|
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 ... |
296-563 |
2.63e-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: 172.10 E-value: 2.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 296 ITKVVMHP-CKVLELQMRK-RGFTMEIGQYIFVNCPSI-SFLEWHPFTLTSAPEEE--FFSIHIRA-AGDWTENLIRTFE 369
Cdd:cd06186 1 IATVELLPdSDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEqdTLSLIIRAkKGFTTRLLRKALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 370 QQHSPM-PRIEVDGPFGTVSEDVFQYEVAVLVGAGIGVTPFASFLKSIWYkfqRAHNKLKTQKIYFYWICRETGAFAWFN 448
Cdd:cd06186 81 SPGGGVsLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLR---RSSKTSRTRRVKLVWVVRDREDLEWFL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 449 NLLNSlEQEMDELGkpdflNYRLFLTgwdsniaghaalnfdratdvltglkqktsfgrpmwdnefsriatahpksvvGVF 528
Cdd:cd06186 158 DELRA-AQELEVDG-----EIEIYVT---------------------------------------------------RVV 180
|
250 260 270
....*....|....*....|....*....|....*
gi 1937369601 529 LCGPPTLAKSLRKCCRRyssldPRKVQFYFNKETF 563
Cdd:cd06186 181 VCGPPGLVDDVRNAVAK-----KGGTGVEFHEESF 210
|
|
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
394-543 |
4.11e-38 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 137.47 E-value: 4.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 394 YEVAVLVGAGIGVTPFASFLKSIWYKFQrahnKLKTQKIYFYWICRETGAFAWFNNLLNSLEQEmdelgKPDFLNYRLFL 473
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSK----KLKTKKIKFYWVVRDLSSLEWFKDVLNELEEL-----KELNIEIHIYL 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369601 474 TGWD--------SNIAGHAALNFDRATDVLTGLKQKTSFGRPMWDNEFSRIATAHPKSVVGVFLCGPPTLAKSLRKCC 543
Cdd:pfam08030 72 TGEYeaedasdqSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
175-416 |
1.05e-27 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 118.03 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 175 LTGVVATVALVLMVTSAMEFIRRNYFELFWYTHHLFIIYIIclgihglggivrgqteesmseshprncSYSFHEWDKyer 254
Cdd:PLN02844 238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLI---------------------------FFLFHAGDR--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 255 scrspHFVgqppeswkWILAPIAFYIFERILRFYRSRQKVVITKVVMHPCKVLELQMRKR-GFTMEIGQYIFVNCPSISF 333
Cdd:PLN02844 288 -----HFY--------MVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISR 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 334 LEWHPFTLTSAP--EEEFFSIHIRAAGDWTENLIRTFEQ-------QHSPMPrIEVDGPFGTVSEDVFQYEVAVLVGAGI 404
Cdd:PLN02844 355 FQWHPFSITSSSniDDHTMSVIIKCEGGWTNSLYNKIQAeldsetnQMNCIP-VAIEGPYGPASVDFLRYDSLLLVAGGI 433
|
250
....*....|..
gi 1937369601 405 GVTPFASFLKSI 416
Cdd:PLN02844 434 GITPFLSILKEI 445
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
94-541 |
1.33e-21 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 97.66 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 94 LDHNLTFHKLVAYMICIFTAIHIIAhlfnferysrsqqAMDGSLASVLSSLfhPEKEDSWLNPiqspnvtvmyaaFTSIA 173
Cdd:COG4097 74 LDRLYRLHKWLGILALVLALAHPLL-------------LLGPKWLVGWGGL--PARLAALLTL------------LRGLA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 174 GLTGVVATVALVLMVTSAmeFIRR--NYfELFWYTHHLFIIYIICLGIHGLGGIvrgqteesmseshprncsysfhewdk 251
Cdd:COG4097 127 ELLGEWAFYLLLALVVLS--LLRRrlPY-ELWRLTHRLLAVAYLLLAFHHLLLG-------------------------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 252 yerscrsPHFVGQPPESWKWI---LAPIAFYIFERILRFYRSRQKV-VITKVVMHPCKVLELQMR---KRGFTMEIGQYI 324
Cdd:COG4097 178 -------GPFYWSPPAGVLWAalaAAGLAAAVYSRLGRPLRSRRHPyRVESVEPEAGDVVELTLRpegGRWLGHRAGQFA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 325 FVNCPSISFLE-WHPFTLTSAPEEE-FFSIHIRAAGDWTENLirtfeQQHSPMPRIEVDGPFGTVSEDVF-QYEVAVLVG 401
Cdd:COG4097 251 FLRFDGSPFWEeAHPFSISSAPGGDgRLRFTIKALGDFTRRL-----GRLKPGTRVYVEGPYGRFTFDRRdTAPRQVWIA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 402 AGIGVTPFASFLKsiwykfQRAHNKLKTQKIYFYWICRETGAFAwFNNLLNSLEQEMDELgkpdflnyRLFLtgWDSNIA 481
Cdd:COG4097 326 GGIGITPFLALLR------ALAARPGDQRPVDLFYCVRDEEDAP-FLEELRALAARLAGL--------RLHL--VVSDED 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 482 GHaaLNFDRATDVLTGLKQktsfgrpmWDnefsriatahpksvvgVFLCGPPTLAKSLRK 541
Cdd:COG4097 389 GR--LTAERLRRLVPDLAE--------AD----------------VFFCGPPGMMDALRR 422
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
74-215 |
2.19e-13 |
|
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: 66.91 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 74 NLLSFLRGTCSFCNHTLRKPLDHNLTFHKLVAYMICIFTAIHIIAHLFNFERYSRsqqamdgslasvlsslfhpekEDSW 153
Cdd:pfam01794 10 PLLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---------------------EGIL 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369601 154 LNPIQSPNVtvmyaaftsiagLTGVVATVALVLMVTSAMEFIRRNYFELFWYTHHLFIIYII 215
Cdd:pfam01794 69 DLLLKRPYN------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFL 118
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
305-546 |
4.35e-11 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 63.34 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 305 KVLELQMRKRGFTMEIGQYIFVNCPSisFLEWHPFTLTSAP-EEEFFSIHIRAAGDWTENLIRTFEQQhspmpRIEVDGP 383
Cdd:COG0543 13 YLLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPrEDGTIELHIRVVGKGTRALAELKPGD-----ELDVRGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 384 FGTVsedvFQYEV----AVLVGAGIGVTPFASFLKSIwykfqRAHNKlktqKIYFYWICRETGAFAWfnnllnslEQEMD 459
Cdd:COG0543 86 LGNG----FPLEDsgrpVLLVAGGTGLAPLRSLAEAL-----LARGR----RVTLYLGARTPEDLYL--------LDELE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 460 ELGkpdflNYRLFLT---GWdsniAGHAALnfdrATDVLTGLKQKTSFGRpmwdnefsriatahpksvvgVFLCGPPTLA 536
Cdd:COG0543 145 ALA-----DFRVVVTtddGW----YGRKGF----VTDALKELLAEDSGDD--------------------VYACGPPPMM 191
|
250
....*....|
gi 1937369601 537 KSLRKCCRRY 546
Cdd:COG0543 192 KAVAELLLER 201
|
|
| |
|
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 ... |
296-563 |
2.63e-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: 172.10 E-value: 2.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 296 ITKVVMHP-CKVLELQMRK-RGFTMEIGQYIFVNCPSI-SFLEWHPFTLTSAPEEE--FFSIHIRA-AGDWTENLIRTFE 369
Cdd:cd06186 1 IATVELLPdSDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEqdTLSLIIRAkKGFTTRLLRKALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 370 QQHSPM-PRIEVDGPFGTVSEDVFQYEVAVLVGAGIGVTPFASFLKSIWYkfqRAHNKLKTQKIYFYWICRETGAFAWFN 448
Cdd:cd06186 81 SPGGGVsLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLR---RSSKTSRTRRVKLVWVVRDREDLEWFL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 449 NLLNSlEQEMDELGkpdflNYRLFLTgwdsniaghaalnfdratdvltglkqktsfgrpmwdnefsriatahpksvvGVF 528
Cdd:cd06186 158 DELRA-AQELEVDG-----EIEIYVT---------------------------------------------------RVV 180
|
250 260 270
....*....|....*....|....*....|....*
gi 1937369601 529 LCGPPTLAKSLRKCCRRyssldPRKVQFYFNKETF 563
Cdd:cd06186 181 VCGPPGLVDDVRNAVAK-----KGGTGVEFHEESF 210
|
|
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
394-543 |
4.11e-38 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 137.47 E-value: 4.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 394 YEVAVLVGAGIGVTPFASFLKSIWYKFQrahnKLKTQKIYFYWICRETGAFAWFNNLLNSLEQEmdelgKPDFLNYRLFL 473
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSK----KLKTKKIKFYWVVRDLSSLEWFKDVLNELEEL-----KELNIEIHIYL 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369601 474 TGWD--------SNIAGHAALNFDRATDVLTGLKQKTSFGRPMWDNEFSRIATAHPKSVVGVFLCGPPTLAKSLRKCC 543
Cdd:pfam08030 72 TGEYeaedasdqSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
175-416 |
1.05e-27 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 118.03 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 175 LTGVVATVALVLMVTSAMEFIRRNYFELFWYTHHLFIIYIIclgihglggivrgqteesmseshprncSYSFHEWDKyer 254
Cdd:PLN02844 238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLI---------------------------FFLFHAGDR--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 255 scrspHFVgqppeswkWILAPIAFYIFERILRFYRSRQKVVITKVVMHPCKVLELQMRKR-GFTMEIGQYIFVNCPSISF 333
Cdd:PLN02844 288 -----HFY--------MVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISR 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 334 LEWHPFTLTSAP--EEEFFSIHIRAAGDWTENLIRTFEQ-------QHSPMPrIEVDGPFGTVSEDVFQYEVAVLVGAGI 404
Cdd:PLN02844 355 FQWHPFSITSSSniDDHTMSVIIKCEGGWTNSLYNKIQAeldsetnQMNCIP-VAIEGPYGPASVDFLRYDSLLLVAGGI 433
|
250
....*....|..
gi 1937369601 405 GVTPFASFLKSI 416
Cdd:PLN02844 434 GITPFLSILKEI 445
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
295-541 |
1.38e-26 |
|
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: 107.92 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 295 VITKVVMHPCKVLELQmRKRGFTMEIGQYIFVNCPSISFLEWHPFTLTSAPEEE-FFSIHIRAA--GDWTENLIRtfeqq 371
Cdd:cd00322 1 VATEDVTDDVRLFRLQ-LPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEgELELTVKIVpgGPFSAWLHD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 372 HSPMPRIEVDGPFGTVSEDVFQYEVAVLVGAGIGVTPFASFLKSIWYKFQRAHnklktqkIYFYWICReTGAFAWFNNLL 451
Cdd:cd00322 75 LKPGDEVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGE-------ITLLYGAR-TPADLLFLDEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 452 NSLEQEMdelgkpdfLNYRLFLTGWDSNIAGHAALNFDRATDvltglkqktSFGRPMWDNEFSRiatahpksvvgVFLCG 531
Cdd:cd00322 147 EELAKEG--------PNFRLVLALSRESEAKLGPGGRIDREA---------EILALLPDDSGAL-----------VYICG 198
|
250
....*....|
gi 1937369601 532 PPTLAKSLRK 541
Cdd:cd00322 199 PPAMAKAVRE 208
|
|
| PLN02292 |
PLN02292 |
ferric-chelate reductase |
170-432 |
1.45e-25 |
|
ferric-chelate reductase
Pssm-ID: 215165 [Multi-domain] Cd Length: 702 Bit Score: 111.50 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 170 TSIAGLTGVVATVALVLMVTSAMEFIRRNYFELFWYTHHLFIIYIICLGIHGlgGIvrgqteesmseshprncSYSFhew 249
Cdd:PLN02292 246 TGVSNLAGEIALVAGLVMWATTYPKIRRRFFEVFFYTHYLYIVFMLFFVFHV--GI-----------------SFAL--- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 250 dkyerscrsphfvgqppeswkwILAPiAFYIF--ERILRFYRSRQKVVITKVVMHPCKVLELQMRKRGFTMEIGQYI-FV 326
Cdd:PLN02292 304 ----------------------ISFP-GFYIFlvDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPMLMYSPTSImFV 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 327 NCPSISFLEWHPFTLTSAP--EEEFFSIHIRAAGDWTENLIRTFE-QQHSPMPRIEVDGPFGTVSEDVFQYEVAVLVGAG 403
Cdd:PLN02292 361 NIPSISKLQWHPFTITSSSklEPEKLSVMIKSQGKWSTKLYHMLSsSDQIDRLAVSVEGPYGPASTDFLRHESLVMVSGG 440
|
250 260
....*....|....*....|....*....
gi 1937369601 404 IGVTPFASFLKSIWYKFQRahNKLKTQKI 432
Cdd:PLN02292 441 SGITPFISIIRDLIYTSST--ETCKIPKI 467
|
|
| FAD_binding_8 |
pfam08022 |
FAD-binding domain; |
298-388 |
2.25e-23 |
|
FAD-binding domain;
Pssm-ID: 285293 [Multi-domain] Cd Length: 108 Bit Score: 94.71 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 298 KVVMHPCKVLELQMRK--RGFTMEIGQYIFVNC-PSISFLEWHPFTLTSAPEEEFFSIHIRAAGDWTENLIRTFEQQ--- 371
Cdd:pfam08022 8 KVALLPDNVLKLRVSKpkKPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANYLSSScpk 87
|
90 100
....*....|....*....|.
gi 1937369601 372 ----HSPMPRIEVDGPFGTVS 388
Cdd:pfam08022 88 spenGKDKPRVLIEGPYGPPS 108
|
|
| PLN02631 |
PLN02631 |
ferric-chelate reductase |
170-427 |
2.04e-22 |
|
ferric-chelate reductase
Pssm-ID: 178238 [Multi-domain] Cd Length: 699 Bit Score: 101.66 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 170 TSIAGLTGVVATVALVLMVTSAMEFIRRNYFELFWYTHHLFIIYIICLGIHglggivrgqteesmseshprncsysfhew 249
Cdd:PLN02631 229 TYVPNLAGTIAMVIGIAMWVTSLPSFRRKKFELFFYTHHLYGLYIVFYVIH----------------------------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 250 dkyerscrsphfVGqppESWKWILAPIAFYIF-ERILRFYRSRQKVVITKVVMHPCKVLELQMRKR-GFTMEIGQYIFVN 327
Cdd:PLN02631 280 ------------VG---DSWFCMILPNIFLFFiDRYLRFLQSTKRSRLVSARILPSDNLELTFSKTpGLHYTPTSILFLH 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 328 CPSISFLEWHPFTLTSAP--EEEFFSIHIRAAGDWTENLirtFEQQHSPMPRIEV--DGPFGTVSEDVFQYEVAVLVGAG 403
Cdd:PLN02631 345 VPSISKLQWHPFTITSSSnlEKDTLSVVIRRQGSWTQKL---YTHLSSSIDSLEVstEGPYGPNSFDVSRHNSLILVSGG 421
|
250 260
....*....|....*....|....
gi 1937369601 404 IGVTPFASFLKSIWYKFQRAHNKL 427
Cdd:PLN02631 422 SGITPFISVIRELIFQSQNPSTKL 445
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
94-541 |
1.33e-21 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 97.66 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 94 LDHNLTFHKLVAYMICIFTAIHIIAhlfnferysrsqqAMDGSLASVLSSLfhPEKEDSWLNPiqspnvtvmyaaFTSIA 173
Cdd:COG4097 74 LDRLYRLHKWLGILALVLALAHPLL-------------LLGPKWLVGWGGL--PARLAALLTL------------LRGLA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 174 GLTGVVATVALVLMVTSAmeFIRR--NYfELFWYTHHLFIIYIICLGIHGLGGIvrgqteesmseshprncsysfhewdk 251
Cdd:COG4097 127 ELLGEWAFYLLLALVVLS--LLRRrlPY-ELWRLTHRLLAVAYLLLAFHHLLLG-------------------------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 252 yerscrsPHFVGQPPESWKWI---LAPIAFYIFERILRFYRSRQKV-VITKVVMHPCKVLELQMR---KRGFTMEIGQYI 324
Cdd:COG4097 178 -------GPFYWSPPAGVLWAalaAAGLAAAVYSRLGRPLRSRRHPyRVESVEPEAGDVVELTLRpegGRWLGHRAGQFA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 325 FVNCPSISFLE-WHPFTLTSAPEEE-FFSIHIRAAGDWTENLirtfeQQHSPMPRIEVDGPFGTVSEDVF-QYEVAVLVG 401
Cdd:COG4097 251 FLRFDGSPFWEeAHPFSISSAPGGDgRLRFTIKALGDFTRRL-----GRLKPGTRVYVEGPYGRFTFDRRdTAPRQVWIA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 402 AGIGVTPFASFLKsiwykfQRAHNKLKTQKIYFYWICRETGAFAwFNNLLNSLEQEMDELgkpdflnyRLFLtgWDSNIA 481
Cdd:COG4097 326 GGIGITPFLALLR------ALAARPGDQRPVDLFYCVRDEEDAP-FLEELRALAARLAGL--------RLHL--VVSDED 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 482 GHaaLNFDRATDVLTGLKQktsfgrpmWDnefsriatahpksvvgVFLCGPPTLAKSLRK 541
Cdd:COG4097 389 GR--LTAERLRRLVPDLAE--------AD----------------VFFCGPPGMMDALRR 422
|
|
| FNR_like_3 |
cd06198 |
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
288-563 |
1.82e-17 |
|
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: 81.15 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 288 YRSRQKVVITKVVMHPckvLELQMRKRGftmeiGQYIFVNCPSISFLEWHPFTLTSAPEEEF-FSIHIRAAGDWTENLIR 366
Cdd:cd06198 1 ARVTEVRPTTTLTLEP---RGPALGHRA-----GQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTIKALGDYTRRLAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 367 TFEqqhsPMPRIEVDGPFGtvsedVFQYEVA----VLVGAGIGVTPFASFLKSiwykFQRAHNklkTQKIYFYWiCRETG 442
Cdd:cd06198 73 RLK----PGTRVTVEGPYG-----RFTFDDRrarqIWIAGGIGITPFLALLEA----LAARGD---ARPVTLFY-CVRDP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 443 AFAWFNNLLNSLEQEMdelgkpdflNYRLfltgwdsniagHaalnfdratdVLTGLKQKTSFGRPMWDNEFSRIATAHpk 522
Cdd:cd06198 136 EDAVFLDELRALAAAA---------GVVL-----------H----------VIDSPSDGRLTLEQLVRALVPDLADAD-- 183
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1937369601 523 svvgVFLCGPPTLAKSLRKCCRRYsSLDPRKvqfyFNKETF 563
Cdd:cd06198 184 ----VWFCGPPGMADALEKGLRAL-GVPARR----FHYERF 215
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
74-215 |
2.19e-13 |
|
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: 66.91 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 74 NLLSFLRGTCSFCNHTLRKPLDHNLTFHKLVAYMICIFTAIHIIAHLFNFERYSRsqqamdgslasvlsslfhpekEDSW 153
Cdd:pfam01794 10 PLLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---------------------EGIL 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369601 154 LNPIQSPNVtvmyaaftsiagLTGVVATVALVLMVTSAMEFIRRNYFELFWYTHHLFIIYII 215
Cdd:pfam01794 69 DLLLKRPYN------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFL 118
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
305-546 |
4.35e-11 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 63.34 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 305 KVLELQMRKRGFTMEIGQYIFVNCPSisFLEWHPFTLTSAP-EEEFFSIHIRAAGDWTENLIRTFEQQhspmpRIEVDGP 383
Cdd:COG0543 13 YLLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPrEDGTIELHIRVVGKGTRALAELKPGD-----ELDVRGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 384 FGTVsedvFQYEV----AVLVGAGIGVTPFASFLKSIwykfqRAHNKlktqKIYFYWICRETGAFAWfnnllnslEQEMD 459
Cdd:COG0543 86 LGNG----FPLEDsgrpVLLVAGGTGLAPLRSLAEAL-----LARGR----RVTLYLGARTPEDLYL--------LDELE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 460 ELGkpdflNYRLFLT---GWdsniAGHAALnfdrATDVLTGLKQKTSFGRpmwdnefsriatahpksvvgVFLCGPPTLA 536
Cdd:COG0543 145 ALA-----DFRVVVTtddGW----YGRKGF----VTDALKELLAEDSGDD--------------------VYACGPPPMM 191
|
250
....*....|
gi 1937369601 537 KSLRKCCRRY 546
Cdd:COG0543 192 KAVAELLLER 201
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
321-545 |
2.62e-08 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 54.80 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 321 GQYIFVNCPSISFLEWHPFTLTSAPEEEFFSIHIR---------------AAGDwtenlirtfeqqhspmpRIEVDGPFG 385
Cdd:COG1018 37 GQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKrvpggggsnwlhdhlKVGD-----------------TLEVSGPRG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 386 TVsedVFQYEVA---VLVGAGIGVTPFASFLKSIwykfqRAHNklKTQKIYFYWICRETGAFAwFNNLLNSLEQEMDelg 462
Cdd:COG1018 100 DF---VLDPEPArplLLIAGGIGITPFLSMLRTL-----LARG--PFRPVTLVYGARSPADLA-FRDELEALAARHP--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 463 kpdflNYRLFLTgwdsniaghaalnFDRATDVLTGlkqktsfgrpmwdnefsRIATAHPKSVVG------VFLCGPPTLA 536
Cdd:COG1018 166 -----RLRLHPV-------------LSREPAGLQG-----------------RLDAELLAALLPdpadahVYLCGPPPMM 210
|
....*....
gi 1937369601 537 KSLRKCCRR 545
Cdd:COG1018 211 EAVRAALAE 219
|
|
| PRK00054 |
PRK00054 |
dihydroorotate dehydrogenase electron transfer subunit; Reviewed |
313-416 |
1.39e-05 |
|
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
Pssm-ID: 234601 [Multi-domain] Cd Length: 250 Bit Score: 46.79 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 313 KRGFTMEIGQYIFVNCPSISFLEWHPFTLtSAPEEEFFSIHIRAAGDWTENLirtFEQQhsPMPRIEVDGPFGTVSEDVF 392
Cdd:PRK00054 27 EKVFDMKPGQFVMVWVPGVEPLLERPISI-SDIDKNEITILYRKVGEGTKKL---SKLK--EGDELDIRGPLGNGFDLEE 100
|
90 100
....*....|....*....|....
gi 1937369601 393 QYEVAVLVGAGIGVTPFASFLKSI 416
Cdd:PRK00054 101 IGGKVLLVGGGIGVAPLYELAKEL 124
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
321-440 |
2.71e-05 |
|
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: 45.62 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 321 GQYIFVNCPSISFLewhPFTLTSAP-EEEFFSIHIRAA--GDWTENLIRTFEQQHSpmprIEVDGPFGTVSEDVFQYEVA 397
Cdd:cd06189 29 GQYLDLLLDDGDKR---PFSIASAPhEDGEIELHIRAVpgGSFSDYVFEELKENGL----VRIEGPLGDFFLREDSDRPL 101
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1937369601 398 VLVGAGIGVTPfasfLKSIwykFQRAHNKLKTQKIYFYWICRE 440
Cdd:cd06189 102 ILIAGGTGFAP----IKSI---LEHLLAQGSKRPIHLYWGART 137
|
|
| DHOD_e_trans_like |
cd06192 |
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ... |
318-414 |
3.84e-04 |
|
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: 42.31 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 318 MEIGQYIFVNCPSISFLEWHPFTLTSA-PEEEFFSIHIRAAGDWTENLIRTFEQQHspmprIEVDGPFGTVSEDVFQYEV 396
Cdd:cd06192 25 FRPGQFVFLRNFESPGLERIPLSLAGVdPEEGTISLLVEIRGPKTKLIAELKPGEK-----LDVMGPLGNGFEGPKKGGT 99
|
90
....*....|....*...
gi 1937369601 397 AVLVGAGIGVTPFASFLK 414
Cdd:cd06192 100 VLLVAGGIGLAPLLPIAK 117
|
|
| sulfite_reductase_like |
cd06221 |
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ... |
307-542 |
4.08e-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: 42.21 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 307 LELQM-RKRGFTMEIGQYIFVNCPSISflEwHPFTLTSAPEE-EFFSIHIRAAGDWTENLirtFEQQhsPMPRIEVDGPF 384
Cdd:cd06221 16 LRLEDdDEELFTFKPGQFVMLSLPGVG--E-APISISSDPTRrGPLELTIRRVGRVTEAL---HELK--PGDTVGLRGPF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 385 GT-VSEDVFQYEVAVLVGAGIGVTPfasfLKSIWYKFQRAHNKLKtqKIYFYWICRETGAFAWfnnllnslEQEMDEL-G 462
Cdd:cd06221 88 GNgFPVEEMKGKDLLLVAGGLGLAP----LRSLINYILDNREDYG--KVTLLYGARTPEDLLF--------KEELKEWaK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 463 KPDFlnyRLFLTgwdsniaghaalnFDRATDVLTGLKqktsfGRPMwdNEFSRIATAHPKSVVgvFLCGPP----TLAKS 538
Cdd:cd06221 154 RSDV---EVILT-------------VDRAEEGWTGNV-----GLVT--DLLPELTLDPDNTVA--IVCGPPimmrFVAKE 208
|
....
gi 1937369601 539 LRKC 542
Cdd:cd06221 209 LLKL 212
|
|
| flavohem_like_fad_nad_binding |
cd06184 |
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ... |
321-456 |
1.11e-03 |
|
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: 41.00 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 321 GQYIFVNCPSISFLEWHP--FTLTSAPEEEFFSIHIR---------------AAGDwtenlirtfeqqhspmpRIEVDGP 383
Cdd:cd06184 40 GQYLSVRVKLPGLGYRQIrqYSLSDAPNGDYYRISVKrepgglvsnylhdnvKVGD-----------------VLEVSAP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 384 FGTvsedvFQYEVA-----VLVGAGIGVTPFASFLKSiwykfqrAHNKLKTQKIYFYWICR--ETGAFA-WFNNLLNSLE 455
Cdd:cd06184 103 AGD-----FVLDEAsdrplVLISAGVGITPMLSMLEA-------LAAEGPGRPVTFIHAARnsAVHAFRdELEELAARLP 170
|
.
gi 1937369601 456 Q 456
Cdd:cd06184 171 N 171
|
|
| FNR_like_1 |
cd06196 |
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ... |
306-434 |
1.43e-03 |
|
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal region may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99793 [Multi-domain] Cd Length: 218 Bit Score: 40.30 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 306 VLELQMRK-RGFTMEIGQYIFVncpSISFLEW----HPFTLTSAPEEEF--FSIHIRAAGD-WTENLIRTfeqqhSPMPR 377
Cdd:cd06196 15 VKRLRFDKpEGYDFTPGQATEV---AIDKPGWrdekRPFTFTSLPEDDVleFVIKSYPDHDgVTEQLGRL-----QPGDT 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369601 378 IEVDGPFGTVSEDvfqyEVAVLVGAGIGVTPFASFLKsiwykfQRAHN-KLKTQKIYF 434
Cdd:cd06196 87 LLIEDPWGAIEYK----GPGVFIAGGAGITPFIAILR------DLAAKgKLEGNTLIF 134
|
|
| FNR_like_2 |
cd06197 |
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ... |
339-475 |
1.60e-03 |
|
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and have a variety of physiological functions in a variety of organisms including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99794 Cd Length: 220 Bit Score: 40.07 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 339 FTLTSAPE----EEFFSIHIRAAGDWTENLI---RTFEQQHSPMPRIEVDGPFGTVSEDVFQYEVAVLVGAGIGVTPFAS 411
Cdd:cd06197 63 FTVSSAPPhdpaTDEFEITVRKKGPVTGFLFqvaRRLREQGLEVPVLGVGGEFTLSLPGEGAERKMVWIAGGVGITPFLA 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937369601 412 FLKSIwykfqrAHNKLKTQKIYFYWICREtgafawfnnllNSLEQEMDELGK-PDFL-NYRLFLTG 475
Cdd:cd06197 143 MLRAI------LSSRNTTWDITLLWSLRE-----------DDLPLVMDTLVRfPGLPvSTTLFITS 191
|
|
| DHOD_e_trans_like2 |
cd06220 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
294-410 |
3.83e-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 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.
Pssm-ID: 99816 [Multi-domain] Cd Length: 233 Bit Score: 39.15 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 294 VVITKVVMHPCKVLELQMRKRgFTMEIGQYIFVNCPSISFLewhPFTLTSAPEEefFSIHIRAAGDWTENLirtfeqqHS 373
Cdd:cd06220 1 VTIKEVIDETPTVKTFVFDWD-FDFKPGQFVMVWVPGVDEI---PMSLSYIDGP--NSITVKKVGEATSAL-------HD 67
|
90 100 110
....*....|....*....|....*....|....*....
gi 1937369601 374 PMP--RIEVDGPFGTVSEDVfqYEVAVLVGAGIGVTPFA 410
Cdd:cd06220 68 LKEgdKLGIRGPYGNGFELV--GGKVLLIGGGIGIAPLA 104
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|
| FNR1 |
cd06195 |
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ... |
336-422 |
8.10e-03 |
|
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: 38.31 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369601 336 WHPFTLTSAPEE---EFFSIHIRAaGDWTENLirtfeQQHSPMPRIEVD-GPFGT-VSEDVFQYEVAVLVGAGIGVTPFA 410
Cdd:cd06195 44 RRAYSIASAPYEenlEFYIILVPD-GPLTPRL-----FKLKPGDTIYVGkKPTGFlTLDEVPPGKRLWLLATGTGIAPFL 117
|
90
....*....|....
gi 1937369601 411 SFLKS--IWYKFQR 422
Cdd:cd06195 118 SMLRDleIWERFDK 131
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