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Conserved domains on  [gi|768474268|gb|AJT86505|]
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Fre5p [Saccharomyces cerevisiae YJM990]

Protein Classification

NOX_Duox_like_FAD_NADP and NAD_binding_6 domain-containing protein( domain architecture ID 10485016)

protein containing domains Ferric_reduct, NOX_Duox_like_FAD_NADP, and NAD_binding_6

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 429-601 7.28e-45

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


:

Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 159.39  E-value: 7.28e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 429 WAKLKLCGES-MIEVRISKSsKWWKAEPGQYIYLYFLRPKIFWQSHPFTVMDS-LVEDGELVVVITVKNGLTKKLQEYLL 506
Cdd:cd06186    1 IATVELLPDSdVIRLTIPKP-KPFKWKPGQHVYLNFPSLLSFWQSHPFTIASSpEDEQDTLSLIIRAKKGFTTRLLRKAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 507 ESEG-YTEMRVLAEGPYGQSTRT-HLFESLLFIAGGAGVPGPLSMAIKAGRQVKSNDSHQMIKFVWSVRNLDLLEVYRKE 584
Cdd:cd06186   80 KSPGgGVSLKVLVEGPYGSSSEDlLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTSRTRRVKLVWVVRDREDLEWFLDE 159

                        170
                 ....*....|....*....
gi 768474268 585 IMVLKELNID--TKIYFTG 601
Cdd:cd06186  160 LRAAQELEVDgeIEIYVTR 178
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
531-673 3.88e-38

Ferric reductase NAD binding domain;


:

Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 138.63  E-value: 3.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268  531 FESLLFIAGGAGVPGPLSMAIKAGRQVKSnDSHQMIKFVWSVRNLDLLEVYRK---EIMVLKELNIDTKIYFTGERKDES 607
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKK-LKTKKIKFYWVVRDLSSLEWFKDvlnELEELKELNIEIHIYLTGEYEAED 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268  608 NTEEGAIANMSTEGRLLTTSKSAEMI--TDFGRPNIDEIIEEAVS--GAKSLLVTCCGSEGFVDKTRELT 673
Cdd:pfam08030  80 ASDQSDSSIRSENFDSLMNEVIGVDFveFHFGRPNWKEVLKDIAKqhPNGSIGVFSCGPPSLVDELRNLV 149
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 274-391 1.25e-25

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


:

Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 101.96  E-value: 1.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268  274 AGILAFAHFPLIVLFGGKNSTMTWLTGIRYTAFITYHKWLGRFMLVDCTIHAIGYTYHAYI---ENYWKYVKYSDLWTSG 350
Cdd:pfam01794   1 LGILALALLPLLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRfslEGILDLLLKRPYNILG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 768474268  351 RHAMIIVGILVFFSFFFFRRHYYELFVITHIILAIGFFHAC 391
Cdd:pfam01794  81 IIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
 
Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 429-601 7.28e-45

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


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 159.39  E-value: 7.28e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 429 WAKLKLCGES-MIEVRISKSsKWWKAEPGQYIYLYFLRPKIFWQSHPFTVMDS-LVEDGELVVVITVKNGLTKKLQEYLL 506
Cdd:cd06186    1 IATVELLPDSdVIRLTIPKP-KPFKWKPGQHVYLNFPSLLSFWQSHPFTIASSpEDEQDTLSLIIRAKKGFTTRLLRKAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 507 ESEG-YTEMRVLAEGPYGQSTRT-HLFESLLFIAGGAGVPGPLSMAIKAGRQVKSNDSHQMIKFVWSVRNLDLLEVYRKE 584
Cdd:cd06186   80 KSPGgGVSLKVLVEGPYGSSSEDlLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTSRTRRVKLVWVVRDREDLEWFLDE 159

                        170
                 ....*....|....*....
gi 768474268 585 IMVLKELNID--TKIYFTG 601
Cdd:cd06186  160 LRAAQELEVDgeIEIYVTR 178
FAD_binding_8 pfam08022
FAD-binding domain;
424-526 2.58e-41

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 145.94  E-value: 2.58e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268  424 IFGMPWAKLKLCGESMIEVRISKSSKWWKAEPGQYIYLYFLRPKIFWQSHPFTVMDSlVEDGELVVVITVKNGLTKKLQE 503
Cdd:pfam08022   1 IFGVPKAKVALLPDNVLKLRVSKPKKPFKYKPGQYMFINFLPPLSFLQSHPFTITSA-PSDDKLSLHIKVKGGWTRKLAN 79

                          90       100
                  ....*....|....*....|....*....
gi 768474268  504 YLLES------EGYTEMRVLAEGPYGQST 526
Cdd:pfam08022  80 YLSSScpkspeNGKDKPRVLIEGPYGPPS 108
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
531-673 3.88e-38

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 138.63  E-value: 3.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268  531 FESLLFIAGGAGVPGPLSMAIKAGRQVKSnDSHQMIKFVWSVRNLDLLEVYRK---EIMVLKELNIDTKIYFTGERKDES 607
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKK-LKTKKIKFYWVVRDLSSLEWFKDvlnELEELKELNIEIHIYLTGEYEAED 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268  608 NTEEGAIANMSTEGRLLTTSKSAEMI--TDFGRPNIDEIIEEAVS--GAKSLLVTCCGSEGFVDKTRELT 673
Cdd:pfam08030  80 ASDQSDSSIRSENFDSLMNEVIGVDFveFHFGRPNWKEVLKDIAKqhPNGSIGVFSCGPPSLVDELRNLV 149
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 274-391 1.25e-25

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 101.96  E-value: 1.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268  274 AGILAFAHFPLIVLFGGKNSTMTWLTGIRYTAFITYHKWLGRFMLVDCTIHAIGYTYHAYI---ENYWKYVKYSDLWTSG 350
Cdd:pfam01794   1 LGILALALLPLLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRfslEGILDLLLKRPYNILG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 768474268  351 RHAMIIVGILVFFSFFFFRRHYYELFVITHIILAIGFFHAC 391
Cdd:pfam01794  81 IIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 273-618 1.14e-16

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 84.13  E-value: 1.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 273 RAGILAFAHFPLIVLFGGKNSTMTWLTGIRYTAFITYHKWLGRFMLVDCTIHAI------GYTYHAYiENYWKYVKYSDL 346
Cdd:PLN02844 158 RFGLLAEACLALLLLPVLRGLALFRLLGIQFEASVRYHVWLGTSMIFFATVHGAstlfiwGISHHIQ-DEIWKWQKTGRI 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 347 WTSGRHAMIIVGILVFFSFFFFRRHYYELFVITH---IILAIGF-FHACWKHCYklgwgeWIMACALFWIADRILRLIK- 421
Cdd:PLN02844 237 YLAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHhlyIVFLIFFlFHAGDRHFY------MVFPGIFLFGLDKLLRIVQs 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 422 ---IAIFGmpwAKLKLCgeSMIEVRISKSSKwWKAEPGQYIYLYFlrPKIF-WQSHPFTVMDSL-VEDGELVVVITVKNG 496
Cdd:PLN02844 311 rpeTCILS---ARLFPC--KAIELVLPKDPG-LKYAPTSVIFMKI--PSISrFQWHPFSITSSSnIDDHTMSVIIKCEGG 382

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 497 LTK----KLQEYL-LESEGYTEMRVLAEGPYGQSTRTHL-FESLLFIAGGAGVPGPLS----MAIKAGRQVKSNDSHQMI 566
Cdd:PLN02844 383 WTNslynKIQAELdSETNQMNCIPVAIEGPYGPASVDFLrYDSLLLVAGGIGITPFLSilkeIASQSSSRYRFPKRVQLI 462

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768474268 567 KFVWSVRNLDLLEVYRKEIM--VLKELNIDTKIYFTGERKDeSNTEEGAIANMS 618
Cdd:PLN02844 463 YVVKKSQDICLLNPISSLLLnqSSNQLNLKLKVFVTQEEKP-NATLRELLNQFS 515
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
309-585 3.22e-13

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 72.23  E-value: 3.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 309 YHKWLGRFMLVDCTIH-AIGYTYHAYIENYWKYVKYSDLWTSGRH-----------AMIIVGILvffsfFFFRRHY-YEL 375
Cdd:COG4097   80 LHKWLGILALVLALAHpLLLLGPKWLVGWGGLPARLAALLTLLRGlaellgewafyLLLALVVL-----SLLRRRLpYEL 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 376 FVITHIILAIGF----FHACW--KHCYKLGWGEWIM-ACALFWIADRILRLikiaiFGMPWAKLKLCGE---------SM 439
Cdd:COG4097  155 WRLTHRLLAVAYlllaFHHLLlgGPFYWSPPAGVLWaALAAAGLAAAVYSR-----LGRPLRSRRHPYRvesvepeagDV 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 440 IEVRIS-KSSKWWKAEPGQYIYLYFLRPKIFWQSHPFTVMDSLVEDGELvvVITVKN--GLTKKLQEylLEsEGyteMRV 516
Cdd:COG4097  230 VELTLRpEGGRWLGHRAGQFAFLRFDGSPFWEEAHPFSISSAPGGDGRL--RFTIKAlgDFTRRLGR--LK-PG---TRV 301

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768474268 517 LAEGPYGQSTRTHLFES--LLFIAGGAGVPGPLSMAikagRQVKSND-SHQMIKFVWSVRNLDLLeVYRKEI 585
Cdd:COG4097  302 YVEGPYGRFTFDRRDTAprQVWIAGGIGITPFLALL----RALAARPgDQRPVDLFYCVRDEEDA-PFLEEL 368
 
Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 429-601 7.28e-45

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


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 159.39  E-value: 7.28e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 429 WAKLKLCGES-MIEVRISKSsKWWKAEPGQYIYLYFLRPKIFWQSHPFTVMDS-LVEDGELVVVITVKNGLTKKLQEYLL 506
Cdd:cd06186    1 IATVELLPDSdVIRLTIPKP-KPFKWKPGQHVYLNFPSLLSFWQSHPFTIASSpEDEQDTLSLIIRAKKGFTTRLLRKAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 507 ESEG-YTEMRVLAEGPYGQSTRT-HLFESLLFIAGGAGVPGPLSMAIKAGRQVKSNDSHQMIKFVWSVRNLDLLEVYRKE 584
Cdd:cd06186   80 KSPGgGVSLKVLVEGPYGSSSEDlLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTSRTRRVKLVWVVRDREDLEWFLDE 159

                        170
                 ....*....|....*....
gi 768474268 585 IMVLKELNID--TKIYFTG 601
Cdd:cd06186  160 LRAAQELEVDgeIEIYVTR 178
FAD_binding_8 pfam08022
FAD-binding domain;
424-526 2.58e-41

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 145.94  E-value: 2.58e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268  424 IFGMPWAKLKLCGESMIEVRISKSSKWWKAEPGQYIYLYFLRPKIFWQSHPFTVMDSlVEDGELVVVITVKNGLTKKLQE 503
Cdd:pfam08022   1 IFGVPKAKVALLPDNVLKLRVSKPKKPFKYKPGQYMFINFLPPLSFLQSHPFTITSA-PSDDKLSLHIKVKGGWTRKLAN 79

                          90       100
                  ....*....|....*....|....*....
gi 768474268  504 YLLES------EGYTEMRVLAEGPYGQST 526
Cdd:pfam08022  80 YLSSScpkspeNGKDKPRVLIEGPYGPPS 108
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
531-673 3.88e-38

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 138.63  E-value: 3.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268  531 FESLLFIAGGAGVPGPLSMAIKAGRQVKSnDSHQMIKFVWSVRNLDLLEVYRK---EIMVLKELNIDTKIYFTGERKDES 607
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKK-LKTKKIKFYWVVRDLSSLEWFKDvlnELEELKELNIEIHIYLTGEYEAED 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268  608 NTEEGAIANMSTEGRLLTTSKSAEMI--TDFGRPNIDEIIEEAVS--GAKSLLVTCCGSEGFVDKTRELT 673
Cdd:pfam08030  80 ASDQSDSSIRSENFDSLMNEVIGVDFveFHFGRPNWKEVLKDIAKqhPNGSIGVFSCGPPSLVDELRNLV 149
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 274-391 1.25e-25

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 101.96  E-value: 1.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268  274 AGILAFAHFPLIVLFGGKNSTMTWLTGIRYTAFITYHKWLGRFMLVDCTIHAIGYTYHAYI---ENYWKYVKYSDLWTSG 350
Cdd:pfam01794   1 LGILALALLPLLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRfslEGILDLLLKRPYNILG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 768474268  351 RHAMIIVGILVFFSFFFFRRHYYELFVITHIILAIGFFHAC 391
Cdd:pfam01794  81 IIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 273-618 1.14e-16

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 84.13  E-value: 1.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 273 RAGILAFAHFPLIVLFGGKNSTMTWLTGIRYTAFITYHKWLGRFMLVDCTIHAI------GYTYHAYiENYWKYVKYSDL 346
Cdd:PLN02844 158 RFGLLAEACLALLLLPVLRGLALFRLLGIQFEASVRYHVWLGTSMIFFATVHGAstlfiwGISHHIQ-DEIWKWQKTGRI 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 347 WTSGRHAMIIVGILVFFSFFFFRRHYYELFVITH---IILAIGF-FHACWKHCYklgwgeWIMACALFWIADRILRLIK- 421
Cdd:PLN02844 237 YLAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHhlyIVFLIFFlFHAGDRHFY------MVFPGIFLFGLDKLLRIVQs 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 422 ---IAIFGmpwAKLKLCgeSMIEVRISKSSKwWKAEPGQYIYLYFlrPKIF-WQSHPFTVMDSL-VEDGELVVVITVKNG 496
Cdd:PLN02844 311 rpeTCILS---ARLFPC--KAIELVLPKDPG-LKYAPTSVIFMKI--PSISrFQWHPFSITSSSnIDDHTMSVIIKCEGG 382

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 497 LTK----KLQEYL-LESEGYTEMRVLAEGPYGQSTRTHL-FESLLFIAGGAGVPGPLS----MAIKAGRQVKSNDSHQMI 566
Cdd:PLN02844 383 WTNslynKIQAELdSETNQMNCIPVAIEGPYGPASVDFLrYDSLLLVAGGIGITPFLSilkeIASQSSSRYRFPKRVQLI 462

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768474268 567 KFVWSVRNLDLLEVYRKEIM--VLKELNIDTKIYFTGERKDeSNTEEGAIANMS 618
Cdd:PLN02844 463 YVVKKSQDICLLNPISSLLLnqSSNQLNLKLKVFVTQEEKP-NATLRELLNQFS 515
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
309-585 3.22e-13

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 72.23  E-value: 3.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 309 YHKWLGRFMLVDCTIH-AIGYTYHAYIENYWKYVKYSDLWTSGRH-----------AMIIVGILvffsfFFFRRHY-YEL 375
Cdd:COG4097   80 LHKWLGILALVLALAHpLLLLGPKWLVGWGGLPARLAALLTLLRGlaellgewafyLLLALVVL-----SLLRRRLpYEL 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 376 FVITHIILAIGF----FHACW--KHCYKLGWGEWIM-ACALFWIADRILRLikiaiFGMPWAKLKLCGE---------SM 439
Cdd:COG4097  155 WRLTHRLLAVAYlllaFHHLLlgGPFYWSPPAGVLWaALAAAGLAAAVYSR-----LGRPLRSRRHPYRvesvepeagDV 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 440 IEVRIS-KSSKWWKAEPGQYIYLYFLRPKIFWQSHPFTVMDSLVEDGELvvVITVKN--GLTKKLQEylLEsEGyteMRV 516
Cdd:COG4097  230 VELTLRpEGGRWLGHRAGQFAFLRFDGSPFWEEAHPFSISSAPGGDGRL--RFTIKAlgDFTRRLGR--LK-PG---TRV 301

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768474268 517 LAEGPYGQSTRTHLFES--LLFIAGGAGVPGPLSMAikagRQVKSND-SHQMIKFVWSVRNLDLLeVYRKEI 585
Cdd:COG4097  302 YVEGPYGRFTFDRRDTAprQVWIAGGIGITPFLALL----RALAARPgDQRPVDLFYCVRDEEDA-PFLEEL 368
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 452-672 1.43e-11

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: 64.78  E-value: 1.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 452 KAEPGQYIYLyFLRPKIFWQSHPFTVMDSLVEDG--ELVVVITVKNGLTKKLQEYLLESEgytemrVLAEGPYGQSTRtH 529
Cdd:cd00322   22 SFKPGQYVDL-HLPGDGRGLRRAYSIASSPDEEGelELTVKIVPGGPFSAWLHDLKPGDE------VEVSGPGGDFFL-P 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 530 LFES--LLFIAGGAGVPGPLSMAikagRQVKSNDSHQMIKFVWSVRNLDLLeVYRKEIMVLKELNIDTKIYFTgerkdes 607
Cdd:cd00322   94 LEESgpVVLIAGGIGITPFRSML----RHLAADKPGGEITLLYGARTPADL-LFLDELEELAKEGPNFRLVLA------- 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768474268 608 nteegaianmstegrllTTSKSAEMITDFGRPNIDEIIEEAVSGAKSLLVTCCGSEGFVDKTREL 672
Cdd:cd00322  162 -----------------LSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREA 209
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 439-585 6.49e-10

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: 59.58  E-value: 6.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 439 MIEVRISKSSKWWKAEPGQYIYLYFLRPKiFWQSHPFTVmdSLVEDGELVVVITVKNgL---TKKLQEYLleSEGyteMR 515
Cdd:cd06198    9 TTTLTLEPRGPALGHRAGQFAFLRFDASG-WEEPHPFTI--SSAPDPDGRLRFTIKA-LgdyTRRLAERL--KPG---TR 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768474268 516 VLAEGPYGQSTRTHLFESLLFIAGGAGVpGP-LSMAikagRQVKSNDSHQMIKFVWSVRNLDLLeVYRKEI 585
Cdd:cd06198   80 VTVEGPYGRFTFDDRRARQIWIAGGIGI-TPfLALL----EALAARGDARPVTLFYCVRDPEDA-VFLDEL 144
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 452-676 1.95e-08

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 55.64  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 452 KAEPGQYIYLYfLRPKIFWQshPFTVMDSLVEDGELVVVITVKNGLTKKLQEYlleSEGyTEMRVlaEGPYGQSTRTHLF 531
Cdd:COG0543   25 KFKPGQFVMLR-VPGDGLRR--PFSIASAPREDGTIELHIRVVGKGTRALAEL---KPG-DELDV--RGPLGNGFPLEDS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 532 ES-LLFIAGGAGVPGPLSMAikagRQVKSNDSHqmIKFVWSVRNLDLLeVYRKEimvLKELNiDTKIYFTgerkdesnTE 610
Cdd:COG0543   96 GRpVLLVAGGTGLAPLRSLA----EALLARGRR--VTLYLGARTPEDL-YLLDE---LEALA-DFRVVVT--------TD 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768474268 611 EGaianmsTEGRllttsksaemitdfgRPNIDEIIEEAVSGAKSLLVTCCGSEGFVDKTRELTAKR 676
Cdd:COG0543  157 DG------WYGR---------------KGFVTDALKELLAEDSGDDVYACGPPPMMKAVAELLLER 201
PLN02292 PLN02292
ferric-chelate reductase
 277-543 1.92e-07

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 54.49  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 277 LAFAHFPLIvlfggKNSTMTWLTGIRYTAFITYHKWLGRFMLVDCTIHAIGYTYHAYIENY------WKYVKYSDLwtSG 350
Cdd:PLN02292 181 LAFLFYPVA-----RGSSLLAAVGLTSESSIKYHIWLGHLVMTLFTSHGLCYIIYWISMNQvsqmleWDRTGVSNL--AG 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 351 RHAMIIVGILVFFSFFFFRRHYYELFVITH---IILAIGF-FHACWKHCYKLGWGEWImacalfWIADRILRLIKiAIFG 426
Cdd:PLN02292 254 EIALVAGLVMWATTYPKIRRRFFEVFFYTHylyIVFMLFFvFHVGISFALISFPGFYI------FLVDRFLRFLQ-SRNN 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 427 MPWAKLKLCGESMIEVRISKSSKWWKAePGQYIYLYFlrPKIF-WQSHPFTVMDSL-VEDGELVVVITVKNGLTKKLQEY 504
Cdd:PLN02292 327 VKLVSARVLPCDTVELNFSKNPMLMYS-PTSIMFVNI--PSISkLQWHPFTITSSSkLEPEKLSVMIKSQGKWSTKLYHM 403

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 768474268 505 LLESEGYTEMRVLAEGPYGQSTRTHL-FESLLFIAGGAGV 543
Cdd:PLN02292 404 LSSSDQIDRLAVSVEGPYGPASTDFLrHESLVMVSGGSGI 443
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
454-676 1.50e-06

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 49.79  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 454 EPGQYIYLYfLRPKIFWQSHPFTVMDSlVEDGELVV-VITVKNG-LTKKLQEYLleSEGyteMRVLAEGPYGQ-STRTHL 530
Cdd:COG1018   35 RPGQFVTLR-LPIDGKPLRRAYSLSSA-PGDGRLEItVKRVPGGgGSNWLHDHL--KVG---DTLEVSGPRGDfVLDPEP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 531 FESLLFIAGGAGVpGP-LSMAikagRQVKSNDSHQMIKFVWSVRNLDLLeVYRKEIMVLKELNIDTKIYFTgerkdesnt 609
Cdd:COG1018  108 ARPLLLIAGGIGI-TPfLSML----RTLLARGPFRPVTLVYGARSPADL-AFRDELEALAARHPRLRLHPV--------- 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768474268 610 eegaianMSTEGRLLTtsksaemitdfGRPNiDEIIEEAVSGAKSLLVTCCGSEGFVDKTRELTAKR 676
Cdd:COG1018  173 -------LSREPAGLQ-----------GRLD-AELLAALLPDPADAHVYLCGPPPMMEAVRAALAEL 220
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 439-557 8.46e-06

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: 47.71  E-value: 8.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 439 MIEVRISKSSKWWKAEPGQYIYLY-FLRPKIFWQshPFTVMDSLVEDGELVVVITVKNGLTKKLQEYlleSEGYTemrVL 517
Cdd:cd06192   11 LVLLTIKAPLAARLFRPGQFVFLRnFESPGLERI--PLSLAGVDPEEGTISLLVEIRGPKTKLIAEL---KPGEK---LD 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 768474268 518 AEGPYGqstrTHLF-----ESLLFIAGGAGVPGPLSMA---IKAGRQV 557
Cdd:cd06192   83 VMGPLG----NGFEgpkkgGTVLLVAGGIGLAPLLPIAkklAANGNKV 126
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 489-681 1.57e-04

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: 43.73  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 489 VVITVK--------NGLTKKLQEylleseGyteMRVLAEGPYGQSTR-THLFESLLFIAGGAGVPGPLSMAikagRQVKS 559
Cdd:cd06215   61 LSITVKrvpgglvsNWLHDNLKV------G---DELWASGPAGEFTLiDHPADKLLLLSAGSGITPMMSMA----RWLLD 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 560 NDSHQMIKFVWSVRNLDLLeVYRKEIMVLKELNIDTKIYFTGERKDESNTeeGAIanmstEGRLlttskSAEMitdfgrp 639
Cdd:cd06215  128 TRPDADIVFIHSARSPADI-IFADELEELARRHPNFRLHLILEQPAPGAW--GGY-----RGRL-----NAEL------- 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 768474268 640 nideiIEEAVSGAKSLLVTCCGSEGFVDKTRELtakrVLEHG 681
Cdd:cd06215  188 -----LALLVPDLKERTVFVCGPAGFMKAVKSL----LAELG 220
PLN02631 PLN02631
ferric-chelate reductase
 278-611 5.78e-04

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 43.11  E-value: 5.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 278 AFAHFPLIvlfggKNSTMTWLTGIRYTAFITYHKWLGRFMLVDCTIHAIGY-TYHAYIENYWKYVKYSDLWTS---GRHA 353
Cdd:PLN02631 165 AFLFFPVT-----RASTILPLVGLTSESSIKYHIWLGHVSNFLFLVHTVVFlIYWAMINKLMETFAWNPTYVPnlaGTIA 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 354 MIIvGILVFFSFF-----------FFRRHYYELFVITHIIlaigffhacwkHCYKlGWGEWIMACALFWIADRILRLIKi 422
Cdd:PLN02631 240 MVI-GIAMWVTSLpsfrrkkfelfFYTHHLYGLYIVFYVI-----------HVGD-SWFCMILPNIFLFFIDRYLRFLQ- 305

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 423 AIFGMPWAKLKLCGESMIEVRISKSSKwWKAEPGQYIYLYFLR-PKIFWqsHPFTVMDSL-VEDGELVVVITVKNGLTKK 500
Cdd:PLN02631 306 STKRSRLVSARILPSDNLELTFSKTPG-LHYTPTSILFLHVPSiSKLQW--HPFTITSSSnLEKDTLSVVIRRQGSWTQK 382

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 501 LQEYLleSEGYTEMRVLAEGPYG-QSTRTHLFESLLFIAGGAGVPgPLSMAIKAGRQVKSNDSHQM--IKFVWSVRN--- 574
Cdd:PLN02631 383 LYTHL--SSSIDSLEVSTEGPYGpNSFDVSRHNSLILVSGGSGIT-PFISVIRELIFQSQNPSTKLpdVLLVCSFKHyhd 459

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 768474268 575 ---LDLLEVYRKEIMVLKELNIDTKIYFTGERKDESNTEE 611
Cdd:PLN02631 460 lafLDLIFPLDISVSDISRLNLRIEAYITREDKKPETTDD 499
DHOD_e_trans_like1 cd06219
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 452-557 8.76e-03

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 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, and then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99815 [Multi-domain]  Cd Length: 248  Bit Score: 38.33  E-value: 8.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768474268 452 KAEPGQYIylyFLRPKIFWQSHPFTVMDSLVEDGELVVVITVKNGLTKKLQEyLLESEGYTEMrvlaEGPYGQSTRTHLF 531
Cdd:cd06219   26 KAKPGQFV---IVRADEKGERIPLTIADWDPEKGTITIVVQVVGKSTRELAT-LEEGDKIHDV----VGPLGKPSEIENY 97

                         90       100
                 ....*....|....*....|....*....
gi 768474268 532 ESLLFIAGGAGVPG--PLSMAIK-AGRQV 557
Cdd:cd06219   98 GTVVFVGGGVGIAPiyPIAKALKeAGNRV 126
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 512-573 9.90e-03

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: 38.39  E-value: 9.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768474268 512 TEMRVLAEGPYGQST-RTHLFESLLFIAGGAGVPGPLSMAIKAGRQVKSNDSHqmIKFVWSVR 573
Cdd:cd06190   77 PGDELELDGPYGLAYlRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSDRP--VDLFYGGR 137
 
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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