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Conserved domains on  [gi|24643188|ref|NP_573359|]
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uncharacterized protein Dmel_CG7914 [Drosophila melanogaster]

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 ...
 55-315 1.31e-41

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: 144.25  E-value: 1.31e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  55 FRLLRREALGPNGQLLLLHFAHAaeegdgdgavDTVLDIPPGHHVMLRVGS----LLRPYSPYWSDFVAKEFRILVKLQP 130
Cdd:cd06183   1 FKLVSKEDISHDTRIFRFELPSP----------DQVLGLPVGQHVELKAPDdgeqVVRPYTPISPDDDKGYFDLLIKIYP 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188 131 EGPMSRHLQAVQPDDLLEFRGPIGQYVHEP-QPAKCIYIIAQGVAIAPTLPLVRQVLDNEEDMSRLWHLVCAHDLLHVYF 209
Cdd:cd06183  71 GGKMSQYLHSLKPGDTVEIRGPFGKFEYKPnGKVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKISLLYANRTEEDILL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188 210 REEMLEFAQ--FWNYRSCLYLphqqcdssacqeaghcaqqcpqlrDNLRYKETAKVSRLDATELATHLNPAIPGQRVLIV 287
Cdd:cd06183 151 REELDELAKkhPDRFKVHYVL------------------------SRPPEGWKGGVGFITKEMIKEHLPPPPSEDTLVLV 206

                       250       260
                ....*....|....*....|....*...
gi 24643188 288 AGDSSFQKNIAQIATQSLDVDPANIYML 315
Cdd:cd06183 207 CGPPPMIEGAVKGLLKELGYKKDNVFKF 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 ...
 55-315 1.31e-41

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: 144.25  E-value: 1.31e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  55 FRLLRREALGPNGQLLLLHFAHAaeegdgdgavDTVLDIPPGHHVMLRVGS----LLRPYSPYWSDFVAKEFRILVKLQP 130
Cdd:cd06183   1 FKLVSKEDISHDTRIFRFELPSP----------DQVLGLPVGQHVELKAPDdgeqVVRPYTPISPDDDKGYFDLLIKIYP 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188 131 EGPMSRHLQAVQPDDLLEFRGPIGQYVHEP-QPAKCIYIIAQGVAIAPTLPLVRQVLDNEEDMSRLWHLVCAHDLLHVYF 209
Cdd:cd06183  71 GGKMSQYLHSLKPGDTVEIRGPFGKFEYKPnGKVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKISLLYANRTEEDILL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188 210 REEMLEFAQ--FWNYRSCLYLphqqcdssacqeaghcaqqcpqlrDNLRYKETAKVSRLDATELATHLNPAIPGQRVLIV 287
Cdd:cd06183 151 REELDELAKkhPDRFKVHYVL------------------------SRPPEGWKGGVGFITKEMIKEHLPPPPSEDTLVLV 206

                       250       260
                ....*....|....*....|....*...
gi 24643188 288 AGDSSFQKNIAQIATQSLDVDPANIYML 315
Cdd:cd06183 207 CGPPPMIEGAVKGLLKELGYKKDNVFKF 234
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
52-218 1.31e-18

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 82.91  E-value: 1.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  52 YTKFRLLRREALGPNgqLLLLHFAHAaeegdgDGAvdTVLDIPPGHHVMLRV----GSLLRPYSpYWSDFVAKEFRILVK 127
Cdd:COG1018   3 FRPLRVVEVRRETPD--VVSFTLEPP------DGA--PLPRFRPGQFVTLRLpidgKPLRRAYS-LSSAPGDGRLEITVK 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188 128 LQPEGPMSRHLQ-AVQPDDLLEFRGPIGQYVHEPQPAKCIYIIAQGVAIAPTLPLVRQVLDNEEDMSrlWHLV-CAHDLL 205
Cdd:COG1018  72 RVPGGGGSNWLHdHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLARGPFRP--VTLVyGARSPA 149

                       170
                ....*....|...
gi 24643188 206 HVYFREEMLEFAQ 218
Cdd:COG1018 150 DLAFRDELEALAA 162
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
88-158 2.02e-13

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 65.29  E-value: 2.02e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24643188    88 DTVLDIPPGHHVMLRV---GSL-LRPYSPYWSDFVAKEFRILVKLQPEGPMSRHLQAVQPDDLLEFRGPIGQYVH 158
Cdd:pfam00970  25 DQVLGLPVGQHLFLRLpidGELvIRSYTPISSDDDKGYLELLVKVYPGGKMSQYLDELKIGDTIDFKGPLGRFEY 99
PLN02252 PLN02252
nitrate reductase [NADPH]
 12-218 2.85e-12

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 67.39  E-value: 2.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188   12 EDQLRDSDCCGNGCTNCILDNKPRPSKRVLLAGKRNVilsytKFRLLRREALGPNgqLLLLHFAHAAEegdgdgavDTVL 91
Cdd:PLN02252 599 SSSASSHPLSAISTASALAAASPAPGRPVALNPREKI-----PCRLVEKISLSHD--VRLFRFALPSE--------DHVL 663

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188   92 DIPPGHHVMLRV---GSL-LRPYSPYWSDFVAKEFRILVKLQ--------PEG-PMSRHLQAVQPDDLLEFRGPIGQYV- 157
Cdd:PLN02252 664 GLPVGKHVFLCAtinGKLcMRAYTPTSSDDEVGHFELVIKVYfknvhpkfPNGgLMSQYLDSLPIGDTIDVKGPLGHIEy 743

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24643188  158 ---------HEPQPAKCIYIIAQGVAIAPTLPLVRQVLDNEEDMSRLwHLVCAH----DLLhvyFREEMLEFAQ 218
Cdd:PLN02252 744 agrgsflvnGKPKFAKKLAMLAGGTGITPMYQVIQAILRDPEDKTEM-SLVYANrtedDIL---LREELDRWAA 813
 
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 ...
 55-315 1.31e-41

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: 144.25  E-value: 1.31e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  55 FRLLRREALGPNGQLLLLHFAHAaeegdgdgavDTVLDIPPGHHVMLRVGS----LLRPYSPYWSDFVAKEFRILVKLQP 130
Cdd:cd06183   1 FKLVSKEDISHDTRIFRFELPSP----------DQVLGLPVGQHVELKAPDdgeqVVRPYTPISPDDDKGYFDLLIKIYP 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188 131 EGPMSRHLQAVQPDDLLEFRGPIGQYVHEP-QPAKCIYIIAQGVAIAPTLPLVRQVLDNEEDMSRLWHLVCAHDLLHVYF 209
Cdd:cd06183  71 GGKMSQYLHSLKPGDTVEIRGPFGKFEYKPnGKVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKISLLYANRTEEDILL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188 210 REEMLEFAQ--FWNYRSCLYLphqqcdssacqeaghcaqqcpqlrDNLRYKETAKVSRLDATELATHLNPAIPGQRVLIV 287
Cdd:cd06183 151 REELDELAKkhPDRFKVHYVL------------------------SRPPEGWKGGVGFITKEMIKEHLPPPPSEDTLVLV 206

                       250       260
                ....*....|....*....|....*...
gi 24643188 288 AGDSSFQKNIAQIATQSLDVDPANIYML 315
Cdd:cd06183 207 CGPPPMIEGAVKGLLKELGYKKDNVFKF 234
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
52-218 1.31e-18

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 82.91  E-value: 1.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  52 YTKFRLLRREALGPNgqLLLLHFAHAaeegdgDGAvdTVLDIPPGHHVMLRV----GSLLRPYSpYWSDFVAKEFRILVK 127
Cdd:COG1018   3 FRPLRVVEVRRETPD--VVSFTLEPP------DGA--PLPRFRPGQFVTLRLpidgKPLRRAYS-LSSAPGDGRLEITVK 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188 128 LQPEGPMSRHLQ-AVQPDDLLEFRGPIGQYVHEPQPAKCIYIIAQGVAIAPTLPLVRQVLDNEEDMSrlWHLV-CAHDLL 205
Cdd:COG1018  72 RVPGGGGSNWLHdHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLARGPFRP--VTLVyGARSPA 149

                       170
                ....*....|...
gi 24643188 206 HVYFREEMLEFAQ 218
Cdd:COG1018 150 DLAFRDELEALAA 162
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 95-219 1.39e-15

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 74.90  E-value: 1.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  95 PGHHVMLRVGSLL--RPYSPYWSDFVAKEFRILVKLqpEGPMSRHLQAVQPDDLLEFRGPIGQYVHEPQPAKCIYIIAQG 172
Cdd:COG0543  28 PGQFVMLRVPGDGlrRPFSIASAPREDGTIELHIRV--VGKGTRALAELKPGDELDVRGPLGNGFPLEDSGRPVLLVAGG 105

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 24643188 173 VAIAPTLPLVRQVLDNEEDMsrlwHLVC-AHDLLHVYFREEMLEFAQF 219
Cdd:COG0543 106 TGLAPLRSLAEALLARGRRV----TLYLgARTPEDLYLLDELEALADF 149
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 95-232 6.57e-15

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: 72.48  E-value: 6.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  95 PGHHVMLRVGS----LLRPYSPYWSDFVAKEFRILVKLQPEGPMSRHLQAVQPDDLLEFRGPIGQYVHEPQPAKCIYIIA 170
Cdd:cd00322  25 PGQYVDLHLPGdgrgLRRAYSIASSPDEEGELELTVKIVPGGPFSAWLHDLKPGDEVEVSGPGGDFFLPLEESGPVVLIA 104

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24643188 171 QGVAIAPTLPLVRQvLDNEEDMSRLWHLVCAHDLLHVYFREEMLEFAQFW-NYRSCLYLPHQQ 232
Cdd:cd00322 105 GGIGITPFRSMLRH-LAADKPGGEITLLYGARTPADLLFLDELEELAKEGpNFRLVLALSRES 166
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
88-158 2.02e-13

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 65.29  E-value: 2.02e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24643188    88 DTVLDIPPGHHVMLRV---GSL-LRPYSPYWSDFVAKEFRILVKLQPEGPMSRHLQAVQPDDLLEFRGPIGQYVH 158
Cdd:pfam00970  25 DQVLGLPVGQHLFLRLpidGELvIRSYTPISSDDDKGYLELLVKVYPGGKMSQYLDELKIGDTIDFKGPLGRFEY 99
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 95-217 1.78e-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 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: 65.75  E-value: 1.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  95 PGHHVMLRVG-----SLLRPYS----PYWSDFVAkefrILVKLQPEGPMSRHL-QAVQPDDLLEFRGPIGQYVHEPQPAK 164
Cdd:cd06217  33 AGQHVDLRLTaidgyTAQRSYSiassPTQRGRVE----LTVKRVPGGEVSPYLhDEVKVGDLLEVRGPIGTFTWNPLHGD 108

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 24643188 165 CIYIIAQGVAIAPTLPLVRQVLDNEedMSRLWHLV-CAHDLLHVYFREEMLEFA 217
Cdd:cd06217 109 PVVLLAGGSGIVPLMSMIRYRRDLG--WPVPFRLLySARTAEDVIFRDELEQLA 160
PLN02252 PLN02252
nitrate reductase [NADPH]
 12-218 2.85e-12

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 67.39  E-value: 2.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188   12 EDQLRDSDCCGNGCTNCILDNKPRPSKRVLLAGKRNVilsytKFRLLRREALGPNgqLLLLHFAHAAEegdgdgavDTVL 91
Cdd:PLN02252 599 SSSASSHPLSAISTASALAAASPAPGRPVALNPREKI-----PCRLVEKISLSHD--VRLFRFALPSE--------DHVL 663

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188   92 DIPPGHHVMLRV---GSL-LRPYSPYWSDFVAKEFRILVKLQ--------PEG-PMSRHLQAVQPDDLLEFRGPIGQYV- 157
Cdd:PLN02252 664 GLPVGKHVFLCAtinGKLcMRAYTPTSSDDEVGHFELVIKVYfknvhpkfPNGgLMSQYLDSLPIGDTIDVKGPLGHIEy 743

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24643188  158 ---------HEPQPAKCIYIIAQGVAIAPTLPLVRQVLDNEEDMSRLwHLVCAH----DLLhvyFREEMLEFAQ 218
Cdd:PLN02252 744 agrgsflvnGKPKFAKKLAMLAGGTGITPMYQVIQAILRDPEDKTEM-SLVYANrtedDIL---LREELDRWAA 813
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 86-217 3.81e-11

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: 61.77  E-value: 3.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  86 AVDTVLDIP--------PGHHVMLRVG----SLLRPYS---PYWSDfvakEFRILVKLQPEGPMSRHL-QAVQPDDLLEF 149
Cdd:cd06191  13 AVTIVFAVPgplqygfrPGQHVTLKLDfdgeELRRCYSlcsSPAPD----EISITVKRVPGGRVSNYLrEHIQPGMTVEV 88

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24643188 150 RGPIGQYVHEPQPAKCIYIIAQGVAIAPTLPLVRQVLDNEEDmsRLWHLVC-AHDLLHVYFREEMLEFA 217
Cdd:cd06191  89 MGPQGHFVYQPQPPGRYLLVAAGSGITPLMAMIRATLQTAPE--SDFTLIHsARTPADMIFAQELRELA 155
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 52-218 2.43e-08

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 54.45  E-value: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188   52 YTKFRLLRREALGPNGqlLLLHFAHAAEEgdgdgavdTVLDIPPGHHVMLRVGS--------LLRPYSPYWSDFVAKEFR 123
Cdd:PTZ00319  33 FQHFKLIKKTEVTHDT--FIFRFALHSPT--------QRLGLPIGQHIVFRCDCttpgkpetVQHSYTPISSDDEKGYVD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  124 ILVK-----LQPEGP----MSRHLQAVQPDDLLEFRGPIGQY---------VHEP------QPAKCIYIIAQGVAIAPTL 179
Cdd:PTZ00319 103 FLIKvyfkgVHPSFPnggrLSQHLYHMKLGDKIEMRGPVGKFeylgngtytVHKGkgglktMHVDAFAMIAGGTGITPML 182

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 24643188  180 PLVRQVLDNEEDMSRLWHLVCAHDLLHVYFREEMLEFAQ 218
Cdd:PTZ00319 183 QIIHAIKKNKEDRTKVFLVYANQTEDDILLRKELDEAAK 221
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 86-252 4.67e-08

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: 52.66  E-value: 4.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  86 AVDTVLDIPPGHHVML-RVGSLLRPYSPYWSDFVAKEFRILVKLQPEGPMSRHL-QAVQPDDLLEFRGPIGQ--YVHEPQ 161
Cdd:cd06194  17 EPDRPLPYLPGQYVNLrRAGGLARSYSPTSLPDGDNELEFHIRRKPNGAFSGWLgEEARPGHALRLQGPFGQafYRPEYG 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188 162 PAKCIyIIAQGVAIAPTLPLVRQVLDNEEDMS-RLWHLvcAHDLLHVYFREE----MLEFAQFwNYRSCLylpHQQCDSS 236
Cdd:cd06194  97 EGPLL-LVGAGTGLAPLWGIARAALRQGHQGEiRLVHG--ARDPDDLYLHPAllwlAREHPNF-RYIPCV---SEGSQGD 169

                       170
                ....*....|....*.
gi 24643188 237 ACQEAGHCAQQCPQLR 252
Cdd:cd06194 170 PRVRAGRIAAHLPPLT 185
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 95-274 5.91e-08

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: 52.61  E-value: 5.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  95 PGHHVMLRV---GSLL-RPYSPYWSD-FVAKEFRILVKLQPEGPMSRHL-QAVQPDDLLEFRGPIGQYV-HEPQPAKCIY 167
Cdd:cd06216  48 AGQHVRLGVeidGVRHwRSYSLSSSPtQEDGTITLTVKAQPDGLVSNWLvNHLAPGDVVELSQPQGDFVlPDPLPPRLLL 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188 168 iIAQGVAIAPTLPLVRQVLDNEEdMSRLWHLVCAHDLLHVYFREEMLEfaqfwnyrsclylphqqcdssacqeaghCAQQ 247
Cdd:cd06216 128 -IAAGSGITPVMSMLRTLLARGP-TADVVLLYYARTREDVIFADELRA----------------------------LAAQ 177

                       170       180
                ....*....|....*....|....*..
gi 24643188 248 CPQLRDNLRYKETAKVSRLDATELATH 274
Cdd:cd06216 178 HPNLRLHLLYTREELDGRLSAAHLDAV 204
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 95-218 4.83e-07

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: 49.86  E-value: 4.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  95 PGHHVMLRV------GSLLRPYSpyWSDFV-AKEFRILVKLQPEGPMSRHL-QAVQPDDLLEFRGPIGQYVHEPQPAKCI 166
Cdd:cd06184  39 PGQYLSVRVklpglgYRQIRQYS--LSDAPnGDYYRISVKREPGGLVSNYLhDNVKVGDVLEVSAPAGDFVLDEASDRPL 116

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 24643188 167 YIIAQGVAIAPTLPLVRQVLDNEEDmSRLWHLVCAHDLLHVYFREEMLEFAQ 218
Cdd:cd06184 117 VLISAGVGITPMLSMLEALAAEGPG-RPVTFIHAARNSAVHAFRDELEELAA 167
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 132-224 1.12e-06

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: 48.76  E-value: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188 132 GPMSRHLQAVQPDDLLEFRGPIGQYVHEPQ-PAKCIYIIAQGVAIAPTLPLVRQVLDNEEDMSRLWHLVCAHDLLHVYFR 210
Cdd:cd06221  66 GRVTEALHELKPGDTVGLRGPFGNGFPVEEmKGKDLLLVAGGLGLAPLRSLINYILDNREDYGKVTLLYGARTPEDLLFK 145

                        90
                ....*....|....
gi 24643188 211 EEMLEfaqfWNYRS 224
Cdd:cd06221 146 EELKE----WAKRS 155
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 90-213 6.30e-06

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 46.79  E-value: 6.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188   90 VLDIPPGHHVMLRV----GSLLRPYSPYWSDfvAKEFRILVKLqpEGPMSRHLQAVQPDDLLEFRGPIGQYVHEPQPAKC 165
Cdd:PRK00054  29 VFDMKPGQFVMVWVpgvePLLERPISISDID--KNEITILYRK--VGEGTKKLSKLKEGDELDIRGPLGNGFDLEEIGGK 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 24643188  166 IYIIAQGVAIAPTLPLVRQVLDNEEDMSRLWHLVCAHDllhVYFREEM 213
Cdd:PRK00054 105 VLLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTKDE---VIFEEEF 149
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 80-190 1.29e-05

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: 45.80  E-value: 1.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  80 EGDGDGAVDTVLDIPPGHHVMLRV-GSLL-RPYS----PYWSDFVakEFriLVKLQPEGPMSRHL-QAVQPDDLLEFRGP 152
Cdd:cd06210  22 QPDDAEGAGIAAEFVPGQFVEIEIpGTDTrRSYSlantPNWDGRL--EF--LIRLLPGGAFSTYLeTRAKVGQRLNLRGP 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 24643188 153 IGQYV---HEPQPakcIYIIAQGVAIAPTLPLVRQVLDNEE 190
Cdd:cd06210  98 LGAFGlreNGLRP---RWFVAGGTGLAPLLSMLRRMAEWGE 135
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
 108-227 1.64e-05

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 45.68  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  108 RPYSPYWSDFVAKEFRILVKLQPEGPMSRHLQAVQPDDLLEFRGPIGQYVHEPQPAKCIYIIAQGVAIAPTLPLVRQVL- 186
Cdd:PTZ00274 104 RFYTPVTANHTKGYFDIIVKRKKDGLMTNHLFGMHVGDKLLFRSVTFKIQYRPNRWKHVGMIAGGTGFTPMLQIIRHSLt 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 24643188  187 ----DNEEDMSRLWHLVCAHDLLHVYFREEMLEFAQFWNYRSCLY 227
Cdd:PTZ00274 184 epwdSGEVDRTKLSFLFCNRTERHILLKGLFDDLARRYSNRFKVY 228
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 95-184 2.83e-05

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: 44.46  E-value: 2.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  95 PGHHVMLRVGS----LL-RPYSPYWSDFVAKEFRILVKLQPEGpmSRHLQAVQPDDLLEFRGPIGQ-YVHEPQPAKCIyI 168
Cdd:cd06218  27 PGQFVMLRVPDgsdpLLrRPISIHDVDPEEGTITLLYKVVGKG--TRLLSELKAGDELDVLGPLGNgFDLPDDDGKVL-L 103

                        90
                ....*....|....*.
gi 24643188 169 IAQGVAIAPTLPLVRQ 184
Cdd:cd06218 104 VGGGIGIAPLLFLAKQ 119
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 91-226 3.21e-05

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


Pssm-ID: 99805 [Multi-domain]  Cd Length: 228  Bit Score: 44.51  E-value: 3.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  91 LDIPPGHHVMLRV-GS-LLRPYSpYWSDFVAKEFRILVKLQPEGPMSRHL-QAVQPDDLLEFRGPIGQ-YVHEPQ-Pakc 165
Cdd:cd06209  29 LAFLPGQYVNLQVpGTdETRSYS-FSSAPGDPRLEFLIRLLPGGAMSSYLrDRAQPGDRLTLTGPLGSfYLREVKrP--- 104

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24643188 166 IYIIAQGVAIAPTLPLVRQVLDNEEDMSRLWHLVCAH--DLLHVyfrEEMLEFAQFW---NYRSCL 226
Cdd:cd06209 105 LLMLAGGTGLAPFLSMLDVLAEDGSAHPVHLVYGVTRdaDLVEL---DRLEALAERLpgfSFRTVV 167
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 95-184 3.75e-05

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: 44.24  E-value: 3.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  95 PGHHVMLRVGSLL----RPYSPYWSDFVAKEFRILVklQPEGPMSRHLQAVQPDDLLEFRGPIGQYVHEPQPAKCIYIIA 170
Cdd:cd06192  27 PGQFVFLRNFESPglerIPLSLAGVDPEEGTISLLV--EIRGPKTKLIAELKPGEKLDVMGPLGNGFEGPKKGGTVLLVA 104

                        90
                ....*....|....
gi 24643188 171 QGVAIAPTLPLVRQ 184
Cdd:cd06192 105 GGIGLAPLLPIAKK 118
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 88-229 5.20e-05

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: 43.71  E-value: 5.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  88 DTVLDIPPGHHVMLRVGS-----LLRPYS----PYwsdfvAKEFRILVKLQPEGPMSRHLQAVQP-DDLLEFRGPIGQYV 157
Cdd:cd06195  20 DIPFRFQAGQFTKLGLPNddgklVRRAYSiasaPY-----EENLEFYIILVPDGPLTPRLFKLKPgDTIYVGKKPTGFLT 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24643188 158 -HEPQPAKCIYIIAQGVAIAPTLPLVRQvLDNEEDMSRLwHLVCA----HDLLhvyFREEMLEFAQ--FWNYRsclYLP 229
Cdd:cd06195  95 lDEVPPGKRLWLLATGTGIAPFLSMLRD-LEIWERFDKI-VLVHGvryaEELA---YQDEIEALAKqyNGKFR---YVP 165
PRK10926 PRK10926
ferredoxin-NADP reductase; Provisional
 130-202 1.74e-03

ferredoxin-NADP reductase; Provisional


Pssm-ID: 182844  Cd Length: 248  Bit Score: 39.30  E-value: 1.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24643188  130 PEGPMSRHLQAVQP-DDLLEFRGPIGQYVHEPQP-AKCIYIIAQGVAIAPTLplvrQVLDNEEDMSRLWHLVCAH 202
Cdd:PRK10926  71 PEGKLSPRLAALKPgDEVQVVSEAAGFFVLDEVPdCETLWMLATGTAIGPYL----SILQEGKDLERFKNLVLVH 141
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 95-218 2.85e-03

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: 38.34  E-value: 2.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  95 PGHHVMLRV---GSLLRPYSPywsDFVAKEFRIL---VKLQPEGPMSRHL-QAVQPDDLLEFRGPIGQ-YVHEPQPAKcI 166
Cdd:cd06187  26 AGQYVNVTVpgrPRTWRAYSP---ANPPNEDGEIefhVRAVPGGRVSNALhDELKVGDRVRLSGPYGTfYLRRDHDRP-V 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 24643188 167 YIIAQGVAIAPTLPLVRQVLdnEEDMSRLWHLVC-AHDLLHVYFREEMLEFAQ 218
Cdd:cd06187 102 LCIAGGTGLAPLRAIVEDAL--RRGEPRPVHLFFgARTERDLYDLEGLLALAA 152
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 95-229 4.86e-03

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: 37.69  E-value: 4.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188  95 PGHHVMLRV--GSLLRPYSPYWSDFVAKEFRILVKLQPEGPMSRHL-QAVQPDDLLEFRGPIGQ-YVHEPQPAKCIYiIA 170
Cdd:cd06211  38 AGQYVNLQApgYEGTRAFSIASSPSDAGEIELHIRLVPGGIATTYVhKQLKEGDELEISGPYGDfFVRDSDQRPIIF-IA 116

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24643188 171 QGVAIAPTLPLVRQVLdnEEDMSR-LWHLVCAHDLLHVYFREEMLEFAQFW-NYRsclYLP 229
Cdd:cd06211 117 GGSGLSSPRSMILDLL--ERGDTRkITLFFGARTRAELYYLDEFEALEKDHpNFK---YVP 172
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 121-191 4.98e-03

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: 37.70  E-value: 4.98e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24643188 121 EFRILVKLQPEGPMSRHL-QAVQPDDLLEFRGPIGQY---VHEPQPakcIYIIAQGVAIAPTLPLVRQVLDNEED 191
Cdd:cd06212  60 RLEFIIKKYPGGLFSSFLdDGLAVGDPVTVTGPYGTCtlrESRDRP---IVLIGGGSGMAPLLSLLRDMAASGSD 131
PRK05802 PRK05802
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
95-188 7.31e-03

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


Pssm-ID: 235613 [Multi-domain]  Cd Length: 320  Bit Score: 37.65  E-value: 7.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643188   95 PGHHVMLRvgsllRPYSPYWSDFV-------AKEFRILVKLQPEGPMSRHLQAVQPDDLLEFRGP-----IG-QYVHEPQ 161
Cdd:PRK05802  97 PGSFVFLR-----NKNSSSFFDVPisimeadTEENIIKVAIEIRGVKTKKIAKLNKGDEILLRGPywngiLGlKNIKSTK 171

                         90       100
                 ....*....|....*....|....*..
gi 24643188  162 PAKCIyIIAQGVAIAPTLPLVRQVLDN 188
Cdd:PRK05802 172 NGKSL-VIARGIGQAPGVPVIKKLYSN 197
 
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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