NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|500663573|ref|WP_011968347|]
View 

dihydroorotate dehydrogenase electron transfer subunit [Clostridium beijerinckii]

Protein Classification

dihydroorotate dehydrogenase electron transfer subunit( domain architecture ID 11477869)

dihydroorotate dehydrogenase electron transfer subunit is part of the enzyme complex that catalyzes the ubiquinone-mediated oxidation of (D)-dihydroorotate to orotate, an essential step in pyrimidine de novo biosynthesis

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 3-247 1.08e-124

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


:

Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 353.79  E-value: 1.08e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   3 ITYRNAKVVSNKEISKDIYKLVV--EDDAEIKAGQFYMLKLNGAT-FLPRPISICEKSKNKLTFLYAVVGNGTKEFTKLK 79
Cdd:PRK00054   2 MKPENMKIVENKEIAPNIYTLVLdgEKVFDMKPGQFVMVWVPGVEpLLERPISISDIDKNEITILYRKVGEGTKKLSKLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  80 EDDEISLTGPLGNGFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFRHDVYLIDELKEyVNEVYISTN 159
Cdd:PRK00054  82 EGDELDIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTKDEVIFEEEFAK-VGDVYVTTD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 160 TGKNGHKGFVTEILKPED--YDTVLCCGPEIMMKKVVDMCKEKNVAVYVSMEKHMACGVGACLVCTCKTKDGHKRTCKDG 237
Cdd:PRK00054 161 DGSYGFKGFVTDVLDELDseYDAIYSCGPEIMMKKVVEILKEKKVPAYVSLERRMKCGIGACGACVCDTETGGKRVCKDG 240

                        250
                 ....*....|
gi 500663573 238 PIFDGYYVEL 247
Cdd:PRK00054 241 PVFSGGELVL 250
 
Name Accession Description Interval E-value
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 3-247 1.08e-124

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 353.79  E-value: 1.08e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   3 ITYRNAKVVSNKEISKDIYKLVV--EDDAEIKAGQFYMLKLNGAT-FLPRPISICEKSKNKLTFLYAVVGNGTKEFTKLK 79
Cdd:PRK00054   2 MKPENMKIVENKEIAPNIYTLVLdgEKVFDMKPGQFVMVWVPGVEpLLERPISISDIDKNEITILYRKVGEGTKKLSKLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  80 EDDEISLTGPLGNGFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFRHDVYLIDELKEyVNEVYISTN 159
Cdd:PRK00054  82 EGDELDIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTKDEVIFEEEFAK-VGDVYVTTD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 160 TGKNGHKGFVTEILKPED--YDTVLCCGPEIMMKKVVDMCKEKNVAVYVSMEKHMACGVGACLVCTCKTKDGHKRTCKDG 237
Cdd:PRK00054 161 DGSYGFKGFVTDVLDELDseYDAIYSCGPEIMMKKVVEILKEKKVPAYVSLERRMKCGIGACGACVCDTETGGKRVCKDG 240

                        250
                 ....*....|
gi 500663573 238 PIFDGYYVEL 247
Cdd:PRK00054 241 PVFSGGELVL 250
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 10-241 2.51e-116

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. 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: 99814 [Multi-domain]  Cd Length: 246  Bit Score: 332.59  E-value: 2.51e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  10 VVSNKEISKDIYKLVVEDD---AEIKAGQFYMLKLNG--ATFLPRPISIC--EKSKNKLTFLYAVVGNGTKEFTKLKEDD 82
Cdd:cd06218    1 VLSNREIADDIYRLVLEAPeiaAAAKPGQFVMLRVPDgsDPLLRRPISIHdvDPEEGTITLLYKVVGKGTRLLSELKAGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  83 EISLTGPLGNGFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNpdQKIDLYAGFR--HDVYLIDELKEYVNEVYISTNT 160
Cdd:cd06218   81 ELDVLGPLGNGFDLPDDDGKVLLVGGGIGIAPLLFLAKQLAERG--IKVTVLLGFRsaDDLFLVEEFEALGAEVYVATDD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 161 GKNGHKGFVTEILKPED----YDTVLCCGPEIMMKKVVDMCKEKNVAVYVSMEKHMACGVGACLVCTCKTKD---GHKRT 233
Cdd:cd06218  159 GSAGTKGFVTDLLKELLaearPDVVYACGPEPMLKAVAELAAERGVPCQVSLEERMACGIGACLGCVVKTKDdegGYKRV 238


                 ....*...
gi 500663573 234 CKDGPIFD 241
Cdd:cd06218  239 CKDGPVFD 246
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 9-247 4.88e-87

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 258.25  E-value: 4.88e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   9 KVVSNKEISKDIYKLVVEDDAE---IKAGQFYMLKLNGAtFLPRPISIC--EKSKNKLTFLYAVVGNGTKEFTKLKEDDE 83
Cdd:COG0543    1 KVVSVERLAPDVYLLRLEAPLIalkFKPGQFVMLRVPGD-GLRRPFSIAsaPREDGTIELHIRVVGKGTRALAELKPGDE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  84 ISLTGPLGNGFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNPdqKIDLYAGFRH--DVYLIDELKEYVN-EVYISTNT 160
Cdd:COG0543   80 LDVRGPLGNGFPLEDSGRPVLLVAGGTGLAPLRSLAEALLARGR--RVTLYLGARTpeDLYLLDELEALADfRVVVTTDD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 161 GKNGHKGFVTEILK----PEDYDTVLCCGPEIMMKKVVDMCKEKNV---AVYVSMEKHMACGVGACLVCTCKTKDGhkrt 233
Cdd:COG0543  158 GWYGRKGFVTDALKellaEDSGDDVYACGPPPMMKAVAELLLERGVppeRIYVSLERRMACGIGMCGGCVVPVGGG---- 233

                        250
                 ....*....|....
gi 500663573 234 CKDGPIFDGYYVEL 247
Cdd:COG0543  234 CKDGPVFDAAEVDW 247
DHODB_Fe-S_bind pfam10418
Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is ...
 209-245 1.20e-13

Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is one of the few organizms with two dihydroorotate dehydrogenases, DHODs, A and B. The B enzyme is a prototype for DHODs in Gram-positive bacteria that use NAD+ as the second substrate. DHODB is a hetero-tetramer composed of a central homodimer of PyrDB subunits resembling the DHODA structure and two PyrK subunits along with three different cofactors: FMN, FAD, and a [2Fe-2S] cluster. The [2Fe-2S] iron-sulfur cluster binds to this C-terminal domain of the PyrK subunit, which is at the interface between the flavin and NAD binding domains and contains three beta-strands. The four cysteine residues at the N-terminal part of this domain are the ones that bind, in pairs, to the iron-sulfur cluster. The conformation of the whole molecule means that the iron-sulfur cluster is localized in a well-ordered part of this domain close to the FAD binding site. The FAD and and NAD binding domains are FAD_binding_6, pfam00970 and NAD_binding_1, pfam00175.


Pssm-ID: 463084 [Multi-domain]  Cd Length: 40  Bit Score: 63.00  E-value: 1.20e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 500663573  209 EKHMACGVGACLVCTCKTKDGH---KRTCKDGPIFDGYYV 245
Cdd:pfam10418   1 EERMACGVGACGGCVVKTKGGDgeyKRVCVDGPVFDADEV 40
 
Name Accession Description Interval E-value
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 3-247 1.08e-124

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 353.79  E-value: 1.08e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   3 ITYRNAKVVSNKEISKDIYKLVV--EDDAEIKAGQFYMLKLNGAT-FLPRPISICEKSKNKLTFLYAVVGNGTKEFTKLK 79
Cdd:PRK00054   2 MKPENMKIVENKEIAPNIYTLVLdgEKVFDMKPGQFVMVWVPGVEpLLERPISISDIDKNEITILYRKVGEGTKKLSKLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  80 EDDEISLTGPLGNGFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFRHDVYLIDELKEyVNEVYISTN 159
Cdd:PRK00054  82 EGDELDIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTKDEVIFEEEFAK-VGDVYVTTD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 160 TGKNGHKGFVTEILKPED--YDTVLCCGPEIMMKKVVDMCKEKNVAVYVSMEKHMACGVGACLVCTCKTKDGHKRTCKDG 237
Cdd:PRK00054 161 DGSYGFKGFVTDVLDELDseYDAIYSCGPEIMMKKVVEILKEKKVPAYVSLERRMKCGIGACGACVCDTETGGKRVCKDG 240

                        250
                 ....*....|
gi 500663573 238 PIFDGYYVEL 247
Cdd:PRK00054 241 PVFSGGELVL 250
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 10-241 2.51e-116

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. 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: 99814 [Multi-domain]  Cd Length: 246  Bit Score: 332.59  E-value: 2.51e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  10 VVSNKEISKDIYKLVVEDD---AEIKAGQFYMLKLNG--ATFLPRPISIC--EKSKNKLTFLYAVVGNGTKEFTKLKEDD 82
Cdd:cd06218    1 VLSNREIADDIYRLVLEAPeiaAAAKPGQFVMLRVPDgsDPLLRRPISIHdvDPEEGTITLLYKVVGKGTRLLSELKAGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  83 EISLTGPLGNGFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNpdQKIDLYAGFR--HDVYLIDELKEYVNEVYISTNT 160
Cdd:cd06218   81 ELDVLGPLGNGFDLPDDDGKVLLVGGGIGIAPLLFLAKQLAERG--IKVTVLLGFRsaDDLFLVEEFEALGAEVYVATDD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 161 GKNGHKGFVTEILKPED----YDTVLCCGPEIMMKKVVDMCKEKNVAVYVSMEKHMACGVGACLVCTCKTKD---GHKRT 233
Cdd:cd06218  159 GSAGTKGFVTDLLKELLaearPDVVYACGPEPMLKAVAELAAERGVPCQVSLEERMACGIGACLGCVVKTKDdegGYKRV 238


                 ....*...
gi 500663573 234 CKDGPIFD 241
Cdd:cd06218  239 CKDGPVFD 246
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 9-247 4.88e-87

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 258.25  E-value: 4.88e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   9 KVVSNKEISKDIYKLVVEDDAE---IKAGQFYMLKLNGAtFLPRPISIC--EKSKNKLTFLYAVVGNGTKEFTKLKEDDE 83
Cdd:COG0543    1 KVVSVERLAPDVYLLRLEAPLIalkFKPGQFVMLRVPGD-GLRRPFSIAsaPREDGTIELHIRVVGKGTRALAELKPGDE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  84 ISLTGPLGNGFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNPdqKIDLYAGFRH--DVYLIDELKEYVN-EVYISTNT 160
Cdd:COG0543   80 LDVRGPLGNGFPLEDSGRPVLLVAGGTGLAPLRSLAEALLARGR--RVTLYLGARTpeDLYLLDELEALADfRVVVTTDD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 161 GKNGHKGFVTEILK----PEDYDTVLCCGPEIMMKKVVDMCKEKNV---AVYVSMEKHMACGVGACLVCTCKTKDGhkrt 233
Cdd:COG0543  158 GWYGRKGFVTDALKellaEDSGDDVYACGPPPMMKAVAELLLERGVppeRIYVSLERRMACGIGMCGGCVVPVGGG---- 233

                        250
                 ....*....|....
gi 500663573 234 CKDGPIFDGYYVEL 247
Cdd:COG0543  234 CKDGPVFDAAEVDW 247
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 8-242 8.34e-54

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: 173.20  E-value: 8.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   8 AKVVSNKEISKDIYKLVVEDDAEIKAGQFYMLKLNGATFLPRPISIcEKSKNKLTFlyAVVGNGTKEFTKLKEDDEISLT 87
Cdd:cd06220    1 VTIKEVIDETPTVKTFVFDWDFDFKPGQFVMVWVPGVDEIPMSLSY-IDGPNSITV--KKVGEATSALHDLKEGDKLGIR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  88 GPLGNGFDLEKEynKVALVSGGIGTAPMLELAKKLRKKNpdqKIDLYAGFRH--DVYLIDELkEYVNEVYISTNTGKNGH 165
Cdd:cd06220   78 GPYGNGFELVGG--KVLLIGGGIGIAPLAPLAERLKKAA---DVTVLLGARTkeELLFLDRL-RKSDELIVTTDDGSYGF 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 166 KGFVTEILK---PEDYDTVLCCGPEIMMKKVVDMCKEKNVAVYVSMEKHMACGVGACLVCtCKTKDGHkRTCKDGPIFDG 242
Cdd:cd06220  152 KGFVTDLLKeldLEEYDAIYVCGPEIMMYKVLEILDERGVRAQFSLERYMKCGIGICGSC-CIDPTGL-RVCRDGPVFDG 229
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 10-241 3.24e-52

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: 169.43  E-value: 3.24e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  10 VVSNKEISKDIYKLVV---EDDAEIKAGQFYMLKL-NGATFLPRPISICE--KSKNKLTFLYAVVGNGTKEFTKLKEDDE 83
Cdd:cd06192    1 IVKKEQLEPNLVLLTIkapLAARLFRPGQFVFLRNfESPGLERIPLSLAGvdPEEGTISLLVEIRGPKTKLIAELKPGEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  84 ISLTGPLGNGFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNpdQKIDLYAGFR--HDVYLIDELKEYVNEVYISTNTG 161
Cdd:cd06192   81 LDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAKKLAANG--NKVTVLAGAKkaKEEFLDEYFELPADVEIWTTDDG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 162 KNGHKGFVTEILKP---EDYDTVLCCGPEIMMKKVVDMCKE--KNVAVYVSMEKHMACGVGACLVCTCKTKDGHKRTCKD 236
Cdd:cd06192  159 ELGLEGKVTDSDKPiplEDVDRIIVAGSDIMMKAVVEALDEwlQLIKASVSNNSPMCCGIGICGACTIETKHGVKRLCKD 238


                 ....*
gi 500663573 237 GPIFD 241
Cdd:cd06192  239 GPVFR 243
DHOD_e_trans_like1 cd06219
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 8-245 1.70e-48

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: 160.05  E-value: 1.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   8 AKVVSNKEISKDIYKLVVEDD---AEIKAGQFYMLKLN-GATFLPRPISICEKSKNKLTFLYAVVGNGTKEFTKLKEDDE 83
Cdd:cd06219    1 YKILEKEELAPNVKLFEIEAPliaKKAKPGQFVIVRADeKGERIPLTIADWDPEKGTITIVVQVVGKSTRELATLEEGDK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  84 IS-LTGPLGNGFDLEKeYNKVALVSGGIGTAPMLELAKKLRKKNpdQKIDLYAGFRHDVYLI--DELKEYVNEVYISTNT 160
Cdd:cd06219   81 IHdVVGPLGKPSEIEN-YGTVVFVGGGVGIAPIYPIAKALKEAG--NRVITIIGARTKDLVIleDEFRAVSDELIITTDD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 161 GKNGHKGFVTEILKP-----EDYDTVLCCGPEIMMKKVVDMCKEKNVAVYVSMEKHMACGVGACLVCTCKTKDGHKRTCK 235
Cdd:cd06219  158 GSYGEKGFVTDPLKEliesgEKVDLVIAIGPPIMMKAVSELTRPYGIPTVVSLNPIMVDGTGMCGACRVTVGGETKFACV 237

                        250
                 ....*....|
gi 500663573 236 DGPIFDGYYV 245
Cdd:cd06219  238 DGPEFDAHKV 247
PRK06222 PRK06222
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
9-245 2.13e-46

sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;


Pssm-ID: 235747 [Multi-domain]  Cd Length: 281  Bit Score: 155.73  E-value: 2.13e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   9 KVVSNKEISKDIYKLVVEDD---AEIKAGQFYMLKL--NGAtflpR-PISICE--KSKNKLTFLYAVVGNGTKEFTKLKE 80
Cdd:PRK06222   3 KILEKEELAPNVFLMEIEAPrvaKKAKPGQFVIVRIdeKGE----RiPLTIADydREKGTITIVFQAVGKSTRKLAELKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  81 DDEI-SLTGPLGNGFDLEKeYNKVALVSGGIGTAPMLELAKKLRKKNpdQKIDLYAGFRHDVYLI--DELKEYVNEVYIS 157
Cdd:PRK06222  79 GDSIlDVVGPLGKPSEIEK-FGTVVCVGGGVGIAPVYPIAKALKEAG--NKVITIIGARNKDLLIleDEMKAVSDELYVT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 158 TNTGKNGHKGFVTEILK-----PEDYDTVLCCGPEIMMKKVVDMCKEKNVAVYVSMEKHMACGVGACLVCTCkTKDGH-K 231
Cdd:PRK06222 156 TDDGSYGRKGFVTDVLKellesGKKVDRVVAIGPVIMMKFVAELTKPYGIKTIVSLNPIMVDGTGMCGACRV-TVGGEtK 234

                        250
                 ....*....|....
gi 500663573 232 RTCKDGPIFDGYYV 245
Cdd:PRK06222 235 FACVDGPEFDGHLV 248
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 10-241 5.65e-46

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: 153.92  E-value: 5.65e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  10 VVSNKEISKDIY--KLVVEDDAE----IKAGQFYMLKLNGATflPRPISICE--KSKNKLTFLYAVVGNGTKEFTKLKED 81
Cdd:cd06221    1 IVEVVDETEDIKtfTLRLEDDDEelftFKPGQFVMLSLPGVG--EAPISISSdpTRRGPLELTIRRVGRVTEALHELKPG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  82 DEISLTGPLGNGFDLEKEYNK-VALVSGGIGTAPMLELAKKLrKKNPDQ--KIDLYAGFRH--DVYLIDELKEYVN---- 152
Cdd:cd06221   79 DTVGLRGPFGNGFPVEEMKGKdLLLVAGGLGLAPLRSLINYI-LDNREDygKVTLLYGARTpeDLLFKEELKEWAKrsdv 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 153 EVYIST---NTGKNGHKGFVTEILKPEDYD----TVLCCGPEIMMKKVVDMCKEKNVA---VYVSMEKHMACGVGACLVC 222
Cdd:cd06221  158 EVILTVdraEEGWTGNVGLVTDLLPELTLDpdntVAIVCGPPIMMRFVAKELLKLGVPeeqIWVSLERRMKCGVGKCGHC 237

                        250
                 ....*....|....*....
gi 500663573 223 TCktkdGHKRTCKDGPIFD 241
Cdd:cd06221  238 QI----GPKYVCKDGPVFS 252
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 9-246 3.53e-39

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 144.11  E-value: 3.53e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   9 KVVSNKEISKDIYKLVVEDD---AEIKAGQFYMLKL-NGATFLPRPISICEKSKNKLTFLYAVVGNGTKEFTKLKEDDEI 84
Cdd:PRK12778   3 KIVEKEIFSEKVFLLEIEAPliaKSRKPGQFVIVRVgEKGERIPLTIADADPEKGTITLVIQEVGLSTTKLCELNEGDYI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  85 S-LTGPLGNGFDLEKeYNKVALVSGGIGTAPMLELAKKLrKKNPDQKIDLYAGFRHD-VYLIDELKEYVNEVYISTNTGK 162
Cdd:PRK12778  83 TdVVGPLGNPSEIEN-YGTVVCAGGGVGVAPMLPIVKAL-KAAGNRVITILGGRSKElIILEDEMRESSDEVIIMTDDGS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 163 NGHKGFVTEILKP-----EDYDTVLCCGPEIMMKKVVDMCKEKNVAVYVSMEKHMACGVGACLVCTCKTKDGHKRTCKDG 237
Cdd:PRK12778 161 YGRKGLVTDGLEEvikreTKVDKVFAIGPAIMMKFVCLLTKKYGIPTIVSLNTIMVDGTGMCGACRVTVGGKTKFACVDG 240


                 ....*....
gi 500663573 238 PIFDGYYVE 246
Cdd:PRK12778 241 PEFDGHLVD 249
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 28-244 8.45e-25

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 99.50  E-value: 8.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  28 DAEI------KAGQFYMLKLNGatFLPRPISICEKSKNKLTFLYAV--VGNGTKEFTKLKEDDEISLTGPLGNGFDLEK- 98
Cdd:PRK08345  29 DPELaesftfKPGQFVQVTIPG--VGEVPISICSSPTRKGFFELCIrrAGRVTTVIHRLKEGDIVGVRGPYGNGFPVDEm 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  99 EYNKVALVSGGIGTAPM---LELAKKLRKKNpdQKIDLYAGFRH--DVYLIDEL-------------------KEYVNEV 154
Cdd:PRK08345 107 EGMDLLLIAGGLGMAPLrsvLLYAMDNRWKY--GNITLIYGAKYyeDLLFYDELikdlaeaenvkiiqsvtrdPEWPGCH 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 155 YISTNTGKNGHKGFVTEILKPEDYDT----VLCCGPEIMMKKVVDMCKEKNVA---VYVSMEKHMACGVGACLVCTCKTK 227
Cdd:PRK08345 185 GLPQGFIERVCKGVVTDLFREANTDPkntyAAICGPPVMYKFVFKELINRGYRperIYVTLERRMRCGIGKCGHCIVGTS 264

                        250
                 ....*....|....*..
gi 500663573 228 DGHKRTCKDGPIFdGYY 244
Cdd:PRK08345 265 TSIKYVCKDGPVF-TYF 280
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
 29-247 1.55e-24

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 101.94  E-value: 1.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   29 AEIKAGQFYMLKL-NGATFLPRPISICEKSKNKLTFLYAVVGNGTKEF-TKLKEDDE-ISLTGPLGNGFDLEKeYNKVAL 105
Cdd:PRK12775   26 ASAEPGHFVMLRLyEGAERIPLTVADFDRKKGTITMVVQALGKTTREMmTKFKAGDTfEDFVGPLGLPQHIDK-AGHVVL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  106 VSGGIGTAPMLelaKKLRK-KNPDQKIDLYAGFRHD--VYLIDELKEYVNEVYISTNTGKNGHKGFVT----EILKPEDY 178
Cdd:PRK12775  105 VGGGLGVAPVY---PQLRAfKEAGARTTGIIGFRNKdlVFWEDKFGKYCDDLIVCTDDGSYGKPGFVTaalkEVCEKDKP 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500663573  179 DTVLCCGPEIMMKKVVDMCKEKNVAVYVSMEKHMACGVGACLVCTCKTKDGHKRTCKDGPIFDGYYVEL 247
Cdd:PRK12775  182 DLVVAIGPLPMMNACVETTRPFGVKTMVSLNAIMVDGTGMCGSCRVTVGGEVKFACVDGPDFDGHKVDF 250
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 11-202 2.38e-24

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: 96.75  E-value: 2.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  11 VSNKEISKDIYKLVVEDDAEI--KAGQFYMLKLNGA-TFLPRPISICE--KSKNKLTFLYAVVGNG--TKEFTKLKEDDE 83
Cdd:cd00322    1 VATEDVTDDVRLFRLQLPNGFsfKPGQYVDLHLPGDgRGLRRAYSIASspDEEGELELTVKIVPGGpfSAWLHDLKPGDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  84 ISLTGPLGNGFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFRH--DVYLIDELKEYVNE-----VYI 156
Cdd:cd00322   81 VEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTpaDLLFLDELEELAKEgpnfrLVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 500663573 157 STNTGKNGHKG---------FVTEILKPEDYDTVLCCGPEIMMKKVVDMCKEKNV 202
Cdd:cd00322  161 ALSRESEAKLGpggridreaEILALLPDDSGALVYICGPPAMAKAVREALVSLGV 215
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
4-203 1.09e-19

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 84.46  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   4 TYRNAKVVSNKEISKDI--YKLVVEDDAEI---KAGQFYMLKLN-GATFLPRPISIC----EKSknkLTFLYAVVGNGtk 73
Cdd:COG1018    2 GFRPLRVVEVRRETPDVvsFTLEPPDGAPLprfRPGQFVTLRLPiDGKPLRRAYSLSsapgDGR---LEITVKRVPGG-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  74 EFT-----KLKEDDEISLTGPLGNgFDLEKEYNK-VALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFRH--DVYLID 145
Cdd:COG1018   77 GGSnwlhdHLKVGDTLEVSGPRGD-FVLDPEPARpLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGARSpaDLAFRD 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500663573 146 ELKEYVNE-----VYISTNTGKNGHKGFVT-----EILKPEDYDTVLCCGPEIMMKKVVDMCKEKNVA 203
Cdd:COG1018  156 ELEALAARhprlrLHPVLSREPAGLQGRLDaellaALLPDPADAHVYLCGPPPMMEAVRAALAELGVP 223
PRK05802 PRK05802
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
50-235 8.04e-19

sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;


Pssm-ID: 235613 [Multi-domain]  Cd Length: 320  Bit Score: 83.49  E-value: 8.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  50 PISICEKS--KNKLTFLYAVVGNGTKEFTKLKEDDEISLTGPLGNG-FDLEKEYN----KVALVSGGIGTAPMLELAKKL 122
Cdd:PRK05802 115 PISIMEADteENIIKVAIEIRGVKTKKIAKLNKGDEILLRGPYWNGiLGLKNIKStkngKSLVIARGIGQAPGVPVIKKL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 123 RKKNpdQKIDLY---AGFRHDvYLIDELKEYVNEVyISTNTGKNGH-----KGFVTEILKPEDYDTVLCCGPEIMMKKVV 194
Cdd:PRK05802 195 YSNG--NKIIVIidkGPFKNN-FIKEYLELYNIEI-IELNLLDDGElseegKDILKEIIKKEDINLIHCGGSDILHYKII 270

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 500663573 195 DMCKE--KNVAVYVSMEKHMACGVGACLVCTCKTKDGH-KRTCK 235
Cdd:PRK05802 271 EYLDKlnEKIKLSCSNNAKMCCGEGICGACTVRYGGHKvKRLCK 314
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 8-203 3.30e-18

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: 80.29  E-value: 3.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   8 AKVVSNKEISKDIYKLVVEDDAEI--KAGQFYMLKLNGATflPRPISI--CEKSKNKLTFLYAVVGNGT---KEFTKLKE 80
Cdd:cd06189    1 CKVESIEPLNDDVYRVRLKPPAPLdfLAGQYLDLLLDDGD--KRPFSIasAPHEDGEIELHIRAVPGGSfsdYVFEELKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  81 DDEISLTGPLGNGFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFRH--DVYLIDEL----KEYVNEV 154
Cdd:cd06189   79 NGLVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQGSKRPIHLYWGARTeeDLYLDELLeawaEAHPNFT 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 500663573 155 YI----STNTGKNGHKGFVTEILKpEDYD-----TVLCCGPEIMMKKVVDMCKEKNVA 203
Cdd:cd06189  159 YVpvlsEPEEGWQGRTGLVHEAVL-EDFPdlsdfDVYACGSPEMVYAARDDFVEKGLP 215
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 9-194 6.78e-16

Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 74.14  E-value: 6.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   9 KVVSNKEISKD--IYKLVVEDDAE---IKAGQFYMLKLNGATFLP-R---PISICEkSKNKLTFLYAVVGNG--TKEFTK 77
Cdd:cd06183    2 KLVSKEDISHDtrIFRFELPSPDQvlgLPVGQHVELKAPDDGEQVvRpytPISPDD-DKGYFDLLIKIYPGGkmSQYLHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  78 LKEDDEISLTGPLGNgFDLE--KEYNKVALVSGGIGTAPMLELAKK-LRKKNPDQKIDLYAGFRH--DVYLIDELKEYVN 152
Cdd:cd06183   81 LKPGDTVEIRGPFGK-FEYKpnGKVKHIGMIAGGTGITPMLQLIRAiLKDPEDKTKISLLYANRTeeDILLREELDELAK 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 500663573 153 E-------VYISTNTGK--NGHKGFVTE------ILKPEDYDT-VLCCGPEIMMKKVV 194
Cdd:cd06183  160 KhpdrfkvHYVLSRPPEgwKGGVGFITKemikehLPPPPSEDTlVLVCGPPPMIEGAV 217
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
 9-246 5.74e-15

putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 74.10  E-value: 5.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   9 KVVSNKEISKDIYKLVVEDDA---EIKAGQFY-MLKLNGATFLPRPISICEKSKNKLTFLYAVVGNGTKEFTKLKEDDEI 84
Cdd:PRK12779 652 TIVGKVQLAGGIVEFTVRAPMvarSAQAGQFVrVLPWEKGELIPLTLADWDAEKGTIDLVVQGMGTSSLEINRMAIGDAF 731

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  85 S-LTGPLGNGFDLEK-EYNK-VALVSGGIGTAPMLELAKK-LRKKNpdqKIDLYAGFRHDVYL--------IDELK-EYV 151
Cdd:PRK12779 732 SgIAGPLGRASELHRyEGNQtVVFCAGGVGLPPVYPIMRAhLRLGN---HVTLISGFRAKEFLfwtgdderVGKLKaEFG 808

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 152 N--EVYISTNTGKNGHKGFVT----EILKP------EDYDTVLCCGPEIMMKKVVDMCKEKNVAVYVSMEKHMACGVGAC 219
Cdd:PRK12779 809 DqlDVIYTTNDGSFGVKGFVTgpleEMLKAnqqgkgRTIAEVIAIGPPLMMRAVSDLTKPYGVKTVASLNSIMVDATGMC 888

                        250       260       270
                 ....*....|....*....|....*....|.
gi 500663573 220 LVCTCK-TKDG---HKRTCKDGPIFDGYYVE 246
Cdd:PRK12779 889 GACMVPvTIDGkmvRKHACIDGPEIDAHIID 919
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 10-203 1.75e-14

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: 70.31  E-value: 1.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  10 VVSNKEISKDIYKLVVEDDAEI--KAGQFYMLKLNGATFLPRPISIC--EKSKNKLTFLYAVVGNG---TKEFTKLKEDD 82
Cdd:cd06187    1 VVSVERLTHDIAVVRLQLDQPLpfWAGQYVNVTVPGRPRTWRAYSPAnpPNEDGEIEFHVRAVPGGrvsNALHDELKVGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  83 EISLTGPLGNGFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFR--HDVYLIDELKE---------YV 151
Cdd:cd06187   81 RVRLSGPYGTFYLRRDHDRPVLCIAGGTGLAPLRAIVEDALRRGEPRPVHLFFGARteRDLYDLEGLLAlaarhpwlrVV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 500663573 152 NEVyiSTNTG-KNGHKGFVTEILkPEDYDT-----VLCCGPEIMMKKVVDMCKEKNVA 203
Cdd:cd06187  161 PVV--SHEEGaWTGRRGLVTDVV-GRDGPDwadhdIYICGPPAMVDATVDALLARGAP 215
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
9-203 4.66e-14

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 70.69  E-value: 4.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   9 KVVSNKEISKDIYKLVVE----DDAEIKAGQFYMLKLNGATFLPRP----ISICEKSKNKLTFLYAVVGNGTKEFTKLKE 80
Cdd:COG4097  218 RVESVEPEAGDVVELTLRpeggRWLGHRAGQFAFLRFDGSPFWEEAhpfsISSAPGGDGRLRFTIKALGDFTRRLGRLKP 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  81 DDEISLTGPLGNgFDLEKEYNK--VALVSGGIGTAPMLELAKKLRKKNPD-QKIDLYAGFRH--DVYLIDELKEYVNE-- 153
Cdd:COG4097  298 GTRVYVEGPYGR-FTFDRRDTAprQVWIAGGIGITPFLALLRALAARPGDqRPVDLFYCVRDeeDAPFLEELRALAARla 376

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 154 ----VYISTntgknGHKGFVT-EILK-----PEDYDtVLCCGPEIMMKKVVDMCKEKNVA 203
Cdd:COG4097  377 glrlHLVVS-----DEDGRLTaERLRrlvpdLAEAD-VFFCGPPGMMDALRRDLRALGVP 430
DHODB_Fe-S_bind pfam10418
Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is ...
 209-245 1.20e-13

Iron-sulfur cluster binding domain of dihydroorotate dehydrogenase B; Lactococcus lactis is one of the few organizms with two dihydroorotate dehydrogenases, DHODs, A and B. The B enzyme is a prototype for DHODs in Gram-positive bacteria that use NAD+ as the second substrate. DHODB is a hetero-tetramer composed of a central homodimer of PyrDB subunits resembling the DHODA structure and two PyrK subunits along with three different cofactors: FMN, FAD, and a [2Fe-2S] cluster. The [2Fe-2S] iron-sulfur cluster binds to this C-terminal domain of the PyrK subunit, which is at the interface between the flavin and NAD binding domains and contains three beta-strands. The four cysteine residues at the N-terminal part of this domain are the ones that bind, in pairs, to the iron-sulfur cluster. The conformation of the whole molecule means that the iron-sulfur cluster is localized in a well-ordered part of this domain close to the FAD binding site. The FAD and and NAD binding domains are FAD_binding_6, pfam00970 and NAD_binding_1, pfam00175.


Pssm-ID: 463084 [Multi-domain]  Cd Length: 40  Bit Score: 63.00  E-value: 1.20e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 500663573  209 EKHMACGVGACLVCTCKTKDGH---KRTCKDGPIFDGYYV 245
Cdd:pfam10418   1 EERMACGVGACGGCVVKTKGGDgeyKRVCVDGPVFDADEV 40
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 8-202 5.87e-12

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate.


Pssm-ID: 99808 [Multi-domain]  Cd Length: 232  Bit Score: 63.12  E-value: 5.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   8 AKVVSNKEISKDIYKLVVE----DDAEIKAGQFYMLKLNGaTFLPRPISICE--KSKNKLTFLYAVVGNG---TKEFTKL 78
Cdd:cd06212    3 GTVVAVEALTHDIRRLRLRleepEPIKFFAGQYVDITVPG-TEETRSFSMANtpADPGRLEFIIKKYPGGlfsSFLDDGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  79 KEDDEISLTGPLGNGFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFR--HDVYLIDELKEYVNEV-- 154
Cdd:cd06212   82 AVGDPVTVTGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDMAASGSDRPVRFFYGARtaRDLFYLEEIAALGEKIpd 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 155 --YI------STNTGKNGHKGFVTEILKPEDYDTVLC----CGPEIMMKKVVDMCKEKNV 202
Cdd:cd06212  162 ftFIpalsesPDDEGWSGETGLVTEVVQRNEATLAGCdvylCGPPPMIDAALPVLEMSGV 221
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 78-202 7.63e-12

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: 62.99  E-value: 7.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  78 LKEDDEISLTGPLG--NGFDLEKEynKVALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFRHDVYLI--DELKEY--- 150
Cdd:cd06215   81 LKVGDELWASGPAGefTLIDHPAD--KLLLLSAGSGITPMMSMARWLLDTRPDADIVFIHSARSPADIIfaDELEELarr 158

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500663573 151 ---VNEVYISTNTGK---NGHKGFVT-EILK--PEDYD--TVLCCGPEIMMKKVVDMCKEKNV 202
Cdd:cd06215  159 hpnFRLHLILEQPAPgawGGYRGRLNaELLAllVPDLKerTVFVCGPAGFMKAVKSLLAELGF 221
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 10-196 7.69e-12

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: 63.04  E-value: 7.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  10 VVSNKEISKDIY--KLVVEDDAEIKAGQFYMLKLNGATfLPRPISIC--EKSKNKLTFLYAVVGNG---TKEFTKLKEDD 82
Cdd:cd06190    1 LVDVRELTHDVAefRFALDGPADFLPGQYALLALPGVE-GARAYSMAnlANASGEWEFIIKRKPGGaasNALFDNLEPGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  83 EISLTGPLGNG-FDLEKEYNKVAlVSGGIGTAPMLELAKKL--RKKNPDQKIDLYAGFR--HDVYL---IDELKEYVN-- 152
Cdd:cd06190   80 ELELDGPYGLAyLRPDEDRDIVC-IAGGSGLAPMLSILRGAarSPYLSDRPVDLFYGGRtpSDLCAldeLSALVALGArl 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 500663573 153 EVYI-------STNTGKNGHKGFVTEIL------KPEDYDTVLcCGPEIMMKKVVDM 196
Cdd:cd06190  159 RVTPavsdagsGSAAGWDGPTGFVHEVVeatlgdRLAEFEFYF-AGPPPMVDAVQRM 214
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 8-189 1.37e-10

Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases.


Pssm-ID: 99807  Cd Length: 238  Bit Score: 59.65  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   8 AKVVSNKEISKDI--YKLVVEDDAEI--KAGQFYMLKL-NGATFlpRPISICEKSKNK----LTFLYAVVGNGTKEFTK- 77
Cdd:cd06211    9 GTVVEIEDLTPTIkgVRLKLDEPEEIefQAGQYVNLQApGYEGT--RAFSIASSPSDAgeieLHIRLVPGGIATTYVHKq 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  78 LKEDDEISLTGPLGNGFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFRH--DVYLIDEL----KEYV 151
Cdd:cd06211   87 LKEGDELEISGPYGDFFVRDSDQRPIIFIAGGSGLSSPRSMILDLLERGDTRKITLFFGARTraELYYLDEFealeKDHP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 500663573 152 NEVYIST------NTGKNGHKGFVTEILKP---------EDYdtvlCCGPEIM 189
Cdd:cd06211  167 NFKYVPAlsreppESNWKGFTGFVHDAAKKhfkndfrghKAY----LCGPPPM 215
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 32-202 4.10e-10

NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 57.65  E-value: 4.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  32 KAGQFYMLKLNGATFL-PRPISIC--EKSKNKLTFLYAVVGNGTKEF-TKLKEDDEISLTGPLGnGFDLEKEYNKVALVS 107
Cdd:cd06198   24 RAGQFAFLRFDASGWEePHPFTISsaPDPDGRLRFTIKALGDYTRRLaERLKPGTRVTVEGPYG-RFTFDDRRARQIWIA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 108 GGIGTAPMLELAKKLRKKNPDQKIDLYAGFR--HDVYLIDELKEYVNEVYISTNTGKNGHKGFVTEIL-------KPEDY 178
Cdd:cd06198  103 GGIGITPFLALLEALAARGDARPVTLFYCVRdpEDAVFLDELRALAAAAGVVLHVIDSPSDGRLTLEQlvralvpDLADA 182

                        170       180
                 ....*....|....*....|....
gi 500663573 179 DtVLCCGPEIMMKKVVDMCKEKNV 202
Cdd:cd06198  183 D-VWFCGPPGMADALEKGLRALGV 205
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 79-189 6.26e-10

Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group.


Pssm-ID: 99805 [Multi-domain]  Cd Length: 228  Bit Score: 57.60  E-value: 6.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  79 KEDDEISLTGPLGNgFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFRHDVYL--IDELKEY------ 150
Cdd:cd06209   82 QPGDRLTLTGPLGS-FYLREVKRPLLMLAGGTGLAPFLSMLDVLAEDGSAHPVHLVYGVTRDADLveLDRLEALaerlpg 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 500663573 151 --VNEVYISTNTGKnGHKGFVTEILKPE-----DYDTVLcCGPEIM 189
Cdd:cd06209  161 fsFRTVVADPDSWH-PRKGYVTDHLEAEdlndgDVDVYL-CGPPPM 204
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 10-193 7.98e-10

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an N-terminal 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 betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99791 [Multi-domain]  Cd Length: 222  Bit Score: 57.28  E-value: 7.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  10 VVSNKEISKDIYKLVVEDDA--EIKAGQFymLKLNGATFLPRPISI--CEKSKNKLTFLYAVVGNGT---KEFTKLKEDD 82
Cdd:cd06194    1 VVSLQRLSPDVLRVRLEPDRplPYLPGQY--VNLRRAGGLARSYSPtsLPDGDNELEFHIRRKPNGAfsgWLGEEARPGH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  83 EISLTGPLGNGFdLEKEY--NKVALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFRH--DVYLIDEL----KEYVNEV 154
Cdd:cd06194   79 ALRLQGPFGQAF-YRPEYgeGPLLLVGAGTGLAPLWGIARAALRQGHQGEIRLVHGARDpdDLYLHPALlwlaREHPNFR 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 500663573 155 YISTNTGKNGHKGFV-------TEILKPEDyDTVLCCGPEIMMKKV 193
Cdd:cd06194  158 YIPCVSEGSQGDPRVragriaaHLPPLTRD-DVVYLCGAPSMVNAV 202
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 6-202 9.56e-10

Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent hydroxylation of methane to methanol. This multicomponent enzyme mediates electron transfer via a hydroxylase (MMOH), a coupling protein, and a reductase which is comprised of an N-terminal [2Fe-2S] ferredoxin domain, an FAD binding subdomain, and an NADH binding subdomain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. Dioxygenases add both atom of oxygen to the substrate, while mono-oxygenases add one atom to the substrate and one atom to water.


Pssm-ID: 99806  Cd Length: 236  Bit Score: 56.97  E-value: 9.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   6 RNAKVVSNKEISKDIYKLVVEDD--------AEIKAGQFYMLKLNGaTFLPRPISICEKSKN--KLTFLYAVVGNGtkEF 75
Cdd:cd06210    2 REAEIVAVDRVSSNVVRLRLQPDdaegagiaAEFVPGQFVEIEIPG-TDTRRSYSLANTPNWdgRLEFLIRLLPGG--AF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  76 TKLKED-----DEISLTGPLGnGFDL-EKEYNKVALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFR--HDVYLIDEL 147
Cdd:cd06210   79 STYLETrakvgQRLNLRGPLG-AFGLrENGLRPRWFVAGGTGLAPLLSMLRRMAEWGEPQEARLFFGVNteAELFYLDEL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500663573 148 KEYVNE-------VYISTNTGK-NGHKGFVTEILK--------PEDydtVLCCGPEIMMKKVVDMCKEKNV 202
Cdd:cd06210  158 KRLADSlpnltvrICVWRPGGEwEGYRGTVVDALRedlassdaKPD---IYLCGPPGMVDAAFAAAREAGV 225
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 105-195 2.23e-09

Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.


Pssm-ID: 425503 [Multi-domain]  Cd Length: 109  Bit Score: 53.42  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  105 LVSGGIGTAPMLELAKKLRKKNPDQ-KIDLYAGFR--HDVYLIDELKEYVNE-------VYISTNT--GKNGHKGFVTEI 172
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKDPtQVVLVFGNRneDDILYREELDELAEKhpgrltvVYVVSRPeaGWTGGKGRVQDA 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 500663573  173 LKpEDYDT-------VLCCGPEIMMKKVVD 195
Cdd:pfam00175  81 LL-EDHLSlpdeethVYVCGPPGMIKAVRK 109
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 9-176 2.77e-09

Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99792 [Multi-domain]  Cd Length: 241  Bit Score: 55.65  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573   9 KVVSNKEISKDIYKLVVEDDA--EIKAGQFYMLKLNGA--TFLPRPISI-CEKSKNKLTFLYAVVGNG--TKEFTKLKED 81
Cdd:cd06195    1 TVLKRRDWTDDLFSFRVTRDIpfRFQAGQFTKLGLPNDdgKLVRRAYSIaSAPYEENLEFYIILVPDGplTPRLFKLKPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  82 DEISLT-GPLGNgFDLEK--EYNKVALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFRHD---VY--LIDELKEYVNE 153
Cdd:cd06195   81 DTIYVGkKPTGF-LTLDEvpPGKRLWLLATGTGIAPFLSMLRDLEIWERFDKIVLVHGVRYAeelAYqdEIEALAKQYNG 159

                        170       180
                 ....*....|....*....|....*...
gi 500663573 154 --VYISTNT---GKNGHKGFVTEILKPE 176
Cdd:cd06195  160 kfRYVPIVSrekENGALTGRIPDLIESG 187
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 78-202 3.76e-09

Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) provides a means of storing redox reaction energy via the transmembrane translocation of Na2+ ions. The C-terminal domain resembles ferredoxin:NADP+ oxidoreductase, and has NADH and FAD binding sites. (Na+-NQR) is distinct from H+-translocating NADH:quinone oxidoreductases and noncoupled NADH:quinone oxidoreductases. The 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 of this group typically contains an iron-sulfur cluster binding domain.


Pssm-ID: 99785 [Multi-domain]  Cd Length: 283  Bit Score: 55.77  E-value: 3.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  78 LKEDDEISLTGPLGNGFDLEKEYNKVaLVSGGIGTAPMLEL-AKKLRKKNPDQKIDLYAGFRH--DVYLIDELK----EY 150
Cdd:cd06188  129 LKPGDKVTASGPFGEFFIKDTDREMV-FIGGGAGMAPLRSHiFHLLKTLKSKRKISFWYGARSlkELFYQEEFEalekEF 207

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500663573 151 VNEVYI------STNTGKNGHKGFVTEIL---------KPEDYDTVLCcGPEIMMKKVVDMCKEKNV 202
Cdd:cd06188  208 PNFKYHpvlsepQPEDNWDGYTGFIHQVLlenylkkhpAPEDIEFYLC-GPPPMNSAVIKMLDDLGV 273
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 32-203 3.72e-08

NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation oxidoreductase. PA oxidoreductases of E. coli hydroxylate PA-CoA in the second step of PA degradation. Members of this group typically fuse a ferredoxin reductase-like domain with an iron-sulfur binding cluster domain. Ferredoxins 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 portion may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. 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 and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99810 [Multi-domain]  Cd Length: 241  Bit Score: 52.55  E-value: 3.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  32 KAGQFYMLKLN-GATFLPRPISIC-EKSKNKLTFlyAV--VGNGTkeF-----TKLKEDDEISLTGPLGN-GFDLEKEYN 101
Cdd:cd06214   34 RPGQFLTLRVPiDGEEVRRSYSICsSPGDDELRI--TVkrVPGGR--FsnwanDELKAGDTLEVMPPAGRfTLPPLPGAR 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 102 KVALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFRH--DVYLIDELKEYVNE---------VYISTNTGKNGHKG--- 167
Cdd:cd06214  110 HYVLFAAGSGITPVLSILKTALAREPASRVTLVYGNRTeaSVIFREELADLKARypdrltvihVLSREQGDPDLLRGrld 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 500663573 168 --FVTEILK----PEDYDTVLCCGPEIMMKKVVDMCKEKNVA 203
Cdd:cd06214  190 aaKLNALLKnlldATEFDEAFLCGPEPMMDAVEAALLELGVP 231
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 75-196 1.18e-07

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: 51.11  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  75 FTKLKEDDEISLTGPLGNGFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFRH--DVYLIDELKEY-- 150
Cdd:cd06217   82 HDEVKVGDLLEVRGPIGTFTWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVPFRLLYSARTaeDVIFRDELEQLar 161

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 500663573 151 ------VNEVYI-STNTGKNGHKGFVT-----EILKPEDYDTVLCCGPEIMMKKVVDM 196
Cdd:cd06217  162 rhpnlhVTEALTrAAPADWLGPAGRITadliaELVPPLAGRRVYVCGPPAFVEAATRL 219
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 78-203 4.46e-07

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: 49.48  E-value: 4.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  78 LKEDDEISLTGPLGNgFDLEKEYNK-VALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFRHDVY--LIDELKEYVNE- 153
Cdd:cd06184   91 VKVGDVLEVSAPAGD-FVLDEASDRpLVLISAGVGITPMLSMLEALAAEGPGRPVTFIHAARNSAVhaFRDELEELAARl 169

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500663573 154 ------VYISTNTG-----KNGHKGFVT-----EILKPEDYDTVLcCGPEIMMKKVVDMCKEKNVA 203
Cdd:cd06184  170 pnlklhVFYSEPEAgdreeDYDHAGRIDlallrELLLPADADFYL-CGPVPFMQAVREGLKALGVP 234
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 51-201 7.26e-07

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: 48.45  E-value: 7.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  51 ISICEKSKNKLTFlYAVVGNG--TKEFTKLKEDDE------ISLTGPLGNGFDLEKEYNKVALVSGGIG---TAPML-EL 118
Cdd:cd06186   50 ASSPEDEQDTLSL-IIRAKKGftTRLLRKALKSPGggvslkVLVEGPYGSSSEDLLSYDNVLLVAGGSGitfVLPILrDL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 119 AKKLRKKNPDQKIDLYAGFRHdvylIDELKEYVNEVYISTNTGKNGH-KGFVTeilkpedydTVLCCGPEIMMKKVVDMC 197
Cdd:cd06186  129 LRRSSKTSRTRRVKLVWVVRD----REDLEWFLDELRAAQELEVDGEiEIYVT---------RVVVCGPPGLVDDVRNAV 195


                 ....
gi 500663573 198 KEKN 201
Cdd:cd06186  196 AKKG 199
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
 47-221 1.92e-06

Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for the regeneration of methionine from homocysteine, as well as the coversion of methyltetrahydrofolate to tetrahydrofolate. In MSR, electrons are transferred from NADPH to FAD to FMN to cob(II)alamin. MSR resembles proteins of the cytochrome p450 family including nitric oxide synthase, the alpha subunit of sulfite reductase, but contains an extended hinge region. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPORs resemble ferredoxin reductase (FNR) but have a connecting subdomain inserted within the flavin binding region, which helps orient the FMN binding doamin with the FNR module. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99800 [Multi-domain]  Cd Length: 398  Bit Score: 48.09  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  47 LPRPISIC---EKSKNKLTFLYAVVGNGTKEF-TKLKEDDEISLTGPLGNGFDLEKEYNK-----------VALVSGGIG 111
Cdd:cd06203  173 QPRPYSIAsspLEGPGKLRFIFSVVEFPAKGLcTSWLESLCLSASSHGVKVPFYLRSSSRfrlppddlrrpIIMVGPGTG 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 112 TAP---MLELAKKLRKKNPDQ---KIDLYAGFRH---DVYLIDELKEYVNE-------VYISTNTGKNGHKGFVTEILKp 175
Cdd:cd06203  253 VAPflgFLQHREKLKESHTETvfgEAWLFFGCRHrdrDYLFRDELEEFLEEgiltrliVAFSRDENDGSTPKYVQDKLE- 331

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 500663573 176 edydtvLCCgpeimmKKVVDMCKEKNVAVYVSME-KHMACGVGACLV 221
Cdd:cd06203  332 ------ERG------KKLVDLLLNSNAKIYVCGDaKGMAKDVRDTFV 366
PLN02252 PLN02252
nitrate reductase [NADPH]
 78-200 2.26e-05

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 45.05  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  78 LKEDDEISLTGPLGN-------GFDLEKE---YNKVALVSGGIGTAPMLELAKKLRkKNPDQKIDLYAGF--RH--DVYL 143
Cdd:PLN02252 726 LPIGDTIDVKGPLGHieyagrgSFLVNGKpkfAKKLAMLAGGTGITPMYQVIQAIL-RDPEDKTEMSLVYanRTedDILL 804

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500663573 144 IDELKEYVNEV-------YISTNTGKNGHK---GFVTE-ILK----PEDYDTV-LCCGPEIMMKKVVDMCKEK 200
Cdd:PLN02252 805 REELDRWAAEHpdrlkvwYVVSQVKREGWKysvGRVTEaMLRehlpEGGDETLaLMCGPPPMIEFACQPNLEK 877
PRK13289 PRK13289
NO-inducible flavohemoprotein;
78-203 5.65e-05

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 43.63  E-value: 5.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  78 LKEDDEISLTGPLGNgFDLEKEYNK-VALVSGGIGTAPMLELAKKLRKKNPDQKI---------DLYAgFRHDVYLIDEL 147
Cdd:PRK13289 239 VNVGDVLELAAPAGD-FFLDVASDTpVVLISGGVGITPMLSMLETLAAQQPKRPVhfihaarngGVHA-FRDEVEALAAR 316

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500663573 148 KEYVNEVYI-------STNTGKNGHKGFVT-----EILKPEDYDTVLcCGPEIMMKKVVDMCKEKNVA 203
Cdd:PRK13289 317 HPNLKAHTWyrepteqDRAGEDFDSEGLMDlewleAWLPDPDADFYF-CGPVPFMQFVAKQLLELGVP 383
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 78-203 1.89e-04

Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal.


Pssm-ID: 99782 [Multi-domain]  Cd Length: 211  Bit Score: 41.31  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  78 LKEDDEISLTGPlGNGFDLEKEYNKVALVSGGIGTAPMLELAKKLRKKNPDQKIdLYAGF-RHDVYLIDELKEYVNE--- 153
Cdd:cd06185   77 LRVGDELEVSAP-RNLFPLDEAARRHLLIAGGIGITPILSMARALAARGADFEL-HYAGRsREDAAFLDELAALPGDrvh 154

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 500663573 154 VYISTntgkNGHKGFVTEILKPEDYDTVL-CCGPEIMMKKVVDMCKEKNVA 203
Cdd:cd06185  155 LHFDD----EGGRLDLAALLAAPPAGTHVyVCGPEGMMDAVRAAAAALGWP 201
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 69-194 3.39e-04

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 40.97  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  69 GNGTKEFTKLKEDDEISLTGP------LGNG-FDLEKEYNKV--------ALVSGGIGTAPMLELAKKLrKKNPDQKIDL 133
Cdd:PTZ00319 120 GRLSQHLYHMKLGDKIEMRGPvgkfeyLGNGtYTVHKGKGGLktmhvdafAMIAGGTGITPMLQIIHAI-KKNKEDRTKV 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 134 YAGF----RHDVYLIDELKEYVNEV-----YISTNTGKNGHK---GFVTE--------ILKPEDYD----TVLCCGPEIM 189
Cdd:PTZ00319 199 FLVYanqtEDDILLRKELDEAAKDPrfhvwYTLDREATPEWKygtGYVDEemlrahlpVPDPQNSGikkvMALMCGPPPM 278


                 ....*
gi 500663573 190 MKKVV 194
Cdd:PTZ00319 279 LQMAV 283
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 102-209 8.27e-04

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 betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99812 [Multi-domain]  Cd Length: 243  Bit Score: 39.52  E-value: 8.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 102 KVALVSGGIGTAPMLELAKKLRKKNPDQKIDL--YAGFRHDVYLIDELKEY--------VNEVYisTNTGKNGHkgFVTE 171
Cdd:cd06216  124 RLLLIAAGSGITPVMSMLRTLLARGPTADVVLlyYARTREDVIFADELRALaaqhpnlrLHLLY--TREELDGR--LSAA 199

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 500663573 172 ILKPEDYD----TVLCCGPEIMMKKVVDMCKEKNVAVYVSME 209
Cdd:cd06216  200 HLDAVVPDladrQVYACGPPGFLDAAEELLEAAGLADRLHTE 241
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 75-215 9.97e-04

CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 39.85  E-value: 9.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573  75 FTKLKEDDEISLTGPLGNGFdLEKEYNK-VALVSGGIGTAPMLELAKKLRKKNPDQKIDLYAGFR--HDVYLIDELKEYV 151
Cdd:PRK07609 179 FGALKERDILRIEGPLGTFF-LREDSDKpIVLLASGTGFAPIKSIVEHLRAKGIQRPVTLYWGARrpEDLYLSALAEQWA 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500663573 152 NEV----YI---STNTGKN---GHKGFVTE-ILkpEDYDT-----VLCCGPEIMmkkvvdmckeknvaVYVSMEKHMACG 215
Cdd:PRK07609 258 EELpnfrYVpvvSDALDDDawtGRTGFVHQaVL--EDFPDlsghqVYACGSPVM--------------VYAARDDFVAAG 321
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH