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Conserved domains on  [gi|2462525906|ref|XP_054225101|]
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NADH-cytochrome b5 reductase 2 isoform X7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02252 super family cl33442
nitrate reductase [NADPH]
 68-245 1.18e-77

nitrate reductase [NADPH]


The actual alignment was detected with superfamily member PLN02252:

Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 251.52  E-value: 1.18e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  68 PITLQDPEAKYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKI 147
Cdd:PLN02252  625 RPVALNPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKV 704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 148 YFKNVHPQYPEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLGIRpdqtSEPKktLADHLGMIAGGTGITPMLQLIR 227
Cdd:PLN02252  705 YFKNVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLVN----GKPK--FAKKLAMLAGGTGITPMYQVIQ 778

                         170
                  ....*....|....*...
gi 2462525906 228 HITKDPSDRTRMSLIFAN 245
Cdd:PLN02252  779 AILRDPEDKTEMSLVYAN 796
 
Name Accession Description Interval E-value
PLN02252 PLN02252
nitrate reductase [NADPH]
 68-245 1.18e-77

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 251.52  E-value: 1.18e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  68 PITLQDPEAKYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKI 147
Cdd:PLN02252  625 RPVALNPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKV 704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 148 YFKNVHPQYPEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLGIRpdqtSEPKktLADHLGMIAGGTGITPMLQLIR 227
Cdd:PLN02252  705 YFKNVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLVN----GKPK--FAKKLAMLAGGTGITPMYQVIQ 778

                         170
                  ....*....|....*...
gi 2462525906 228 HITKDPSDRTRMSLIFAN 245
Cdd:PLN02252  779 AILRDPEDKTEMSLVYAN 796
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 80-246 1.69e-73

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: 223.98  E-value: 1.69e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  80 LPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYFknvhpqypeG 159
Cdd:cd06183     1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYP---------G 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 160 GKMTQYLENMKIGETIFFRGPRGRLFYHGPGNlgirpdqtsepkktlADHLGMIAGGTGITPMLQLIRHITKDPSDRTRM 239
Cdd:cd06183    72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGK---------------VKHIGMIAGGTGITPMLQLIRAILKDPEDKTKI 136


                  ....*..
gi 2462525906 240 SLIFANQ 246
Cdd:cd06183   137 SLLYANR 143
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
79-186 2.03e-49

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 157.74  E-value: 2.03e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  79 PLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypE 158
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVY---------P 71

                          90       100
                  ....*....|....*....|....*...
gi 2462525906 159 GGKMTQYLENMKIGETIFFRGPRGRLFY 186
Cdd:pfam00970  72 GGKMSQYLDELKIGDTIDFKGPLGRFEY 99
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
78-251 6.60e-19

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 82.53  E-value: 6.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  78 YPLPLIEKEKISHNTRRFRF----GLPSPDHvlgLPvGNYVQLLAKIDNELVVRAYTPVSSDDDRGfvdliIKIYFKNVh 153
Cdd:COG1018     4 RPLRVVEVRRETPDVVSFTLeppdGAPLPRF---RP-GQFVTLRLPIDGKPLRRAYSLSSAPGDGR-----LEITVKRV- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 154 pqypEGGKMTQYL-ENMKIGETIFFRGPRGRLFYHGPGnlgirpdqtsepkktlADHLGMIAGGTGITPMLQLIRHITKD 232
Cdd:COG1018    74 ----PGGGGSNWLhDHLKVGDTLEVSGPRGDFVLDPEP----------------ARPLLLIAGGIGITPFLSMLRTLLAR 133

                         170
                  ....*....|....*....
gi 2462525906 233 PSDRtRMSLIFANQAGSTA 251
Cdd:COG1018   134 GPFR-PVTLVYGARSPADL 151
 
Name Accession Description Interval E-value
PLN02252 PLN02252
nitrate reductase [NADPH]
 68-245 1.18e-77

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 251.52  E-value: 1.18e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  68 PITLQDPEAKYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKI 147
Cdd:PLN02252  625 RPVALNPREKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKV 704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 148 YFKNVHPQYPEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLGIRpdqtSEPKktLADHLGMIAGGTGITPMLQLIR 227
Cdd:PLN02252  705 YFKNVHPKFPNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGRGSFLVN----GKPK--FAKKLAMLAGGTGITPMYQVIQ 778

                         170
                  ....*....|....*...
gi 2462525906 228 HITKDPSDRTRMSLIFAN 245
Cdd:PLN02252  779 AILRDPEDKTEMSLVYAN 796
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 80-246 1.69e-73

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: 223.98  E-value: 1.69e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  80 LPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYFknvhpqypeG 159
Cdd:cd06183     1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYP---------G 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 160 GKMTQYLENMKIGETIFFRGPRGRLFYHGPGNlgirpdqtsepkktlADHLGMIAGGTGITPMLQLIRHITKDPSDRTRM 239
Cdd:cd06183    72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGK---------------VKHIGMIAGGTGITPMLQLIRAILKDPEDKTKI 136


                  ....*..
gi 2462525906 240 SLIFANQ 246
Cdd:cd06183   137 SLLYANR 143
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 65-246 9.03e-70

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 216.62  E-value: 9.03e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  65 RREPITLqDPEAKYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDN----ELVVRAYTPVSSDDDRGF 140
Cdd:PTZ00319   22 RSPPVAL-DPDMFQHFKLIKKTEVTHDTFIFRFALHSPTQRLGLPIGQHIVFRCDCTTpgkpETVQHSYTPISSDDEKGY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 141 VDLIIKIYFKNVHPQYPEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLGIRPDQtSEPKKTLADHLGMIAGGTGIT 220
Cdd:PTZ00319  101 VDFLIKVYFKGVHPSFPNGGRLSQHLYHMKLGDKIEMRGPVGKFEYLGNGTYTVHKGK-GGLKTMHVDAFAMIAGGTGIT 179

                         170       180
                  ....*....|....*....|....*.
gi 2462525906 221 PMLQLIRHITKDPSDRTRMSLIFANQ 246
Cdd:PTZ00319  180 PMLQIIHAIKKNKEDRTKVFLVYANQ 205
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
79-186 2.03e-49

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 157.74  E-value: 2.03e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  79 PLPLIEKEKISHNTRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypE 158
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVY---------P 71

                          90       100
                  ....*....|....*....|....*...
gi 2462525906 159 GGKMTQYLENMKIGETIFFRGPRGRLFY 186
Cdd:pfam00970  72 GGKMSQYLDELKIGDTIDFKGPLGRFEY 99
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 83-246 2.25e-26

Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99778 [Multi-domain]  Cd Length: 223  Bit Score: 102.53  E-value: 2.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  83 IEKEKISHNTRRFRFGLPSPdhvLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKM 162
Cdd:cd00322     1 VATEDVTDDVRLFRLQLPNG---FSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGELELTVKIV---------PGGPF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 163 TQYLENMKIGETIFFRGPRGRLFYHGPGNlgirpdqtsepkktlaDHLGMIAGGTGITPMLQLIRHITKDPSDRTrMSLI 242
Cdd:cd00322    69 SAWLHDLKPGDEVEVSGPGGDFFLPLEES----------------GPVVLIAGGIGITPFRSMLRHLAADKPGGE-ITLL 131


                  ....
gi 2462525906 243 FANQ 246
Cdd:cd00322   132 YGAR 135
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
 63-246 3.14e-19

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 85.36  E-value: 3.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  63 SRRREPITLQDPeakypLPliekekISHNTRRFRFGLPSPDHvLGLPVGNYVQLLAKID---NELVVRAYTPVSSDDDRG 139
Cdd:PTZ00274   49 SQRYEPYQLGEV-----IP------ITHDTALFRFLLHSEEE-FNLKPCSTLQACYKYGvqpMDQCQRFYTPVTANHTKG 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 140 FVDLIIKiyfknvhpqYPEGGKMTQYLENMKIGETIFFRGPRGRLFYhgpgnlgiRPDQTSepkktladHLGMIAGGTGI 219
Cdd:PTZ00274  117 YFDIIVK---------RKKDGLMTNHLFGMHVGDKLLFRSVTFKIQY--------RPNRWK--------HVGMIAGGTGF 171

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462525906 220 TPMLQLIRHITKDP-----SDRTRMSLIFANQ 246
Cdd:PTZ00274  172 TPMLQIIRHSLTEPwdsgeVDRTKLSFLFCNR 203
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
78-251 6.60e-19

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 82.53  E-value: 6.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  78 YPLPLIEKEKISHNTRRFRF----GLPSPDHvlgLPvGNYVQLLAKIDNELVVRAYTPVSSDDDRGfvdliIKIYFKNVh 153
Cdd:COG1018     4 RPLRVVEVRRETPDVVSFTLeppdGAPLPRF---RP-GQFVTLRLPIDGKPLRRAYSLSSAPGDGR-----LEITVKRV- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 154 pqypEGGKMTQYL-ENMKIGETIFFRGPRGRLFYHGPGnlgirpdqtsepkktlADHLGMIAGGTGITPMLQLIRHITKD 232
Cdd:COG1018    74 ----PGGGGSNWLhDHLKVGDTLEVSGPRGDFVLDPEP----------------ARPLLLIAGGIGITPFLSMLRTLLAR 133

                         170
                  ....*....|....*....
gi 2462525906 233 PSDRtRMSLIFANQAGSTA 251
Cdd:COG1018   134 GPFR-PVTLVYGARSPADL 151
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 83-229 2.74e-17

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 78.37  E-value: 2.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  83 IEKEKISHNTRRFRFGLPsPDHVLGLPvGNYVQLlaKIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypegGKM 162
Cdd:COG0543     3 VSVERLAPDVYLLRLEAP-LIALKFKP-GQFVML--RVPGDGLRRPFSIASAPREDGTIELHIRVV-----------GKG 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462525906 163 TQYLENMKIGETIFFRGPRGRLFyhgpgnlgirpDQTSEPKKTLadhlgMIAGGTGITPMLQLIRHI 229
Cdd:COG0543    68 TRALAELKPGDELDVRGPLGNGF-----------PLEDSGRPVL-----LVAGGTGLAPLRSLAEAL 118
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 80-246 4.07e-15

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: 72.24  E-value: 4.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  80 LPLIEKEKISHNTRRFRFGLPSPDHVLGLPvGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfkNVhpqypEG 159
Cdd:cd06215     1 LRCVKIIQETPDVKTFRFAAPDGSLFAYKP-GQFLTLELEIDGETVYRAYTLSSSPSRPDSLSITVK----RV-----PG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 160 GKMTQYL-ENMKIGETIFFRGPRGRlFYhgpgnlgirpdqtsePKKTLADHLGMIAGGTGITPMLQLIRHITKDPSD--- 235
Cdd:cd06215    71 GLVSNWLhDNLKVGDELWASGPAGE-FT---------------LIDHPADKLLLLSAGSGITPMMSMARWLLDTRPDadi 134

                         170
                  ....*....|....*..
gi 2462525906 236 ------RTRMSLIFANQ 246
Cdd:cd06215   135 vfihsaRSPADIIFADE 151
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 90-246 1.27e-13

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: 68.06  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  90 HNTRRFRFGLP---SPDHvlgLPvGNYVQL-LAKIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKMTQY 165
Cdd:cd06217    14 PTVKTFRLAVPdgvPPPF---LA-GQHVDLrLTAIDGYTAQRSYSIASSPTQRGRVELTVKRV---------PGGEVSPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 166 L-ENMKIGETIFFRGPRGRlFYHGPGnlgirpdqtsepkktLADHLGMIAGGTGITPMLQLIRHITkDPSDRTRMSLIFA 244
Cdd:cd06217    81 LhDEVKVGDLLEVRGPIGT-FTWNPL---------------HGDPVVLLAGGSGIVPLMSMIRYRR-DLGWPVPFRLLYS 143


                  ..
gi 2462525906 245 NQ 246
Cdd:cd06217   144 AR 145
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 82-243 8.36e-13

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: 65.74  E-value: 8.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  82 LIEKEKISHNTRRFRFGLPSPDHVLglPvGNYVQLlaKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfknvhpQYPeGGK 161
Cdd:cd06190     1 LVDVRELTHDVAEFRFALDGPADFL--P-GQYALL--ALPGVEGARAYSMANLANASGEWEFIIK--------RKP-GGA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 162 MTQYL-ENMKIGETIFFRGPRGRLFyhgpgnlgIRPDqtsEPKKTLadhlgMIAGGTGITPMLQLIRHITKDPSDRTRMS 240
Cdd:cd06190    67 ASNALfDNLEPGDELELDGPYGLAY--------LRPD---EDRDIV-----CIAGGSGLAPMLSILRGAARSPYLSDRPV 130


                  ...
gi 2462525906 241 LIF 243
Cdd:cd06190   131 DLF 133
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 86-243 1.89e-12

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: 64.92  E-value: 1.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  86 EKISHNTRRFRFGLPSPDHVLGLPvGNYVQLlaKIDNELVVRAYTPVSSDDDRGFVDLIikiyfKNVhpqypEGGKMTQY 165
Cdd:cd06209    10 ERLSDSTIGLTLELDEAGALAFLP-GQYVNL--QVPGTDETRSYSFSSAPGDPRLEFLI-----RLL-----PGGAMSSY 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462525906 166 LENM-KIGETIFFRGPRGRlFYHGPGNlgiRPdqtsepkktladhLGMIAGGTGITPMLQLIRHITKDPSDRtRMSLIF 243
Cdd:cd06209    77 LRDRaQPGDRLTLTGPLGS-FYLREVK---RP-------------LLMLAGGTGLAPFLSMLDVLAEDGSAH-PVHLVY 137
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 82-237 2.08e-11

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: 61.96  E-value: 2.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  82 LIEKEKISHNTRRFRFGLPSPDHVLGLPvGNYVQLlaKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfknvhpqYPEGGK 161
Cdd:cd06211    11 VVEIEDLTPTIKGVRLKLDEPEEIEFQA-GQYVNL--QAPGYEGTRAFSIASSPSDAGEIELHIR---------LVPGGI 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462525906 162 MTQYL-ENMKIGETIFFRGPRGRLFYHgpgnlgirpDQTSEPkktladhLGMIAGGTGITPMLQLIRHITKDPSDRT 237
Cdd:cd06211    79 ATTYVhKQLKEGDELEISGPYGDFFVR---------DSDQRP-------IIFIAGGSGLSSPRSMILDLLERGDTRK 139
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 212-246 8.26e-11

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: 57.65  E-value: 8.26e-11
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462525906 212 MIAGGTGITPMLQLIRHITKDPSDRTRMSLIFANQ 246
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKDPTQVVLVFGNR 35
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 111-227 4.31e-10

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: 58.39  E-value: 4.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 111 GNYVQLLAKIDNELVVRAYTPVSSDDDR-GFVDLIIKIyfknvHPqypeGGKMTQYL-ENMKIGETIFFRGPRGRlFYhg 188
Cdd:cd06216    49 GQHVRLGVEIDGVRHWRSYSLSSSPTQEdGTITLTVKA-----QP----DGLVSNWLvNHLAPGDVVELSQPQGD-FV-- 116

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462525906 189 pgnlgiRPDQTSEPkktladhLGMIAGGTGITPMLQLIR 227
Cdd:cd06216   117 ------LPDPLPPR-------LLLIAAGSGITPVMSMLR 142
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 78-246 1.73e-09

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


Pssm-ID: 99793 [Multi-domain]  Cd Length: 218  Bit Score: 56.09  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  78 YPLPLIEKEKISHNTRRFRFGLPspdHVLGLPVGNYVQL-LAKIDNELVVRAYTPVSSDDDRgFVDLIIKIYfknvhpqy 156
Cdd:cd06196     1 HTVTLLSIEPVTHDVKRLRFDKP---EGYDFTPGQATEVaIDKPGWRDEKRPFTFTSLPEDD-VLEFVIKSY-------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 157 PEGGKMTQYLENMKIGETIFFRGPRGRLFYHGPGNLgirpdqtsepkktladhlgmIAGGTGITPMLQLIRHITKDP--S 234
Cdd:cd06196    69 PDHDGVTEQLGRLQPGDTLLIEDPWGAIEYKGPGVF--------------------IAGGAGITPFIAILRDLAAKGklE 128

                         170
                  ....*....|..
gi 2462525906 235 DRTrmsLIFANQ 246
Cdd:cd06196   129 GNT---LIFANK 137
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 78-246 2.75e-09

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: 56.01  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  78 YPLPLIEKEKISHNTRRFRFGLPSP-DHVLGLPVGNYVQLLAKIDNELVVRAY---TPVSSDDdrgfvdliIKIYFKNVh 153
Cdd:cd06214     2 HPLTVAEVVRETADAVSITFDVPEElRDAFRYRPGQFLTLRVPIDGEEVRRSYsicSSPGDDE--------LRITVKRV- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 154 pqypEGGKMTQYL-ENMKIGETIFFRGPRGRLFYhgpgnlgirpdqtsePKKTLADHLGMIAGGTGITPMLQLIRHITKD 232
Cdd:cd06214    73 ----PGGRFSNWAnDELKAGDTLEVMPPAGRFTL---------------PPLPGARHYVLFAAGSGITPVLSILKTALAR 133

                         170
                  ....*....|....
gi 2462525906 233 PSDRtRMSLIFANQ 246
Cdd:cd06214   134 EPAS-RVTLVYGNR 146
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 86-255 4.60e-09

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: 55.43  E-value: 4.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  86 EKISHNTRRFRFGlPSPDHVLGLPV----GNYVQLlaKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfknVHPqypeGGK 161
Cdd:cd06210    10 DRVSSNVVRLRLQ-PDDAEGAGIAAefvpGQFVEI--EIPGTDTRRSYSLANTPNWDGRLEFLIR-----LLP----GGA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 162 MTQYLEN-MKIGETIFFRGPRGR--LFYHGPgnlgiRPdqtsepkktladhLGMIAGGTGITPMLQLIRHITK--DPSDR 236
Cdd:cd06210    78 FSTYLETrAKVGQRLNLRGPLGAfgLRENGL-----RP-------------RWFVAGGTGLAPLLSMLRRMAEwgEPQEA 139

                         170
                  ....*....|....*....
gi 2462525906 237 TrmsLIFanqaGSTAQASL 255
Cdd:cd06210   140 R---LFF----GVNTEAEL 151
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 83-235 2.81e-08

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: 52.93  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  83 IEKEKISHNTRRFRFGLPSPDHVlGLPvGNYVQLLAKIDNELVVRayTPVS---SDDDRGFVDLIIKIYfknvhpqypeg 159
Cdd:cd06218     2 LSNREIADDIYRLVLEAPEIAAA-AKP-GQFVMLRVPDGSDPLLR--RPISihdVDPEEGTITLLYKVV----------- 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462525906 160 GKMTQYLENMKIGETIFFRGPRGRLFyhgpgnlgirpDQTSEPKKTLadhlgMIAGGTGITPMLQLIRHITKDPSD 235
Cdd:cd06218    67 GKGTRLLSELKAGDELDVLGPLGNGF-----------DLPDDDGKVL-----LVGGGIGIAPLLFLAKQLAERGIK 126
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 83-229 3.03e-08

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: 52.60  E-value: 3.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  83 IEKEKISHNTRRFRFGLPSPDHVLGlpvGNYVQLLAkIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKM 162
Cdd:cd06187     2 VSVERLTHDIAVVRLQLDQPLPFWA---GQYVNVTV-PGRPRTWRAYSPANPPNEDGEIEFHVRAV---------PGGRV 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462525906 163 TQYLEN-MKIGETIFFRGPRGRLFYHGPGNlgiRPdqtsepkktladhLGMIAGGTGITPMLQLIRHI 229
Cdd:cd06187    69 SNALHDeLKVGDRVRLSGPYGTFYLRRDHD---RP-------------VLCIAGGTGLAPLRAIVEDA 120
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 92-233 3.97e-08

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 53.63  E-value: 3.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906   92 TRRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfknvhpqyPEGGKMTQYLENMKI 171
Cdd:PTZ00306   932 SRVLRFNLPGALQRSGLTLGQFIAIRGDWDGQQLIGYYSPITLPDDLGVISILAR----------GDKGTLKEWISALRP 1001

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462525906  172 GETIFFRGPRGRLFYHGPGnlgirpDQTSEPKKTLADHLGMIAGGTGITPMLQLIRHITKDP 233
Cdd:PTZ00306  1002 GDSVEMKACGGLRIERRPA------DKQFVFRGHVIRKLALIAGGTGVAPMLQIIRAALKKP 1057
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 80-244 7.29e-08

Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with a C-terminal iron-sulfur binding cluster domain. FNR was intially identified as a chloroplast reductase activity catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methnae assimilation in a variety of 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: 99788 [Multi-domain]  Cd Length: 231  Bit Score: 51.76  E-value: 7.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  80 LPLIEKEKISHNTRRFRFGLPSPDHVLGLPvGNYVQLLAKIDNELVVRAYTPVSSD-DDRgfvdliIKIYFKNVhpqypE 158
Cdd:cd06191     1 LRVAEVRSETPDAVTIVFAVPGPLQYGFRP-GQHVTLKLDFDGEELRRCYSLCSSPaPDE------ISITVKRV-----P 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 159 GGKMTQYL-ENMKIGETIFFRGPRGRLFYhgpgnlgirpdQTSEPKKTLAdhlgmIAGGTGITPMLQLIR--HITKDPSD 235
Cdd:cd06191    69 GGRVSNYLrEHIQPGMTVEVMGPQGHFVY-----------QPQPPGRYLL-----VAAGSGITPLMAMIRatLQTAPESD 132

                         170
                  ....*....|....*.
gi 2462525906 236 -------RTRMSLIFA 244
Cdd:cd06191   133 ftlihsaRTPADMIFA 148
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 86-253 2.21e-07

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: 50.41  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  86 EKISHNTRRFRFGLPSPDHVLGLPvGNYVQLLakIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKMTQY 165
Cdd:cd06212     9 EALTHDIRRLRLRLEEPEPIKFFA-GQYVDIT--VPGTEETRSFSMANTPADPGRLEFIIKKY---------PGGLFSSF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 166 LEN-MKIGETIFFRGPRGRLFyhgpgnlgIRPDQTSEpkktladhLGMIAGGTGITPMLQLIRHITKDPSD--------- 235
Cdd:cd06212    77 LDDgLAVGDPVTVTGPYGTCT--------LRESRDRP--------IVLIGGGSGMAPLLSLLRDMAASGSDrpvrffyga 140

                         170
                  ....*....|....*...
gi 2462525906 236 RTRMSLIFANQAGSTAQA 253
Cdd:cd06212   141 RTARDLFYLEEIAALGEK 158
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 160-243 3.19e-07

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: 49.94  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 160 GKMTQYLENMKIGETIFFRGPRGRLFyhgpgnlgirpdqTSEPKKTLAdhlgmIAGGTGITPMLQLIRHITKD------P 233
Cdd:cd06220    59 GEATSALHDLKEGDKLGIRGPYGNGF-------------ELVGGKVLL-----IGGGIGIAPLAPLAERLKKAadvtvlL 120

                          90
                  ....*....|
gi 2462525906 234 SDRTRMSLIF 243
Cdd:cd06220   121 GARTKEELLF 130
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 131-243 3.83e-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: 49.91  E-value: 3.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 131 PVSSDDDRGFVDLIIKiyfkNVhpqypegGKMTQYLENMKIGETIFFRGPRGRLFyhgpgnlgirpdqtsePKKTLADH- 209
Cdd:cd06221    48 ISSDPTRRGPLELTIR----RV-------GRVTEALHELKPGDTVGLRGPFGNGF----------------PVEEMKGKd 100

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462525906 210 LGMIAGGTGITPMLQLIRHITKDPSDRTRMSLIF 243
Cdd:cd06221   101 LLLVAGGLGLAPLRSLINYILDNREDYGKVTLLY 134
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 77-229 5.25e-07

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 49.87  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  77 KYPLPLIEKEKISHNTRRFRFGLPSPDHVLGLPvGNYVQLLAKiDNElvVRAYTPVSSDDDRGFVDLiikiyfknvHPQY 156
Cdd:PRK07609  102 KLPCRVASLERVAGDVMRLKLRLPATERLQYLA-GQYIEFILK-DGK--RRSYSIANAPHSGGPLEL---------HIRH 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462525906 157 PEGGKMTQYL-ENMKIGETIFFRGPRGRLFYHgpgnlgirpdqtSEPKKTLAdhlgMIAGGTGITPMLQLIRHI 229
Cdd:PRK07609  169 MPGGVFTDHVfGALKERDILRIEGPLGTFFLR------------EDSDKPIV----LLASGTGFAPIKSIVEHL 226
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
129-245 1.07e-06

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 49.12  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 129 YTPVSSDDDRGFVDLIIKiyfknvhpqypEGGKMTQYLENMKIGETIFFRGPRGRLFYHGpgnlgiRPDqtsepkktlAD 208
Cdd:COG4097   266 FSISSAPGGDGRLRFTIK-----------ALGDFTRRLGRLKPGTRVYVEGPYGRFTFDR------RDT---------AP 319

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462525906 209 HLGMIAGGTGITPMLQLIRHITKDPSDRTRMSLIFAN 245
Cdd:COG4097   320 RQVWIAGGIGITPFLALLRALAARPGDQRPVDLFYCV 356
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 106-228 1.45e-06

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: 47.94  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 106 LGLPVGnyvqllakiDNELVVRAYTPVSSDDDRGFVDLIIKIyfknvhpqypEGGKMTQYLENMKIGETIF-FRGPRGRL 184
Cdd:cd06195    33 LGLPND---------DGKLVRRAYSIASAPYEENLEFYIILV----------PDGPLTPRLFKLKPGDTIYvGKKPTGFL 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462525906 185 FyhgpgnlgIRPDQTSEpkktladHLGMIAGGTGITPMLQLIRH 228
Cdd:cd06195    94 T--------LDEVPPGK-------RLWLLATGTGIAPFLSMLRD 122
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 82-227 3.37e-05

FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 43.85  E-value: 3.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  82 LIEKEKISHNTRRFRFGLPSPDHvLGLPvGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKIyfknvhpqypeGGK 161
Cdd:cd06192     1 IVKKEQLEPNLVLLTIKAPLAAR-LFRP-GQFVFLRNFESPGLERIPLSLAGVDPEEGTISLLVEI-----------RGP 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462525906 162 MTQYLENMKIGETIFFRGPRGRLFYHGPGNlgirpdqtsepKKTLadhlgMIAGGTGITPMLQLIR 227
Cdd:cd06192    68 KTKLIAELKPGEKLDVMGPLGNGFEGPKKG-----------GTVL-----LVAGGIGLAPLLPIAK 117
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 86-236 3.50e-05

NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.


Pssm-ID: 99786 [Multi-domain]  Cd Length: 224  Bit Score: 43.69  E-value: 3.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  86 EKISHNTRRFRFGLPSPDHVLGlpvGNYVQLLAKiDNELvvRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGKMTQY 165
Cdd:cd06189     7 EPLNDDVYRVRLKPPAPLDFLA---GQYLDLLLD-DGDK--RPFSIASAPHEDGEIELHIRAV---------PGGSFSDY 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462525906 166 -LENMKIGETIFFRGPRGRLFYHgpgnlgirpDQTSEPkktladhLGMIAGGTGITPMLQLIRHITKDPSDR 236
Cdd:cd06189    72 vFEELKENGLVRIEGPLGDFFLR---------EDSDRP-------LILIAGGTGFAPIKSILEHLLAQGSKR 127
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 131-243 6.29e-05

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 43.32  E-value: 6.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 131 PVS-SDDDRGFVDLIIKIYfknvhpqypegGKMTQYLENMKIGETIFFRGPRGRLFyhgpgnlgirpDQTSEPKKTLAdh 209
Cdd:PRK00054   52 PISiSDIDKNEITILYRKV-----------GEGTKKLSKLKEGDELDIRGPLGNGF-----------DLEEIGGKVLL-- 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462525906 210 lgmIAGGTGITPMLQLIRHITK-------DPSDRTRMSLIF 243
Cdd:PRK00054  108 ---VGGGIGVAPLYELAKELKKkgvevttVLGARTKDEVIF 145
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 158-250 7.64e-05

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: 42.93  E-value: 7.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 158 EGGKMTQYL-ENMKIGETIFFRGPRGRLFYhgpgnlgirPDQTSEPkktladhLGMIAGGTGITPMLQLIRHITKDPSDR 236
Cdd:cd06184    79 PGGLVSNYLhDNVKVGDVLEVSAPAGDFVL---------DEASDRP-------LVLISAGVGITPMLSMLEALAAEGPGR 142

                          90
                  ....*....|....
gi 2462525906 237 tRMSLIFANQAGST 250
Cdd:cd06184   143 -PVTFIHAARNSAV 155
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 122-243 1.12e-04

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: 42.68  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 122 NELVVRAYTPVSSDDDRGFVDLIIKIyfKNVHPQYPEG--GKMTQYLENMKIGETIFFRGPRGrlFYHgpgnlgirpdqT 199
Cdd:cd06188    82 DEPVSRAYSLANYPAEEGELKLNVRI--ATPPPGNSDIppGIGSSYIFNLKPGDKVTASGPFG--EFF-----------I 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462525906 200 SEPKKTLAdhlgMIAGGTGITPMLQLIRHITKDPSDRTRMSLIF 243
Cdd:cd06188   147 KDTDREMV----FIGGGAGMAPLRSHIFHLLKTLKSKRKISFWY 186
PRK05802 PRK05802
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
130-228 2.45e-04

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


Pssm-ID: 235613 [Multi-domain]  Cd Length: 320  Bit Score: 41.50  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 130 TPVS---SDDDRGFVDLIIKIYfknvhpqypegGKMTQYLENMKIGETIFFRGPrgrlFYHGPgnLGIRPDQTSEPKKTL 206
Cdd:PRK05802  114 VPISimeADTEENIIKVAIEIR-----------GVKTKKIAKLNKGDEILLRGP----YWNGI--LGLKNIKSTKNGKSL 176

                          90       100
                  ....*....|....*....|..
gi 2462525906 207 adhlgMIAGGTGITPMLQLIRH 228
Cdd:PRK05802  177 -----VIARGIGQAPGVPVIKK 193
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 129-238 5.79e-04

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: 39.98  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 129 YTPVSS-DDDRGFVDLIIKiyfknvhpqyPEGGKMT---QYLENMKIGE---TIFFRGPrgrlfYHGPGNLGIRpdqtse 201
Cdd:cd06186    47 FTIASSpEDEQDTLSLIIR----------AKKGFTTrllRKALKSPGGGvslKVLVEGP-----YGSSSEDLLS------ 105

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462525906 202 pkktlADHLGMIAGGTGITPMLQLIRHITKDPSDRTR 238
Cdd:cd06186   106 -----YDNVLLVAGGSGITFVLPILRDLLRRSSKTSR 137
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 75-228 6.76e-04

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. 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. 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: 99798 [Multi-domain]  Cd Length: 289  Bit Score: 40.39  E-value: 6.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  75 EAKYPLPLIE----KEKISHNTRRFRFGLP-SPDHVLGLP---VGNYVQLLAKidNELVVRAYTPVSSDDDrGFVDLIIK 146
Cdd:cd06201    43 PRTKALELVErkdyGAAVQAPTAILRFKPAkRKLSGKGLPsfeAGDLLGILPP--GSDVPRFYSLASSSSD-GFLEICVR 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906 147 iyfknVHPqypeGGKMTQYLENMKIGETI--FFRGprgrlfyhgpgNLGIRPDQTSEPkktladhLGMIAGGTGITPMLQ 224
Cdd:cd06201   120 -----KHP----GGLCSGYLHGLKPGDTIkaFIRP-----------NPSFRPAKGAAP-------VILIGAGTGIAPLAG 172


                  ....
gi 2462525906 225 LIRH 228
Cdd:cd06201   173 FIRA 176
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 82-228 1.30e-03

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: 39.17  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  82 LIEKEKISHNTRRFRFglpSPDHVLGLPVGNYVQLlakIDNELVVRAYTPVSSDDDRGFVDLIIKIYfknvhpqypEGGK 161
Cdd:cd06194     1 VVSLQRLSPDVLRVRL---EPDRPLPYLPGQYVNL---RRAGGLARSYSPTSLPDGDNELEFHIRRK---------PNGA 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462525906 162 MTQYL-ENMKIGETIFFRGPRGRLFYhgpgnlgiRPDQtsepkktLADHLGMIAGGTGITPMLQLIRH 228
Cdd:cd06194    66 FSGWLgEEARPGHALRLQGPFGQAFY--------RPEY-------GEGPLLLVGAGTGLAPLWGIARA 118
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 208-244 2.20e-03

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 39.06  E-value: 2.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2462525906 208 DHLGMIAGGTGITPMLQLIRHITKDPSDR----TRMSLIFA 244
Cdd:PLN02844  424 DSLLLVAGGIGITPFLSILKEIASQSSSRyrfpKRVQLIYV 464
siderophore_interacting cd06193
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like ...
 94-187 4.25e-03

Siderophore interacting proteins share the domain structure of the ferredoxin reductase like family. Siderophores are produced in various bacteria (and some plants) to extract iron from hosts. Binding constants are high, so iron can be pilfered from transferrin and lactoferrin for bacterial uptake, contributing to pathogen virulence. 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 a variety of 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 two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99790 [Multi-domain]  Cd Length: 235  Bit Score: 37.63  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  94 RFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVRAYTPVSSDDDRGFVDLIIKiyfknVHpqyPEGGKMTQYLENMKIGE 173
Cdd:cd06193    32 HVKLLFPDPGQAPPVLPVLGRRRWPPEEPRPVMRTYTVRRFDPEAGELDIDFV-----LH---GDEGPASRWAASAQPGD 103

                          90
                  ....*....|....
gi 2462525906 174 TIFFRGPRGRLFYH 187
Cdd:cd06193   104 TLGIAGPGGSFLPP 117
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 81-222 8.03e-03

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 37.09  E-value: 8.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462525906  81 PLIEKEKIShntrRFRFGLPSPDHVLGLPVGNYVQLLAKIDNELVVrayTPVSSDDDRGFVDLIIKiyfknvhpqypEGG 160
Cdd:PRK08345   15 DLTEREKLF----LLRFEDPELAESFTFKPGQFVQVTIPGVGEVPI---SICSSPTRKGFFELCIR-----------RAG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462525906 161 KMTQYLENMKIGETIFFRGPRGRLFyhgpgnlgirPDQTSEPKKTLadhlgMIAGGTGITPM 222
Cdd:PRK08345   77 RVTTVIHRLKEGDIVGVRGPYGNGF----------PVDEMEGMDLL-----LIAGGLGMAPL 123
 
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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