|
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 |
1.32e-51 |
|
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: 175.57 E-value: 1.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 296 ITKVVMHP-SNVLELQMRK-RGFSMEVGQYIFVNCPSI-SFLEWHPFTLTSAPEEE--FFSVHIRA-AGDWTRNLIRTFE 369
Cdd:cd06186 1 IATVELLPdSDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEqdTLSLIIRAkKGFTTRLLRKALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 370 QQHSPM-PRIEVDGPFGTVSEDVFQYEVAVLVGAGIGVTPFASILKSIWYkfqRADNKLKTQKIYFYWICRETGAFAWFN 448
Cdd:cd06186 81 SPGGGVsLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLR---RSSKTSRTRRVKLVWVVRDREDLEWFL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 449 NLLNSlEQEMEELGkmdflNYRLFLTgwdsniaghaalnfdratdiltglkqktsfgrpmwdnefsriatahpksavGVF 528
Cdd:cd06186 158 DELRA-AQELEVDG-----EIEIYVT---------------------------------------------------RVV 180
|
250 260 270
....*....|....*....|....*....|....*
gi 26251303 529 LCGPRTLAKSLRKRCQRyssldPRKVQFYFNKETF 563
Cdd:cd06186 181 VCGPPGLVDDVRNAVAK-----KGGTGVEFHEESF 210
|
|
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
394-543 |
9.46e-38 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 136.32 E-value: 9.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 394 YEVAVLVGAGIGVTPFASILKSIWYKFQradnKLKTQKIYFYWICRETGAFAWFNNLLNSLEQEMEElgkmdFLNYRLFL 473
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSK----KLKTKKIKFYWVVRDLSSLEWFKDVLNELEELKEL-----NIEIHIYL 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26251303 474 TGWD--------SNIAGHAALNFDRATDILTGLKQKTSFGRPMWDNEFSRIATAHPKSAVGVFLCGPRTLAKSLRKRC 543
Cdd:pfam08030 72 TGEYeaedasdqSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
175-416 |
8.05e-27 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 115.33 E-value: 8.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 175 LTGVIATVALVLMVTSAMEFIRRNYFELFWYTHHLFIVYIICLgihglggivrgqteeslgeshphncshSFHEWDDHkg 254
Cdd:PLN02844 238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFF---------------------------LFHAGDRH-- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 255 scrhphfaghppesWKWILAPIAFYIFERILRFYRSQQKVVITKVVMHPSNVLELQMRKR-GFSMEVGQYIFVNCPSISF 333
Cdd:PLN02844 289 --------------FYMVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISR 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 334 LEWHPFTLTSAP--EEEFFSVHIRAAGDWTRNLIRTFEQ-------QHSPMPrIEVDGPFGTVSEDVFQYEVAVLVGAGI 404
Cdd:PLN02844 355 FQWHPFSITSSSniDDHTMSVIIKCEGGWTNSLYNKIQAeldsetnQMNCIP-VAIEGPYGPASVDFLRYDSLLLVAGGI 433
|
250
....*....|..
gi 26251303 405 GVTPFASILKSI 416
Cdd:PLN02844 434 GITPFLSILKEI 445
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
94-541 |
1.58e-23 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 103.43 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 94 LDHNLTFHKLVAymicIFTVIHIIAHLFnferyrrSQQAMDGSLASVLSslshPEKEDSWLNPIQSPNMTVmyaaftsia 173
Cdd:COG4097 74 LDRLYRLHKWLG----ILALVLALAHPL-------LLLGPKWLVGWGGL----PARLAALLTLLRGLAELL--------- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 174 gltGVIATVALVLMVTSAmeFIRR--NYfELFWYTHHLFIVYIICLGIHGLGGIvrgqteeslgeshphncshsfhewdd 251
Cdd:COG4097 130 ---GEWAFYLLLALVVLS--LLRRrlPY-ELWRLTHRLLAVAYLLLAFHHLLLG-------------------------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 252 hkgscrhPHFAGHPPESWKWI---LAPIAFYIFERILRFYRSQQKV-VITKVVMHPSNVLELQMR---KRGFSMEVGQYI 324
Cdd:COG4097 178 -------GPFYWSPPAGVLWAalaAAGLAAAVYSRLGRPLRSRRHPyRVESVEPEAGDVVELTLRpegGRWLGHRAGQFA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 325 FVNCPSISFL-EWHPFTLTSAPEE----EFfsvHIRAAGDWTRNLirtfeQQHSPMPRIEVDGPFGTVSEDVF-QYEVAV 398
Cdd:COG4097 251 FLRFDGSPFWeEAHPFSISSAPGGdgrlRF---TIKALGDFTRRL-----GRLKPGTRVYVEGPYGRFTFDRRdTAPRQV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 399 LVGAGIGVTPFASILKsiwykfQRADNKLKTQKIYFYWICRETGAFAwFNNLLNSLEQEMEELgkmdflnyRLFLtgWDS 478
Cdd:COG4097 323 WIAGGIGITPFLALLR------ALAARPGDQRPVDLFYCVRDEEDAP-FLEELRALAARLAGL--------RLHL--VVS 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26251303 479 NIAGHaaLNFDRATDILTGLKQktsfgrpmWDnefsriatahpksavgVFLCGPRTLAKSLRK 541
Cdd:COG4097 386 DEDGR--LTAERLRRLVPDLAE--------AD----------------VFFCGPPGMMDALRR 422
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
74-215 |
2.90e-14 |
|
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: 69.22 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 74 NLLSFLRGTCSFCNRTLRKPLDHNLTFHKLVAYMICIFTVIHIIAHLFNFERYrrsqqamdgslasvlsslshpEKEDSW 153
Cdd:pfam01794 10 PLLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRF---------------------SLEGIL 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26251303 154 LNPIQSPNMtvmyaaftsiagLTGVIATVALVLMVTSAMEFIRRNYFELFWYTHHLFIVYII 215
Cdd:pfam01794 69 DLLLKRPYN------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFL 118
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
306-546 |
3.44e-11 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 63.73 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 306 VLELQMRKRGFSMEVGQYIFVNCPSisFLEWHPFTLTSAP-EEEFFSVHIRAAGDWTRNLIRTFEQQhspmpRIEVDGPF 384
Cdd:COG0543 14 LLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPrEDGTIELHIRVVGKGTRALAELKPGD-----ELDVRGPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 385 GTVsedvFQYEV----AVLVGAGIGVTPFASILKsiwyKFQRADNklktqKIYFYWICRETGAFAWfnnllnslEQEMEE 460
Cdd:COG0543 87 GNG----FPLEDsgrpVLLVAGGTGLAPLRSLAE----ALLARGR-----RVTLYLGARTPEDLYL--------LDELEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 461 LGkmdflNYRLFLT---GWdsniAGHAALnfdrATDILTGLKQKTSFGRpmwdnefsriatahpksavgVFLCGPRTLAK 537
Cdd:COG0543 146 LA-----DFRVVVTtddGW----YGRKGF----VTDALKELLAEDSGDD--------------------VYACGPPPMMK 192
|
....*....
gi 26251303 538 SLRKRCQRY 546
Cdd:COG0543 193 AVAELLLER 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 |
1.32e-51 |
|
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: 175.57 E-value: 1.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 296 ITKVVMHP-SNVLELQMRK-RGFSMEVGQYIFVNCPSI-SFLEWHPFTLTSAPEEE--FFSVHIRA-AGDWTRNLIRTFE 369
Cdd:cd06186 1 IATVELLPdSDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEqdTLSLIIRAkKGFTTRLLRKALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 370 QQHSPM-PRIEVDGPFGTVSEDVFQYEVAVLVGAGIGVTPFASILKSIWYkfqRADNKLKTQKIYFYWICRETGAFAWFN 448
Cdd:cd06186 81 SPGGGVsLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLR---RSSKTSRTRRVKLVWVVRDREDLEWFL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 449 NLLNSlEQEMEELGkmdflNYRLFLTgwdsniaghaalnfdratdiltglkqktsfgrpmwdnefsriatahpksavGVF 528
Cdd:cd06186 158 DELRA-AQELEVDG-----EIEIYVT---------------------------------------------------RVV 180
|
250 260 270
....*....|....*....|....*....|....*
gi 26251303 529 LCGPRTLAKSLRKRCQRyssldPRKVQFYFNKETF 563
Cdd:cd06186 181 VCGPPGLVDDVRNAVAK-----KGGTGVEFHEESF 210
|
|
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
394-543 |
9.46e-38 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 136.32 E-value: 9.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 394 YEVAVLVGAGIGVTPFASILKSIWYKFQradnKLKTQKIYFYWICRETGAFAWFNNLLNSLEQEMEElgkmdFLNYRLFL 473
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSK----KLKTKKIKFYWVVRDLSSLEWFKDVLNELEELKEL-----NIEIHIYL 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26251303 474 TGWD--------SNIAGHAALNFDRATDILTGLKQKTSFGRPMWDNEFSRIATAHPKSAVGVFLCGPRTLAKSLRKRC 543
Cdd:pfam08030 72 TGEYeaedasdqSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
175-416 |
8.05e-27 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 115.33 E-value: 8.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 175 LTGVIATVALVLMVTSAMEFIRRNYFELFWYTHHLFIVYIICLgihglggivrgqteeslgeshphncshSFHEWDDHkg 254
Cdd:PLN02844 238 LAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFF---------------------------LFHAGDRH-- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 255 scrhphfaghppesWKWILAPIAFYIFERILRFYRSQQKVVITKVVMHPSNVLELQMRKR-GFSMEVGQYIFVNCPSISF 333
Cdd:PLN02844 289 --------------FYMVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISR 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 334 LEWHPFTLTSAP--EEEFFSVHIRAAGDWTRNLIRTFEQ-------QHSPMPrIEVDGPFGTVSEDVFQYEVAVLVGAGI 404
Cdd:PLN02844 355 FQWHPFSITSSSniDDHTMSVIIKCEGGWTNSLYNKIQAeldsetnQMNCIP-VAIEGPYGPASVDFLRYDSLLLVAGGI 433
|
250
....*....|..
gi 26251303 405 GVTPFASILKSI 416
Cdd:PLN02844 434 GITPFLSILKEI 445
|
|
| PLN02292 |
PLN02292 |
ferric-chelate reductase |
170-432 |
4.83e-26 |
|
ferric-chelate reductase
Pssm-ID: 215165 [Multi-domain] Cd Length: 702 Bit Score: 112.65 E-value: 4.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 170 TSIAGLTGVIATVALVLMVTSAMEFIRRNYFELFWYTHHLFIVYIICLGIHGlgGIvrgqteeslgeshphncSHSFhew 249
Cdd:PLN02292 246 TGVSNLAGEIALVAGLVMWATTYPKIRRRFFEVFFYTHYLYIVFMLFFVFHV--GI-----------------SFAL--- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 250 ddhkgscrhphfaghppeswkwILAPiAFYIF--ERILRFYRSQQKVVITKVVMHPSNVLELQMRKRGFSMEVGQYI-FV 326
Cdd:PLN02292 304 ----------------------ISFP-GFYIFlvDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPMLMYSPTSImFV 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 327 NCPSISFLEWHPFTLTSAP--EEEFFSVHIRAAGDWTRNLIRTFEQQ-HSPMPRIEVDGPFGTVSEDVFQYEVAVLVGAG 403
Cdd:PLN02292 361 NIPSISKLQWHPFTITSSSklEPEKLSVMIKSQGKWSTKLYHMLSSSdQIDRLAVSVEGPYGPASTDFLRHESLVMVSGG 440
|
250 260
....*....|....*....|....*....
gi 26251303 404 IGVTPFASILKSIWYKFQRadNKLKTQKI 432
Cdd:PLN02292 441 SGITPFISIIRDLIYTSST--ETCKIPKI 467
|
|
| FAD_binding_8 |
pfam08022 |
FAD-binding domain; |
298-388 |
1.16e-25 |
|
FAD-binding domain;
Pssm-ID: 285293 [Multi-domain] Cd Length: 108 Bit Score: 101.26 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 298 KVVMHPSNVLELQMRK--RGFSMEVGQYIFVNC-PSISFLEWHPFTLTSAPEEEFFSVHIRAAGDWTRNLIRTFEQQ--- 371
Cdd:pfam08022 8 KVALLPDNVLKLRVSKpkKPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANYLSSScpk 87
|
90 100
....*....|....*....|.
gi 26251303 372 ----HSPMPRIEVDGPFGTVS 388
Cdd:pfam08022 88 spenGKDKPRVLIEGPYGPPS 108
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
314-541 |
3.06e-25 |
|
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: 104.07 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 314 RGFSMEVGQYIFVNCPSISFLEWHPFTLTSAPEEE-FFSVHIRAA--GDWTRNLIRtfeqqHSPMPRIEVDGPFGTVSED 390
Cdd:cd00322 19 NGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEgELELTVKIVpgGPFSAWLHD-----LKPGDEVEVSGPGGDFFLP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 391 VFQYEVAVLVGAGIGVTPFASILKSIWYKFQRAdnklktqKIYFYWICReTGAFAWFNNLLNSLEQEMEelgkmdflNYR 470
Cdd:cd00322 94 LEESGPVVLIAGGIGITPFRSMLRHLAADKPGG-------EITLLYGAR-TPADLLFLDELEELAKEGP--------NFR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26251303 471 LFLTGWDSNIAGHAALNFDRATDILTGLKQKTSFGRpmwdnefsriatahpksavgVFLCGPRTLAKSLRK 541
Cdd:cd00322 158 LVLALSRESEAKLGPGGRIDREAEILALLPDDSGAL--------------------VYICGPPAMAKAVRE 208
|
|
| PLN02631 |
PLN02631 |
ferric-chelate reductase |
170-427 |
2.86e-24 |
|
ferric-chelate reductase
Pssm-ID: 178238 [Multi-domain] Cd Length: 699 Bit Score: 107.44 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 170 TSIAGLTGVIATVALVLMVTSAMEFIRRNYFELFWYTHHLFIVYIIclgihglggivrgqteeslgeshphncshsfhew 249
Cdd:PLN02631 229 TYVPNLAGTIAMVIGIAMWVTSLPSFRRKKFELFFYTHHLYGLYIV---------------------------------- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 250 ddhkgscrhpHFAGHPPESWKWILAPIAFYIF-ERILRFYRSQQKVVITKVVMHPSNVLELQMRKR-GFSMEVGQYIFVN 327
Cdd:PLN02631 275 ----------FYVIHVGDSWFCMILPNIFLFFiDRYLRFLQSTKRSRLVSARILPSDNLELTFSKTpGLHYTPTSILFLH 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 328 CPSISFLEWHPFTLTSAP--EEEFFSVHIRAAGDWTRNLirtFEQQHSPMPRIEV--DGPFGTVSEDVFQYEVAVLVGAG 403
Cdd:PLN02631 345 VPSISKLQWHPFTITSSSnlEKDTLSVVIRRQGSWTQKL---YTHLSSSIDSLEVstEGPYGPNSFDVSRHNSLILVSGG 421
|
250 260
....*....|....*....|....
gi 26251303 404 IGVTPFASILKSIWYKFQRADNKL 427
Cdd:PLN02631 422 SGITPFISVIRELIFQSQNPSTKL 445
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
94-541 |
1.58e-23 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 103.43 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 94 LDHNLTFHKLVAymicIFTVIHIIAHLFnferyrrSQQAMDGSLASVLSslshPEKEDSWLNPIQSPNMTVmyaaftsia 173
Cdd:COG4097 74 LDRLYRLHKWLG----ILALVLALAHPL-------LLLGPKWLVGWGGL----PARLAALLTLLRGLAELL--------- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 174 gltGVIATVALVLMVTSAmeFIRR--NYfELFWYTHHLFIVYIICLGIHGLGGIvrgqteeslgeshphncshsfhewdd 251
Cdd:COG4097 130 ---GEWAFYLLLALVVLS--LLRRrlPY-ELWRLTHRLLAVAYLLLAFHHLLLG-------------------------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 252 hkgscrhPHFAGHPPESWKWI---LAPIAFYIFERILRFYRSQQKV-VITKVVMHPSNVLELQMR---KRGFSMEVGQYI 324
Cdd:COG4097 178 -------GPFYWSPPAGVLWAalaAAGLAAAVYSRLGRPLRSRRHPyRVESVEPEAGDVVELTLRpegGRWLGHRAGQFA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 325 FVNCPSISFL-EWHPFTLTSAPEE----EFfsvHIRAAGDWTRNLirtfeQQHSPMPRIEVDGPFGTVSEDVF-QYEVAV 398
Cdd:COG4097 251 FLRFDGSPFWeEAHPFSISSAPGGdgrlRF---TIKALGDFTRRL-----GRLKPGTRVYVEGPYGRFTFDRRdTAPRQV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 399 LVGAGIGVTPFASILKsiwykfQRADNKLKTQKIYFYWICRETGAFAwFNNLLNSLEQEMEELgkmdflnyRLFLtgWDS 478
Cdd:COG4097 323 WIAGGIGITPFLALLR------ALAARPGDQRPVDLFYCVRDEEDAP-FLEELRALAARLAGL--------RLHL--VVS 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26251303 479 NIAGHaaLNFDRATDILTGLKQktsfgrpmWDnefsriatahpksavgVFLCGPRTLAKSLRK 541
Cdd:COG4097 386 DEDGR--LTAERLRRLVPDLAE--------AD----------------VFFCGPPGMMDALRR 422
|
|
| FNR_like_3 |
cd06198 |
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
299-541 |
1.90e-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: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 299 VVMHPSNVLELQMRKRGFSMEV--GQYIFVNCPSISFLEWHPFTLTSAPEEE---FFSvhIRAAGDWTRNLIRTFEqqhs 373
Cdd:cd06198 2 RVTEVRPTTTLTLEPRGPALGHraGQFAFLRFDASGWEEPHPFTISSAPDPDgrlRFT--IKALGDYTRRLAERLK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 374 PMPRIEVDGPFGtvsedVFQYEVA----VLVGAGIGVTPFASILKSiwykFQRADNklkTQKIYFYWICRETGAFAwfnn 449
Cdd:cd06198 76 PGTRVTVEGPYG-----RFTFDDRrarqIWIAGGIGITPFLALLEA----LAARGD---ARPVTLFYCVRDPEDAV---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 450 llnsLEQEMEELGKMDFLNYRLFLTgwdsniaghaalnfdratdiltglkqktsfGRPMWDNEFSRIATAHPKSA-VGVF 528
Cdd:cd06198 140 ----FLDELRALAAAAGVVLHVIDS------------------------------PSDGRLTLEQLVRALVPDLAdADVW 185
|
250
....*....|...
gi 26251303 529 LCGPRTLAKSLRK 541
Cdd:cd06198 186 FCGPPGMADALEK 198
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
74-215 |
2.90e-14 |
|
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: 69.22 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 74 NLLSFLRGTCSFCNRTLRKPLDHNLTFHKLVAYMICIFTVIHIIAHLFNFERYrrsqqamdgslasvlsslshpEKEDSW 153
Cdd:pfam01794 10 PLLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRF---------------------SLEGIL 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26251303 154 LNPIQSPNMtvmyaaftsiagLTGVIATVALVLMVTSAMEFIRRNYFELFWYTHHLFIVYII 215
Cdd:pfam01794 69 DLLLKRPYN------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFL 118
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
306-546 |
3.44e-11 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 63.73 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 306 VLELQMRKRGFSMEVGQYIFVNCPSisFLEWHPFTLTSAP-EEEFFSVHIRAAGDWTRNLIRTFEQQhspmpRIEVDGPF 384
Cdd:COG0543 14 LLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPrEDGTIELHIRVVGKGTRALAELKPGD-----ELDVRGPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 385 GTVsedvFQYEV----AVLVGAGIGVTPFASILKsiwyKFQRADNklktqKIYFYWICRETGAFAWfnnllnslEQEMEE 460
Cdd:COG0543 87 GNG----FPLEDsgrpVLLVAGGTGLAPLRSLAE----ALLARGR-----RVTLYLGARTPEDLYL--------LDELEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 461 LGkmdflNYRLFLT---GWdsniAGHAALnfdrATDILTGLKQKTSFGRpmwdnefsriatahpksavgVFLCGPRTLAK 537
Cdd:COG0543 146 LA-----DFRVVVTtddGW----YGRKGF----VTDALKELLAEDSGDD--------------------VYACGPPPMMK 192
|
....*....
gi 26251303 538 SLRKRCQRY 546
Cdd:COG0543 193 AVAELLLER 201
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
293-545 |
5.09e-07 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 50.94 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 293 KVVITKVVMHPSNVLELQMR----KRGFSMEVGQYIFVNCPSISFLEWHPFTLTSAPEEEFFSVHIR------------- 355
Cdd:COG1018 5 PLRVVEVRRETPDVVSFTLEppdgAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKrvpggggsnwlhd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 356 --AAGDwtrnlirtfeqqhspmpRIEVDGPFGTVsedVFQYEVA---VLVGAGIGVTPFASILKSiwykfqrADNKLKTQ 430
Cdd:COG1018 85 hlKVGD-----------------TLEVSGPRGDF---VLDPEPArplLLIAGGIGITPFLSMLRT-------LLARGPFR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 431 KIYFYWICR--ETGAFAwfnnllnsleQEMEEL-GKMDFLNYRLFLTgwdsniaghaalnfdRATDILTGlkqktsfgrp 507
Cdd:COG1018 138 PVTLVYGARspADLAFR----------DELEALaARHPRLRLHPVLS---------------REPAGLQG---------- 182
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 26251303 508 mwdnefsRIATAHPKSAVG------VFLCGPRTLAKSLRKRCQR 545
Cdd:COG1018 183 -------RLDAELLAALLPdpadahVYLCGPPPMMEAVRAALAE 219
|
|
| DHOD_e_trans_like |
cd06192 |
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ... |
296-414 |
8.51e-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: 47.32 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 296 ITKVVMHPSNVLELQMR--KRGFSMEVGQYIFVNCPSISFLEWHPFTLTSA-PEEEFFSVHIRAAGDWTRNLIRTFEQQH 372
Cdd:cd06192 1 IVKKEQLEPNLVLLTIKapLAARLFRPGQFVFLRNFESPGLERIPLSLAGVdPEEGTISLLVEIRGPKTKLIAELKPGEK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 26251303 373 spmprIEVDGPFGTVSEDVFQYEVAVLVGAGIGVTPFASILK 414
Cdd:cd06192 81 -----LDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAK 117
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
321-440 |
1.70e-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: 46.39 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 321 GQYIFVNCPSISFLewhPFTLTSAP-EEEFFSVHIRAAGDWT-RNLIRTFEQQHSPmprIEVDGPFGTVSEDVFQYEVAV 398
Cdd:cd06189 29 GQYLDLLLDDGDKR---PFSIASAPhEDGEIELHIRAVPGGSfSDYVFEELKENGL---VRIEGPLGDFFLREDSDRPLI 102
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 26251303 399 LVGAGIGvtpFASIlKSIwykFQRADNKLKTQKIYFYWICRE 440
Cdd:cd06189 103 LIAGGTG---FAPI-KSI---LEHLLAQGSKRPIHLYWGART 137
|
|
| PRK00054 |
PRK00054 |
dihydroorotate dehydrogenase electron transfer subunit; Reviewed |
313-416 |
7.34e-05 |
|
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
Pssm-ID: 234601 [Multi-domain] Cd Length: 250 Bit Score: 44.48 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 313 KRGFSMEVGQYIFVNCPSISFLEWHPFTLtSAPEEEFFSVHIRAAGDWTRNLirtFEQQhsPMPRIEVDGPFGTVSEDVF 392
Cdd:PRK00054 27 EKVFDMKPGQFVMVWVPGVEPLLERPISI-SDIDKNEITILYRKVGEGTKKL---SKLK--EGDELDIRGPLGNGFDLEE 100
|
90 100
....*....|....*....|....
gi 26251303 393 QYEVAVLVGAGIGVTPFASILKSI 416
Cdd:PRK00054 101 IGGKVLLVGGGIGVAPLYELAKEL 124
|
|
| PRK08345 |
PRK08345 |
cytochrome-c3 hydrogenase subunit gamma; Provisional |
314-439 |
1.64e-04 |
|
cytochrome-c3 hydrogenase subunit gamma; Provisional
Pssm-ID: 236247 [Multi-domain] Cd Length: 289 Bit Score: 43.64 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 314 RGFSMEVGQYIFVNCPSISFLewhPFTLTSAPEEE-FFSVHIRAAGDWTrnlirTFEQQHSPMPRIEVDGPFGT-VSEDV 391
Cdd:PRK08345 34 ESFTFKPGQFVQVTIPGVGEV---PISICSSPTRKgFFELCIRRAGRVT-----TVIHRLKEGDIVGVRGPYGNgFPVDE 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 26251303 392 FQYEVAVLVGAGIGVTPFASILksiWYKFqraDNKLKTQKIYFYWICR 439
Cdd:PRK08345 106 MEGMDLLLIAGGLGMAPLRSVL---LYAM---DNRWKYGNITLIYGAK 147
|
|
| FNR_like_1 |
cd06196 |
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ... |
305-427 |
1.79e-04 |
|
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: 43.00 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 305 NVLELQMRK-RGFSMEVGQYIFVncpSISFLEW----HPFTLTSAPEEEF--FSVHIRAAGDWTRNLIRTFEqqhsPMPR 377
Cdd:cd06196 14 DVKRLRFDKpEGYDFTPGQATEV---AIDKPGWrdekRPFTFTSLPEDDVleFVIKSYPDHDGVTEQLGRLQ----PGDT 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 26251303 378 IEVDGPFGTVSEDvfqyEVAVLVGAGIGVTPFASILKSIWYKFQRADNKL 427
Cdd:cd06196 87 LLIEDPWGAIEYK----GPGVFIAGGAGITPFIAILRDLAAKGKLEGNTL 132
|
|
| flavohem_like_fad_nad_binding |
cd06184 |
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ... |
321-456 |
5.39e-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: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 321 GQYIFVNCPSISFLEWHP--FTLTSAPEEEF--FSV--------------HIRAaGDwtrnlirtfeqqhspmpRIEVDG 382
Cdd:cd06184 40 GQYLSVRVKLPGLGYRQIrqYSLSDAPNGDYyrISVkrepgglvsnylhdNVKV-GD-----------------VLEVSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 383 PFGTvsedvFQYEVA-----VLVGAGIGVTPFASILKSiwykfqrADNKLKTQKIYFYWICR--ETGAFA-WFNNLLNSL 454
Cdd:cd06184 102 PAGD-----FVLDEAsdrplVLISAGVGITPMLSMLEA-------LAAEGPGRPVTFIHAARnsAVHAFRdELEELAARL 169
|
..
gi 26251303 455 EQ 456
Cdd:cd06184 170 PN 171
|
|
| DHOD_e_trans_like2 |
cd06220 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
294-415 |
1.18e-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: 40.69 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 294 VVITKVVMHPSNVLELQMRKRgFSMEVGQYIFVNCPSISFLewhPFTLTSAPEEefFSVHIRAAGDWTRNLirtfeqqHS 373
Cdd:cd06220 1 VTIKEVIDETPTVKTFVFDWD-FDFKPGQFVMVWVPGVDEI---PMSLSYIDGP--NSITVKKVGEATSAL-------HD 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 26251303 374 PMP--RIEVDGPFGTVSEDVfqYEVAVLVGAGIGVTPFASILKS 415
Cdd:cd06220 68 LKEgdKLGIRGPYGNGFELV--GGKVLLIGGGIGIAPLAPLAER 109
|
|
| FNR_iron_sulfur_binding_3 |
cd06217 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
316-461 |
1.45e-03 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99813 [Multi-domain] Cd Length: 235 Bit Score: 40.33 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 316 FSMEVGQYIFVNCPSIS-FLEWHPFTLTSAP-EEEFFSVHIR--AAGDWTRNLIRTFEqqhsPMPRIEVDGPFGTVSEDV 391
Cdd:cd06217 29 PPFLAGQHVDLRLTAIDgYTAQRSYSIASSPtQRGRVELTVKrvPGGEVSPYLHDEVK----VGDLLEVRGPIGTFTWNP 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 392 FQYEVAVLVGAGIGVTPFASILKsiwykfQRADNKLKTQkIYFYWICRETGAFaWFNNLLNSLEQEMEEL 461
Cdd:cd06217 105 LHGDPVVLLAGGSGIVPLMSMIR------YRRDLGWPVP-FRLLYSARTAEDV-IFRDELEQLARRHPNL 166
|
|
| FNR_iron_sulfur_binding_1 |
cd06215 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
314-439 |
3.02e-03 |
|
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: 39.50 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 314 RGFSMEVGQYIFVNCPSISFLEWHPFTLTSAP-EEEFFSVHIR--AAGDWTRNLIRTFEqqhsPMPRIEVDGPFGTVSED 390
Cdd:cd06215 24 SLFAYKPGQFLTLELEIDGETVYRAYTLSSSPsRPDSLSITVKrvPGGLVSNWLHDNLK----VGDELWASGPAGEFTLI 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 26251303 391 VFQYEVAVLVGAGIGVTPFASILKSIwykfqrADNKLKTqKIYFYWICR 439
Cdd:cd06215 100 DHPADKLLLLSAGSGITPMMSMARWL------LDTRPDA-DIVFIHSAR 141
|
|
| O2ase_reductase_like |
cd06187 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
321-413 |
7.21e-03 |
|
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.
Pssm-ID: 99784 [Multi-domain] Cd Length: 224 Bit Score: 38.34 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26251303 321 GQYIFVNCPSISfLEWHPFTLTSAPEE----EFfsvHIRAA-GDWTRNLIRTFEQqhsPMPRIEVDGPFGT------VSE 389
Cdd:cd06187 27 GQYVNVTVPGRP-RTWRAYSPANPPNEdgeiEF---HVRAVpGGRVSNALHDELK---VGDRVRLSGPYGTfylrrdHDR 99
|
90 100
....*....|....*....|....
gi 26251303 390 DVfqyevaVLVGAGIGVTPFASIL 413
Cdd:cd06187 100 PV------LCIAGGTGLAPLRAIV 117
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