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Conserved domains on  [gi|1950962799|ref|WP_198929010|]
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MULTISPECIES: hybrid-cluster NAD(P)-dependent oxidoreductase [Rhizobium]

Protein Classification

hybrid-cluster NAD(P)-dependent oxidoreductase( domain architecture ID 10153117)

NAD(P)-dependent oxidoreductase that is a hybrid-cluster protein containing both [2Fe-2S] (or [4Fe-4S]) and [4Fe-2S-2O] clusters, may transfer electrons to carrier proteins such as ferredoxin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 23-254 6.29e-125

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: 358.44  E-value: 6.29e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  23 LECLSVTPEAPDVMTFTFRSDKDNWFRYLPGQFVTLELPTAPESVMRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFEN 102
Cdd:cd06215     1 LRCVKIIQETPDVKTFRFAAPDGSLFAYKPGQFLTLELEIDGETVYRAYTLSSSPSRPDSLSITVKRVPGGLVSNWLHDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 103 LKPGMRIKAFGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMP 182
Cdd:cd06215    81 LKVGDELWASGPAGEFTLIDHPADKLLLLSAGSGITPMMSMARWLLDTRPDADIVFIHSARSPADIIFADELEELARRHP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950962799 183 NLNLGLIVEGcGRTDLWSGLKGRIDKAKIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESF 254
Cdd:cd06215   161 NFRLHLILEQ-PAPGAWGGYRGRLNAELLALLVPDLKERTVFVCGPAGFMKAVKSLLAELGFPMSRFHQESF 231
Fdx COG0633
Ferredoxin [Energy production and conversion];
276-360 1.00e-28

Ferredoxin [Energy production and conversion];


:

Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 106.86  E-value: 1.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 276 TTIRFTMAGKDVVCAAGQTVLQAARGAGVRIGAACESGLCGTCRVMKLSGEVEMSHNGGILDDEIEEGYILACCSRPKTD 355
Cdd:COG0633     2 PKVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARPTSD 81


                  ....*
gi 1950962799 356 VQVEA 360
Cdd:COG0633    82 LVVEL 86
 
Name Accession Description Interval E-value
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 23-254 6.29e-125

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: 358.44  E-value: 6.29e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  23 LECLSVTPEAPDVMTFTFRSDKDNWFRYLPGQFVTLELPTAPESVMRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFEN 102
Cdd:cd06215     1 LRCVKIIQETPDVKTFRFAAPDGSLFAYKPGQFLTLELEIDGETVYRAYTLSSSPSRPDSLSITVKRVPGGLVSNWLHDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 103 LKPGMRIKAFGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMP 182
Cdd:cd06215    81 LKVGDELWASGPAGEFTLIDHPADKLLLLSAGSGITPMMSMARWLLDTRPDADIVFIHSARSPADIIFADELEELARRHP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950962799 183 NLNLGLIVEGcGRTDLWSGLKGRIDKAKIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESF 254
Cdd:cd06215   161 NFRLHLILEQ-PAPGAWGGYRGRLNAELLALLVPDLKERTVFVCGPAGFMKAVKSLLAELGFPMSRFHQESF 231
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
18-253 5.29e-83

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 252.02  E-value: 5.29e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  18 DRQHLLECLSVTPEAPDVMTFTFRS-DKDNWFRYLPGQFVTLELPTAPESVMRTYTLSSTPSRPfSVAVTVKAQRDSIGT 96
Cdd:COG1018     1 AGFRPLRVVEVRRETPDVVSFTLEPpDGAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDG-RLEITVKRVPGGGGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  97 RWMFENLKPGMRIKAFGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEY 176
Cdd:COG1018    80 NWLHDHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGARSPADLAFRDELEA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950962799 177 LARFMPNLNLGLIVegcgrTDLWSGLKGRIDKAKIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQES 253
Cdd:COG1018   160 LAARHPRLRLHPVL-----SREPAGLQGRLDAELLAALLPDPADAHVYLCGPPPMMEAVRAALAELGVPEERIHFER 231
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 27-359 4.80e-69

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 219.58  E-value: 4.80e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  27 SVTPEAPDVMTFTFRSDkdNWFRYLPGQFVTLELPTAPESvMRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFENLKPG 106
Cdd:PRK10684   16 SIVQETPDVWTISLICH--DFYPYRAGQYALVSIRNSAET-LRAYTLSSTPGVSEFITLTVRRIDDGVGSQWLTRDVKRG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 107 MRIKAFGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMPNLNL 186
Cdd:PRK10684   93 DYLWLSDAMGEFTCDDKAEDKYLLLAAGCGVTPIMSMRRWLLKNRPQADVQVIFNVRTPQDVIFADEWRQLKQRYPQLNL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 187 GLIVEgcgrTDLWSG-LKGRIDKAKIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESFQPanaatplaE 265
Cdd:PRK10684  173 TLVAE----NNATEGfIAGRLTRELLQQAVPDLASRTVMTCGPAPYMDWVEQEVKALGVTADRFFKEKFFT--------P 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 266 VTDDASTDAATTIRftMAGKDVVCAAGQTVLQAARGAGVRIGAACESGLCGTCRVMKLSGEVEMSHNGGILDDEIEEGYI 345
Cdd:PRK10684  241 VAEAATSGLTFTKL--QPAREFYAPVGTTLLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVSSTMTLTPAEIAQGYV 318

                         330
                  ....*....|....
gi 1950962799 346 LACCSRPKTDVQVE 359
Cdd:PRK10684  319 LACSCHPQGDLVLA 332
Fdx COG0633
Ferredoxin [Energy production and conversion];
276-360 1.00e-28

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 106.86  E-value: 1.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 276 TTIRFTMAGKDVVCAAGQTVLQAARGAGVRIGAACESGLCGTCRVMKLSGEVEMSHNGGILDDEIEEGYILACCSRPKTD 355
Cdd:COG0633     2 PKVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARPTSD 81


                  ....*
gi 1950962799 356 VQVEA 360
Cdd:COG0633    82 LVVEL 86
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 277-359 9.92e-23

2Fe-2S iron-sulfur cluster 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). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 90.53  E-value: 9.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 277 TIRFTMAGKDVVCAAGQTVLQAARGAGVRIGAACESGLCGTCRVMKLSGEVEMSHNGGILDDEIEEGYILACCSRPKTDV 356
Cdd:cd00207     2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTDGL 81


                  ...
gi 1950962799 357 QVE 359
Cdd:cd00207    82 VIE 84
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 278-360 8.11e-15

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 74.52  E-value: 8.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 278 IRFTMAGKDVVCAAGQTVLQAARGAGVRIGAACESGLCGTCRVMKLSGEVEMS-HNGGIL-DDEIEEGYILACCSRPKTD 355
Cdd:PRK07609    5 VTLQPSGRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQGpHQASALsGEERAAGEALTCCAKPLSD 84


                  ....*
gi 1950962799 356 VQVEA 360
Cdd:PRK07609   85 LVLEA 89
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
284-353 7.98e-13

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 63.31  E-value: 7.98e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950962799 284 GKDVVCAAGQT-VLQAARGAGVRIGAACESGLCGTCRVMKLSGEvEMSHNGGILDDEIEEGY-ILACCSRPK 353
Cdd:pfam00111   7 GVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGE-DQSDQSFLEDDELAAGYvVLACQTYPK 77
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 130-236 1.29e-12

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: 63.43  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 130 FVSAGSGVTPMMAMTRYMA-DTAPLSDITFVNCSRSPADIIFRSELEYLARFMPN-LNLGLIVEGCGRTdlWSGLKGRID 207
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILeDPKDPTQVVLVFGNRNEDDILYREELDELAEKHPGrLTVVYVVSRPEAG--WTGGKGRVQ 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1950962799 208 KAKIGLLAPDFMDRT-IFCCGPEVFMDAVR 236
Cdd:pfam00175  79 DALLEDHLSLPDEEThVYVCGPPGMIKAVR 108
 
Name Accession Description Interval E-value
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 23-254 6.29e-125

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: 358.44  E-value: 6.29e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  23 LECLSVTPEAPDVMTFTFRSDKDNWFRYLPGQFVTLELPTAPESVMRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFEN 102
Cdd:cd06215     1 LRCVKIIQETPDVKTFRFAAPDGSLFAYKPGQFLTLELEIDGETVYRAYTLSSSPSRPDSLSITVKRVPGGLVSNWLHDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 103 LKPGMRIKAFGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMP 182
Cdd:cd06215    81 LKVGDELWASGPAGEFTLIDHPADKLLLLSAGSGITPMMSMARWLLDTRPDADIVFIHSARSPADIIFADELEELARRHP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950962799 183 NLNLGLIVEGcGRTDLWSGLKGRIDKAKIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESF 254
Cdd:cd06215   161 NFRLHLILEQ-PAPGAWGGYRGRLNAELLALLVPDLKERTVFVCGPAGFMKAVKSLLAELGFPMSRFHQESF 231
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
18-253 5.29e-83

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 252.02  E-value: 5.29e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  18 DRQHLLECLSVTPEAPDVMTFTFRS-DKDNWFRYLPGQFVTLELPTAPESVMRTYTLSSTPSRPfSVAVTVKAQRDSIGT 96
Cdd:COG1018     1 AGFRPLRVVEVRRETPDVVSFTLEPpDGAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDG-RLEITVKRVPGGGGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  97 RWMFENLKPGMRIKAFGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEY 176
Cdd:COG1018    80 NWLHDHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGARSPADLAFRDELEA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950962799 177 LARFMPNLNLGLIVegcgrTDLWSGLKGRIDKAKIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQES 253
Cdd:COG1018   160 LAARHPRLRLHPVL-----SREPAGLQGRLDAELLAALLPDPADAHVYLCGPPPMMEAVRAALAELGVPEERIHFER 231
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 23-254 2.32e-71

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: 222.02  E-value: 2.32e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  23 LECLSVTPEAPDVMTFTFRSDKDNWFRYLPGQFVTLELPTAPESVMRTYTLSSTPSrPFSVAVTVKAQRDSIGTRWMFEN 102
Cdd:cd06191     1 LRVAEVRSETPDAVTIVFAVPGPLQYGFRPGQHVTLKLDFDGEELRRCYSLCSSPA-PDEISITVKRVPGGRVSNYLREH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 103 LKPGMRIKAFGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMP 182
Cdd:cd06191    80 IQPGMTVEVMGPQGHFVYQPQPPGRYLLVAAGSGITPLMAMIRATLQTAPESDFTLIHSARTPADMIFAQELRELADKPQ 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950962799 183 NLNLGLIVEGCGRTDLWSGLKGRIDKAKIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESF 254
Cdd:cd06191   160 RLRLLCIFTRETLDSDLLHGRIDGEQSLGAALIPDRLEREAFICGPAGMMDAVETALKELGMPPERIHTERF 231
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 27-359 4.80e-69

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 219.58  E-value: 4.80e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  27 SVTPEAPDVMTFTFRSDkdNWFRYLPGQFVTLELPTAPESvMRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFENLKPG 106
Cdd:PRK10684   16 SIVQETPDVWTISLICH--DFYPYRAGQYALVSIRNSAET-LRAYTLSSTPGVSEFITLTVRRIDDGVGSQWLTRDVKRG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 107 MRIKAFGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMPNLNL 186
Cdd:PRK10684   93 DYLWLSDAMGEFTCDDKAEDKYLLLAAGCGVTPIMSMRRWLLKNRPQADVQVIFNVRTPQDVIFADEWRQLKQRYPQLNL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 187 GLIVEgcgrTDLWSG-LKGRIDKAKIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESFQPanaatplaE 265
Cdd:PRK10684  173 TLVAE----NNATEGfIAGRLTRELLQQAVPDLASRTVMTCGPAPYMDWVEQEVKALGVTADRFFKEKFFT--------P 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 266 VTDDASTDAATTIRftMAGKDVVCAAGQTVLQAARGAGVRIGAACESGLCGTCRVMKLSGEVEMSHNGGILDDEIEEGYI 345
Cdd:PRK10684  241 VAEAATSGLTFTKL--QPAREFYAPVGTTLLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVSSTMTLTPAEIAQGYV 318

                         330
                  ....*....|....
gi 1950962799 346 LACCSRPKTDVQVE 359
Cdd:PRK10684  319 LACSCHPQGDLVLA 332
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 16-254 5.17e-60

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: 193.59  E-value: 5.17e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  16 WSDRQHLLECLSVTPEAPDVMTFTFRSDKdNWFRYLPGQFVTLELPTAPESVMRTYTLSSTPSRPFS-VAVTVKAQRDSI 94
Cdd:cd06216    13 WSARELRARVVAVRPETADMVTLTLRPNR-GWPGHRAGQHVRLGVEIDGVRHWRSYSLSSSPTQEDGtITLTVKAQPDGL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  95 GTRWMFENLKPGMRIKAFGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSEL 174
Cdd:cd06216    92 VSNWLVNHLAPGDVVELSQPQGDFVLPDPLPPRLLLIAAGSGITPVMSMLRTLLARGPTADVVLLYYARTREDVIFADEL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 175 EYLARFMPNLNLGLIVEGcgrtdlwSGLKGRIDKAKIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDmKRYHQESF 254
Cdd:cd06216   172 RALAAQHPNLRLHLLYTR-------EELDGRLSAAHLDAVVPDLADRQVYACGPPGFLDAAEELLEAAGLA-DRLHTERF 243
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 28-254 2.35e-59

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: 191.33  E-value: 2.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  28 VTPEAPDVMTFTFRSDKDNWFRYLPGQFVTLELpTAPE--SVMRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFENLKP 105
Cdd:cd06217     9 IIQETPTVKTFRLAVPDGVPPPFLAGQHVDLRL-TAIDgyTAQRSYSIASSPTQRGRVELTVKRVPGGEVSPYLHDEVKV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 106 GMRIKAFGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMPNLN 185
Cdd:cd06217    88 GDLLEVRGPIGTFTWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVPFRLLYSARTAEDVIFRDELEQLARRHPNLH 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1950962799 186 LGLIVEGCGRTDlWSGLKGRIDKAKIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESF 254
Cdd:cd06217   168 VTEALTRAAPAD-WLGPAGRITADLIAELVPPLAGRRVYVCGPPAFVEAATRLLLELGVPRDRIRTEAF 235
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 21-254 5.79e-55

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: 180.43  E-value: 5.79e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  21 HLLECLSVTPEAPDVMTFTFR---SDKDNwFRYLPGQFVTLELPTAPESVMRTYTLSSTPSRPFsVAVTVKAQRDSIGTR 97
Cdd:cd06214     2 HPLTVAEVVRETADAVSITFDvpeELRDA-FRYRPGQFLTLRVPIDGEEVRRSYSICSSPGDDE-LRITVKRVPGGRFSN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  98 WMFENLKPGMRIKAFGPLGDFTHIRHPGEK-YLFVSAGSGVTPMMAMTRymadTA----PLSDITFVNCSRSPADIIFRS 172
Cdd:cd06214    80 WANDELKAGDTLEVMPPAGRFTLPPLPGARhYVLFAAGSGITPVLSILK----TAlarePASRVTLVYGNRTEASVIFRE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 173 ELEYL-ARFMPNLNLGLIVEgcgR-TDLWSGLKGRIDKAKIGLLAPDFMDRT----IFCCGPEVFMDAVRSMLEAHGFDM 246
Cdd:cd06214   156 ELADLkARYPDRLTVIHVLS---ReQGDPDLLRGRLDAAKLNALLKNLLDATefdeAFLCGPEPMMDAVEAALLELGVPA 232


                  ....*...
gi 1950962799 247 KRYHQESF 254
Cdd:cd06214   233 ERIHRELF 240
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 26-252 6.03e-53

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: 174.56  E-value: 6.03e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  26 LSVTPEAPDVMTFTFrsDKDNWFRYLPGQFVTLELPTAPESVMRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFeNLKP 105
Cdd:cd00322     1 VATEDVTDDVRLFRL--QLPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGELELTVKIVPGGPFSAWLH-DLKP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 106 GMRIKAFGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMPNLN 185
Cdd:cd00322    78 GDEVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTPADLLFLDELEELAKEGPNFR 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950962799 186 LgLIVEGCGRTDLWSGLKGRIDKAKIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQE 252
Cdd:cd00322   158 L-VLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
15-255 2.66e-50

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 173.93  E-value: 2.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  15 PWSDRQHLLECLSVTPEAPDVMTFTFRSDKDNWFRYLPGQFVTLELPTAPESvmRT---YTLSSTPSRPFSVAVTVKAQR 91
Cdd:COG4097   209 PLRSRRHPYRVESVEPEAGDVVELTLRPEGGRWLGHRAGQFAFLRFDGSPFW--EEahpFSISSAPGGDGRLRFTIKALG 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  92 DsiGTRWMfENLKPGMRIKAFGPLGDFTHIRHP-GEKYLFVSAGSGVTPMMAMTRYMAD-TAPLSDITFVNCSRSPADII 169
Cdd:COG4097   287 D--FTRRL-GRLKPGTRVYVEGPYGRFTFDRRDtAPRQVWIAGGIGITPFLALLRALAArPGDQRPVDLFYCVRDEEDAP 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 170 FRSELEYLARFMPNLNLGLIVegcgrtdlwSGLKGRIDKAKIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRY 249
Cdd:COG4097   364 FLEELRALAARLAGLRLHLVV---------SDEDGRLTAERLRRLVPDLAEADVFFCGPPGMMDALRRDLRALGVPARRI 434


                  ....*.
gi 1950962799 250 HQESFQ 255
Cdd:COG4097   435 HQERFE 440
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 28-257 1.01e-40

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: 143.47  E-value: 1.01e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  28 VTPEAPDVMTFTFRS-DKDNWFRYLPGQFVT--LELPTAPESVMRTYTLSSTPSRPfSVAVTVKAQRDSIGTRWMFENLK 104
Cdd:cd06184    14 KVAESEDITSFYLEPaDGGPLPPFLPGQYLSvrVKLPGLGYRQIRQYSLSDAPNGD-YYRISVKREPGGLVSNYLHDNVK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 105 PGMRIKAFGPLGDFThIRHPGEKYL-FVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMPN 183
Cdd:cd06184    93 VGDVLEVSAPAGDFV-LDEASDRPLvLISAGVGITPMLSMLEALAAEGPGRPVTFIHAARNSAVHAFRDELEELAARLPN 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1950962799 184 LNLGLIVEGCGRTDLWSG--LKGRIDKAKIGLLAPDfMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESFQPA 257
Cdd:cd06184   172 LKLHVFYSEPEAGDREEDydHAGRIDLALLRELLLP-ADADFYLCGPVPFMQAVREGLKALGVPAERIHYEVFGPG 246
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 28-254 2.56e-39

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: 138.93  E-value: 2.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  28 VTPEAPDVMTFTFRsDKDNWFRYLPGQFVTLELPTAPESVMRTYTLSSTPSRPFSVAVTVKAQRDsiGTRWMFENLKPGM 107
Cdd:cd06198     2 RVTEVRPTTTLTLE-PRGPALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGRLRFTIKALGD--YTRRLAERLKPGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 108 RIKAFGPLGDFTHiRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMpNLNLG 187
Cdd:cd06198    79 RVTVEGPYGRFTF-DDRRARQIWIAGGIGITPFLALLEALAARGDARPVTLFYCVRDPEDAVFLDELRALAAAA-GVVLH 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950962799 188 LIvegCGRTDLWSGLKGRIDKakiglLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESF 254
Cdd:cd06198   157 VI---DSPSDGRLTLEQLVRA-----LVPDLADADVWFCGPPGMADALEKGLRALGVPARRFHYERF 215
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 26-248 2.61e-33

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 123.82  E-value: 2.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  26 LSVTPEAPDVMTFTFRSDKDNwFRYLPGQFVTLELPTAPESvmRTYTLSSTPSRPFSVAVTVkaQRDSIGTRWMFEnLKP 105
Cdd:COG0543     3 VSVERLAPDVYLLRLEAPLIA-LKFKPGQFVMLRVPGDGLR--RPFSIASAPREDGTIELHI--RVVGKGTRALAE-LKP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 106 GMRIKAFGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPlsDITFVNCSRSPADIIFRSELEYLArfmpNLN 185
Cdd:COG0543    77 GDELDVRGPLGNGFPLEDSGRPVLLVAGGTGLAPLRSLAEALLARGR--RVTLYLGARTPEDLYLLDELEALA----DFR 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1950962799 186 LGLIVEgcgrtDLWSGLKGRIDKAKIGLLAPDFMDRtIFCCGPEVFMDAVRSMLEAHGFDMKR 248
Cdd:COG0543   151 VVVTTD-----DGWYGRKGFVTDALKELLAEDSGDD-VYACGPPPMMKAVAELLLERGVPPER 207
Fdx COG0633
Ferredoxin [Energy production and conversion];
276-360 1.00e-28

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 106.86  E-value: 1.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 276 TTIRFTMAGKDVVCAAGQTVLQAARGAGVRIGAACESGLCGTCRVMKLSGEVEMSHNGGILDDEIEEGYILACCSRPKTD 355
Cdd:COG0633     2 PKVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQARPTSD 81


                  ....*
gi 1950962799 356 VQVEA 360
Cdd:COG0633    82 LVVEL 86
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 23-250 3.33e-28

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: 109.96  E-value: 3.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  23 LECLSVTPEAPDVMTFTFR-SDKDNWFRYLPGQFVTLELPTAPESVMRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMfE 101
Cdd:cd06183     1 FKLVSKEDISHDTRIFRFElPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYL-H 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 102 NLKPGMRIKAFGPLGDFTHirHPGEKY---LFVSAGSGVTPMMAMTRY-MADTAPLSDITFVNCSRSPADIIFRSELEYL 177
Cdd:cd06183    80 SLKPGDTVEIRGPFGKFEY--KPNGKVkhiGMIAGGTGITPMLQLIRAiLKDPEDKTKISLLYANRTEEDILLREELDEL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1950962799 178 ARFMP-NLNLGLIV--EGCGrtdlWSGLKGRIDKAKIG--LLAPDFMDRTIFCCGPEVFMD-AVRSMLEAHGFDMKRYH 250
Cdd:cd06183   158 AKKHPdRFKVHYVLsrPPEG----WKGGVGFITKEMIKehLPPPPSEDTLVLVCGPPPMIEgAVKGLLKELGYKKDNVF 232
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 27-255 8.97e-27

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: 105.26  E-value: 8.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  27 SVTPEAPDVMTFTFRS-DKDNWFRYLPGQFVTLELPTAPEsvmRTYTLSSTPSRPFSVAVTVKAQRDSI-GTRWMFENLK 104
Cdd:cd06185     2 RIRDEAPDIRSFELEApDGAPLPAFEPGAHIDVHLPNGLV---RQYSLCGDPADRDRYRIAVLREPASRgGSRYMHELLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 105 PGMRIKAFGPLGDFtHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAplSDITFVNCSRSPADIIFRSELEYLARfmpnl 184
Cdd:cd06185    79 VGDELEVSAPRNLF-PLDEAARRHLLIAGGIGITPILSMARALAARG--ADFELHYAGRSREDAAFLDELAALPG----- 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950962799 185 nlglivegcGRTDLWSGLKG-RIDKAKIgLLAPDfMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESFQ 255
Cdd:cd06185   151 ---------DRVHLHFDDEGgRLDLAAL-LAAPP-AGTHVYVCGPEGMMDAVRAAAAALGWPEARLHFERFA 211
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 26-254 9.42e-27

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: 105.75  E-value: 9.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  26 LSVTPEAPDVMTFTFRSDKDnwFRYLPGQFVTLELPTAPESVmRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFENLKP 105
Cdd:cd06187     2 VSVERLTHDIAVVRLQLDQP--LPFWAGQYVNVTVPGRPRTW-RAYSPANPPNEDGEIEFHVRAVPGGRVSNALHDELKV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 106 GMRIKAFGPLGDFtHIRHPGEK-YLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMPNL 184
Cdd:cd06187    79 GDRVRLSGPYGTF-YLRRDHDRpVLCIAGGTGLAPLRAIVEDALRRGEPRPVHLFFGARTERDLYDLEGLLALAARHPWL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 185 NLGLIVEgcGRTDLWSGLKGRIDKAkIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESF 254
Cdd:cd06187   158 RVVPVVS--HEEGAWTGRRGLVTDV-VGRDGPDWADHDIYICGPPAMVDATVDALLARGAPPERIHFDKF 224
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 27-254 2.08e-25

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: 102.29  E-value: 2.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  27 SVTPEAPDVMTFTFRSDKDNWFRYLPGQFVTLELPTApeSVMRTYTLSSTPSRPfSVAVTVKAQRDSIGTRWMFENLKPG 106
Cdd:cd06209     8 EVERLSDSTIGLTLELDEAGALAFLPGQYVNLQVPGT--DETRSYSFSSAPGDP-RLEFLIRLLPGGAMSSYLRDRAQPG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 107 MRIKAFGPLGDFtHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMPNLNL 186
Cdd:cd06209    85 DRLTLTGPLGSF-YLREVKRPLLMLAGGTGLAPFLSMLDVLAEDGSAHPVHLVYGVTRDADLVELDRLEALAERLPGFSF 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950962799 187 GLIVEgcgRTDLWSGLKGRIdkakIGLLAPDFM---DRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESF 254
Cdd:cd06209   164 RTVVA---DPDSWHPRKGYV----TDHLEAEDLndgDVDVYLCGPPPMVDAVRSWLDEQGIEPANFYYEKF 227
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 32-239 1.27e-24

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: 100.02  E-value: 1.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  32 APDVMTFTFRSDKDnwFRYLPGQFVTLELPTAPesVMRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFENLKPGMRIKA 111
Cdd:cd06190     8 THDVAEFRFALDGP--ADFLPGQYALLALPGVE--GARAYSMANLANASGEWEFIIKRKPGGAASNALFDNLEPGDELEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 112 FGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSD--ITFVNCSRSPADIIFRSELEYLARFMPNLNLGLI 189
Cdd:cd06190    84 DGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSDrpVDLFYGGRTPSDLCALDELSALVALGARLRVTPA 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1950962799 190 V--EGCGRTDLWSGLKGRIDKAKIGLLAPDFMDRTIFCCGPEVFMDAVRSML 239
Cdd:cd06190   164 VsdAGSGSAAGWDGPTGFVHEVVEATLGDRLAEFEFYFAGPPPMVDAVQRML 215
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 26-248 2.19e-24

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: 99.99  E-value: 2.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  26 LSVTPEAPDVMTFTFR--SDKDNWFRYLPGQFVTLELPTAPESvmrTYTLSSTPSRPFSVAVTVKAqrdsIG--TRWMFE 101
Cdd:cd06221     2 VEVVDETEDIKTFTLRleDDDEELFTFKPGQFVMLSLPGVGEA---PISISSDPTRRGPLELTIRR----VGrvTEALHE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 102 nLKPGMRIKAFGPLGD-FTHIRHPGEKYLFVSAGSGVTPMMAMTRY-MADTAPLSDITFVNCSRSPADIIFRSELEYLAR 179
Cdd:cd06221    75 -LKPGDTVGLRGPFGNgFPVEEMKGKDLLLVAGGLGLAPLRSLINYiLDNREDYGKVTLLYGARTPEDLLFKEELKEWAK 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1950962799 180 fMPNLNLGLIVEGcgRTDLWSGLKGRIDKAkIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKR 248
Cdd:cd06221   154 -RSDVEVILTVDR--AEEGWTGNVGLVTDL-LPELTLDPDNTVAIVCGPPIMMRFVAKELLKLGVPEEQ 218
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 26-254 3.14e-24

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: 98.88  E-value: 3.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  26 LSVTPEAPDVMTFTFRSDKDnwFRYLPGQFVTLelpTAPESVMRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFENLKP 105
Cdd:cd06194     2 VSLQRLSPDVLRVRLEPDRP--LPYLPGQYVNL---RRAGGLARSYSPTSLPDGDNELEFHIRRKPNGAFSGWLGEEARP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 106 GMRIKAFGPLGDFTHIRHPGE-KYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMPNL 184
Cdd:cd06194    77 GHALRLQGPFGQAFYRPEYGEgPLLLVGAGTGLAPLWGIARAALRQGHQGEIRLVHGARDPDDLYLHPALLWLAREHPNF 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950962799 185 NLGLIVEGCgrtdlwSGLKGRIDKAKIGL-LAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESF 254
Cdd:cd06194   157 RYIPCVSEG------SQGDPRVRAGRIAAhLPPLTRDDVVYLCGAPSMVNAVRRRAFLAGAPMKRIYADPF 221
PRK13289 PRK13289
NO-inducible flavohemoprotein;
27-257 8.02e-23

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 98.33  E-value: 8.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  27 SVTPEAPDVMTFTFR-SDKDNWFRYLPGQFVTLELPTAPESV--MRTYTLSSTPSRPfSVAVTVKaqRDSIGT--RWMFE 101
Cdd:PRK13289  161 KKVPESEVITSFYLEpVDGGPVADFKPGQYLGVRLDPEGEEYqeIRQYSLSDAPNGK-YYRISVK--REAGGKvsNYLHD 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 102 NLKPGMRIKAFGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFM 181
Cdd:PRK13289  238 HVNVGDVLELAAPAGDFFLDVASDTPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIHAARNGGVHAFRDEVEALAARH 317

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1950962799 182 PNLNLGLI---VEGCGRTDLWSGLKGRIDKAKIGLLAPDfMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESFQPA 257
Cdd:PRK13289  318 PNLKAHTWyrePTEQDRAGEDFDSEGLMDLEWLEAWLPD-PDADFYFCGPVPFMQFVAKQLLELGVPEERIHYEFFGPA 395
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 277-359 9.92e-23

2Fe-2S iron-sulfur cluster 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). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 90.53  E-value: 9.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 277 TIRFTMAGKDVVCAAGQTVLQAARGAGVRIGAACESGLCGTCRVMKLSGEVEMSHNGGILDDEIEEGYILACCSRPKTDV 356
Cdd:cd00207     2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTDGL 81


                  ...
gi 1950962799 357 QVE 359
Cdd:cd00207    82 VIE 84
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 24-254 7.49e-22

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 95.70  E-value: 7.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  24 ECLSVTPEAPDVMTFTFRSDKDNWFRYLPGQFVTLELP---------------------TAPESVMRTYTLSSTPSRP-- 80
Cdd:COG2871   135 TVVSNENVTTFIKELVLELPEGEEIDFKAGQYIQIEVPpyevdfkdfdipeeekfglfdKNDEEVTRAYSMANYPAEKgi 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  81 --FSV--AVTVKAQRDSIGTRWMFeNLKPGMRIKAFGPLGDFtHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLS-D 155
Cdd:COG2871   215 ieLNIriATPPMDVPPGIGSSYIF-SLKPGDKVTISGPYGEF-FLRDSDREMVFIGGGAGMAPLRSHIFDLLERGKTDrK 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 156 ITFVNCSRSPADIIFRSELEYLARFMPNLNLGLIVEGCGRTDLWSGLKGRIDKA-KIGLLA--PDFMDRTIFCCGPEVFM 232
Cdd:COG2871   293 ITFWYGARSLRELFYLEEFRELEKEHPNFKFHPALSEPLPEDNWDGETGFIHEVlYENYLKdhPAPEDCEAYLCGPPPMI 372

                         250       260
                  ....*....|....*....|..
gi 1950962799 233 DAVRSMLEAHGFDMKRYHQESF 254
Cdd:COG2871   373 DAVIKMLDDLGVEEENIYFDDF 394
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 27-243 9.92e-22

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: 92.39  E-value: 9.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  27 SVTPEAPDVMTFTFRSDKDNWFRYLPGQFVTLELPTAPESvmRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFENLKPG 106
Cdd:cd06212     7 AVEALTHDIRRLRLRLEEPEPIKFFAGQYVDITVPGTEET--RSFSMANTPADPGRLEFIIKKYPGGLFSSFLDDGLAVG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 107 MRIKAFGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMPNLNL 186
Cdd:cd06212    85 DPVTVTGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDMAASGSDRPVRFFYGARTARDLFYLEEIAALGEKIPDFTF 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1950962799 187 GLIVEGCGRTDLWSGLKGRIDKAkIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHG 243
Cdd:cd06212   165 IPALSESPDDEGWSGETGLVTEV-VQRNEATLAGCDVYLCGPPPMIDAALPVLEMSG 220
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 33-254 2.25e-21

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: 91.62  E-value: 2.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  33 PDVMTFTFRSDKDNWFRYLPGQFVTLELPtaPESVMRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFENLKPGMRIKAF 112
Cdd:cd06211    19 PTIKGVRLKLDEPEEIEFQAGQYVNLQAP--GYEGTRAFSIASSPSDAGEIELHIRLVPGGIATTYVHKQLKEGDELEIS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 113 GPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMPNLNLGLIVEG 192
Cdd:cd06211    97 GPYGDFFVRDSDQRPIIFIAGGSGLSSPRSMILDLLERGDTRKITLFFGARTRAELYYLDEFEALEKDHPNFKYVPALSR 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950962799 193 CGRTDLWSGLKGRIDKAKIGLLAPDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESF 254
Cdd:cd06211   177 EPPESNWKGFTGFVHDAAKKHFKNDFRGHKAYLCGPPPMIDACIKTLMQGRLFERDIYYEKF 238
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 33-248 1.06e-19

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: 86.85  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  33 PDVMTFTFRSDKDnwFRYLPGQFVTLELPTAPES-VMRTYTLSSTPSRP----FSVAVtvkaqRDSIGTRWMFeNLKPGM 107
Cdd:cd06195    10 DDLFSFRVTRDIP--FRFQAGQFTKLGLPNDDGKlVRRAYSIASAPYEEnlefYIILV-----PDGPLTPRLF-KLKPGD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 108 RIKAF-GPLGDFThIR--HPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFM-PN 183
Cdd:cd06195    82 TIYVGkKPTGFLT-LDevPPGKRLWLLATGTGIAPFLSMLRDLEIWERFDKIVLVHGVRYAEELAYQDEIEALAKQYnGK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1950962799 184 LNLGLIVEgcgRTDLWSGLKGRID--------KAKIGLLAPDFMDRtIFCCG-PEvFMDAVRSMLEAHGFDMKR 248
Cdd:cd06195   161 FRYVPIVS---REKENGALTGRIPdliesgelEEHAGLPLDPETSH-VMLCGnPQ-MIDDTQELLKEKGFSKNH 229
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 28-249 1.21e-19

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: 86.53  E-value: 1.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  28 VTPEAPDVMTFTFRSDkdnwFRYLPGQFVTLELPTAPESVMrtyTLSSTPSRpfsVAVTVKAQRDSigTRWMFeNLKPGM 107
Cdd:cd06220     6 VIDETPTVKTFVFDWD----FDFKPGQFVMVWVPGVDEIPM---SLSYIDGP---NSITVKKVGEA--TSALH-DLKEGD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 108 RIKAFGPLGdfTHIRHPGEKYLFVSAGSGVTPMMAMTRymaDTAPLSDITFVNCSRSPADIIFRSELEYLARfmpnlnlg 187
Cdd:cd06220    73 KLGIRGPYG--NGFELVGGKVLLIGGGIGIAPLAPLAE---RLKKAADVTVLLGARTKEELLFLDRLRKSDE-------- 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950962799 188 LIVEgcgrTDLWS-GLKGRIDKAKIGLLAPDFmdRTIFCCGPEVFMDAVRSMLEAHG----FDMKRY 249
Cdd:cd06220   140 LIVT----TDDGSyGFKGFVTDLLKELDLEEY--DAIYVCGPEIMMYKVLEILDERGvraqFSLERY 200
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 21-243 1.55e-19

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: 85.76  E-value: 1.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  21 HLLECLSVTPEAPDVMTFTFrsDKDNWFRYLPGQFVTLELpTAP--ESVMRTYTLSSTPSRPFsVAVTVKAQRDSIGTRW 98
Cdd:cd06196     1 HTVTLLSIEPVTHDVKRLRF--DKPEGYDFTPGQATEVAI-DKPgwRDEKRPFTFTSLPEDDV-LEFVIKSYPDHDGVTE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  99 MFENLKPGMRIKAFGPLGDFTHiRHPGekyLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYla 178
Cdd:cd06196    77 QLGRLQPGDTLLIEDPWGAIEY-KGPG---VFIAGGAGITPFIAILRDLAAKGKLEGNTLIFANKTEKDIILKDELEK-- 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1950962799 179 rfMPNLNLGLIVEGCGRTDLwsgLKGRIDKAKIGLLAPDFmDRTIFCCGPEVFMDAVRSMLEAHG 243
Cdd:cd06196   151 --MLGLKFINVVTDEKDPGY---AHGRIDKAFLKQHVTDF-NQHFYVCGPPPMEEAINGALKELG 209
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 19-243 4.48e-19

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: 85.82  E-value: 4.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  19 RQHLLECLSVTPEAPDVMTFTFRSDKDNWFRYLPGQFVTLELPTAP-----------------------------ESVMR 69
Cdd:cd06188     8 KKWECTVISNDNVATFIKELVLKLPSGEEIAFKAGGYIQIEIPAYEiayadfdvaekyradwdkfglwqlvfkhdEPVSR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  70 TYTLSSTPSRP----FSVAV-TVKAQRDS----IGTRWMFeNLKPGMRIKAFGPLGDFtHIRHPGEKYLFVSAGSGVTPM 140
Cdd:cd06188    88 AYSLANYPAEEgelkLNVRIaTPPPGNSDippgIGSSYIF-NLKPGDKVTASGPFGEF-FIKDTDREMVFIGGGAGMAPL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 141 MAMTRYMADT-APLSDITFVNCSRSPADIIFRSELEYLARFMPNLNLGLIVEGCGRTDLWSGLKGRIDKAKI-GLLAPDF 218
Cdd:cd06188   166 RSHIFHLLKTlKSKRKISFWYGARSLKELFYQEEFEALEKEFPNFKYHPVLSEPQPEDNWDGYTGFIHQVLLeNYLKKHP 245

                         250       260
                  ....*....|....*....|....*..
gi 1950962799 219 MDRTI--FCCGPEVFMDAVRSMLEAHG 243
Cdd:cd06188   246 APEDIefYLCGPPPMNSAVIKMLDDLG 272
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 26-243 8.93e-19

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: 84.52  E-value: 8.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  26 LSVTPEAPDVMTFTFRSDkDNWFRYLPGQFVTLELPTAPESVMRtytlsstpsRPFSVAvTVKAQRDSI---------GT 96
Cdd:cd06218     2 LSNREIADDIYRLVLEAP-EIAAAAKPGQFVMLRVPDGSDPLLR---------RPISIH-DVDPEEGTItllykvvgkGT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  97 RWMfENLKPGMRIKAFGPLGD-FThIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAplSDITFVNCSRSPADIIFRSELE 175
Cdd:cd06218    71 RLL-SELKAGDELDVLGPLGNgFD-LPDDDGKVLLVGGGIGIAPLLFLAKQLAERG--IKVTVLLGFRSADDLFLVEEFE 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950962799 176 ylarfmpnlNLGLIVEGCgrTDLWS-GLKGRIdkakIGLLAPDFMDR---TIFCCGPEVFMDAVRSMLEAHG 243
Cdd:cd06218   147 ---------ALGAEVYVA--TDDGSaGTKGFV----TDLLKELLAEArpdVVYACGPEPMLKAVAELAAERG 203
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 27-249 1.05e-18

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 84.15  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  27 SVTPEAPDVMTFTFRSDKDNWFRylPGQFVTLELPTApesvmrtytlSSTPSRPFSVA------VTVKAQRDSIGTRWMF 100
Cdd:PRK00054   11 ENKEIAPNIYTLVLDGEKVFDMK--PGQFVMVWVPGV----------EPLLERPISISdidkneITILYRKVGEGTKKLS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 101 EnLKPGMRIKAFGPLGD-FThIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPlsDITFVNCSRSPADIIFRSELEYLAR 179
Cdd:PRK00054   79 K-LKEGDELDIRGPLGNgFD-LEEIGGKVLLVGGGIGVAPLYELAKELKKKGV--EVTTVLGARTKDEVIFEEEFAKVGD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 180 fmpnlnlgLIVEgcgrTDLWS-GLKGRIdkakigllaPDFMDR------TIFCCGPEVFMDAVRSMLEAHG----FDMKR 248
Cdd:PRK00054  155 --------VYVT----TDDGSyGFKGFV---------TDVLDEldseydAIYSCGPEIMMKKVVEILKEKKvpayVSLER 213


                  .
gi 1950962799 249 Y 249
Cdd:PRK00054  214 R 214
COG3894 COG3894
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain ...
 277-359 1.39e-18

Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain [Function unknown];


Pssm-ID: 443101 [Multi-domain]  Cd Length: 621  Bit Score: 87.17  E-value: 1.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 277 TIRFTMAGKDVVCAAGQTVLQAARGAGVRIGAAC-ESGLCGTCRVMKLSGE---VEMSHNGGILDDEIEEGYILACCSRP 352
Cdd:COG3894     5 KVTFLPSGKRVEVEAGTTLLDAAREAGVDIDAPCgGRGTCGKCKVKVEEGEfspVTEEERRLLSPEELAEGYRLACQARV 84


                  ....*..
gi 1950962799 353 KTDVQVE 359
Cdd:COG3894    85 LGDLVVE 91
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 27-254 2.33e-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: 82.60  E-value: 2.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  27 SVTPEAPDVMTFTFRSDKdnWFRYLPGQFVTLELPtapESVMRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFENLKPG 106
Cdd:cd06189     5 SIEPLNDDVYRVRLKPPA--PLDFLAGQYLDLLLD---DGDKRPFSIASAPHEDGEIELHIRAVPGGSFSDYVFEELKEN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 107 --MRIKafGPLGDFtHIRH-PGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMPN 183
Cdd:cd06189    80 glVRIE--GPLGDF-FLREdSDRPLILIAGGTGFAPIKSILEHLLAQGSKRPIHLYWGARTEEDLYLDELLEAWAEAHPN 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1950962799 184 LNLGLIVEGcgRTDLWSGLKGRIDKAkigLLA--PDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESF 254
Cdd:cd06189   157 FTYVPVLSE--PEEGWQGRTGLVHEA---VLEdfPDLSDFDVYACGSPEMVYAARDDFVEKGLPEENFFSDAF 224
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 48-255 3.08e-17

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: 79.69  E-value: 3.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  48 FRYLPGQFVTLELPTAPESvmRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFENLKPGMRIKAFGPLGDFTHIRHPGEK 127
Cdd:cd06210    33 AEFVPGQFVEIEIPGTDTR--RSYSLANTPNWDGRLEFLIRLLPGGAFSTYLETRAKVGQRLNLRGPLGAFGLRENGLRP 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 128 YLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMPNLNLGLIVEGCGRTdlWSGLKG--- 204
Cdd:cd06210   111 RWFVAGGTGLAPLLSMLRRMAEWGEPQEARLFFGVNTEAELFYLDELKRLADSLPNLTVRICVWRPGGE--WEGYRGtvv 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1950962799 205 ---RIDKAKIGlLAPDfmdrtIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESFQ 255
Cdd:cd06210   189 dalREDLASSD-AKPD-----IYLCGPPGMVDAAFAAAREAGVPDEQVYLEKFL 236
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 32-254 3.83e-17

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate while mono-oxygenases add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99809  Cd Length: 227  Bit Score: 79.28  E-value: 3.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  32 APDVMTFTFRSDKDnwFRYLPGQFVTLELPTAPESvmRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFENLKPGMRIKA 111
Cdd:cd06213    12 THDIVRLTVQLDRP--IAYKAGQYAELTLPGLPAA--RSYSFANAPQGDGQLSFHIRKVPGGAFSGWLFGADRTGERLTV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 112 FGPLGDFtHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLA-RFMPNLNLGLIV 190
Cdd:cd06213    88 RGPFGDF-WLRPGDAPILCIAGGSGLAPILAILEQARAAGTKRDVTLLFGARTQRDLYALDEIAAIAaRWRGRFRFIPVL 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1950962799 191 EGCGRTDLWSGLKGRIDKAkiglLAPDFMDRT-IFCCGPEVFMDAVRSMLEAHGFDMKRYHQESF 254
Cdd:cd06213   167 SEEPADSSWKGARGLVTEH----IAEVLLAATeAYLCGPPAMIDAAIAVLRALGIAREHIHADRF 227
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 284-360 5.77e-17

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 81.45  E-value: 5.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 284 GKDVVCAAGQTVLQAARGAGVRIGAACE-SGLCGTCRVMKLSGEVEM--SHNGGILDDEIEEGYILACCSRPKTDVQVEA 360
Cdd:COG2871    43 GKEIEVEEGQTLLDALLRQGIFLPSACGgGGTCGQCKVKVLEGGGDIlpTETFHLSDRERKEGYRLACQVKVKSDMEIEV 122
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 278-360 8.11e-15

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 74.52  E-value: 8.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 278 IRFTMAGKDVVCAAGQTVLQAARGAGVRIGAACESGLCGTCRVMKLSGEVEMS-HNGGIL-DDEIEEGYILACCSRPKTD 355
Cdd:PRK07609    5 VTLQPSGRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQGpHQASALsGEERAAGEALTCCAKPLSD 84


                  ....*
gi 1950962799 356 VQVEA 360
Cdd:PRK07609   85 LVLEA 89
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 32-254 2.35e-13

FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (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 have a variety of physiological functions in a variety of organisms including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which varies 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: 99794  Cd Length: 220  Bit Score: 68.57  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  32 APDVMTFTFR-SDKDNWFRYLPGQFVTL----EL--------PTAPESV----MRTYTLSSTPSRPFS---VAVTVKaqR 91
Cdd:cd06197     7 TPTLTRFTFElSPPDVVGKWTPGQYITLdfssELdsgyshmaDDDPQSLnddfVRTFTVSSAPPHDPAtdeFEITVR--K 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  92 DSIGTRWMFENLK----PGMRIKAFGPLGDFThIRHPGE----KYLFVSAGSGVTPMMAMTRYMADTAPLS-DITFVNCS 162
Cdd:cd06197    85 KGPVTGFLFQVARrlreQGLEVPVLGVGGEFT-LSLPGEgaerKMVWIAGGVGITPFLAMLRAILSSRNTTwDITLLWSL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 163 RSPADIIFRSEleylarfmpnlnLGLIVEGCGRTDLwsglkgridkakigllapdFMDRTIFCCGPEVFMDAVRSMLEAh 242
Cdd:cd06197   164 REDDLPLVMDT------------LVRFPGLPVSTTL-------------------FITSEVYLCGPPALEKAVLEWLEG- 211

                         250
                  ....*....|..
gi 1950962799 243 gfdmKRYHQESF 254
Cdd:cd06197   212 ----KKVHRESF 219
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
284-353 7.98e-13

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 63.31  E-value: 7.98e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950962799 284 GKDVVCAAGQT-VLQAARGAGVRIGAACESGLCGTCRVMKLSGEvEMSHNGGILDDEIEEGY-ILACCSRPK 353
Cdd:pfam00111   7 GVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGE-DQSDQSFLEDDELAAGYvVLACQTYPK 77
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 130-236 1.29e-12

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: 63.43  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 130 FVSAGSGVTPMMAMTRYMA-DTAPLSDITFVNCSRSPADIIFRSELEYLARFMPN-LNLGLIVEGCGRTdlWSGLKGRID 207
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILeDPKDPTQVVLVFGNRNEDDILYREELDELAEKHPGrLTVVYVVSRPEAG--WTGGKGRVQ 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1950962799 208 KAKIGLLAPDFMDRT-IFCCGPEVFMDAVR 236
Cdd:pfam00175  79 DALLEDHLSLPDEEThVYVCGPPGMIKAVR 108
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 21-244 1.74e-12

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 67.14  E-value: 1.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  21 HLLECLSVTPEAPDVMTFTFR---SDKDNWFRYLPGQFVTLELPTAPESvmrTYTLSSTPSRPFSVAVTV-KAQRdsiGT 96
Cdd:PRK08345    6 HDAKILEVYDLTEREKLFLLRfedPELAESFTFKPGQFVQVTIPGVGEV---PISICSSPTRKGFFELCIrRAGR---VT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  97 RWMFEnLKPGMRIKAFGPLGD-FTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAP-LSDITFVNCSRSPADIIFRSEL 174
Cdd:PRK08345   80 TVIHR-LKEGDIVGVRGPYGNgFPVDEMEGMDLLLIAGGLGMAPLRSVLLYAMDNRWkYGNITLIYGAKYYEDLLFYDEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 175 EYLARFMPNLNlglIVEGCGRTDLWSGLKGR----IDKAKIGLLAPDFMDRT-------IFCCGPEVFMDAVRSMLEAHG 243
Cdd:PRK08345  159 IKDLAEAENVK---IIQSVTRDPEWPGCHGLpqgfIERVCKGVVTDLFREANtdpkntyAAICGPPVMYKFVFKELINRG 235


                  .
gi 1950962799 244 F 244
Cdd:PRK08345  236 Y 236
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 31-254 2.65e-12

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: 65.40  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  31 EAPDVMTFTFRsdKDNWFRYLPGQFVTLELPTapesvmrtyTLSSTPSRPFSVAVTVKAQRDSI---------GTRWMFE 101
Cdd:cd06186     8 PDSDVIRLTIP--KPKPFKWKPGQHVYLNFPS---------LLSFWQSHPFTIASSPEDEQDTLsliirakkgFTTRLLR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 102 NL----KPGMRIKAF--GPLGDFTHIRHPGEKYLFVSAGSGVTPMMA----MTRYMADTAPLSDITFVNCSRSPADII-F 170
Cdd:cd06186    77 KAlkspGGGVSLKVLveGPYGSSSEDLLSYDNVLLVAGGSGITFVLPilrdLLRRSSKTSRTRRVKLVWVVRDREDLEwF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 171 RSELEYLARFMPNLNLGLIVEGcgrtdlwsglkgridkakigllapdfmdrtIFCCGPEVFMDAVRSMLEAHGFDMKRYH 250
Cdd:cd06186   157 LDELRAAQELEVDGEIEIYVTR------------------------------VVVCGPPGLVDDVRNAVAKKGGTGVEFH 206


                  ....
gi 1950962799 251 QESF 254
Cdd:cd06186   207 EESF 210
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 32-257 5.64e-11

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 62.97  E-value: 5.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  32 APDVMTFTFRSDKDNWFRYLPGQFVTLELPTApesVMRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFENLKPG--MRI 109
Cdd:PRK07609  114 AGDVMRLKLRLPATERLQYLAGQYIEFILKDG---KRRSYSIANAPHSGGPLELHIRHMPGGVFTDHVFGALKERdiLRI 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 110 KafGPLGDFtHIRHPGEKYL-FVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMPNLNLGL 188
Cdd:PRK07609  191 E--GPLGTF-FLREDSDKPIvLLASGTGFAPIKSIVEHLRAKGIQRPVTLYWGARRPEDLYLSALAEQWAEELPNFRYVP 267

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950962799 189 IVEGCGRTDLWSGLKGRIDKAkigLLA--PDFMDRTIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESFQPA 257
Cdd:PRK07609  268 VVSDALDDDAWTGRTGFVHQA---VLEdfPDLSGHQVYACGSPVMVYAARDDFVAAGLPAEEFFADAFTYA 335
petF CHL00134
ferredoxin; Validated
 284-358 1.64e-10

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 57.42  E-value: 1.64e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950962799 284 GKDVV--CAAGQTVLQAARGAGVRIGAACESGLCGTCRVMKLSGEVEMSHNGGILDDEIEEGYILACCSRPKTDVQV 358
Cdd:CHL00134   14 GIDVTidCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTCVAYPTSDCTI 90
PTZ00038 PTZ00038
ferredoxin; Provisional
 285-359 2.37e-10

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 59.08  E-value: 2.37e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1950962799 285 KDVVCAAGQTVLQAARGAGVRIGAACESGLCGTCRVMKLSGEVEMSHNGGILDDEIEEGYILACCSRPKTDVQVE 359
Cdd:PTZ00038  107 KVIECDEDEYILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKGYCLLCTCYPKSDCTIE 181
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 26-243 1.23e-09

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: 58.11  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  26 LSVTPEAPDVMTFTFRSdKDNWFRYLPGQFVTLELPTAPESVMRTYTLSSTPSRPFSVAVTVKaQRDsIGTRWMFEnLKP 105
Cdd:cd06192     2 VKKEQLEPNLVLLTIKA-PLAARLFRPGQFVFLRNFESPGLERIPLSLAGVDPEEGTISLLVE-IRG-PKTKLIAE-LKP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 106 GMRIKAFGPLGDFTHIRHPGEKYLFVSAGSGVTPMMAMTRYMADTAplSDITFVNCSRSPADIIFRSELEylarfmpnln 185
Cdd:cd06192    78 GEKLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAKKLAANG--NKVTVLAGAKKAKEEFLDEYFE---------- 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950962799 186 LGLIVEgcgrtdLWSGLKGRID-KAKIGLLAPDFMDRT---IFCCGPEVFMDAVRSMLEAHG 243
Cdd:cd06192   146 LPADVE------IWTTDDGELGlEGKVTDSDKPIPLEDvdrIIVAGSDIMMKAVVEALDEWL 201
PLN03136 PLN03136
Ferredoxin; Provisional
 286-359 2.10e-09

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 55.53  E-value: 2.10e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1950962799 286 DVVCAAGQTVLQAARGAGVRIGAACESGLCGTCRVMKLSGEVEMSHNGGILDDEIEEGYILACCSRPKTDVQVE 359
Cdd:PLN03136   67 EVECEEDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDEQISEGYVLTCVAYPTSDVVIE 140
PLN02252 PLN02252
nitrate reductase [NADPH]
 100-245 2.27e-09

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 58.92  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 100 FENLKPGMRIKAFGPLGdftHIRHPG-------------EKYLFVSAGSGVTPMMAMTR-YMADTAPLSDITFVNCSRSP 165
Cdd:PLN02252  723 LDSLPIGDTIDVKGPLG---HIEYAGrgsflvngkpkfaKKLAMLAGGTGITPMYQVIQaILRDPEDKTEMSLVYANRTE 799

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 166 ADIIFRSELEYLARFMP-NLNLGLIVEGCGRTDlWSGLKGRIDKAKIGLLAPDFMDRTI-FCCGPEVFM-DAVRSMLEAH 242
Cdd:PLN02252  800 DDILLREELDRWAAEHPdRLKVWYVVSQVKREG-WKYSVGRVTEAMLREHLPEGGDETLaLMCGPPPMIeFACQPNLEKM 878


                  ...
gi 1950962799 243 GFD 245
Cdd:PLN02252  879 GYD 881
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
276-359 9.32e-08

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 48.96  E-value: 9.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 276 TTIRFTMAGKDVVC-AAGQTVLQAARGAGVRIGAACESGLCGTCRVMKLSGEVEMSHNGGILddeIEEGYILACCSRPKT 354
Cdd:PRK10713    2 ARVTLRITGTQLLCqDEHPSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAEPLAF---IQPGEILPCCCRAKG 78


                  ....*
gi 1950962799 355 DVQVE 359
Cdd:PRK10713   79 DIEIE 83
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
27-120 3.82e-07

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 47.58  E-value: 3.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  27 SVTPEAPDVMTFTFRSD-KDNWFRYLPGQFVTLELPTAPESVMRTYTLSSTPSRPFSVAVTVKAQRDSIGTRwMFENLKP 105
Cdd:pfam00970   6 EKELVSHDTRIFRFALPhPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVYPGGKMSQ-YLDELKI 84

                          90
                  ....*....|....*
gi 1950962799 106 GMRIKAFGPLGDFTH 120
Cdd:pfam00970  85 GDTIDFKGPLGRFEY 99
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
50-259 1.04e-05

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 46.66  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  50 YLPGQFVTLELPTAPESvmRTYTLSSTPSRPFSVAVTVKAQRDSIGTRWMFENLKPGMRIKAFGPLGDFtHIRHPGEKYL 129
Cdd:PRK11872  137 FLPGQYARLQIPGTDDW--RSYSFANRPNATNQLQFLIRLLPDGVMSNYLRERCQVGDEILFEAPLGAF-YLREVERPLV 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 130 FVSAGSGVTPMMAMTRYMADTAPLSDITFVNCSRSPADIIFRSELEYLARFMPNLNLGLIVEGCgrTDLWSGLKGRI--- 206
Cdd:PRK11872  214 FVAGGTGLSAFLGMLDELAEQGCSPPVHLYYGVRHAADLCELQRLAAYAERLPNFRYHPVVSKA--SADWQGKRGYIheh 291

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1950962799 207 -DKAKIGLLAPDfmdrtIFCCGPEVFMDAVRSMLEAHGFDMKRYHQESFQPANA 259
Cdd:PRK11872  292 fDKAQLRDQAFD-----MYLCGPPPMVEAVKQWLDEQALENYRLYYEKFTQSNT 340
PRK06214 PRK06214
sulfite reductase subunit alpha;
69-175 2.26e-04

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 43.14  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  69 RTYTLSSTP-SRPFSVAVTVKAQRDSIGTR--------WMFENLKPGMRIKAF-GPLGDFTHIRHPGEKYLFVSAGSGVT 138
Cdd:PRK06214  317 RLYSISSSPkATPGRVSLTVDAVRYEIGSRlrlgvastFLGERLAPGTRVRVYvQKAHGFALPADPNTPIIMVGPGTGIA 396

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1950962799 139 PMMAMTRY-MADTAPLSDITFVNCSRSPADIIFRSELE 175
Cdd:PRK06214  397 PFRAFLHErAATKAPGRNWLFFGHQRSATDFFYEDELN 434
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 103-250 2.67e-04

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 42.84  E-value: 2.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  103 LKPG--MRIKAFGPL--------GDFTHIRHPGEKYLFVSAGSGVTPMM-----AMTRYMADTapLSDITFVNCSRSPAD 167
Cdd:PTZ00306   999 LRPGdsVEMKACGGLrierrpadKQFVFRGHVIRKLALIAGGTGVAPMLqiiraALKKPYVDS--IESIRLIYAAEDVSE 1076

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  168 IIFRSELEYLAR-----FMPNLNLGLIVEGcgrtdlWSGLKGRIDKAKI-GLLAPDFMDRTIFCCGPEVFMDAVRSMLEA 241
Cdd:PTZ00306  1077 LTYRELLESYRKenpgkFKCHFVLNNPPEG------WTDGVGFVDRALLqSALQPPSKDLLVAICGPPVMQRAVKADLLA 1150


                   ....*....
gi 1950962799  242 HGFDMKRYH 250
Cdd:PTZ00306  1151 LGYNMELVR 1159
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 61-244 9.93e-04

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 40.59  E-value: 9.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  61 PTAPESVMRTYT-LSSTPSR---PFSVAVTVKAQRDSI--GTRW--MFENLKPGMRIKAFGPLGDFTHIR------HPGE 126
Cdd:PTZ00319   79 PGKPETVQHSYTpISSDDEKgyvDFLIKVYFKGVHPSFpnGGRLsqHLYHMKLGDKIEMRGPVGKFEYLGngtytvHKGK 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 127 K---------YLFVSAGSGVTPMMAMTR-YMADTAPLSDITFVNCSRSPADIIFRSELEYLARfMPNLNLGLIVEGCGRT 196
Cdd:PTZ00319  159 GglktmhvdaFAMIAGGTGITPMLQIIHaIKKNKEDRTKVFLVYANQTEDDILLRKELDEAAK-DPRFHVWYTLDREATP 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1950962799 197 DlWSGLKGRIDKAKIGLLAP-------DFMDRTIFCCGPEVFM-DAVRSMLEAHGF 244
Cdd:PTZ00319  238 E-WKYGTGYVDEEMLRAHLPvpdpqnsGIKKVMALMCGPPPMLqMAVKPNLEKIGY 292
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
 131-235 1.20e-03

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 40.29  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 131 VSAGSGVTPMMAMTRY---------MADTAPLSditFVNCSRSPADIIFRSELEYLARFMPN-LNLGLIVEGCGRTDLWS 200
Cdd:PTZ00274  165 IAGGTGFTPMLQIIRHsltepwdsgEVDRTKLS---FLFCNRTERHILLKGLFDDLARRYSNrFKVYYTIDQAVEPDKWN 241

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1950962799 201 GLKGRIDKAKI--GLLAPDFMDRTIFCCGPEVFMDAV 235
Cdd:PTZ00274  242 HFLGYVTKEMVrrTMPAPEEKKKIIMLCGPDQLLNHV 278
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 276-320 1.21e-03

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 40.87  E-value: 1.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1950962799 276 TTIRFTMAGKDVVCAAGQTVLQAARGAGVRIGAAC------ESGLCGTCRV 320
Cdd:PRK12814    2 NTISLTINGRSVTAAPGTSILEAAASAGITIPTLCfhqeleATGSCWMCIV 52
PRK06222 PRK06222
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
52-175 1.66e-03

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


Pssm-ID: 235747 [Multi-domain]  Cd Length: 281  Bit Score: 39.79  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799  52 PGQFVTLELPTAPESVmrtytlsstpsrPFSVA--------VTVKAQRDSIGTRwMFENLKPGMRIKAF-GPLGDFTHIR 122
Cdd:PRK06222   30 PGQFVIVRIDEKGERI------------PLTIAdydrekgtITIVFQAVGKSTR-KLAELKEGDSILDVvGPLGKPSEIE 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1950962799 123 HPGeKYLFVSAGSGVTPMMAMTRYMADTAplSDITFVNCSRSPADIIFRSELE 175
Cdd:PRK06222   97 KFG-TVVCVGGGVGIAPVYPIAKALKEAG--NKVITIIGARNKDLLILEDEMK 146
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
290-359 1.72e-03

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 39.71  E-value: 1.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 290 AAGQTVLQAARGAGVRIGAACESGLCGTCRVMKLSGEVEMSHNGGILDDEIEEGYILACCSRPKTDVQVE 359
Cdd:PRK05713   14 PAGSNLLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEDALPEALAAEKREQGWRLACQCRVVGDLRVE 83
Fer2_4 pfam13510
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 275-320 4.99e-03

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.


Pssm-ID: 433268 [Multi-domain]  Cd Length: 82  Bit Score: 35.59  E-value: 4.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1950962799 275 ATTIRFTMAGKDVVCAAGQTVLQAARGAGVRI----------GAACESGLCGTCRV 320
Cdd:pfam13510   1 SRPVTFTFDGRPVTAPEGDTIAAALLANGVRVprsckygrprGIFCAMGECRNCLV 56
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 102-183 7.43e-03

These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but lack the FAD-binding region connecting sub-domain. Ferredoxin-NADP+ reductase (FNR) 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. CYPOR serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases, sulfite reducatase, and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal FNR-like FAD and NAD binding module, an FMN-binding domain, and an additional connecting domain (inserted within the FAD binding region) that orients the FNR and FMN -binding domains. 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: 99804 [Multi-domain]  Cd Length: 286  Bit Score: 37.69  E-value: 7.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950962799 102 NLKPGMRIKAFGPLGDFTHI-RHPGEKYLFVSAGSGVTPMMAMTRYM-----ADTAPLSDITFVNCSRSPADIIFRSELE 175
Cdd:cd06208   111 DLKPGDDVQITGPVGKTMLLpEDPNATLIMIATGTGIAPFRSFLRRLfrekhADYKFTGLAWLFFGVPNSDSLLYDDELE 190


                  ....*...
gi 1950962799 176 YLARFMPN 183
Cdd:cd06208   191 KYPKQYPD 198
 
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.
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