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Conserved domains on  [gi|2100284677|gb|KAH0607062|]
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hypothetical protein H6S33_003050 [Morchella sextelata]

Protein Classification

ferric reductase family protein( domain architecture ID 10484952)

ferric reductase family protein functions as an oxidoreductase, such as human NADPH oxidase 1, a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes and other tissues

EC:  1.-.-.-
Gene Ontology:  GO:0050661|GO:0016491|GO:0016020

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 334-605 1.34e-59

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: 197.91  E-value: 1.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 334 TATVEILP-GEAIRVTLKLARPWKFRPGQHVYLYVPSV-GLWTSHPFTIAWGEQLQQNHkmdderlsfhrqdlmhigekt 411
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDT--------------------- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 412 MSLVIRRRTGFTNALFNKADATPNKVITLKALAEGPYG-KVDSLASYGTVVLVAGGVGITHPVPHIRDLVEGYAKgTVAT 490
Cdd:cd06186    60 LSLIIRAKKGFTTRLLRKALKSPGGGVSLKVLVEGPYGsSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSK-TSRT 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 491 KRIVLVWVVQSPEHLEWIRPWMTDILAMErrrEVLEIQLFVTRpsstkaihspsatvqmfpgrpnidtildreidrrmgt 570
Cdd:cd06186   139 RRVKLVWVVRDREDLEWFLDELRAAQELE---VDGEIEIYVTR------------------------------------- 178

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2100284677 571 mgVTVCGSGSLSDDVRRAVrAKMDIANIDFIEEAF 605
Cdd:cd06186   179 --VVVCGPPGLVDDVRNAV-AKKGGTGVEFHEESF 210
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 169-290 5.25e-24

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: 97.34  E-value: 5.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 169 TGVLSTINLVPLFLLAGRNNPLIQLMGISFDTYNLVHRWLGRIVVTEAFAHSACWAAAKVMKGGWAPVGAAIQGSvFIQM 248
Cdd:pfam01794   1 LGILALALLPLLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSLEGILDLLLKRP-YNIL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2100284677 249 GFVGTCAFVFLMCHSPSSLRHAFYETFLFLHIVAAAVALGGL 290
Cdd:pfam01794  80 GIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
 
Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 334-605 1.34e-59

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: 197.91  E-value: 1.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 334 TATVEILP-GEAIRVTLKLARPWKFRPGQHVYLYVPSV-GLWTSHPFTIAWGEQLQQNHkmdderlsfhrqdlmhigekt 411
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDT--------------------- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 412 MSLVIRRRTGFTNALFNKADATPNKVITLKALAEGPYG-KVDSLASYGTVVLVAGGVGITHPVPHIRDLVEGYAKgTVAT 490
Cdd:cd06186    60 LSLIIRAKKGFTTRLLRKALKSPGGGVSLKVLVEGPYGsSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSK-TSRT 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 491 KRIVLVWVVQSPEHLEWIRPWMTDILAMErrrEVLEIQLFVTRpsstkaihspsatvqmfpgrpnidtildreidrrmgt 570
Cdd:cd06186   139 RRVKLVWVVRDREDLEWFLDELRAAQELE---VDGEIEIYVTR------------------------------------- 178

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2100284677 571 mgVTVCGSGSLSDDVRRAVrAKMDIANIDFIEEAF 605
Cdd:cd06186   179 --VVVCGPPGLVDDVRNAV-AKKGGTGVEFHEESF 210
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 169-290 5.25e-24

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: 97.34  E-value: 5.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 169 TGVLSTINLVPLFLLAGRNNPLIQLMGISFDTYNLVHRWLGRIVVTEAFAHSACWAAAKVMKGGWAPVGAAIQGSvFIQM 248
Cdd:pfam01794   1 LGILALALLPLLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSLEGILDLLLKRP-YNIL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2100284677 249 GFVGTCAFVFLMCHSPSSLRHAFYETFLFLHIVAAAVALGGL 290
Cdd:pfam01794  80 GIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
457-589 1.54e-22

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 93.94  E-value: 1.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 457 YGTVVLVAGGVGITHPVPHIRDLVEGYAKgtVATKRIVLVWVVQSPEHLEWIRPWMTDIlaMERRREVLEIQLFVTRP-- 534
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKK--LKTKKIKFYWVVRDLSSLEWFKDVLNEL--EELKELNIEIHIYLTGEye 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2100284677 535 ------SSTKAIHSPSAT-----------VQMFPGRPNIDTILDREIDRRMG-TMGVTVCGSGSLSDDVRRAV 589
Cdd:pfam08030  77 aedasdQSDSSIRSENFDslmnevigvdfVEFHFGRPNWKEVLKDIAKQHPNgSIGVFSCGPPSLVDELRNLV 149
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
130-607 2.66e-21

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 96.89  E-value: 2.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 130 TRFESFFLIGYVVGNIVFSL-----HKIDWDSETTAILGEIRNRTGVLSTINLVPLFLLAGRNNPLIQLMGiSFD-TYNL 203
Cdd:COG4097     2 KRLRALLLIALYALLVLLPLlwllaDPLPAPAGGRGLRTALGQLTGLLALALMSLQFLLAARPPWLERPFG-GLDrLYRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 204 vHRWLGRIVVTEAFAHSACWAAAKVMKG-GWAPVGAA----IQGSVFIQMGFVGTCAFVFLMchSPSSLRHAF-YETFLF 277
Cdd:COG4097    81 -HKWLGILALVLALAHPLLLLGPKWLVGwGGLPARLAalltLLRGLAELLGEWAFYLLLALV--VLSLLRRRLpYELWRL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 278 LHIVAAAVALGGLWMHLDYKKYR---------WLVYVKIAIALWVfdrsVRLFRIIYRNIGKRITTATVEILPGEAIRVT 348
Cdd:COG4097   158 THRLLAVAYLLLAFHHLLLGGPFywsppagvlWAALAAAGLAAAV----YSRLGRPLRSRRHPYRVESVEPEAGDVVELT 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 349 LKL--ARPWKFRPGQHVYLYVP-SVGLWTSHPFTI--AWGeqlqqnhkmDDERLSFHrqdlmhigektmslvIRRRTGFT 423
Cdd:COG4097   234 LRPegGRWLGHRAGQFAFLRFDgSPFWEEAHPFSIssAPG---------GDGRLRFT---------------IKALGDFT 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 424 NALfnkADATPNKvitlKALAEGPYGKVDSLASYGT--VVLVAGGVGIThPvphIRDLVEGYAKGTVATKRIVLVWVVQS 501
Cdd:COG4097   290 RRL---GRLKPGT----RVYVEGPYGRFTFDRRDTAprQVWIAGGIGIT-P---FLALLRALAARPGDQRPVDLFYCVRD 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 502 PEHLewirPWMTDILAMERRREVLEIQLFVTRPSstkaihspsatvqmfpGRPNIDTILdREIDRRMGTMgVTVCGSGSL 581
Cdd:COG4097   359 EEDA----PFLEELRALAARLAGLRLHLVVSDED----------------GRLTAERLR-RLVPDLAEAD-VFFCGPPGM 416

                         490       500
                  ....*....|....*....|....*.
gi 2100284677 582 SDDVRRAVRAkMDIANIDFIEEAFSW 607
Cdd:COG4097   417 MDALRRDLRA-LGVPARRIHQERFEF 441
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 168-550 1.89e-14

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 76.81  E-value: 1.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 168 RTGVLSTINLVPLFLLAGRNNPLIQLMGISFDTYNLVHRWLGRIVVTEAFAHSAC----WAAAKVMK---GGWAPVGAA- 239
Cdd:PLN02844  158 RFGLLAEACLALLLLPVLRGLALFRLLGIQFEASVRYHVWLGTSMIFFATVHGAStlfiWGISHHIQdeiWKWQKTGRIy 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 240 IQGSVFIQMGFVgtcafvfLMCHSPSSLRHAFYETFLFLHIVAAaVALGGLWMHLDYKKYRWlvyVKIAIALWVFDRsvr 319
Cdd:PLN02844  238 LAGEIALVTGLV-------IWITSLPQIRRKRFEIFYYTHHLYI-VFLIFFLFHAGDRHFYM---VFPGIFLFGLDK--- 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 320 LFRIIYRNIGKRITTAtvEILPGEAIRVTLKLARPWKFRPGQHVYLYVPSVGLWTSHPFTIAWGEqlqqnhkmdderlsf 399
Cdd:PLN02844  304 LLRIVQSRPETCILSA--RLFPCKAIELVLPKDPGLKYAPTSVIFMKIPSISRFQWHPFSITSSS--------------- 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 400 hrqdlmHIGEKTMSLVIRRRTGFTNALFNK----ADATPNKVITLKALAEGPYG--KVDSLaSYGTVVLVAGGVGITHPV 473
Cdd:PLN02844  367 ------NIDDHTMSVIIKCEGGWTNSLYNKiqaeLDSETNQMNCIPVAIEGPYGpaSVDFL-RYDSLLLVAGGIGITPFL 439

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2100284677 474 PHIRDLVEGYAKGTVATKRIVLVWVVQSPEHLEWIRPWMTDILAMERRREVLEIQLFVTRPSstkaihSPSATVQMF 550
Cdd:PLN02844  440 SILKEIASQSSSRYRFPKRVQLIYVVKKSQDICLLNPISSLLLNQSSNQLNLKLKVFVTQEE------KPNATLREL 510
 
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 ...
 334-605 1.34e-59

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: 197.91  E-value: 1.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 334 TATVEILP-GEAIRVTLKLARPWKFRPGQHVYLYVPSV-GLWTSHPFTIAWGEQLQQNHkmdderlsfhrqdlmhigekt 411
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDT--------------------- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 412 MSLVIRRRTGFTNALFNKADATPNKVITLKALAEGPYG-KVDSLASYGTVVLVAGGVGITHPVPHIRDLVEGYAKgTVAT 490
Cdd:cd06186    60 LSLIIRAKKGFTTRLLRKALKSPGGGVSLKVLVEGPYGsSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSK-TSRT 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 491 KRIVLVWVVQSPEHLEWIRPWMTDILAMErrrEVLEIQLFVTRpsstkaihspsatvqmfpgrpnidtildreidrrmgt 570
Cdd:cd06186   139 RRVKLVWVVRDREDLEWFLDELRAAQELE---VDGEIEIYVTR------------------------------------- 178

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2100284677 571 mgVTVCGSGSLSDDVRRAVrAKMDIANIDFIEEAF 605
Cdd:cd06186   179 --VVVCGPPGLVDDVRNAV-AKKGGTGVEFHEESF 210
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 169-290 5.25e-24

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: 97.34  E-value: 5.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 169 TGVLSTINLVPLFLLAGRNNPLIQLMGISFDTYNLVHRWLGRIVVTEAFAHSACWAAAKVMKGGWAPVGAAIQGSvFIQM 248
Cdd:pfam01794   1 LGILALALLPLLLLLALRNNPLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSLEGILDLLLKRP-YNIL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2100284677 249 GFVGTCAFVFLMCHSPSSLRHAFYETFLFLHIVAAAVALGGL 290
Cdd:pfam01794  80 GIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
457-589 1.54e-22

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 93.94  E-value: 1.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 457 YGTVVLVAGGVGITHPVPHIRDLVEGYAKgtVATKRIVLVWVVQSPEHLEWIRPWMTDIlaMERRREVLEIQLFVTRP-- 534
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKK--LKTKKIKFYWVVRDLSSLEWFKDVLNEL--EELKELNIEIHIYLTGEye 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2100284677 535 ------SSTKAIHSPSAT-----------VQMFPGRPNIDTILDREIDRRMG-TMGVTVCGSGSLSDDVRRAV 589
Cdd:pfam08030  77 aedasdQSDSSIRSENFDslmnevigvdfVEFHFGRPNWKEVLKDIAKQHPNgSIGVFSCGPPSLVDELRNLV 149
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
130-607 2.66e-21

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 96.89  E-value: 2.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 130 TRFESFFLIGYVVGNIVFSL-----HKIDWDSETTAILGEIRNRTGVLSTINLVPLFLLAGRNNPLIQLMGiSFD-TYNL 203
Cdd:COG4097     2 KRLRALLLIALYALLVLLPLlwllaDPLPAPAGGRGLRTALGQLTGLLALALMSLQFLLAARPPWLERPFG-GLDrLYRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 204 vHRWLGRIVVTEAFAHSACWAAAKVMKG-GWAPVGAA----IQGSVFIQMGFVGTCAFVFLMchSPSSLRHAF-YETFLF 277
Cdd:COG4097    81 -HKWLGILALVLALAHPLLLLGPKWLVGwGGLPARLAalltLLRGLAELLGEWAFYLLLALV--VLSLLRRRLpYELWRL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 278 LHIVAAAVALGGLWMHLDYKKYR---------WLVYVKIAIALWVfdrsVRLFRIIYRNIGKRITTATVEILPGEAIRVT 348
Cdd:COG4097   158 THRLLAVAYLLLAFHHLLLGGPFywsppagvlWAALAAAGLAAAV----YSRLGRPLRSRRHPYRVESVEPEAGDVVELT 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 349 LKL--ARPWKFRPGQHVYLYVP-SVGLWTSHPFTI--AWGeqlqqnhkmDDERLSFHrqdlmhigektmslvIRRRTGFT 423
Cdd:COG4097   234 LRPegGRWLGHRAGQFAFLRFDgSPFWEEAHPFSIssAPG---------GDGRLRFT---------------IKALGDFT 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 424 NALfnkADATPNKvitlKALAEGPYGKVDSLASYGT--VVLVAGGVGIThPvphIRDLVEGYAKGTVATKRIVLVWVVQS 501
Cdd:COG4097   290 RRL---GRLKPGT----RVYVEGPYGRFTFDRRDTAprQVWIAGGIGIT-P---FLALLRALAARPGDQRPVDLFYCVRD 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 502 PEHLewirPWMTDILAMERRREVLEIQLFVTRPSstkaihspsatvqmfpGRPNIDTILdREIDRRMGTMgVTVCGSGSL 581
Cdd:COG4097   359 EEDA----PFLEELRALAARLAGLRLHLVVSDED----------------GRLTAERLR-RLVPDLAEAD-VFFCGPPGM 416

                         490       500
                  ....*....|....*....|....*.
gi 2100284677 582 SDDVRRAVRAkMDIANIDFIEEAFSW 607
Cdd:COG4097   417 MDALRRDLRA-LGVPARRIHQERFEF 441
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 331-602 1.39e-18

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: 84.81  E-value: 1.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 331 RITTATVEIlpgeaIRVTLKLARPWKFRPGQHVYLYVPSVGLWTSHPFTIAwgeqlqqnhKMDDERLSFHrqdlmhigek 410
Cdd:cd00322     2 ATEDVTDDV-----RLFRLQLPNGFSFKPGQYVDLHLPGDGRGLRRAYSIA---------SSPDEEGELE---------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 411 tmsLVIRRRTG--FTNALFNKAdatPNKVITLKalaeGPYGK-VDSLASYGTVVLVAGGVGITHPVPHIRDLVEgyakgT 487
Cdd:cd00322    58 ---LTVKIVPGgpFSAWLHDLK---PGDEVEVS----GPGGDfFLPLEESGPVVLIAGGIGITPFRSMLRHLAA-----D 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 488 VATKRIVLVWVVQSPEHLeWIRPwmtDILAMERRREVLEIQLFVTRPSSTKaihspsatvqMFPGRPNIDTILDREIDRR 567
Cdd:cd00322   123 KPGGEITLLYGARTPADL-LFLD---ELEELAKEGPNFRLVLALSRESEAK----------LGPGGRIDREAEILALLPD 188

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2100284677 568 MGTMGVTVCGSGSLSDDVRRAVRAKMDIANIDFIE 602
Cdd:cd00322   189 DSGALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 168-550 1.89e-14

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 76.81  E-value: 1.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 168 RTGVLSTINLVPLFLLAGRNNPLIQLMGISFDTYNLVHRWLGRIVVTEAFAHSAC----WAAAKVMK---GGWAPVGAA- 239
Cdd:PLN02844  158 RFGLLAEACLALLLLPVLRGLALFRLLGIQFEASVRYHVWLGTSMIFFATVHGAStlfiWGISHHIQdeiWKWQKTGRIy 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 240 IQGSVFIQMGFVgtcafvfLMCHSPSSLRHAFYETFLFLHIVAAaVALGGLWMHLDYKKYRWlvyVKIAIALWVFDRsvr 319
Cdd:PLN02844  238 LAGEIALVTGLV-------IWITSLPQIRRKRFEIFYYTHHLYI-VFLIFFLFHAGDRHFYM---VFPGIFLFGLDK--- 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 320 LFRIIYRNIGKRITTAtvEILPGEAIRVTLKLARPWKFRPGQHVYLYVPSVGLWTSHPFTIAWGEqlqqnhkmdderlsf 399
Cdd:PLN02844  304 LLRIVQSRPETCILSA--RLFPCKAIELVLPKDPGLKYAPTSVIFMKIPSISRFQWHPFSITSSS--------------- 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 400 hrqdlmHIGEKTMSLVIRRRTGFTNALFNK----ADATPNKVITLKALAEGPYG--KVDSLaSYGTVVLVAGGVGITHPV 473
Cdd:PLN02844  367 ------NIDDHTMSVIIKCEGGWTNSLYNKiqaeLDSETNQMNCIPVAIEGPYGpaSVDFL-RYDSLLLVAGGIGITPFL 439

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2100284677 474 PHIRDLVEGYAKGTVATKRIVLVWVVQSPEHLEWIRPWMTDILAMERRREVLEIQLFVTRPSstkaihSPSATVQMF 550
Cdd:PLN02844  440 SILKEIASQSSSRYRFPKRVQLIYVVKKSQDICLLNPISSLLLNQSSNQLNLKLKVFVTQEE------KPNATLREL 510
FAD_binding_8 pfam08022
FAD-binding domain;
330-449 3.69e-14

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 68.90  E-value: 3.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 330 KRITTATVEILPGEAIRVTL-KLARPWKFRPGQHVYLY-VPSVGLWTSHPFTIAWGEQlqqnhkmDDErlsfhrqdlmhi 407
Cdd:pfam08022   2 FGVPKAKVALLPDNVLKLRVsKPKKPFKYKPGQYMFINfLPPLSFLQSHPFTITSAPS-------DDK------------ 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2100284677 408 gektMSLVIRRRTGFTNALFNK-----ADATPNKVITLKALAEGPYG 449
Cdd:pfam08022  63 ----LSLHIKVKGGWTRKLANYlssscPKSPENGKDKPRVLIEGPYG 105
PLN02631 PLN02631
ferric-chelate reductase
 168-533 6.23e-14

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 75.08  E-value: 6.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 168 RTGVLSTINLVPLFLLAGRNNPLIQLMGISFDTYNLVHRWLGRIVVTEAFAHSAC----WAAA-KVMKG-GWAPVGAA-I 240
Cdd:PLN02631  155 RIGYVGHICWAFLFFPVTRASTILPLVGLTSESSIKYHIWLGHVSNFLFLVHTVVfliyWAMInKLMETfAWNPTYVPnL 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 241 QGSVFIQMGfvgtcafVFLMCHSPSSLRHAFYETFLFLHivaaavALGGLWM--HLDYKKYRWLVYVKIAIALWVFDRSV 318
Cdd:PLN02631  235 AGTIAMVIG-------IAMWVTSLPSFRRKKFELFFYTH------HLYGLYIvfYVIHVGDSWFCMILPNIFLFFIDRYL 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 319 RLFRIIyrnigKRITTATVEILPGEAIRVTLKLARPWKFRPGQHVYLYVPSVGLWTSHPFTIAWGEQLQQNhkmdderls 398
Cdd:PLN02631  302 RFLQST-----KRSRLVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNLEKD--------- 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 399 fhrqdlmhigekTMSLVIRRRTGFTNALFNKADATpnkVITLKALAEGPYGKVD-SLASYGTVVLVAGGVGITHPVPHIR 477
Cdd:PLN02631  368 ------------TLSVVIRRQGSWTQKLYTHLSSS---IDSLEVSTEGPYGPNSfDVSRHNSLILVSGGSGITPFISVIR 432

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2100284677 478 DLVEGYAKGTVATKRIVLVWVVQSPEHLEWIR-PWMTDILAMERRREVLEIQLFVTR 533
Cdd:PLN02631  433 ELIFQSQNPSTKLPDVLLVCSFKHYHDLAFLDlIFPLDISVSDISRLNLRIEAYITR 489
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 336-606 1.84e-12

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: 66.90  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 336 TVEILPGEAIRVTLKlARPWKFRPGQHVYLYVPSVGLWTSHPFTIAwgeqlqqNHKMDDERLSFhrqdlmhigektmslV 415
Cdd:cd06198     3 VTEVRPTTTLTLEPR-GPALGHRAGQFAFLRFDASGWEEPHPFTIS-------SAPDPDGRLRF---------------T 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 416 IRRRTGFTNALfnKADATPNKvitlKALAEGPYGKVDSLASYGTVVLVAGGVGIThPvphIRDLVEGYAKGTvATKRIVL 495
Cdd:cd06198    60 IKALGDYTRRL--AERLKPGT----RVTVEGPYGRFTFDDRRARQIWIAGGIGIT-P---FLALLEALAARG-DARPVTL 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 496 VWVVQSPEhlewiRPWMTDIL-AMERRREVlEIQLFVTRPsstkaihspsatvqmfPGRPNIDTILDREIDRRMGTmGVT 574
Cdd:cd06198   129 FYCVRDPE-----DAVFLDELrALAAAAGV-VLHVIDSPS----------------DGRLTLEQLVRALVPDLADA-DVW 185

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2100284677 575 VCGSGSLSDDVRRAVRAKmDIANIDFIEEAFS 606
Cdd:cd06198   186 FCGPPGMADALEKGLRAL-GVPARRFHYERFE 216
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 346-511 7.61e-11

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 62.57  E-value: 7.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 346 RVTLKL-ARPWKFRPGQHVYLYVPSVGLWTshPFTIAwgeqlqqNHKMDDERLSFHrqdlmhigektmslvIRRRTGFTN 424
Cdd:COG0543    14 LLRLEApLIALKFKPGQFVMLRVPGDGLRR--PFSIA-------SAPREDGTIELH---------------IRVVGKGTR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 425 ALFNKAdatPNKVITLkalaEGPYGKVDSL-ASYGTVVLVAGGVGIThPVPHI-RDLVEGYakgtvatKRIVLVWVVQSP 502
Cdd:COG0543    70 ALAELK---PGDELDV----RGPLGNGFPLeDSGRPVLLVAGGTGLA-PLRSLaEALLARG-------RRVTLYLGARTP 134

                         170
                  ....*....|..
gi 2100284677 503 EHL---EWIRPW 511
Cdd:COG0543   135 EDLyllDELEAL 146
PLN02292 PLN02292
ferric-chelate reductase
 152-533 2.08e-09

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 60.65  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 152 IDWDSETTAILGEIRNRTGVLSTINLVPLFLLAGRNNPLIQLMGISFDTYNLVHRWLGRIVVTEAFAHSAC----WAAAK 227
Cdd:PLN02292  156 TDGESLWQARLDSIAVRLGLVGNICLAFLFYPVARGSSLLAAVGLTSESSIKYHIWLGHLVMTLFTSHGLCyiiyWISMN 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 228 VMKG--GWAPVGAA-IQGSVFIQMGFVgtcafvfLMCHSPSSLRHAFYETFLFLHIVAAAVALgglwmhldykkyRWLVY 304
Cdd:PLN02292  236 QVSQmlEWDRTGVSnLAGEIALVAGLV-------MWATTYPKIRRRFFEVFFYTHYLYIVFML------------FFVFH 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 305 VKIAIALWVF--------DRSVRLFRiiYRNigkRITTATVEILPGEAIRVTLKLARPWKFRPGQHVYLYVPSVGLWTSH 376
Cdd:PLN02292  297 VGISFALISFpgfyiflvDRFLRFLQ--SRN---NVKLVSARVLPCDTVELNFSKNPMLMYSPTSIMFVNIPSISKLQWH 371

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 377 PFTIAWGEQLQqnhkmdderlsfhrqdlmhigEKTMSLVIRRRTGFTNALFNKAdATPNKVITLKALAEGPYG--KVDSL 454
Cdd:PLN02292  372 PFTITSSSKLE---------------------PEKLSVMIKSQGKWSTKLYHML-SSSDQIDRLAVSVEGPYGpaSTDFL 429

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 455 aSYGTVVLVAGGVGITHPVPHIRDLVEGYAKGTVATKRIVLVWVVQSPEH---LEWIRPwmTDILAMERRREV-LEIQLF 530
Cdd:PLN02292  430 -RHESLVMVSGGSGITPFISIIRDLIYTSSTETCKIPKITLICAFKNSSDlsmLDLILP--TSGLETELSSFIdIQIKAF 506


                  ...
gi 2100284677 531 VTR 533
Cdd:PLN02292  507 VTR 509
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
347-591 2.36e-08

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 55.18  E-value: 2.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 347 VTLKLARP-----WKFRPGQHVYLYVPSVGLWTSHPFTIAWGEqlqqnhkmDDERLSFHrqdlmhigektmslVIRRRTG 421
Cdd:COG1018    19 VSFTLEPPdgaplPRFRPGQFVTLRLPIDGKPLRRAYSLSSAP--------GDGRLEIT--------------VKRVPGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 422 -FTNALFNkaDATPNKVITLKalaeGPYGK-VDSLASYGTVVLVAGGVGIThPV-PHIRDLVEgyakgTVATKRIVLVWV 498
Cdd:COG1018    77 gGSNWLHD--HLKVGDTLEVS----GPRGDfVLDPEPARPLLLIAGGIGIT-PFlSMLRTLLA-----RGPFRPVTLVYG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 499 VQSPEHLewirPWMTDILAMERRREVLEIQLFVTRPSSTkaihspsatvqmFPGRPN---IDTILDREIDRRmgtmgVTV 575
Cdd:COG1018   145 ARSPADL----AFRDELEALAARHPRLRLHPVLSREPAG------------LQGRLDaelLAALLPDPADAH-----VYL 203

                         250
                  ....*....|....*.
gi 2100284677 576 CGSGSLSDDVRRAVRA 591
Cdd:COG1018   204 CGPPPMMEAVRAALAE 219
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 334-532 8.83e-07

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: 50.68  E-value: 8.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 334 TATVEILPGEAIrVTLKLA----RPWKFRPGQHVYLYVPSVGlwtSHPFTIAWGEqlqqnhkMDDERLsfhrqdlmhige 409
Cdd:cd06221     2 VEVVDETEDIKT-FTLRLEdddeELFTFKPGQFVMLSLPGVG---EAPISISSDP-------TRRGPL------------ 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 410 ktmSLVIRRRTGFTNALFnkaDATPNKVITLKalaeGPYGK---VDSLASYgTVVLVAGGVGITHPVPHIRDLVEGYAKG 486
Cdd:cd06221    59 ---ELTIRRVGRVTEALH---ELKPGDTVGLR----GPFGNgfpVEEMKGK-DLLLVAGGLGLAPLRSLINYILDNREDY 127

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2100284677 487 tvatKRIVLVWVVQSPEHLEWIRpwmtdilAMERRREVLEIQLFVT 532
Cdd:cd06221   128 ----GKVTLLYGARTPEDLLFKE-------ELKEWAKRSDVEVILT 162
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 345-511 1.06e-04

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: 44.08  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 345 IRVTLKLARPWKFRPGQHVYLYVPSVglwTSHPFTIAwgeqlqqNHKMDDERLSFHrqdlmhigektmslvIRRRTG--F 422
Cdd:cd06189    14 YRVRLKPPAPLDFLAGQYLDLLLDDG---DKRPFSIA-------SAPHEDGEIELH---------------IRAVPGgsF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 423 TNALFNKadATPNKVITLkalaEGPYGKVdSL--ASYGTVVLVAGGVGIThpvpHIRDLVEgYAKGTVATKRIVLVWVVQ 500
Cdd:cd06189    69 SDYVFEE--LKENGLVRI----EGPLGDF-FLreDSDRPLILIAGGTGFA----PIKSILE-HLLAQGSKRPIHLYWGAR 136

                         170
                  ....*....|....
gi 2100284677 501 SPEHL---EWIRPW 511
Cdd:cd06189   137 TEEDLyldELLEAW 150
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 345-505 1.31e-04

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: 43.74  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 345 IRVTLKLARPWKFRPGQHVYLYVPSVG-LWTSHPFTIAWGEqlqqnhkmdDERLSFHrqdlmhigektmslvIRRRTG-- 421
Cdd:cd06187    12 AVVRLQLDQPLPFWAGQYVNVTVPGRPrTWRAYSPANPPNE---------DGEIEFH---------------VRAVPGgr 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 422 FTNALFNkaDATPNKVITLkalaEGPYGK-VDSLASYGTVVLVAGGVGIThPvphIRDLVEGYAKGTVaTKRIVLVWVVQ 500
Cdd:cd06187    68 VSNALHD--ELKVGDRVRL----SGPYGTfYLRRDHDRPVLCIAGGTGLA-P---LRAIVEDALRRGE-PRPVHLFFGAR 136


                  ....*
gi 2100284677 501 SPEHL 505
Cdd:cd06187   137 TERDL 141
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 336-488 2.11e-04

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 43.32  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 336 TVEILPGeaIRvTLKLARPWKF--RPGQHVYLYVPSVGLWTSHPFTIAWgeqlqqnhkmdderlsfhrqdlmhIGEKTMS 413
Cdd:PRK00054   12 NKEIAPN--IY-TLVLDGEKVFdmKPGQFVMVWVPGVEPLLERPISISD------------------------IDKNEIT 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2100284677 414 LVIRRRTGFTNALFNKADATpnkviTLKALaeGPYGK-VDSLASYGTVVLVAGGVGITHPVPHIRDLVEGYAKGTV 488
Cdd:PRK00054   65 ILYRKVGEGTKKLSKLKEGD-----ELDIR--GPLGNgFDLEEIGGKVLLVGGGIGVAPLYELAKELKKKGVEVTT 133
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 333-469 2.21e-04

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. 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 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: 99809  Cd Length: 227  Bit Score: 43.07  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 333 TTATVEILPGEAIRVTLKLARPWKFRPGQHVYLYVPSVGLWTSHPFTIAWGEqlqqnhkmdDERLSFHrqdlmhigektm 412
Cdd:cd06213     4 TIVAQERLTHDIVRLTVQLDRPIAYKAGQYAELTLPGLPAARSYSFANAPQG---------DGQLSFH------------ 62

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2100284677 413 slvIRRRTG--FTNALFNKadATPNKVITLkalaEGPYGKVDSLASYGTVVLVAGGVGI 469
Cdd:cd06213    63 ---IRKVPGgaFSGWLFGA--DRTGERLTV----RGPFGDFWLRPGDAPILCIAGGSGL 112
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 330-469 2.57e-03

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: 40.00  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 330 KRITTATVEIlpgeAIRVTLKLARpwkFRPGQHVYLYVPSVGLWTSHPFTIAWGeqlqqnhkmDDErlsfhrqdlmhigE 409
Cdd:cd06192     5 EQLEPNLVLL----TIKAPLAARL---FRPGQFVFLRNFESPGLERIPLSLAGV---------DPE-------------E 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2100284677 410 KTMSLVIRRRTGFTNALFNKADATPNKVItlkalaeGPYGK-VDSLASYGTVVLVAGGVGI 469
Cdd:cd06192    56 GTISLLVEIRGPKTKLIAELKPGEKLDVM-------GPLGNgFEGPKKGGTVLLVAGGIGL 109
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 348-469 6.91e-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: 38.38  E-value: 6.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100284677 348 TLKLARPWKFRPGQHVYLYVPSVGlwtSHPFTIAwgeqlqqnhkmdderlsfhrqdlmhIGEKTMSLVIRRRTGFTNALF 427
Cdd:cd06220    15 TFVFDWDFDFKPGQFVMVWVPGVD---EIPMSLS-------------------------YIDGPNSITVKKVGEATSALH 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2100284677 428 NKAdatPNKVITLKalaeGPYGKVDSLASyGTVVLVAGGVGI 469
Cdd:cd06220    67 DLK---EGDKLGIR----GPYGNGFELVG-GKVLLIGGGIGI 100
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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