|
Name |
Accession |
Description |
Interval |
E-value |
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
530-698 |
7.75e-38 |
|
Ferric reductase NAD binding domain;
:
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 137.86 E-value: 7.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 530 FDNVLLLAGGSGLPGPISHALELGKTTAASGKNFVQLVIAVRGLDMLNACKK---ELMALKGLNVQVHIYNSKQELASAE 606
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDvlnELEELKELNIEIHIYLTGEYEAEDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 607 KISSNEVKNGETTAEKAPSSLSNsekapsesentelplslndtsisdlEFATFHVGRPNVEEILNESVN--HSGSLAVVC 684
Cdd:pfam08030 81 SDQSDSSIRSENFDSLMNEVIGV-------------------------DFVEFHFGRPNWKEVLKDIAKqhPNGSIGVFS 135
|
170
....*....|....
gi 767243135 685 CGPPIFVDTARNQT 698
Cdd:pfam08030 136 CGPPSLVDELRNLV 149
|
|
| NOX_Duox_like_FAD_NADP |
cd06186 |
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
428-596 |
2.17e-35 |
|
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: 133.20 E-value: 2.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 428 KADLQLVG-SDLVRVTVKKPKKFWKAkPGQYVFVSFLRPLCFWQSHPFTVMDSCVND-RELVIVLKAKKGVTK-LVRNFV 504
Cdd:cd06186 1 IATVELLPdSDVIRLTIPKPKPFKWK-PGQHVYLNFPSLLSFWQSHPFTIASSPEDEqDTLSLIIRAKKGFTTrLLRKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 505 ERKGGKASMRLAIEGPYGSKST-AHRFDNVLLLAGGSGLPGPISHALELGKTTAASGKN-FVQLVIAVRGLDMLNACKKE 582
Cdd:cd06186 80 KSPGGGVSLKVLVEGPYGSSSEdLLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTSRTrRVKLVWVVRDREDLEWFLDE 159
|
170
....*....|....*.
gi 767243135 583 LMALKGLNVQ--VHIY 596
Cdd:cd06186 160 LRAAQELEVDgeIEIY 175
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
273-390 |
2.03e-33 |
|
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: 124.30 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 273 SGILSFAHLPLIVLFAGRNNFLQLISGLKHTSFIVFHKWLGRMMFLDAIIHAAGFTNYYLYY---KKWNTVRLRVYWKFG 349
Cdd:pfam01794 1 LGILALALLPLLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFsleGILDLLLKRPYNILG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767243135 350 IAATCLAGMLIFFSIAAFRRHYYETFMALHIVFAALFLYTC 390
Cdd:pfam01794 81 IIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
530-698 |
7.75e-38 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 137.86 E-value: 7.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 530 FDNVLLLAGGSGLPGPISHALELGKTTAASGKNFVQLVIAVRGLDMLNACKK---ELMALKGLNVQVHIYNSKQELASAE 606
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDvlnELEELKELNIEIHIYLTGEYEAEDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 607 KISSNEVKNGETTAEKAPSSLSNsekapsesentelplslndtsisdlEFATFHVGRPNVEEILNESVN--HSGSLAVVC 684
Cdd:pfam08030 81 SDQSDSSIRSENFDSLMNEVIGV-------------------------DFVEFHFGRPNWKEVLKDIAKqhPNGSIGVFS 135
|
170
....*....|....
gi 767243135 685 CGPPIFVDTARNQT 698
Cdd:pfam08030 136 CGPPSLVDELRNLV 149
|
|
| NOX_Duox_like_FAD_NADP |
cd06186 |
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
428-596 |
2.17e-35 |
|
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: 133.20 E-value: 2.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 428 KADLQLVG-SDLVRVTVKKPKKFWKAkPGQYVFVSFLRPLCFWQSHPFTVMDSCVND-RELVIVLKAKKGVTK-LVRNFV 504
Cdd:cd06186 1 IATVELLPdSDVIRLTIPKPKPFKWK-PGQHVYLNFPSLLSFWQSHPFTIASSPEDEqDTLSLIIRAKKGFTTrLLRKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 505 ERKGGKASMRLAIEGPYGSKST-AHRFDNVLLLAGGSGLPGPISHALELGKTTAASGKN-FVQLVIAVRGLDMLNACKKE 582
Cdd:cd06186 80 KSPGGGVSLKVLVEGPYGSSSEdLLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTSRTrRVKLVWVVRDREDLEWFLDE 159
|
170
....*....|....*.
gi 767243135 583 LMALKGLNVQ--VHIY 596
Cdd:cd06186 160 LRAAQELEVDgeIEIY 175
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
273-390 |
2.03e-33 |
|
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: 124.30 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 273 SGILSFAHLPLIVLFAGRNNFLQLISGLKHTSFIVFHKWLGRMMFLDAIIHAAGFTNYYLYY---KKWNTVRLRVYWKFG 349
Cdd:pfam01794 1 LGILALALLPLLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFsleGILDLLLKRPYNILG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767243135 350 IAATCLAGMLIFFSIAAFRRHYYETFMALHIVFAALFLYTC 390
Cdd:pfam01794 81 IIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
|
|
| FAD_binding_8 |
pfam08022 |
FAD-binding domain; |
424-525 |
2.02e-32 |
|
FAD-binding domain;
Pssm-ID: 285293 [Multi-domain] Cd Length: 108 Bit Score: 120.90 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 424 LGFPKADLQLVGSDLVRVTVKKPKKFWKAKPGQYVFVSFLRPLCFWQSHPFTVMDSCVNDrELVIVLKAKKGVTKLVRNF 503
Cdd:pfam08022 2 FGVPKAKVALLPDNVLKLRVSKPKKPFKYKPGQYMFINFLPPLSFLQSHPFTITSAPSDD-KLSLHIKVKGGWTRKLANY 80
|
90 100
....*....|....*....|....*...
gi 767243135 504 VERK------GGKASMRLAIEGPYGSKS 525
Cdd:pfam08022 81 LSSScpkspeNGKDKPRVLIEGPYGPPS 108
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
273-541 |
7.71e-19 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 89.95 E-value: 7.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 273 SGILSFAHLPLIVLFAGRNNFL-QLISGLKHTsfIVFHKWLGRMMFLDAIIH-AAGFTNYYLYYKKWNTVRLRVYW---- 346
Cdd:COG4097 46 TGLLALALMSLQFLLAARPPWLeRPFGGLDRL--YRLHKWLGILALVLALAHpLLLLGPKWLVGWGGLPARLAALLtllr 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 347 ----KFGIAAtcLAGMLIFFSIAAFRRHY-YETFMALHIVFAALFLYTCWEHVT---NFSGIEWIY--------AAIAIW 410
Cdd:COG4097 124 glaeLLGEWA--FYLLLALVVLSLLRRRLpYELWRLTHRLLAVAYLLLAFHHLLlggPFYWSPPAGvlwaalaaAGLAAA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 411 GVDRIVRITRIALLGFPKADLQLVGSDLVRVTVKKPKKFWKA-KPGQYVFVSFLRPLCFWQSHPFTVMDSCVNDRELVIV 489
Cdd:COG4097 202 VYSRLGRPLRSRRHPYRVESVEPEAGDVVELTLRPEGGRWLGhRAGQFAFLRFDGSPFWEEAHPFSISSAPGGDGRLRFT 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767243135 490 LKA----KKGVTKLvrnfverkggKASMRLAIEGPYGSKSTAHRFDN--VLLLAGGSG 541
Cdd:COG4097 282 IKAlgdfTRRLGRL----------KPGTRVYVEGPYGRFTFDRRDTAprQVWIAGGIG 329
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
269-605 |
9.57e-15 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 77.97 E-value: 9.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 269 VAYRSGILSFAHLPLIVLFAGRNNFLQLISGLKHTSFIVFHKWLGRMMFLDAIIHAAGF-----TNYYLYYKKWNTVRL- 342
Cdd:PLN02844 155 VATRFGLLAEACLALLLLPVLRGLALFRLLGIQFEASVRYHVWLGTSMIFFATVHGASTlfiwgISHHIQDEIWKWQKTg 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 343 RVYWKFGIAatCLAGMLIFF-SIAAFRRHYYETFMALH---IVFAALFLYtcweHVTNfSGIEWIYAAIAIWGVDRIVRI 418
Cdd:PLN02844 235 RIYLAGEIA--LVTGLVIWItSLPQIRRKRFEIFYYTHhlyIVFLIFFLF----HAGD-RHFYMVFPGIFLFGLDKLLRI 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 419 ----TRIALLG---FPKADLQLVGSDLVRVTvkkpkkfwkAKPGQYVFVSfLRPLCFWQSHPFTVMDSC-VNDRELVIVL 490
Cdd:PLN02844 308 vqsrPETCILSarlFPCKAIELVLPKDPGLK---------YAPTSVIFMK-IPSISRFQWHPFSITSSSnIDDHTMSVII 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 491 KAKKGVTKLVRNFVERK-----GGKASMRLAIEGPYGSKSTAH-RFDNVLLLAGGSGlpgpISHALELGKTTAASGKNF- 563
Cdd:PLN02844 378 KCEGGWTNSLYNKIQAEldsetNQMNCIPVAIEGPYGPASVDFlRYDSLLLVAGGIG----ITPFLSILKEIASQSSSRy 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 767243135 564 -----VQLVIAVR---GLDMLNACKKELM--ALKGLNVQVHIYNSKQELASA 605
Cdd:PLN02844 454 rfpkrVQLIYVVKksqDICLLNPISSLLLnqSSNQLNLKLKVFVTQEEKPNA 505
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
414-593 |
1.53e-09 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 59.11 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 414 RIVRITRIAllgfpkadlqlvgSDLVRVTVKKPKKFWKAKPGQYVFVS----FLRplcfwqsHPFTVMDSCVNDRELVIV 489
Cdd:COG0543 1 KVVSVERLA-------------PDVYLLRLEAPLIALKFKPGQFVMLRvpgdGLR-------RPFSIASAPREDGTIELH 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 490 LKAKKGVTKLVRNFverkggKASMRLAIEGPYGSKSTAHRFD-NVLLLAGGSGLPgPIshaLELGKTTAASGKNfVQLVI 568
Cdd:COG0543 61 IRVVGKGTRALAEL------KPGDELDVRGPLGNGFPLEDSGrPVLLVAGGTGLA-PL---RSLAEALLARGRR-VTLYL 129
|
170 180
....*....|....*....|....*
gi 767243135 569 AVRGLDMLnACKKELMALKGLNVQV 593
Cdd:COG0543 130 GARTPEDL-YLLDELEALADFRVVV 153
|
|
| FNR_like_3 |
cd06198 |
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
454-618 |
4.11e-09 |
|
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: 57.27 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 454 PGQYVFVSFLRPLCfWQSHPFTVMDSCVNDRELVIVLKAKKGVTKLVRNFVerkggKASMRLAIEGPYGSKSTAHRFDNV 533
Cdd:cd06198 25 AGQFAFLRFDASGW-EEPHPFTISSAPDPDGRLRFTIKALGDYTRRLAERL-----KPGTRVTVEGPYGRFTFDDRRARQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 534 LLLAGGSGLpGPISHALELGKTTAASGKnfVQLVIAVRGLDMLNACkKELMAL-KGLNVQVH-IYNSKQELASAEKISSN 611
Cdd:cd06198 99 IWIAGGIGI-TPFLALLEALAARGDARP--VTLFYCVRDPEDAVFL-DELRALaAAAGVVLHvIDSPSDGRLTLEQLVRA 174
|
....*..
gi 767243135 612 EVKNGET 618
Cdd:cd06198 175 LVPDLAD 181
|
|
| PLN02292 |
PLN02292 |
ferric-chelate reductase |
269-547 |
3.40e-07 |
|
ferric-chelate reductase
Pssm-ID: 215165 [Multi-domain] Cd Length: 702 Bit Score: 53.72 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 269 VAYRSGILSFAHLPLIVLFAGRNNFLQLISGLKHTSFIVFHKWLGRMMFldAIIHAAGFTnYYLYYKKWNTVRLRVYW-K 347
Cdd:PLN02292 169 IAVRLGLVGNICLAFLFYPVARGSSLLAAVGLTSESSIKYHIWLGHLVM--TLFTSHGLC-YIIYWISMNQVSQMLEWdR 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 348 FGIA-----ATCLAGMLIFFSI-AAFRRHYYETFMALH---IVFAALFLYtcweHVtnfsGIEwiYAAIA-----IWGVD 413
Cdd:PLN02292 246 TGVSnlageIALVAGLVMWATTyPKIRRRFFEVFFYTHylyIVFMLFFVF----HV----GIS--FALISfpgfyIFLVD 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 414 RIVRITRiallgfPKADLQLVG-----SDLVRVTVKKPKKFWKAkPGQYVFVSfLRPLCFWQSHPFTVMDSC-VNDRELV 487
Cdd:PLN02292 316 RFLRFLQ------SRNNVKLVSarvlpCDTVELNFSKNPMLMYS-PTSIMFVN-IPSISKLQWHPFTITSSSkLEPEKLS 387
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767243135 488 IVLKAK-KGVTKLvRNFVERKGGKASMRLAIEGPYGSKSTAH-RFDNVLLLAGGSGLPGPIS 547
Cdd:PLN02292 388 VMIKSQgKWSTKL-YHMLSSSDQIDRLAVSVEGPYGPASTDFlRHESLVMVSGGSGITPFIS 448
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
530-698 |
7.75e-38 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 137.86 E-value: 7.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 530 FDNVLLLAGGSGLPGPISHALELGKTTAASGKNFVQLVIAVRGLDMLNACKK---ELMALKGLNVQVHIYNSKQELASAE 606
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDvlnELEELKELNIEIHIYLTGEYEAEDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 607 KISSNEVKNGETTAEKAPSSLSNsekapsesentelplslndtsisdlEFATFHVGRPNVEEILNESVN--HSGSLAVVC 684
Cdd:pfam08030 81 SDQSDSSIRSENFDSLMNEVIGV-------------------------DFVEFHFGRPNWKEVLKDIAKqhPNGSIGVFS 135
|
170
....*....|....
gi 767243135 685 CGPPIFVDTARNQT 698
Cdd:pfam08030 136 CGPPSLVDELRNLV 149
|
|
| NOX_Duox_like_FAD_NADP |
cd06186 |
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
428-596 |
2.17e-35 |
|
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: 133.20 E-value: 2.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 428 KADLQLVG-SDLVRVTVKKPKKFWKAkPGQYVFVSFLRPLCFWQSHPFTVMDSCVND-RELVIVLKAKKGVTK-LVRNFV 504
Cdd:cd06186 1 IATVELLPdSDVIRLTIPKPKPFKWK-PGQHVYLNFPSLLSFWQSHPFTIASSPEDEqDTLSLIIRAKKGFTTrLLRKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 505 ERKGGKASMRLAIEGPYGSKST-AHRFDNVLLLAGGSGLPGPISHALELGKTTAASGKN-FVQLVIAVRGLDMLNACKKE 582
Cdd:cd06186 80 KSPGGGVSLKVLVEGPYGSSSEdLLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTSRTrRVKLVWVVRDREDLEWFLDE 159
|
170
....*....|....*.
gi 767243135 583 LMALKGLNVQ--VHIY 596
Cdd:cd06186 160 LRAAQELEVDgeIEIY 175
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
273-390 |
2.03e-33 |
|
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: 124.30 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 273 SGILSFAHLPLIVLFAGRNNFLQLISGLKHTSFIVFHKWLGRMMFLDAIIHAAGFTNYYLYY---KKWNTVRLRVYWKFG 349
Cdd:pfam01794 1 LGILALALLPLLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFsleGILDLLLKRPYNILG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767243135 350 IAATCLAGMLIFFSIAAFRRHYYETFMALHIVFAALFLYTC 390
Cdd:pfam01794 81 IIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
|
|
| FAD_binding_8 |
pfam08022 |
FAD-binding domain; |
424-525 |
2.02e-32 |
|
FAD-binding domain;
Pssm-ID: 285293 [Multi-domain] Cd Length: 108 Bit Score: 120.90 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 424 LGFPKADLQLVGSDLVRVTVKKPKKFWKAKPGQYVFVSFLRPLCFWQSHPFTVMDSCVNDrELVIVLKAKKGVTKLVRNF 503
Cdd:pfam08022 2 FGVPKAKVALLPDNVLKLRVSKPKKPFKYKPGQYMFINFLPPLSFLQSHPFTITSAPSDD-KLSLHIKVKGGWTRKLANY 80
|
90 100
....*....|....*....|....*...
gi 767243135 504 VERK------GGKASMRLAIEGPYGSKS 525
Cdd:pfam08022 81 LSSScpkspeNGKDKPRVLIEGPYGPPS 108
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
273-541 |
7.71e-19 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 89.95 E-value: 7.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 273 SGILSFAHLPLIVLFAGRNNFL-QLISGLKHTsfIVFHKWLGRMMFLDAIIH-AAGFTNYYLYYKKWNTVRLRVYW---- 346
Cdd:COG4097 46 TGLLALALMSLQFLLAARPPWLeRPFGGLDRL--YRLHKWLGILALVLALAHpLLLLGPKWLVGWGGLPARLAALLtllr 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 347 ----KFGIAAtcLAGMLIFFSIAAFRRHY-YETFMALHIVFAALFLYTCWEHVT---NFSGIEWIY--------AAIAIW 410
Cdd:COG4097 124 glaeLLGEWA--FYLLLALVVLSLLRRRLpYELWRLTHRLLAVAYLLLAFHHLLlggPFYWSPPAGvlwaalaaAGLAAA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 411 GVDRIVRITRIALLGFPKADLQLVGSDLVRVTVKKPKKFWKA-KPGQYVFVSFLRPLCFWQSHPFTVMDSCVNDRELVIV 489
Cdd:COG4097 202 VYSRLGRPLRSRRHPYRVESVEPEAGDVVELTLRPEGGRWLGhRAGQFAFLRFDGSPFWEEAHPFSISSAPGGDGRLRFT 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767243135 490 LKA----KKGVTKLvrnfverkggKASMRLAIEGPYGSKSTAHRFDN--VLLLAGGSG 541
Cdd:COG4097 282 IKAlgdfTRRLGRL----------KPGTRVYVEGPYGRFTFDRRDTAprQVWIAGGIG 329
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
269-605 |
9.57e-15 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 77.97 E-value: 9.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 269 VAYRSGILSFAHLPLIVLFAGRNNFLQLISGLKHTSFIVFHKWLGRMMFLDAIIHAAGF-----TNYYLYYKKWNTVRL- 342
Cdd:PLN02844 155 VATRFGLLAEACLALLLLPVLRGLALFRLLGIQFEASVRYHVWLGTSMIFFATVHGASTlfiwgISHHIQDEIWKWQKTg 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 343 RVYWKFGIAatCLAGMLIFF-SIAAFRRHYYETFMALH---IVFAALFLYtcweHVTNfSGIEWIYAAIAIWGVDRIVRI 418
Cdd:PLN02844 235 RIYLAGEIA--LVTGLVIWItSLPQIRRKRFEIFYYTHhlyIVFLIFFLF----HAGD-RHFYMVFPGIFLFGLDKLLRI 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 419 ----TRIALLG---FPKADLQLVGSDLVRVTvkkpkkfwkAKPGQYVFVSfLRPLCFWQSHPFTVMDSC-VNDRELVIVL 490
Cdd:PLN02844 308 vqsrPETCILSarlFPCKAIELVLPKDPGLK---------YAPTSVIFMK-IPSISRFQWHPFSITSSSnIDDHTMSVII 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 491 KAKKGVTKLVRNFVERK-----GGKASMRLAIEGPYGSKSTAH-RFDNVLLLAGGSGlpgpISHALELGKTTAASGKNF- 563
Cdd:PLN02844 378 KCEGGWTNSLYNKIQAEldsetNQMNCIPVAIEGPYGPASVDFlRYDSLLLVAGGIG----ITPFLSILKEIASQSSSRy 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 767243135 564 -----VQLVIAVR---GLDMLNACKKELM--ALKGLNVQVHIYNSKQELASA 605
Cdd:PLN02844 454 rfpkrVQLIYVVKksqDICLLNPISSLLLnqSSNQLNLKLKVFVTQEEKPNA 505
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
414-593 |
1.53e-09 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 59.11 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 414 RIVRITRIAllgfpkadlqlvgSDLVRVTVKKPKKFWKAKPGQYVFVS----FLRplcfwqsHPFTVMDSCVNDRELVIV 489
Cdd:COG0543 1 KVVSVERLA-------------PDVYLLRLEAPLIALKFKPGQFVMLRvpgdGLR-------RPFSIASAPREDGTIELH 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 490 LKAKKGVTKLVRNFverkggKASMRLAIEGPYGSKSTAHRFD-NVLLLAGGSGLPgPIshaLELGKTTAASGKNfVQLVI 568
Cdd:COG0543 61 IRVVGKGTRALAEL------KPGDELDVRGPLGNGFPLEDSGrPVLLVAGGTGLA-PL---RSLAEALLARGRR-VTLYL 129
|
170 180
....*....|....*....|....*
gi 767243135 569 AVRGLDMLnACKKELMALKGLNVQV 593
Cdd:COG0543 130 GARTPEDL-YLLDELEALADFRVVV 153
|
|
| FNR_like_3 |
cd06198 |
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
454-618 |
4.11e-09 |
|
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: 57.27 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 454 PGQYVFVSFLRPLCfWQSHPFTVMDSCVNDRELVIVLKAKKGVTKLVRNFVerkggKASMRLAIEGPYGSKSTAHRFDNV 533
Cdd:cd06198 25 AGQFAFLRFDASGW-EEPHPFTISSAPDPDGRLRFTIKALGDYTRRLAERL-----KPGTRVTVEGPYGRFTFDDRRARQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 534 LLLAGGSGLpGPISHALELGKTTAASGKnfVQLVIAVRGLDMLNACkKELMAL-KGLNVQVH-IYNSKQELASAEKISSN 611
Cdd:cd06198 99 IWIAGGIGI-TPFLALLEALAARGDARP--VTLFYCVRDPEDAVFL-DELRALaAAAGVVLHvIDSPSDGRLTLEQLVRA 174
|
....*..
gi 767243135 612 EVKNGET 618
Cdd:cd06198 175 LVPDLAD 181
|
|
| PLN02292 |
PLN02292 |
ferric-chelate reductase |
269-547 |
3.40e-07 |
|
ferric-chelate reductase
Pssm-ID: 215165 [Multi-domain] Cd Length: 702 Bit Score: 53.72 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 269 VAYRSGILSFAHLPLIVLFAGRNNFLQLISGLKHTSFIVFHKWLGRMMFldAIIHAAGFTnYYLYYKKWNTVRLRVYW-K 347
Cdd:PLN02292 169 IAVRLGLVGNICLAFLFYPVARGSSLLAAVGLTSESSIKYHIWLGHLVM--TLFTSHGLC-YIIYWISMNQVSQMLEWdR 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 348 FGIA-----ATCLAGMLIFFSI-AAFRRHYYETFMALH---IVFAALFLYtcweHVtnfsGIEwiYAAIA-----IWGVD 413
Cdd:PLN02292 246 TGVSnlageIALVAGLVMWATTyPKIRRRFFEVFFYTHylyIVFMLFFVF----HV----GIS--FALISfpgfyIFLVD 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 414 RIVRITRiallgfPKADLQLVG-----SDLVRVTVKKPKKFWKAkPGQYVFVSfLRPLCFWQSHPFTVMDSC-VNDRELV 487
Cdd:PLN02292 316 RFLRFLQ------SRNNVKLVSarvlpCDTVELNFSKNPMLMYS-PTSIMFVN-IPSISKLQWHPFTITSSSkLEPEKLS 387
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767243135 488 IVLKAK-KGVTKLvRNFVERKGGKASMRLAIEGPYGSKSTAH-RFDNVLLLAGGSGLPGPIS 547
Cdd:PLN02292 388 VMIKSQgKWSTKL-YHMLSSSDQIDRLAVSVEGPYGPASTDFlRHESLVMVSGGSGITPFIS 448
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
454-606 |
3.43e-05 |
|
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: 45.52 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 454 PGQYVFVsFLRPLCFWQSHPFTV--MDSCVNDRELVIVLKAKKGVTKLVRNfverkgGKASMRLAIEGPYGsKSTAHRF- 530
Cdd:cd00322 25 PGQYVDL-HLPGDGRGLRRAYSIasSPDEEGELELTVKIVPGGPFSAWLHD------LKPGDEVEVSGPGG-DFFLPLEe 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 531 -DNVLLLAGGSGLPGPIS---HALELGKTTAasgknfVQLVIAVRGLDMLnACKKEL--MALKGLNVQVHIYNSKQELAS 604
Cdd:cd00322 97 sGPVVLIAGGIGITPFRSmlrHLAADKPGGE------ITLLYGARTPADL-LFLDELeeLAKEGPNFRLVLALSRESEAK 169
|
..
gi 767243135 605 AE 606
Cdd:cd00322 170 LG 171
|
|
| DHOD_e_trans_like |
cd06192 |
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ... |
434-569 |
3.86e-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: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 434 VGSDLVRVTVKKPKKFWKAKPGQYVFVS-FLRPLCFWQshPFTVMDSCVNDRELVIVLKAKKGVTKLVRNfvERKGGKAS 512
Cdd:cd06192 7 LEPNLVLLTIKAPLAARLFRPGQFVFLRnFESPGLERI--PLSLAGVDPEEGTISLLVEIRGPKTKLIAE--LKPGEKLD 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767243135 513 MRlaieGPYGSKSTAHRF-DNVLLLAGGSGLPGpishALELGKTTAASGKNFVQLVIA 569
Cdd:cd06192 83 VM----GPLGNGFEGPKKgGTVLLVAGGIGLAP----LLPIAKKLAANGNKVTVLAGA 132
|
|
| PLN02631 |
PLN02631 |
ferric-chelate reductase |
243-552 |
6.05e-05 |
|
ferric-chelate reductase
Pssm-ID: 178238 [Multi-domain] Cd Length: 699 Bit Score: 46.57 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 243 IFMAYKYQYDPYHIIFAAH-RAEV--AHFVAYRSGILSFAHLPLIVLF--AGRNNFLQLISGLKHTSFIVFHKWLGRMMF 317
Cdd:PLN02631 121 AWSLYNYLYLSYHVHLHNDdNAKIwqAKFRAFGLRIGYVGHICWAFLFfpVTRASTILPLVGLTSESSIKYHIWLGHVSN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 318 LDAIIHAAGFTNYYLYYKK------WNTVRlrVYWKFGIAATCLAGMLIFFSIAAFRRHYYETFMALHIVFAaLFLYTCW 391
Cdd:PLN02631 201 FLFLVHTVVFLIYWAMINKlmetfaWNPTY--VPNLAGTIAMVIGIAMWVTSLPSFRRKKFELFFYTHHLYG-LYIVFYV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 392 EHVtnfsGIEW---IYAAIAIWGVDRIVRI---TRIALLgfpkADLQLVGSDLVRVTVKKPKKFWKAkPGQYVFVSfLRP 465
Cdd:PLN02631 278 IHV----GDSWfcmILPNIFLFFIDRYLRFlqsTKRSRL----VSARILPSDNLELTFSKTPGLHYT-PTSILFLH-VPS 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 466 LCFWQSHPFTVMDSCVNDRELVIVLKAKKGvTKLVRNFVERKGGKASMRLAIEGPYGSKS-TAHRFDNVLLLAGGSGLPG 544
Cdd:PLN02631 348 ISKLQWHPFTITSSSNLEKDTLSVVIRRQG-SWTQKLYTHLSSSIDSLEVSTEGPYGPNSfDVSRHNSLILVSGGSGITP 426
|
....*...
gi 767243135 545 PISHALEL 552
Cdd:PLN02631 427 FISVIREL 434
|
|
| DHOD_e_trans_like1 |
cd06219 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
454-577 |
3.38e-04 |
|
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD, forming FADH2 via a semiquinone intermediate, and then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99815 [Multi-domain] Cd Length: 248 Bit Score: 42.95 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 454 PGQYVFVsflrplcfwQSH------PFTVMDScvnDRElvivlkaKKGVTklvrnFVERKGGKASMRLA----------I 517
Cdd:cd06219 29 PGQFVIV---------RADekgeriPLTIADW---DPE-------KGTIT-----IVVQVVGKSTRELAtleegdkihdV 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767243135 518 EGPYGSKSTAHRFDNVLLLAGGSGLPG--PISHAL-ELGkttaasgkNFVQLVIAVRGLDMLN 577
Cdd:cd06219 85 VGPLGKPSEIENYGTVVFVGGGVGIAPiyPIAKALkEAG--------NRVITIIGARTKDLVI 139
|
|
| T4MO_e_transfer_like |
cd06190 |
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ... |
503-607 |
6.76e-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: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243135 503 FVERK--GGKAS----------MRLAIEGPYGsKSTAHRFD--NVLLLAGGSGlpgpISHALELGKTTAASGKNF---VQ 565
Cdd:cd06190 57 FIIKRkpGGAASnalfdnlepgDELELDGPYG-LAYLRPDEdrDIVCIAGGSG----LAPMLSILRGAARSPYLSdrpVD 131
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 767243135 566 LVIAVRGLDMLnACKKELMALKGLNVQVHIYNSKQELASAEK 607
Cdd:cd06190 132 LFYGGRTPSDL-CALDELSALVALGARLRVTPAVSDAGSGSA 172
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
516-576 |
9.62e-03 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 39.43 E-value: 9.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767243135 516 AIEGPYGSKSTAHRFD---NVLLLAGGSGLPG--PISHA-LELGkttaasgkNFVQLVIAVRGLDML 576
Cdd:PRK12779 733 GIAGPLGRASELHRYEgnqTVVFCAGGVGLPPvyPIMRAhLRLG--------NHVTLISGFRAKEFL 791
|
|
| |
