHhkqFNLWYTL---DRPPSDWKYSSGFVSADMIkEHLPPPGEDTLILVCGPPPLIQAAA 158
Cdd:cd06217   149 DVIFRDELEQLARRH---PNLHVTEaltRAAPADWLGPAGRITADLI-AELVPPLAGRRVYVCGPPAFVEAAT 217
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 6-159 5.74e-24

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: 93.76  E-value: 5.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   6 ENMKIGDTILFRGPTGRLFYnepgtllikanktsePEKKLVHHLGMIAGGTGITPMLQLIRHITKdTSDETRMSLLFANQ 85
Cdd:cd06214    83 DELKAGDTLEVMPPAGRFTL---------------PPLPGARHYVLFAAGSGITPVLSILKTALA-REPASRVTLVYGNR 146

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720423028  86 TEEDILLRKELEEVATTHHKQFNLWYTLDRPPSDWKYSSGFVSADMIKE---HLPPPGEDTLILVCGPPPLIQAAAH 159
Cdd:cd06214   147 TEASVIFREELADLKARYPDRLTVIHVLSREQGDPDLLRGRLDAAKLNAllkNLLDATEFDEAFLCGPEPMMDAVEA 223
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 1-158 3.22e-23

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 91.85  E-value: 3.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYLENMKIGDTILFRGPTGRLFynepgtllikanKTSEPEKKLVhhlgMIAGGTGITPMLQLIRHITKdtsDETRMSL 80
Cdd:COG0543    67 GTRALAELKPGDELDVRGPLGNGF------------PLEDSGRPVL----LVAGGTGLAPLRSLAEALLA---RGRRVTL 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720423028  81 LFANQTEEDILLRKELEEVAtthhkQFNLWYTLDRppsDWKYSSGFVsADMIKEHLpPPGEDTLILVCGPPPLIQAAA 158
Cdd:COG0543   128 YLGARTPEDLYLLDELEALA-----DFRVVVTTDD---GWYGRKGFV-TDALKELL-AEDSGDDVYACGPPPMMKAVA 195
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
2-159 1.04e-21

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 90.72  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   2 TQYLENMKIGDTILFRGPTGRLFYNEPGTllikanktsepEKKLVhhlgMIAGGTGITPMLQLIRHITKDTSDETRMSLL 81
Cdd:COG4097   289 TRRLGRLKPGTRVYVEGPYGRFTFDRRDT-----------APRQV----WIAGGIGITPFLALLRALAARPGDQRPVDLF 353

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720423028  82 FANQTEEDILLRKELEEVAtTHHKQFNLWYTLDRPpsdwkysSGFVSADMIKEHLPPPgEDTLILVCGPPPLIQAAAH 159
Cdd:COG4097   354 YCVRDEEDAPFLEELRALA-ARLAGLRLHLVVSDE-------DGRLTAERLRRLVPDL-AEADVFFCGPPGMMDALRR 422
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 43-172 2.12e-21

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 90.22  E-value: 2.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   43 KKLVHHLGMIAGGTGITPMLQLIRHITK----DTSDETRmsLLFANQTEEDILLRKELEEVATTHHKQFNLWYTLDRPPS 118
Cdd:PTZ00306  1028 GHVIRKLALIAGGTGVAPMLQIIRAALKkpyvDSIESIR--LIYAAEDVSELTYRELLESYRKENPGKFKCHFVLNNPPE 1105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720423028  119 DWKYSSGFVSADMIKEHLPPPGEDTLILVCGpPPLIQAAAHPSLEQLSYTKDMI 172
Cdd:PTZ00306  1106 GWTDGVGFVDRALLQSALQPPSKDLLVAICG-PPVMQRAVKADLLALGYNMELV 1158
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 2-157 6.42e-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 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: 83.02  E-value: 6.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   2 TQYL-ENMKIGDTILFRGPTGRlFYNEPGtllikanktsePEKKLVhhlgMIAGGTGITPMLQLIRHITkDTSDETRMSL 80
Cdd:cd06215    74 SNWLhDNLKVGDELWASGPAGE-FTLIDH-----------PADKLL----LLSAGSGITPMMSMARWLL-DTRPDADIVF 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720423028  81 LFANQTEEDILLRKELEEVAtTHHKQFNLWYTLDRP-PSDWKYSSGFVSADMIKEHLPPPGEDTlILVCGPPPLIQAA 157
Cdd:cd06215   137 IHSARSPADIIFADELEELA-RRHPNFRLHLILEQPaPGAWGGYRGRLNAELLALLVPDLKERT-VFVCGPAGFMKAV 212
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 1-157 1.20e-17

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: 77.26  E-value: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYL-ENMKIGDTILFRGPTGRLFYNEPgtllikanktsEPEKKLvhhlgMIAGGTGITPMLQLIRHItKDTSDETRMS 79
Cdd:cd06216    92 VSNWLvNHLAPGDVVELSQPQGDFVLPDP-----------LPPRLL-----LIAAGSGITPVMSMLRTL-LARGPTADVV 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720423028  80 LLFANQTEEDILLRKELEEVATTH-HKQFNLWYTLDRPpsdwkysSGFVSADMIKEHlPPPGEDTLILVCGPPPLIQAA 157
Cdd:cd06216   155 LLYYARTREDVIFADELRALAAQHpNLRLHLLYTREEL-------DGRLSAAHLDAV-VPDLADRQVYACGPPGFLDAA 225
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 4-173 2.35e-17

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: 76.44  E-value: 2.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   4 YL-ENMKIGDTILFRGPTGRLFYNEpgtllikanktsEPEKKLVhhlgMIAGGTGITPMLQLIRHITKDTSDeTRMSLLF 82
Cdd:cd06184    86 YLhDNVKVGDVLEVSAPAGDFVLDE------------ASDRPLV----LISAGVGITPMLSMLEALAAEGPG-RPVTFIH 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  83 ANQTEEDILLRKELEEVATTHHK-QFNLWYtlDRPPSDWKY----SSGFVSADMIKEHLPPPgeDTLILVCGPPPLIQAA 157
Cdd:cd06184   149 AARNSAVHAFRDELEELAARLPNlKLHVFY--SEPEAGDREedydHAGRIDLALLRELLLPA--DADFYLCGPVPFMQAV 224

                         170
                  ....*....|....*.
gi 1720423028 158 AHpSLEQLSYTKDMIF 173
Cdd:cd06184   225 RE-GLKALGVPAERIH 239
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 2-156 1.66e-16

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: 73.81  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   2 TQYLENMKIGDTILFRGPTGRLFYNEPGTLlikanktsepekklvhhlgmIAGGTGITPMLQLIRHITKDTSDETRmSLL 81
Cdd:cd06196    75 TEQLGRLQPGDTLLIEDPWGAIEYKGPGVF--------------------IAGGAGITPFIAILRDLAAKGKLEGN-TLI 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720423028  82 FANQTEEDILLRKELEevattHHKQFNLWYTLDRPPsDWKYSSGFVSADMIKEHLPPPGEDtlILVCGPPPLIQA 156
Cdd:cd06196   134 FANKTEKDIILKDELE-----KMLGLKFINVVTDEK-DPGYAHGRIDKAFLKQHVTDFNQH--FYVCGPPPMEEA 200
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 6-158 3.89e-16

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


Pssm-ID: 99788 [Multi-domain]  Cd Length: 231  Bit Score: 72.94  E-value: 3.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   6 ENMKIGDTILFRGPTGRLFYnepgtllikanKTSEPEKKLvhhlgMIAGGTGITPMLQLIRhITKDTSDETRMSLLFANQ 85
Cdd:cd06191    78 EHIQPGMTVEVMGPQGHFVY-----------QPQPPGRYL-----LVAAGSGITPLMAMIR-ATLQTAPESDFTLIHSAR 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720423028  86 TEEDILLRKELEEVATTHHK-QFNLWYTLDRPPSDWKYSSGFVSADMIKEHLPPPGEDTlILVCGPPPLIQAAA 158
Cdd:cd06191   141 TPADMIFAQELRELADKPQRlRLLCIFTRETLDSDLLHGRIDGEQSLGAALIPDRLERE-AFICGPAGMMDAVE 213
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 4-157 4.76e-16

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: 72.76  E-value: 4.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   4 YLEN-MKIGDTILFRGPTGR--LFYNEPGTLlikanktsepekklvhhlGMIAGGTGITPMLQLIRHItKDTSDETRMSL 80
Cdd:cd06210    81 YLETrAKVGQRLNLRGPLGAfgLRENGLRPR------------------WFVAGGTGLAPLLSMLRRM-AEWGEPQEARL 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720423028  81 LFANQTEEDILLRKELEEVATTHhKQFNLWYTLDRPPSDWKYSSGFVsADMIKEHLPPPGEDTLILVCGPPPLIQAA 157
Cdd:cd06210   142 FFGVNTEAELFYLDELKRLADSL-PNLTVRICVWRPGGEWEGYRGTV-VDALREDLASSDAKPDIYLCGPPGMVDAA 216
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 1-173 5.94e-16

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


Pssm-ID: 99805 [Multi-domain]  Cd Length: 228  Bit Score: 72.24  E-value: 5.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYLENM-KIGDTILFRGPTGRlFYnepgtllikankTSEPEKKLVhhlgMIAGGTGITPMLQLIRHITKDTSDEtRMS 79
Cdd:cd06209    73 MSSYLRDRaQPGDRLTLTGPLGS-FY------------LREVKRPLL----MLAGGTGLAPFLSMLDVLAEDGSAH-PVH 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  80 LLFANQTEEDILlrkELEEVATTHHKQFNLWY--TLDRPPSdWKYSSGFVSADMIKEHLppPGEDTLILVCGPPPLIQAA 157
Cdd:cd06209   135 LVYGVTRDADLV---ELDRLEALAERLPGFSFrtVVADPDS-WHPRKGYVTDHLEAEDL--NDGDVDVYLCGPPPMVDAV 208

                         170
                  ....*....|....*.
gi 1720423028 158 AHpSLEQLSYTKDMIF 173
Cdd:cd06209   209 RS-WLDEQGIEPANFY 223
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 1-157 8.60e-16

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: 71.90  E-value: 8.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYL-ENMKIGDTILFRGPTGRLFYNEpgtllikanktsEPEKKLVhhlgMIAGGTGITPMLQLIRHITKDTSDETR-M 78
Cdd:cd06190    67 ASNALfDNLEPGDELELDGPYGLAYLRP------------DEDRDIV----CIAGGSGLAPMLSILRGAARSPYLSDRpV 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  79 SLLFANQTEEDILLRKELEEVAtthHKQFNLWYTL---DRPPSD---WKYSSGFVsADMIKEHLPPPGEDTLILVCGPPP 152
Cdd:cd06190   131 DLFYGGRTPSDLCALDELSALV---ALGARLRVTPavsDAGSGSaagWDGPTGFV-HEVVEATLGDRLAEFEFYFAGPPP 206


                  ....*
gi 1720423028 153 LIQAA 157
Cdd:cd06190   207 MVDAV 211
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 1-173 5.77e-15

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


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 71.43  E-value: 5.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYLENMKIGDTILFRGPTGRLFYNEpgtllikankTSEPekkLVhhlgMIAGGTGITPMLQLIRHITKDTSDETRMSL 80
Cdd:COG2871   233 GSSYIFSLKPGDKVTISGPYGEFFLRD----------SDRE---MV----FIGGGAGMAPLRSHIFDLLERGKTDRKITF 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  81 LFANQTEEDILLRKELEEVATTHhkqFNLWYT--LDRPP--SDWKYSSGFVSADMIKEHL--PPPGEDTLILVCGPPPLI 154
Cdd:COG2871   296 WYGARSLRELFYLEEFRELEKEH---PNFKFHpaLSEPLpeDNWDGETGFIHEVLYENYLkdHPAPEDCEAYLCGPPPMI 372

                         170
                  ....*....|....*....
gi 1720423028 155 QAAAhPSLEQLSYTKDMIF 173
Cdd:COG2871   373 DAVI-KMLDDLGVEEENIY 390
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 6-173 2.41e-14

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: 68.13  E-value: 2.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   6 ENMKIGDTILFRGPTGRLFYNEPGTLLIKanktsepekklvhhlgMIAGGTGITPMLQLIRHITkDTSDETRMSLLFANQ 85
Cdd:cd06212    79 DGLAVGDPVTVTGPYGTCTLRESRDRPIV----------------LIGGGSGMAPLLSLLRDMA-ASGSDRPVRFFYGAR 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  86 TEEDILLRKELEEVATThHKQFNLWYTLDRPPSD--WKYSSGFVSaDMIKEHLPPPgEDTLILVCGPPPLIQAAAhPSLE 163
Cdd:cd06212   142 TARDLFYLEEIAALGEK-IPDFTFIPALSESPDDegWSGETGLVT-EVVQRNEATL-AGCDVYLCGPPPMIDAAL-PVLE 217

                         170
                  ....*....|
gi 1720423028 164 QLSYTKDMIF 173
Cdd:cd06212   218 MSGVPPDQIF 227
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 9-157 3.07e-14

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: 67.62  E-value: 3.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   9 KIGDTILFRGPTGRLF--YNEPGTLLikanktsepekklvhhlgMIAGGTGITPMLQLIRHITKdTSDETRMSLLFANQT 86
Cdd:cd06187    77 KVGDRVRLSGPYGTFYlrRDHDRPVL------------------CIAGGTGLAPLRAIVEDALR-RGEPRPVHLFFGART 137

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720423028  87 EEDILLRKELEEVATTHHkqfNLWYT--LDRPPSDWKYSSGFVsADMIKEHLpPPGEDTLILVCGPPPLIQAA 157
Cdd:cd06187   138 ERDLYDLEGLLALAARHP---WLRVVpvVSHEEGAWTGRRGLV-TDVVGRDG-PDWADHDIYICGPPAMVDAT 205
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 2-157 4.28e-14

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: 67.73  E-value: 4.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   2 TQYL-ENMKIGDTILFRGPTGRLFYNEpgtllikanktSEPEKKLvhhlgMIAGGTGITPmlqlIRHITKD--TSDETR- 77
Cdd:cd06211    80 TTYVhKQLKEGDELEISGPYGDFFVRD-----------SDQRPII-----FIAGGSGLSS----PRSMILDllERGDTRk 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  78 MSLLFANQTEEDILLRKELEEVATTHHKqFNLWYTLDRPP--SDWKYSSGFVSaDMIKEHLPPPGEDTLILVCGPPPLIQ 155
Cdd:cd06211   140 ITLFFGARTRAELYYLDEFEALEKDHPN-FKYVPALSREPpeSNWKGFTGFVH-DAAKKHFKNDFRGHKAYLCGPPPMID 217


                  ..
gi 1720423028 156 AA 157
Cdd:cd06211   218 AC 219
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 1-173 4.24e-13

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: 65.40  E-value: 4.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYLENMKIGDTILFRGPTGRLFynepgtllikankTSEPEKKLVhhlgMIAGGTGITPMLQLIRHITKDTSDETRMSL 80
Cdd:cd06188   122 GSSYIFNLKPGDKVTASGPFGEFF-------------IKDTDREMV----FIGGGAGMAPLRSHIFHLLKTLKSKRKISF 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  81 LFANQTEEDILLRKELEEVAtTHHKQFNLWYTLDRP-PSD-WKYSSGFVS---ADMIKEHLPPPgEDTLILVCGPPPLIQ 155
Cdd:cd06188   185 WYGARSLKELFYQEEFEALE-KEFPNFKYHPVLSEPqPEDnWDGYTGFIHqvlLENYLKKHPAP-EDIEFYLCGPPPMNS 262

                         170
                  ....*....|....*...
gi 1720423028 156 AAAHpSLEQLSYTKDMIF 173
Cdd:cd06188   263 AVIK-MLDDLGVPRENIA 279
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 1-157 5.46e-13

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: 64.49  E-value: 5.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQY-LENMKIGDTILFRGPTGRLFYNEpgtllikanktsEPEKKLVhhlgMIAGGTGITPMLQLIRHITKdTSDETRMS 79
Cdd:cd06189    68 FSDYvFEELKENGLVRIEGPLGDFFLRE------------DSDRPLI----LIAGGTGFAPIKSILEHLLA-QGSKRPIH 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  80 LLFANQTEEDILLRKELEEVATTHHkqfNLWYT--LDRPPSDWKYSSGFVsADMIKEHLPPPgEDTLILVCGPPPLIQAA 157
Cdd:cd06189   131 LYWGARTEEDLYLDELLEAWAEAHP---NFTYVpvLSEPEEGWQGRTGLV-HEAVLEDFPDL-SDFDVYACGSPEMVYAA 205
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 1-151 2.40e-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: 62.97  E-value: 2.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYLENMKIGDTI-LFRGPTGRLfynepgTLlikaNKTSEPEkklvhHLGMIAGGTGITPMLQLIRHITKDTsDETRMS 79
Cdd:cd06195    70 LTPRLFKLKPGDTIyVGKKPTGFL------TL----DEVPPGK-----RLWLLATGTGIAPFLSMLRDLEIWE-RFDKIV 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720423028  80 LLFANQTEEDILLRKELEEVATTHHKQFNLWYTLDRPPSDWKYS---SGFVSADMIKEH--LPPPGEDTLILVCGPP 151
Cdd:cd06195   134 LVHGVRYAEELAYQDEIEALAKQYNGKFRYVPIVSREKENGALTgriPDLIESGELEEHagLPLDPETSHVMLCGNP 210
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 52-156 2.41e-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: 62.27  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  52 IAGGTGITPMLQLIRHiTKDTSDETRMSLLFANQTEEDILLRKELEEVATTHHKQFNLwytLDRPPSDWkyssgfVSADM 131
Cdd:cd06198   101 IAGGIGITPFLALLEA-LAARGDARPVTLFYCVRDPEDAVFLDELRALAAAAGVVLHV---IDSPSDGR------LTLEQ 170

                          90       100
                  ....*....|....*....|....*
gi 1720423028 132 IKEHLPPPGEDTLILVCGPPPLIQA 156
Cdd:cd06198   171 LVRALVPDLADADVWFCGPPGMADA 195
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 11-157 2.74e-11

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: 59.63  E-value: 2.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  11 GDTILFRGPTGRlFYNEPGTllikanktsepekklvHHLGMIAGGTGITPMLQLIRHITKDtsDETR-MSLLFANQTEED 89
Cdd:cd06213    82 GERLTVRGPFGD-FWLRPGD----------------APILCIAGGSGLAPILAILEQARAA--GTKRdVTLLFGARTQRD 142

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  90 ILLRKELEEVATTHHKQFNLWYTLDRPP--SDWKYSSGFVSaDMIKEHLPPPGEDTLilvCGPPPLIQAA 157
Cdd:cd06213   143 LYALDEIAAIAARWRGRFRFIPVLSEEPadSSWKGARGLVT-EHIAEVLLAATEAYL---CGPPAMIDAA 208
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 2-156 1.08e-10

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 58.35  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   2 TQYLENMKIGDTILFRGPTGRLFynepgtllikaNKTSEPEKKLVhhlgmIAGGTGITPMLQLIRHITKDTSDETrmSLL 81
Cdd:PRK00054   74 TKKLSKLKEGDELDIRGPLGNGF-----------DLEEIGGKVLL-----VGGGIGVAPLYELAKELKKKGVEVT--TVL 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720423028  82 FAnQTEEDILLRKELEEVATTHhkqfnlwYTLDrppsDWKY-SSGFVSaDMIKEHLPppgEDTLILVCGPPPLIQA 156
Cdd:PRK00054  136 GA-RTKDEVIFEEEFAKVGDVY-------VTTD----DGSYgFKGFVT-DVLDELDS---EYDAIYSCGPEIMMKK 195
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 2-158 1.16e-10

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


Pssm-ID: 99814 [Multi-domain]  Cd Length: 246  Bit Score: 58.33  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   2 TQYLENMKIGDTILFRGPTGRLFynepgtllikanKTSEPEKKLVhhlgMIAGGTGITPMLQLIRHITKdtsDETRMSLL 81
Cdd:cd06218    70 TRLLSELKAGDELDVLGPLGNGF------------DLPDDDGKVL----LVGGGIGIAPLLFLAKQLAE---RGIKVTVL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  82 FANQTEEDILLRKELEEVATTHHkqfnlWYTLDrppsdwkySS----GFVSaDMIKEHLPPPGEDtLILVCGPPPLIQAA 157
Cdd:cd06218   131 LGFRSADDLFLVEEFEALGAEVY-----VATDD--------GSagtkGFVT-DLLKELLAEARPD-VVYACGPEPMLKAV 195


                  .
gi 1720423028 158 A 158
Cdd:cd06218   196 A 196
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 2-153 2.22e-10

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


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 57.26  E-value: 2.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   2 TQYLENMKIGDTILFRGPTGRLFYNEPGTLLIkanktsepekklvhhlgmIAGGTGITPMLQLIRHITKdtsdETRMSLL 81
Cdd:cd06220    62 TSALHDLKEGDKLGIRGPYGNGFELVGGKVLL------------------IGGGIGIAPLAPLAERLKK----AADVTVL 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720423028  82 FANQTEEDILLRKELEEVAtthhkqfNLWYTLDrppsDWKYS-SGFVsADMIKEHLppPGEDTLILVCGPPPL 153
Cdd:cd06220   120 LGARTKEELLFLDRLRKSD-------ELIVTTD----DGSYGfKGFV-TDLLKELD--LEEYDAIYVCGPEIM 178
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 1-174 5.51e-10

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 56.74  E-value: 5.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYLENMKIGDTILFRGPTGRLFynepgtllikanktseP-EKKLVHHLGMIAGGTGITPMLQLIRHITKDTSDETRMS 79
Cdd:PRK08345   78 VTTVIHRLKEGDIVGVRGPYGNGF----------------PvDEMEGMDLLLIAGGLGMAPLRSVLLYAMDNRWKYGNIT 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  80 LLFANQTEEDILLRKELEEVaTTHHKQFNLWYTLDRPPsDW------------KYSSGFVSADMIKEHLPPpgEDTLILV 147
Cdd:PRK08345  142 LIYGAKYYEDLLFYDELIKD-LAEAENVKIIQSVTRDP-EWpgchglpqgfieRVCKGVVTDLFREANTDP--KNTYAAI 217

                         170       180
                  ....*....|....*....|....*..
gi 1720423028 148 CGPPPLIQAAAHpSLEQLSYTKDMIFI 174
Cdd:PRK08345  218 CGPPVMYKFVFK-ELINRGYRPERIYV 243
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 1-158 9.01e-10

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: 55.35  E-value: 9.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYL-ENMKIGDTILFRGPTGRLFYnepgtllikanKTSEPEKKLVhhlgMIAGGTGITPMLQLIRH-ITKDTSDEtrM 78
Cdd:cd06194    66 FSGWLgEEARPGHALRLQGPFGQAFY-----------RPEYGEGPLL----LVGAGTGLAPLWGIARAaLRQGHQGE--I 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  79 SLLFANQTEEDILLRKELEEVATTHhKQFNLWYTLDRPPSdwkySSGFVSADMIKEHLPPPGEDTLILVCGPPPLIQAAA 158
Cdd:cd06194   129 RLVHGARDPDDLYLHPALLWLAREH-PNFRYIPCVSEGSQ----GDPRVRAGRIAAHLPPLTRDDVVYLCGAPSMVNAVR 203
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
1-156 8.43e-09

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 53.59  E-value: 8.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYL-ENMKIGDTILFRGPTGRlFYnepgtllikankTSEPEKKLVhhlgMIAGGTGITPMLQLIRHITKDTSDETrMS 79
Cdd:PRK11872  180 MSNYLrERCQVGDEILFEAPLGA-FY------------LREVERPLV----FVAGGTGLSAFLGMLDELAEQGCSPP-VH 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720423028  80 LLFANQTEEDILlrkELEEVATTHHKQFNLWYT--LDRPPSDWKYSSGFVSADMIKEHLPPPGEDtlILVCGPPPLIQA 156
Cdd:PRK11872  242 LYYGVRHAADLC---ELQRLAAYAERLPNFRYHpvVSKASADWQGKRGYIHEHFDKAQLRDQAFD--MYLCGPPPMVEA 315
PRK13289 PRK13289
NO-inducible flavohemoprotein;
4-158 2.31e-08

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 52.11  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   4 YL-ENMKIGDTILFRGPTGRLFYNEpgtllikanktsEPEKKLVhhlgMIAGGTGITPMLQLIRHITkdtsdetrmsllf 82
Cdd:PRK13289  234 YLhDHVNVGDVLELAAPAGDFFLDV------------ASDTPVV----LISGGVGITPMLSMLETLA------------- 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  83 ANQTEEDIL------------LRKELEEVATTHhKQFNL--WYT----LDRPPSDWKYSsGFVSADMIKEHLPPPGEDtl 144
Cdd:PRK13289  285 AQQPKRPVHfihaarnggvhaFRDEVEALAARH-PNLKAhtWYRepteQDRAGEDFDSE-GLMDLEWLEAWLPDPDAD-- 360

                         170
                  ....*....|....
gi 1720423028 145 ILVCGPPPLIQAAA 158
Cdd:PRK13289  361 FYFCGPVPFMQFVA 374
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 4-115 2.67e-08

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: 51.94  E-value: 2.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   4 YLENMKIGDTILFRGPTGRLFY--NEPGTLLIkanktsepekklvhhlgMIAGGTGITPMLQLIRHITKDTSDETR---- 77
Cdd:cd06208   108 YLCDLKPGDDVQITGPVGKTMLlpEDPNATLI-----------------MIATGTGIAPFRSFLRRLFREKHADYKftgl 170

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1720423028  78 MSLLFANQTEEDILLRKELEEVATTHHKQFNLWYTLDR 115
Cdd:cd06208   171 AWLFFGVPNSDSLLYDDELEKYPKQYPDNFRIDYAFSR 208
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 2-159 5.64e-08

FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 50.79  E-value: 5.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   2 TQYLENMKIGDTILFRGPTGRlfynepGTLLIKANKTSepekkLVhhlgmIAGGTGITPMLQLIRhitKDTSDETRMSLL 81
Cdd:cd06192    69 TKLIAELKPGEKLDVMGPLGN------GFEGPKKGGTV-----LL-----VAGGIGLAPLLPIAK---KLAANGNKVTVL 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720423028  82 FANQTEEDILLRKELEEVATthhkqfNLWYTLDRPPSDWKYSSGFVSADMIKEhlpppgEDTLILVCGPPPLIQAAAH 159
Cdd:cd06192   130 AGAKKAKEEFLDEYFELPAD------VEIWTTDDGELGLEGKVTDSDKPIPLE------DVDRIIVAGSDIMMKAVVE 195
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
1-25 6.39e-07

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 45.65  E-value: 6.39e-07
                          10        20
                  ....*....|....*....|....*
gi 1720423028   1 MTQYLENMKIGDTILFRGPTGRLFY 25
Cdd:pfam00970  75 MSQYLDELKIGDTIDFKGPLGRFEY 99
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 6-157 2.36e-05

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: 42.86  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   6 ENMKIGDTILFRGPTGrLFynePgtlLIKANKtsepekklvHHLgMIAGGTGITPMLQLIRHITKdtsDETRMSLLFANQ 85
Cdd:cd06185    75 ELLRVGDELEVSAPRN-LF---P---LDEAAR---------RHL-LIAGGIGITPILSMARALAA---RGADFELHYAGR 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720423028  86 TEEDILLRKELEEVattHHKQFNLWYTLDRPPSDwkyssgfvsadmIKEHLPPPGEDTLILVCGPPPLIQAA 157
Cdd:cd06185   135 SREDAAFLDELAAL---PGDRVHLHFDDEGGRLD------------LAALLAAPPAGTHVYVCGPEGMMDAV 191
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 51-173 2.65e-04

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 40.46  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  51 MIAGGTGITPMLQLIRHITKDtSDETRMSLLFANQTEEDILLRKELEEVATThHKQFNLWYTLDRPPSDwKYSSGFVSAD 130
Cdd:PRK10684  116 LLAAGCGVTPIMSMRRWLLKN-RPQADVQVIFNVRTPQDVIFADEWRQLKQR-YPQLNLTLVAENNATE-GFIAGRLTRE 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720423028 131 MIKEHLPPPGEDTlILVCGPPPLIQAAAHPSLeQLSYTKDMIF 173
Cdd:PRK10684  193 LLQQAVPDLASRT-VMTCGPAPYMDWVEQEVK-ALGVTADRFF 233
PRK05802 PRK05802
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
2-67 4.79e-04

sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;


Pssm-ID: 235613 [Multi-domain]  Cd Length: 320  Bit Score: 39.58  E-value: 4.79e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720423028   2 TQYLENMKIGDTILFRGPtgrlFYNepGTLLIKANKTSEPEKKLVhhlgmIAGGTGITPMLQLIRH 67
Cdd:PRK05802  139 TKKIAKLNKGDEILLRGP----YWN--GILGLKNIKSTKNGKSLV-----IARGIGQAPGVPVIKK 193
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 1-157 5.13e-04

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 39.47  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028   1 MTQYL-ENMKIGDTILFRGPTGRLFYNEpgtllikanktsEPEKKLVhhlgMIAGGTGITPMLQLIRHItKDTSDETRMS 79
Cdd:PRK07609  174 FTDHVfGALKERDILRIEGPLGTFFLRE------------DSDKPIV----LLASGTGFAPIKSIVEHL-RAKGIQRPVT 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720423028  80 LLFANQTEEDILLRKELEEVATTHHkqfNLWYTL----DRPPSDWKYSSGFVSADMIKEHlpPPGEDTLILVCGPPPLIQ 155
Cdd:PRK07609  237 LYWGARRPEDLYLSALAEQWAEELP---NFRYVPvvsdALDDDAWTGRTGFVHQAVLEDF--PDLSGHQVYACGSPVMVY 311


                  ..
gi 1720423028 156 AA 157
Cdd:PRK07609  312 AA 313
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 49-109 7.43e-04

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 39.06  E-value: 7.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720423028  49 LGMIAGGTGITPMLQLIRHITKDTSDE----TRMSLLFANQTEEDI-LLRKELEEVATTHHKQFNL 109
Cdd:PLN02844  426 LLLVAGGIGITPFLSILKEIASQSSSRyrfpKRVQLIYVVKKSQDIcLLNPISSLLLNQSSNQLNL 491
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 52-97 1.11e-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: 38.14  E-value: 1.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720423028  52 IAGGTGITPMLQLIRHITKDTSDETRMSLLFANQTEEDILLRKELE 97
Cdd:cd06197   131 IAGGVGITPFLAMLRAILSSRNTTWDITLLWSLREDDLPLVMDTLV 176
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
48-109 9.61e-03

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 35.01  E-value: 9.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720423028  48 HLGMIAGGTGITPMLQLIRHITK--DTSDETRMSLLFANQTEEDI-LLRKELEEVATTHHKQFNL 109
Cdd:pfam08030   3 NVLLVAGGIGITPFISILKDLGNksKKLKTKKIKFYWVVRDLSSLeWFKDVLNELEELKELNIEI 67
 
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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