|
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 ... |
287-553 |
2.07e-50 |
|
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: 172.49 E-value: 2.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 287 IISVISHP-SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLL 362
Cdd:cd06186 1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 363 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 441
Cdd:cd06186 81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 442 IQSFRWFADLLCMlhnkfWQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrprwkllfdeiakynrgktvgVF 521
Cdd:cd06186 150 REDLEWFLDELRA-----AQELEVDG-EIEIYVTR-------------------------------------------VV 180
|
250 260 270
....*....|....*....|....*....|..
gi 119579759 522 CCGPNSLSKTLHKLSNQNNsyGTRFEYNKESF 553
Cdd:cd06186 181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
|
|
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
399-536 |
4.57e-27 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 106.66 E-value: 4.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 399 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFRWFADLLCML----------HNKFWQENRPDYV 468
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNELeelkelnieiHIYLTGEYEAEDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119579759 469 NIQLYLSQTD-GIQKIIGEKYHALNSRLFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLS 536
Cdd:pfam08030 81 SDQSDSSIRSeNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
45-455 |
1.83e-16 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 82.59 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 45 SLILLPMCRTL-LAYLRGSQKVPSRRtrrlldksrtFHITCGVTICIFSGVHVAAHLvnalnfsvnysedFVELNAARYR 123
Cdd:PLN02844 168 ALLLLPVLRGLaLFRLLGIQFEASVR----------YHVWLGTSMIFFATVHGASTL-------------FIWGISHHIQ 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 124 DEdPRKLLFTTVPGLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgci 203
Cdd:PLN02844 225 DE-IWKWQKTGRIYLAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG------------------ 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 204 slnrtssqnislpeyfSEHFHEPFPEGFskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNK 283
Cdd:PLN02844 286 ----------------DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRP 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 284 PVTIISVISHPSDVMEIRMVKE-NFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLL 362
Cdd:PLN02844 313 ETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQ 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 363 PPSSQDSEILPFIQSRnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCR 440
Cdd:PLN02844 393 AELDSETNQMNCIPVA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVK 466
|
410
....*....|....*
gi 119579759 441 DIQSfrwfadlLCML 455
Cdd:PLN02844 467 KSQD-------ICLL 474
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
250-441 |
6.41e-15 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 76.86 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 250 PRFQANFPQTWLWIS-GPLCLYCAerLYRYIRSN-----KPVTIISVISHPSDVMEIRMVKEN---FKARPGQ--YITLH 318
Cdd:COG4097 178 GPFYWSPPAGVLWAAlAAAGLAAA--VYSRLGRPlrsrrHPYRVESVEPEAGDVVELTLRPEGgrwLGHRAGQfaFLRFD 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 319 CPSVSaLENHPFTLTMCPTET-KATFGVhlKIVGDWTERFRDLllPPSSqdseilpfiqsrnypKLYIDGPFGS-PFEES 396
Cdd:COG4097 256 GSPFW-EEAHPFSISSAPGGDgRLRFTI--KALGDFTRRLGRL--KPGT---------------RVYVEGPYGRfTFDRR 315
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 119579759 397 LNYEVSLCVAGGIGVTPFASILNTLldDWKPYKLRRLYFIWVCRD 441
Cdd:COG4097 316 DTAPRQVWIAGGIGITPFLALLRAL--AARPGDQRPVDLFYCVRD 358
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
45-181 |
6.71e-15 |
|
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: 71.15 E-value: 6.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 45 SLILLPMcrTLLAYLRGSqkVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRD 124
Cdd:pfam01794 5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 119579759 125 edprkllfttvpgLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 181
Cdd:pfam01794 78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
|
|
| PLN02292 |
PLN02292 |
ferric-chelate reductase |
149-422 |
1.56e-10 |
|
ferric-chelate reductase
Pssm-ID: 215165 [Multi-domain] Cd Length: 702 Bit Score: 63.73 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 149 LMITASTY-AIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgcislnrTSSQNISLPEYFsehfhepf 227
Cdd:PLN02292 261 LVMWATTYpKIRRRFFEVFFYTHYLYIVFMLFFVFHVG----------------------ISFALISFPGFY-------- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 228 pegfskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNKPVTIISVISHPSDVMEIRMVKEN- 306
Cdd:PLN02292 311 -----------------------------------------IFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPm 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 307 FKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLlppSSQDSeilpfiqsRNYPKLYID 386
Cdd:PLN02292 350 LMYSPTSIMFVNIPSISKLQWHPFTITSSSKLEPEKLSVMIKSQGKWSTKLYHML---SSSDQ--------IDRLAVSVE 418
|
250 260 270
....*....|....*....|....*....|....*.
gi 119579759 387 GPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLL 422
Cdd:PLN02292 419 GPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLI 454
|
|
| |
|
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 ... |
287-553 |
2.07e-50 |
|
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: 172.49 E-value: 2.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 287 IISVISHP-SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLL 362
Cdd:cd06186 1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 363 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 441
Cdd:cd06186 81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 442 IQSFRWFADLLCMlhnkfWQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrprwkllfdeiakynrgktvgVF 521
Cdd:cd06186 150 REDLEWFLDELRA-----AQELEVDG-EIEIYVTR-------------------------------------------VV 180
|
250 260 270
....*....|....*....|....*....|..
gi 119579759 522 CCGPNSLSKTLHKLSNQNNsyGTRFEYNKESF 553
Cdd:cd06186 181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
|
|
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
399-536 |
4.57e-27 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 106.66 E-value: 4.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 399 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFRWFADLLCML----------HNKFWQENRPDYV 468
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNELeelkelnieiHIYLTGEYEAEDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119579759 469 NIQLYLSQTD-GIQKIIGEKYHALNSRLFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLS 536
Cdd:pfam08030 81 SDQSDSSIRSeNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
45-455 |
1.83e-16 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 82.59 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 45 SLILLPMCRTL-LAYLRGSQKVPSRRtrrlldksrtFHITCGVTICIFSGVHVAAHLvnalnfsvnysedFVELNAARYR 123
Cdd:PLN02844 168 ALLLLPVLRGLaLFRLLGIQFEASVR----------YHVWLGTSMIFFATVHGASTL-------------FIWGISHHIQ 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 124 DEdPRKLLFTTVPGLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgci 203
Cdd:PLN02844 225 DE-IWKWQKTGRIYLAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG------------------ 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 204 slnrtssqnislpeyfSEHFHEPFPEGFskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNK 283
Cdd:PLN02844 286 ----------------DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRP 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 284 PVTIISVISHPSDVMEIRMVKE-NFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLL 362
Cdd:PLN02844 313 ETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQ 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 363 PPSSQDSEILPFIQSRnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCR 440
Cdd:PLN02844 393 AELDSETNQMNCIPVA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVK 466
|
410
....*....|....*
gi 119579759 441 DIQSfrwfadlLCML 455
Cdd:PLN02844 467 KSQD-------ICLL 474
|
|
| FAD_binding_8 |
pfam08022 |
FAD-binding domain; |
283-392 |
1.26e-15 |
|
FAD-binding domain;
Pssm-ID: 285293 [Multi-domain] Cd Length: 108 Bit Score: 72.75 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 283 KPVTIISVISHPSDVMEIRMVKEN--FKARPGQYITLHC-PSVSALENHPFTLTMCPTETKATfgVHLKIVGDWTERFRD 359
Cdd:pfam08022 2 FGVPKAKVALLPDNVLKLRVSKPKkpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLS--LHIKVKGGWTRKLAN 79
|
90 100 110
....*....|....*....|....*....|...
gi 119579759 360 LLLPpssqdSEILPFIQSRNYPKLYIDGPFGSP 392
Cdd:pfam08022 80 YLSS-----SCPKSPENGKDKPRVLIEGPYGPP 107
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
296-525 |
3.12e-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: 75.18 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 296 DVMEIRMVKEN-FKARPGQYITLHCPSVSALENHPFTLTMCPTETKA-TFGVHLKIVGDWTERFRDLLLppssqDSEILp 373
Cdd:cd00322 9 DVRLFRLQLPNgFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGElELTVKIVPGGPFSAWLHDLKP-----GDEVE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 374 fiqsrnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQSFrWFADLLC 453
Cdd:cd00322 83 -----------VSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPG---GEITLLYGARTPADL-LFLDELE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119579759 454 MLHNKFwqenrpdyVNIQLYLSQTDGiqkiigekyhalnSRLFIGRPRWKLLFDEIAKY-NRGKTVGVFCCGP 525
Cdd:cd00322 148 ELAKEG--------PNFRLVLALSRE-------------SEAKLGPGGRIDREAEILALlPDDSGALVYICGP 199
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
250-441 |
6.41e-15 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 76.86 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 250 PRFQANFPQTWLWIS-GPLCLYCAerLYRYIRSN-----KPVTIISVISHPSDVMEIRMVKEN---FKARPGQ--YITLH 318
Cdd:COG4097 178 GPFYWSPPAGVLWAAlAAAGLAAA--VYSRLGRPlrsrrHPYRVESVEPEAGDVVELTLRPEGgrwLGHRAGQfaFLRFD 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 319 CPSVSaLENHPFTLTMCPTET-KATFGVhlKIVGDWTERFRDLllPPSSqdseilpfiqsrnypKLYIDGPFGS-PFEES 396
Cdd:COG4097 256 GSPFW-EEAHPFSISSAPGGDgRLRFTI--KALGDFTRRLGRL--KPGT---------------RVYVEGPYGRfTFDRR 315
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 119579759 397 LNYEVSLCVAGGIGVTPFASILNTLldDWKPYKLRRLYFIWVCRD 441
Cdd:COG4097 316 DTAPRQVWIAGGIGITPFLALLRAL--AARPGDQRPVDLFYCVRD 358
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
45-181 |
6.71e-15 |
|
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: 71.15 E-value: 6.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 45 SLILLPMcrTLLAYLRGSqkVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRD 124
Cdd:pfam01794 5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 119579759 125 edprkllfttvpgLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 181
Cdd:pfam01794 78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
286-441 |
4.44e-14 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 72.20 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 286 TIISVISHPSDV--MEIRMVKENFKARPGQYITLHCPSvsALENHPFTLTMCPTEtKATFGVHLKIVGDWTERFRDLllp 363
Cdd:COG0543 1 KVVSVERLAPDVylLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPRE-DGTIELHIRVVGKGTRALAEL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 364 pssQDSEilpfiqsrnypKLYIDGPFGSPFEeslnYEVS----LCVAGGIGVTPFASILNTLLDdwkpyKLRRLYFIWVC 439
Cdd:COG0543 75 ---KPGD-----------ELDVRGPLGNGFP----LEDSgrpvLLVAGGTGLAPLRSLAEALLA-----RGRRVTLYLGA 131
|
..
gi 119579759 440 RD 441
Cdd:COG0543 132 RT 133
|
|
| FNR_like_3 |
cd06198 |
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
293-554 |
1.43e-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: 61.12 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 293 HPSDVMEIRMVKENFKARPGQYITLHCPSVSALENHPFTLTMCPTETK-ATFGVhlKIVGDWTERFRDLLLPPSsqdsei 371
Cdd:cd06198 7 RPTTTLTLEPRGPALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTI--KALGDYTRRLAERLKPGT------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 372 lpfiqsrnypKLYIDGPFGSpFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQSFrWFADL 451
Cdd:cd06198 79 ----------RVTVEGPYGR-FTFDDRRARQIWIAGGIGITPFLALLEALAARGDA---RPVTLFYCVRDPEDA-VFLDE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 452 LcmlhnkfWQENRPDYVNIQLYLSQTDGiqkiigekyhalnsRLFIGRPRWKLLFDeiakynrGKTVGVFCCGPNSLSKT 531
Cdd:cd06198 144 L-------RALAAAAGVVLHVIDSPSDG--------------RLTLEQLVRALVPD-------LADADVWFCGPPGMADA 195
|
250 260
....*....|....*....|...
gi 119579759 532 LHKLSNQNNSYGTRFEYnkESFS 554
Cdd:cd06198 196 LEKGLRALGVPARRFHY--ERFE 216
|
|
| PLN02292 |
PLN02292 |
ferric-chelate reductase |
149-422 |
1.56e-10 |
|
ferric-chelate reductase
Pssm-ID: 215165 [Multi-domain] Cd Length: 702 Bit Score: 63.73 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 149 LMITASTY-AIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgcislnrTSSQNISLPEYFsehfhepf 227
Cdd:PLN02292 261 LVMWATTYpKIRRRFFEVFFYTHYLYIVFMLFFVFHVG----------------------ISFALISFPGFY-------- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 228 pegfskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNKPVTIISVISHPSDVMEIRMVKEN- 306
Cdd:PLN02292 311 -----------------------------------------IFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPm 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 307 FKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLlppSSQDSeilpfiqsRNYPKLYID 386
Cdd:PLN02292 350 LMYSPTSIMFVNIPSISKLQWHPFTITSSSKLEPEKLSVMIKSQGKWSTKLYHML---SSSDQ--------IDRLAVSVE 418
|
250 260 270
....*....|....*....|....*....|....*.
gi 119579759 387 GPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLL 422
Cdd:PLN02292 419 GPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLI 454
|
|
| PLN02631 |
PLN02631 |
ferric-chelate reductase |
269-451 |
1.89e-10 |
|
ferric-chelate reductase
Pssm-ID: 178238 [Multi-domain] Cd Length: 699 Bit Score: 63.52 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 269 LYCAERLYRYIRSNKPVTIISVISHPSDVMEIRMVK-ENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHL 347
Cdd:PLN02631 294 LFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKtPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNLEKDTLSVVI 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 348 KIVGDWTERFRDLLlpPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP 427
Cdd:PLN02631 374 RRQGSWTQKLYTHL--SSSIDS-----------LEVSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRELIFQSQN 440
|
170 180
....*....|....*....|....
gi 119579759 428 YKLRRLYFIWVCrdiqSFRWFADL 451
Cdd:PLN02631 441 PSTKLPDVLLVC----SFKHYHDL 460
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
284-525 |
2.98e-08 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 54.41 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 284 PVTIISVISHPSDVMEIRMV----KENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGV-------------- 345
Cdd:COG1018 5 PLRVVEVRRETPDVVSFTLEppdgAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVkrvpggggsnwlhd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 346 HLKiVGDwterfrdlllppssqdseilpfiqsrnypKLYIDGPFGS---PFEESLNYevsLCVAGGIGVTPFASILNTLL 422
Cdd:COG1018 85 HLK-VGD-----------------------------TLEVSGPRGDfvlDPEPARPL---LLIAGGIGITPFLSMLRTLL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 423 dDWKPYklRRLYFIWVCRDIQSFrWFADLLCMLHNKfwqenrpdYVNIQLYLSQTDGiqkiigekyhalnSRLFIGRPRW 502
Cdd:COG1018 132 -ARGPF--RPVTLVYGARSPADL-AFRDELEALAAR--------HPRLRLHPVLSRE-------------PAGLQGRLDA 186
|
250 260
....*....|....*....|...
gi 119579759 503 KLLFDEIAKYNRGKtvgVFCCGP 525
Cdd:COG1018 187 ELLAALLPDPADAH---VYLCGP 206
|
|
| DHOD_e_trans_like2 |
cd06220 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
285-427 |
2.38e-06 |
|
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: 48.78 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 285 VTIISVIshpsdvMEIRMVK-----ENFKARPGQYITLHCPSVSALenhPFTLTMCPTEtkatFGVHLKIVGDWTERFRD 359
Cdd:cd06220 1 VTIKEVI------DETPTVKtfvfdWDFDFKPGQFVMVWVPGVDEI---PMSLSYIDGP----NSITVKKVGEATSALHD 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119579759 360 LllppssqdseilpfiqsRNYPKLYIDGPFGSPFEesLNYEVSLCVAGGIGVTPfasiLNTLLDDWKP 427
Cdd:cd06220 68 L-----------------KEGDKLGIRGPYGNGFE--LVGGKVLLIGGGIGIAP----LAPLAERLKK 112
|
|
| PRK00054 |
PRK00054 |
dihydroorotate dehydrogenase electron transfer subunit; Reviewed |
285-417 |
2.60e-06 |
|
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
Pssm-ID: 234601 [Multi-domain] Cd Length: 250 Bit Score: 49.10 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 285 VTIISVISHPSDVMEIRM-VKENFKARPGQYITLHCPSVSALENHPFTLTMCPTEtKATFGVhlKIVGDWTERFRDLllp 363
Cdd:PRK00054 7 MKIVENKEIAPNIYTLVLdGEKVFDMKPGQFVMVWVPGVEPLLERPISISDIDKN-EITILY--RKVGEGTKKLSKL--- 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 119579759 364 pSSQDSeilpfiqsrnypkLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASI 417
Cdd:PRK00054 81 -KEGDE-------------LDIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYEL 120
|
|
| cyt_b5_reduct_like |
cd06183 |
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ... |
382-525 |
1.52e-05 |
|
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: 46.41 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 382 KLYIDGPFGS-PFEESLNYEVSLCVAGGIGVTPFASILNTLLDDwkPYKLRRLYFIWVCRDIQsfrwfaDLLCMLHNKFW 460
Cdd:cd06183 86 TVEIRGPFGKfEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKD--PEDKTKISLLYANRTEE------DILLREELDEL 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119579759 461 QENRPDYVNIQLYLSQTDGIQKIigekyhalnsrlFIGRPRWKLLFDEIAKYNRGKTVgVFCCGP 525
Cdd:cd06183 158 AKKHPDRFKVHYVLSRPPEGWKG------------GVGFITKEMIKEHLPPPPSEDTL-VLVCGP 209
|
|
| DHOD_e_trans_like |
cd06192 |
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ... |
297-418 |
2.80e-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: 45.78 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 297 VMEIRMVKENFKARPGQYITLHCPSVSALENHPFTLtMCPTETKATFGVHLKIVGDWTERFrdLLLPPSSqdseilpfiq 376
Cdd:cd06192 13 LLTIKAPLAARLFRPGQFVFLRNFESPGLERIPLSL-AGVDPEEGTISLLVEIRGPKTKLI--AELKPGE---------- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 119579759 377 srnypKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASIL 418
Cdd:cd06192 80 -----KLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIA 116
|
|
| flavohem_like_fad_nad_binding |
cd06184 |
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ... |
405-451 |
5.43e-04 |
|
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: 41.77 E-value: 5.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 119579759 405 VAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQS--FR-WFADL 451
Cdd:cd06184 119 ISAGVGITPMLSMLEALAAEGPG---RPVTFIHAARNSAVhaFRdELEEL 165
|
|
| sulfite_reductase_like |
cd06221 |
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ... |
382-525 |
6.98e-04 |
|
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: 41.44 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 382 KLYIDGPFGSPF--EESLNYEVsLCVAGGIGVTPFASILNTLLDDWKPYKlrRLYFiwvcrdIQSFRWFADLLCMLHNKF 459
Cdd:cd06221 80 TVGLRGPFGNGFpvEEMKGKDL-LLVAGGLGLAPLRSLINYILDNREDYG--KVTL------LYGARTPEDLLFKEELKE 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119579759 460 WQenrpDYVNIQLYLSQTDGiqkIIGEKYHalnsrlfIGRPrwKLLFDEIAkYNRGKTVgVFCCGP 525
Cdd:cd06221 151 WA----KRSDVEVILTVDRA---EEGWTGN-------VGLV--TDLLPELT-LDPDNTV-AIVCGP 198
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
285-468 |
1.33e-03 |
|
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: 40.61 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 285 VTIISVISHpsDVMEIR-MVKENFKARPGQYITLHCPSVSALenhPFTLTMCPTETkATFGVHLKIVGDWteRFRDlllp 363
Cdd:cd06189 3 VESIEPLND--DVYRVRlKPPAPLDFLAGQYLDLLLDDGDKR---PFSIASAPHED-GEIELHIRAVPGG--SFSD---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 364 pssqdsEILPFIQSRNypKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDwkpyKLRR-LYFIWVCRDI 442
Cdd:cd06189 71 ------YVFEELKENG--LVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQ----GSKRpIHLYWGARTE 138
|
170 180
....*....|....*....|....*...
gi 119579759 443 QSFrwFADLLCmlhnKFWQENRP--DYV 468
Cdd:cd06189 139 EDL--YLDELL----EAWAEAHPnfTYV 160
|
|
| NAD_binding_1 |
pfam00175 |
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ... |
405-479 |
2.53e-03 |
|
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: 37.62 E-value: 2.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119579759 405 VAGGIGVTPFASILNTLLDDWKPykLRRLYFIWVCRDiqsfrwFADLLCMLHNKFWQENRPDYVNIQLYLSQTDG 479
Cdd:pfam00175 2 IAGGTGIAPVRSMLRAILEDPKD--PTQVVLVFGNRN------EDDILYREELDELAEKHPGRLTVVYVVSRPEA 68
|
|
| T4MO_e_transfer_like |
cd06190 |
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ... |
382-441 |
5.29e-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: 38.77 E-value: 5.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119579759 382 KLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPYKlRRLYFIWVCRD 441
Cdd:cd06190 80 ELELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSD-RPVDLFYGGRT 138
|
|
| |
