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Conserved domains on  [gi|1210675834|ref|NP_001339911|]
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oxidoreductase NAD-binding domain-containing protein 1 isoform 3 [Homo sapiens]

Protein Classification

FAD-dependent oxidoreductase( domain architecture ID 10085328)

FAD-dependent oxidoreductase, similar to ferredoxin- and rubredoxin-NAD(+) reductases including human oxidoreductase NAD-binding domain-containing protein 1, may act on an iron-sulfur protein as electron donor with NAD(+) or NADP(+) as acceptor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 48-282 1.18e-57

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: 184.19  E-value: 1.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  48 SPSVKSLRLlVADQDFSFKAGQWVDFFIP--GVSVVGGFSICSSPrllEQERVIELAVK-YTNHPPALWVHNTCtLDCEV 124
Cdd:cd00322     7 TDDVRLFRL-QLPNGFSFKPGQYVDLHLPgdGRGLRRAYSIASSP---DEEGELELTVKiVPGGPFSAWLHDLK-PGDEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 125 AVRVGGEFFFdpQPADASRNLVLIAGGVGINPLLSILRHAADLLreqankrngyEIGTIKLFYSAKNTSELLFKKNILDL 204
Cdd:cd00322    82 EVSGPGGDFF--LPLEESGPVVLIAGGIGITPFRSMLRHLAADK----------PGGEITLLYGARTPADLLFLDELEEL 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1210675834 205 VNEFPekiaCSLHVTKQTTQINAELKPYITEGRITEKEIRDHISKETLFYICGPPPMTDFFSKQLENNHVPKEHICFE 282
Cdd:cd00322   150 AKEGP----NFRLVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
 
Name Accession Description Interval E-value
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 48-282 1.18e-57

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: 184.19  E-value: 1.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  48 SPSVKSLRLlVADQDFSFKAGQWVDFFIP--GVSVVGGFSICSSPrllEQERVIELAVK-YTNHPPALWVHNTCtLDCEV 124
Cdd:cd00322     7 TDDVRLFRL-QLPNGFSFKPGQYVDLHLPgdGRGLRRAYSIASSP---DEEGELELTVKiVPGGPFSAWLHDLK-PGDEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 125 AVRVGGEFFFdpQPADASRNLVLIAGGVGINPLLSILRHAADLLreqankrngyEIGTIKLFYSAKNTSELLFKKNILDL 204
Cdd:cd00322    82 EVSGPGGDFF--LPLEESGPVVLIAGGIGITPFRSMLRHLAADK----------PGGEITLLYGARTPADLLFLDELEEL 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1210675834 205 VNEFPekiaCSLHVTKQTTQINAELKPYITEGRITEKEIRDHISKETLFYICGPPPMTDFFSKQLENNHVPKEHICFE 282
Cdd:cd00322   150 AKEGP----NFRLVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
39-283 6.10e-40

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 138.77  E-value: 6.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  39 AKVCGAASESPSVKSLRLLVAD--QDFSFKAGQWVDFFIP--GVSVVGGFSICSSPRlleqERVIELAVKYTNHPPA-LW 113
Cdd:COG1018     6 LRVVEVRRETPDVVSFTLEPPDgaPLPRFRPGQFVTLRLPidGKPLRRAYSLSSAPG----DGRLEITVKRVPGGGGsNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 114 VHNTctldcevaVRVG---------GEFFFDPQPAdasRNLVLIAGGVGINPLLSILRHaadLLREQANKRngyeigtIK 184
Cdd:COG1018    82 LHDH--------LKVGdtlevsgprGDFVLDPEPA---RPLLLIAGGIGITPFLSMLRT---LLARGPFRP-------VT 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 185 LFYSAKNTSELLFKKNILDLVNEFPekiacSLHVTKQTTQINAELkpyitEGRITEKEIRDHIS--KETLFYICGPPPMT 262
Cdd:COG1018   141 LVYGARSPADLAFRDELEALAARHP-----RLRLHPVLSREPAGL-----QGRLDAELLAALLPdpADAHVYLCGPPPMM 210

                         250       260
                  ....*....|....*....|.
gi 1210675834 263 DFFSKQLENNHVPKEHICFEK 283
Cdd:COG1018   211 EAVRAALAELGVPEERIHFER 231
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 61-279 4.22e-19

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 84.86  E-value: 4.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  61 QDFSFKAGQWVDFFIPGVSVVGgFSICSSPRlleQERVIELAVKYTNHPPALwVHNTCTLDCeVAVR--VGGEFffdpqP 138
Cdd:PRK08345   34 ESFTFKPGQFVQVTIPGVGEVP-ISICSSPT---RKGFFELCIRRAGRVTTV-IHRLKEGDI-VGVRgpYGNGF-----P 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 139 ADA--SRNLVLIAGGVGINPLLSILRHAADllreqankrNGYEIGTIKLFYSAKNTSELLFKKNILDLVNEfPEKIACSL 216
Cdd:PRK08345  103 VDEmeGMDLLLIAGGLGMAPLRSVLLYAMD---------NRWKYGNITLIYGAKYYEDLLFYDELIKDLAE-AENVKIIQ 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1210675834 217 HVTKQT---TQINAELK--PYITEGRITEKEIRDHIS-KETLFYICGPPPMTDFFSKQLENNHVPKEHI 279
Cdd:PRK08345  173 SVTRDPewpGCHGLPQGfiERVCKGVVTDLFREANTDpKNTYAAICGPPVMYKFVFKELINRGYRPERI 241
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 147-267 8.39e-16

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: 71.52  E-value: 8.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 147 LIAGGVGINPLLSILRHaadLLREQANKRNgyeigtIKLFYSAKNTSELLFKKNILDLVNEFPEKiacsLHVTKQTTQIN 226
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRA---ILEDPKDPTQ------VVLVFGNRNEDDILYREELDELAEKHPGR----LTVVYVVSRPE 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1210675834 227 AElkPYITEGRITEKEIRDHISK---ETLFYICGPPPMTDFFSK 267
Cdd:pfam00175  68 AG--WTGGKGRVQDALLEDHLSLpdeETHVYVCGPPGMIKAVRK 109
BenC NF040810
benzoate 1,2-dioxygenase electron transfer component BenC;
48-283 6.09e-07

benzoate 1,2-dioxygenase electron transfer component BenC;


Pssm-ID: 468751 [Multi-domain]  Cd Length: 333  Bit Score: 49.82  E-value: 6.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  48 SPSVKSLRL-LVADQDFSFKAGQWVDFFIPGVSVVGGFSICSSPrlleQERVIELAVKytNHPPAL---WVHNTCtldce 123
Cdd:NF040810  116 SDSTIELSLdLDDDAALAFLPGQYVNIQVPGTGQTRSYSFSSLP----GAREASFLIR--NVPGGLmssYLTERA----- 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 124 vavRVG---------GEFFFdpqpADASRNLVLIAGGVGINPLLSILRHaadlLREQANKRngyeigTIKLFYSAKNTse 194
Cdd:NF040810  185 ---KPGdrlsltgplGSFYL----REVTRPLLMLAGGTGLAPFLSMLEV----LAEQGSEQ------PVHLIYGVTRD-- 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 195 llfkkniLDLV-----NEFPEKIAcslHVTKQTTQINAE----LKPYITegritekeirDHISKETL------FYICGPP 259
Cdd:NF040810  246 -------ADLVeverlEAFAARLP---NFTFRTCVADAAsahpRKGYVT----------QHIEAEWLndgdvdVYLCGPP 305

                         250       260
                  ....*....|....*....|....
gi 1210675834 260 PMTDFFSKQLENNHVPKEHICFEK 283
Cdd:NF040810  306 PMVDAVRGWFREQGITPASFHYEK 329
 
Name Accession Description Interval E-value
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 48-282 1.18e-57

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: 184.19  E-value: 1.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  48 SPSVKSLRLlVADQDFSFKAGQWVDFFIP--GVSVVGGFSICSSPrllEQERVIELAVK-YTNHPPALWVHNTCtLDCEV 124
Cdd:cd00322     7 TDDVRLFRL-QLPNGFSFKPGQYVDLHLPgdGRGLRRAYSIASSP---DEEGELELTVKiVPGGPFSAWLHDLK-PGDEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 125 AVRVGGEFFFdpQPADASRNLVLIAGGVGINPLLSILRHAADLLreqankrngyEIGTIKLFYSAKNTSELLFKKNILDL 204
Cdd:cd00322    82 EVSGPGGDFF--LPLEESGPVVLIAGGIGITPFRSMLRHLAADK----------PGGEITLLYGARTPADLLFLDELEEL 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1210675834 205 VNEFPekiaCSLHVTKQTTQINAELKPYITEGRITEKEIRDHISKETLFYICGPPPMTDFFSKQLENNHVPKEHICFE 282
Cdd:cd00322   150 AKEGP----NFRLVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
39-283 6.10e-40

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 138.77  E-value: 6.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  39 AKVCGAASESPSVKSLRLLVAD--QDFSFKAGQWVDFFIP--GVSVVGGFSICSSPRlleqERVIELAVKYTNHPPA-LW 113
Cdd:COG1018     6 LRVVEVRRETPDVVSFTLEPPDgaPLPRFRPGQFVTLRLPidGKPLRRAYSLSSAPG----DGRLEITVKRVPGGGGsNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 114 VHNTctldcevaVRVG---------GEFFFDPQPAdasRNLVLIAGGVGINPLLSILRHaadLLREQANKRngyeigtIK 184
Cdd:COG1018    82 LHDH--------LKVGdtlevsgprGDFVLDPEPA---RPLLLIAGGIGITPFLSMLRT---LLARGPFRP-------VT 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 185 LFYSAKNTSELLFKKNILDLVNEFPekiacSLHVTKQTTQINAELkpyitEGRITEKEIRDHIS--KETLFYICGPPPMT 262
Cdd:COG1018   141 LVYGARSPADLAFRDELEALAARHP-----RLRLHPVLSREPAGL-----QGRLDAELLAALLPdpADAHVYLCGPPPMM 210

                         250       260
                  ....*....|....*....|.
gi 1210675834 263 DFFSKQLENNHVPKEHICFEK 283
Cdd:COG1018   211 EAVRAALAELGVPEERIHFER 231
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 39-284 2.31e-31

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: 116.60  E-value: 2.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  39 AKVCGAASESPSVKSLRLLVADQD-FSFKAGQWVDFF---IPGVSVVGGFSICSSPrllEQERVIELAVKytnHPPALWV 114
Cdd:cd06217     4 LRVTEIIQETPTVKTFRLAVPDGVpPPFLAGQHVDLRltaIDGYTAQRSYSIASSP---TQRGRVELTVK---RVPGGEV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 115 HNTCTlDCevaVRVG---------GEFFFDPQPADasrNLVLIAGGVGINPLLSILRHaadlLREQANKRNgyeigtIKL 185
Cdd:cd06217    78 SPYLH-DE---VKVGdllevrgpiGTFTWNPLHGD---PVVLLAGGSGIVPLMSMIRY----RRDLGWPVP------FRL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 186 FYSAKNTSELLFKKNILDLVNEFPekiacSLHVTKQTTQInaelKPYIT---EGRIT----EKEIRDHISKEtlFYICGP 258
Cdd:cd06217   141 LYSARTAEDVIFRDELEQLARRHP-----NLHVTEALTRA----APADWlgpAGRITadliAELVPPLAGRR--VYVCGP 209

                         250       260
                  ....*....|....*....|....*.
gi 1210675834 259 PPMTDFFSKQLENNHVPKEHICFEKW 284
Cdd:cd06217   210 PAFVEAATRLLLELGVPRDRIRTEAF 235
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 61-282 9.94e-28

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: 107.24  E-value: 9.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  61 QDFSFKAGQWVDFFIP--GVSVVGGFSICSSPrlleQERVIELAVK------YTNhppalWVHNTctldcevaVRVG--- 129
Cdd:cd06214    29 DAFRYRPGQFLTLRVPidGEEVRRSYSICSSP----GDDELRITVKrvpggrFSN-----WANDE--------LKAGdtl 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 130 ------GEFFFDPQPADasRNLVLIAGGVGINPLLSILRHAadLLREQAnkrngyeiGTIKLFYSAKNTSELLFKKNILD 203
Cdd:cd06214    92 evmppaGRFTLPPLPGA--RHYVLFAAGSGITPVLSILKTA--LAREPA--------SRVTLVYGNRTEASVIFREELAD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 204 LVNEFPEKiaCSL-HVTKQTTQINAELKPYITEGRITEKEIRDHISKE-TLFYICGPPPMTDFFSKQLENNHVPKEHICF 281
Cdd:cd06214   160 LKARYPDR--LTViHVLSREQGDPDLLRGRLDAAKLNALLKNLLDATEfDEAFLCGPEPMMDAVEAALLELGVPAERIHR 237


                  .
gi 1210675834 282 E 282
Cdd:cd06214   238 E 238
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 47-282 1.95e-25

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: 101.09  E-value: 1.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  47 ESPSVKSLRLLVADQDF--SFKAGQW--VDFFIPGVS--VVGGFSICSSPRllEQERVIelAVKY------TNhppalWV 114
Cdd:cd06184    17 ESEDITSFYLEPADGGPlpPFLPGQYlsVRVKLPGLGyrQIRQYSLSDAPN--GDYYRI--SVKRepgglvSN-----YL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 115 HNTctldcevaVRVG---------GEFFFDPqpaDASRNLVLIAGGVGINPLLSILRHAAdllrEQANKRNgyeigtIKL 185
Cdd:cd06184    88 HDN--------VKVGdvlevsapaGDFVLDE---ASDRPLVLISAGVGITPMLSMLEALA----AEGPGRP------VTF 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 186 FYSAKNTSELLFKKNILDLVNEFPekiACSLHVTKQTTQINAELKPYITEGRITEKEIRDH-ISKETLFYICGPPPMTDF 264
Cdd:cd06184   147 IHAARNSAVHAFRDELEELAARLP---NLKLHVFYSEPEAGDREEDYDHAGRIDLALLRELlLPADADFYLCGPVPFMQA 223

                         250
                  ....*....|....*...
gi 1210675834 265 FSKQLENNHVPKEHICFE 282
Cdd:cd06184   224 VREGLKALGVPAERIHYE 241
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 47-279 1.61e-23

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 96.09  E-value: 1.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  47 ESPSVKSLRLLVADQDFSFKAGQWVDFFIPGVSVVGGFSICSSPRlleQERVIELAVK----YTNhppalWVHNTCTLDc 122
Cdd:COG0543     8 LAPDVYLLRLEAPLIALKFKPGQFVMLRVPGDGLRRPFSIASAPR---EDGTIELHIRvvgkGTR-----ALAELKPGD- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 123 EVAVRvG--GEFFfdpQPADASRNLVLIAGGVGINPLLSILRHAADLLREqankrngyeigtIKLFYSAKNTSELLFKKN 200
Cdd:COG0543    79 ELDVR-GplGNGF---PLEDSGRPVLLVAGGTGLAPLRSLAEALLARGRR------------VTLYLGARTPEDLYLLDE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 201 ILDLVNefpekiaCSLHVTkqttqinAELKPYITEGRITEKeIRDHI--SKETLFYICGPPPMTDFFSKQLENNHVPKEH 278
Cdd:COG0543   143 LEALAD-------FRVVVT-------TDDGWYGRKGFVTDA-LKELLaeDSGDDVYACGPPPMMKAVAELLLERGVPPER 207


                  .
gi 1210675834 279 I 279
Cdd:COG0543   208 I 208
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 38-283 1.76e-23

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: 95.48  E-value: 1.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  38 AAKVCGAASESPSVKSLRL-LVADQDFSFKAGQWVDFFIPGVSVVGGFSICSSPRlleQERVIELAVKytNHPPALWvhn 116
Cdd:cd06212     2 VGTVVAVEALTHDIRRLRLrLEEPEPIKFFAGQYVDITVPGTEETRSFSMANTPA---DPGRLEFIIK--KYPGGLF--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 117 TCTLDCEVA----VRVGGEF--FFDPQPADasRNLVLIAGGVGINPLLSILRHAAdllrEQANKRngyeigTIKLFYSAK 190
Cdd:cd06212    74 SSFLDDGLAvgdpVTVTGPYgtCTLRESRD--RPIVLIGGGSGMAPLLSLLRDMA----ASGSDR------PVRFFYGAR 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 191 NTSELLFKKNILDLVNEFP--EKIACSLHVTKQtTQINAElKPYITE--GRiTEKEIRDHISketlfYICGPPPMTDFFS 266
Cdd:cd06212   142 TARDLFYLEEIAALGEKIPdfTFIPALSESPDD-EGWSGE-TGLVTEvvQR-NEATLAGCDV-----YLCGPPPMIDAAL 213

                         250
                  ....*....|....*..
gi 1210675834 267 KQLENNHVPKEHICFEK 283
Cdd:cd06212   214 PVLEMSGVPPDQIFYDK 230
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
38-282 3.38e-23

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 98.04  E-value: 3.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  38 AAKVCGAASESPSVKSLRL-LVADQDFSFKAGQ--WVDFFIPGVSVvGG--FSICSSPrllEQERVIELAVK----YTNh 108
Cdd:COG4097   216 PYRVESVEPEAGDVVELTLrPEGGRWLGHRAGQfaFLRFDGSPFWE-EAhpFSISSAP---GGDGRLRFTIKalgdFTR- 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 109 ppalwvhntcTLDcevAVRVG---------GEFFFDPqpADASRNLVLIAGGVGINPLLSILRHAADLLREQAnkrngye 179
Cdd:COG4097   291 ----------RLG---RLKPGtrvyvegpyGRFTFDR--RDTAPRQVWIAGGIGITPFLALLRALAARPGDQR------- 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 180 igTIKLFYSAKNTSELLFKKNILDLVNEFPekiacslhvtkqttqiNAELKPYIT--EGRITEKEIRDHIS--KETLFYI 255
Cdd:COG4097   349 --PVDLFYCVRDEEDAPFLEELRALAARLA----------------GLRLHLVVSdeDGRLTAERLRRLVPdlAEADVFF 410

                         250       260
                  ....*....|....*....|....*..
gi 1210675834 256 CGPPPMTDFFSKQLENNHVPKEHICFE 282
Cdd:COG4097   411 CGPPGMMDALRRDLRALGVPARRIHQE 437
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 31-283 2.64e-22

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: 92.39  E-value: 2.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  31 PFTSIVSAAKvcgaaSESPSVKSLRL-LVADQDFSFKAGQWVDFFIPGVSVVGGFSICSSPRlleQERVIELAVKYTnhP 109
Cdd:cd06211     6 DFEGTVVEIE-----DLTPTIKGVRLkLDEPEEIEFQAGQYVNLQAPGYEGTRAFSIASSPS---DAGEIELHIRLV--P 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 110 PALwvhntCTLDCEVAVRVG---------GEFFFDPQpadASRNLVLIAGGVGINPLLSILRHaadlLREQANKRNgyei 180
Cdd:cd06211    76 GGI-----ATTYVHKQLKEGdeleisgpyGDFFVRDS---DQRPIIFIAGGSGLSSPRSMILD----LLERGDTRK---- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 181 gtIKLFYSAKNTSELLFKKNILDLVNEFPE-KIACSLHVTKQTTQINAElKPYITE--GRITEKEIRDHISketlfYICG 257
Cdd:cd06211   140 --ITLFFGARTRAELYYLDEFEALEKDHPNfKYVPALSREPPESNWKGF-TGFVHDaaKKHFKNDFRGHKA-----YLCG 211

                         250       260
                  ....*....|....*....|....*.
gi 1210675834 258 PPPMTDFFSKQLENNHVPKEHICFEK 283
Cdd:cd06211   212 PPPMIDACIKTLMQGRLFERDIYYEK 237
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 48-283 6.37e-20

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: 88.38  E-value: 6.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  48 SPSVKSLRL-LVADQDFSFKAGQWVDFFIPGV-----------------------SVVGGFSICSSPrllEQERVIELAV 103
Cdd:COG2871   143 TTFIKELVLeLPEGEEIDFKAGQYIQIEVPPYevdfkdfdipeeekfglfdkndeEVTRAYSMANYP---AEKGIIELNI 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 104 KY----TNHPPAL---WVHNtctldcevaVRVG---------GEFFFDpqpaDASRNLVLIAGGVGINPLLSILRhaaDL 167
Cdd:COG2871   220 RIatppMDVPPGIgssYIFS---------LKPGdkvtisgpyGEFFLR----DSDREMVFIGGGAGMAPLRSHIF---DL 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 168 LREQANKRNgyeigtIKLFYSAKNTSELLFKKNILDLVNEFPekiacslhvtkqttqiNAELKPYITE-----------G 236
Cdd:COG2871   284 LERGKTDRK------ITFWYGARSLRELFYLEEFRELEKEHP----------------NFKFHPALSEplpednwdgetG 341

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1210675834 237 RIT----EKEIRDHISKE-TLFYICGPPPMTDFFSKQLENNHVPKEHICFEK 283
Cdd:COG2871   342 FIHevlyENYLKDHPAPEdCEAYLCGPPPMIDAVIKMLDDLGVEEENIYFDD 393
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 47-282 1.26e-19

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: 84.62  E-value: 1.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  47 ESPSVKSLRLLVADQDFSFKAGQ--WVDFFIPGVSVVGGFSICSSPRlleQERVIELAVK----YTNhppalwvhntcTL 120
Cdd:cd06198     5 EVRPTTTLTLEPRGPALGHRAGQfaFLRFDASGWEEPHPFTISSAPD---PDGRLRFTIKalgdYTR-----------RL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 121 DCEVAV--RV---G--GEFFFDpqpaDASRNLVLIAGGVGINPLLSILRHAADllreqankrnGYEIGTIKLFYSAKNTS 193
Cdd:cd06198    71 AERLKPgtRVtveGpyGRFTFD----DRRARQIWIAGGIGITPFLALLEALAA----------RGDARPVTLFYCVRDPE 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 194 ELLFkkniLDLVNEFPEKIACSLHVtkqttqINAELKPYITEGRITEKEIRDHisKETLFYICGPPPMTDFFSKQLENNH 273
Cdd:cd06198   137 DAVF----LDELRALAAAAGVVLHV------IDSPSDGRLTLEQLVRALVPDL--ADADVWFCGPPGMADALEKGLRALG 204


                  ....*....
gi 1210675834 274 VPKEHICFE 282
Cdd:cd06198   205 VPARRFHYE 213
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 46-279 3.79e-19

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: 84.20  E-value: 3.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  46 SESPSVKSLRLLVADQD---FSFKAGQWVDFFIPGVsvvgG---FSICSSPrllEQERVIELAVK----YTNhppALwvH 115
Cdd:cd06221     6 DETEDIKTFTLRLEDDDeelFTFKPGQFVMLSLPGV----GeapISISSDP---TRRGPLELTIRrvgrVTE---AL--H 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 116 NTCTLDCeVAVRvgGEF---FfdPQPADASRNLVLIAGGVGINPLLSILRHAADllreqankrNGYEIGTIKLFYSAKNT 192
Cdd:cd06221    74 ELKPGDT-VGLR--GPFgngF--PVEEMKGKDLLLVAGGLGLAPLRSLINYILD---------NREDYGKVTLLYGARTP 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 193 SELLFKKNIldlvnefpEKIACSLHVTKQTTQINAELKPYITEGRITEkEIRDHI--SKETLFYICGPPPMTDFFSKQLE 270
Cdd:cd06221   140 EDLLFKEEL--------KEWAKRSDVEVILTVDRAEEGWTGNVGLVTD-LLPELTldPDNTVAIVCGPPIMMRFVAKELL 210


                  ....*....
gi 1210675834 271 NNHVPKEHI 279
Cdd:cd06221   211 KLGVPEEQI 219
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 61-279 4.22e-19

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 84.86  E-value: 4.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  61 QDFSFKAGQWVDFFIPGVSVVGgFSICSSPRlleQERVIELAVKYTNHPPALwVHNTCTLDCeVAVR--VGGEFffdpqP 138
Cdd:PRK08345   34 ESFTFKPGQFVQVTIPGVGEVP-ISICSSPT---RKGFFELCIRRAGRVTTV-IHRLKEGDI-VGVRgpYGNGF-----P 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 139 ADA--SRNLVLIAGGVGINPLLSILRHAADllreqankrNGYEIGTIKLFYSAKNTSELLFKKNILDLVNEfPEKIACSL 216
Cdd:PRK08345  103 VDEmeGMDLLLIAGGLGMAPLRSVLLYAMD---------NRWKYGNITLIYGAKYYEDLLFYDELIKDLAE-AENVKIIQ 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1210675834 217 HVTKQT---TQINAELK--PYITEGRITEKEIRDHIS-KETLFYICGPPPMTDFFSKQLENNHVPKEHI 279
Cdd:PRK08345  173 SVTRDPewpGCHGLPQGfiERVCKGVVTDLFREANTDpKNTYAAICGPPVMYKFVFKELINRGYRPERI 241
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 47-261 4.36e-19

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: 83.79  E-value: 4.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  47 ESPSVKSLRLLVADQD-FSFKAGQWV--DFFIPGVSVVGGFSICSSPrllEQERVIELAVKYTnhPPAL---WVHNTCTL 120
Cdd:cd06215     9 ETPDVKTFRFAAPDGSlFAYKPGQFLtlELEIDGETVYRAYTLSSSP---SRPDSLSITVKRV--PGGLvsnWLHDNLKV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 121 DCEVAVR-VGGEFFFDPQPADasrNLVLIAGGVGINPLLSILRHAADlLREQANkrngyeigtIKLFYSAKNTSELLFKK 199
Cdd:cd06215    84 GDELWASgPAGEFTLIDHPAD---KLLLLSAGSGITPMMSMARWLLD-TRPDAD---------IVFIHSARSPADIIFAD 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1210675834 200 NILDLVNEFPEkiaCSLHVTKQTTQINAELKPyitEGRITEKEIRDHIS--KETLFYICGPPPM 261
Cdd:cd06215   151 ELEELARRHPN---FRLHLILEQPAPGAWGGY---RGRLNAELLALLVPdlKERTVFVCGPAGF 208
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 48-284 2.84e-16

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: 75.71  E-value: 2.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  48 SPSVKSLRLlVADQDFSFKAGQWVDFFIPGV-SVVGGFSICSSPRlleQERVIELAVKytnHPPALWVhnTCTLDCEVAV 126
Cdd:cd06187     8 THDIAVVRL-QLDQPLPFWAGQYVNVTVPGRpRTWRAYSPANPPN---EDGEIEFHVR---AVPGGRV--SNALHDELKV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 127 ----RVG---GEFFFDPqpaDASRNLVLIAGGVGINPLLSILRhaaDLLREQANKRngyeigtIKLFYSAKNTSELLFKK 199
Cdd:cd06187    79 gdrvRLSgpyGTFYLRR---DHDRPVLCIAGGTGLAPLRAIVE---DALRRGEPRP-------VHLFFGARTERDLYDLE 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 200 NILDLVNEFPEkiacsLHVTKQTTQINAELKPYitEGRITEKEIRDHiskETL----FYICGPPPMTDFFSKQLENNHVP 275
Cdd:cd06187   146 GLLALAARHPW-----LRVVPVVSHEEGAWTGR--RGLVTDVVGRDG---PDWadhdIYICGPPAMVDATVDALLARGAP 215


                  ....*....
gi 1210675834 276 KEHICFEKW 284
Cdd:cd06187   216 PERIHFDKF 224
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 130-264 3.96e-16

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


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 75.68  E-value: 3.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 130 GEFFFDPQpaDASRNLVLIAGGVGINPLLSILRHAADllreqankrNGYEIGTIKLFYSAKNTSELLFKKNILDLVNEFP 209
Cdd:cd06183    94 GKFEYKPN--GKVKHIGMIAGGTGITPMLQLIRAILK---------DPEDKTKISLLYANRTEEDILLREELDELAKKHP 162

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1210675834 210 EKIACSLHVTKQTTQINAElkpyitEGRITEKEIRDHI----SKETLFYICGPPPMTDF 264
Cdd:cd06183   163 DRFKVHYVLSRPPEGWKGG------VGFITKEMIKEHLppppSEDTLVLVCGPPPMIEG 215
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 147-267 8.39e-16

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: 71.52  E-value: 8.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 147 LIAGGVGINPLLSILRHaadLLREQANKRNgyeigtIKLFYSAKNTSELLFKKNILDLVNEFPEKiacsLHVTKQTTQIN 226
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRA---ILEDPKDPTQ------VVLVFGNRNEDDILYREELDELAEKHPGR----LTVVYVVSRPE 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1210675834 227 AElkPYITEGRITEKEIRDHISK---ETLFYICGPPPMTDFFSK 267
Cdd:pfam00175  68 AG--WTGGKGRVQDALLEDHLSLpdeETHVYVCGPPGMIKAVRK 109
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 64-283 8.46e-16

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: 74.60  E-value: 8.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  64 SFKAGQWVDFFIPGVSVVGGFSICSSPrllEQERVIELAVKytnHPP--ALwvhnTCTL--DCEVAVRVG-----GEFFF 134
Cdd:cd06190    23 DFLPGQYALLALPGVEGARAYSMANLA---NASGEWEFIIK---RKPggAA----SNALfdNLEPGDELEldgpyGLAYL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 135 DPqpaDASRNLVLIAGGVGINPLLSILRHAAdllreqankRNGYEIG-TIKLFYSAKNTSELLFkkniLDLVNEFPEKIA 213
Cdd:cd06190    93 RP---DEDRDIVCIAGGSGLAPMLSILRGAA---------RSPYLSDrPVDLFYGGRTPSDLCA----LDELSALVALGA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1210675834 214 cSLHVTKQTTQINAELKPYIT--EGRITEkEIRDHIS---KETLFYICGPPPMTDFFSKQLENNH-VPKEHICFEK 283
Cdd:cd06190   157 -RLRVTPAVSDAGSGSAAGWDgpTGFVHE-VVEATLGdrlAEFEFYFAGPPPMVDAVQRMLMIEGvVPFDQIHFDR 230
PRK13289 PRK13289
NO-inducible flavohemoprotein;
130-282 1.40e-15

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 75.99  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 130 GEFFFDPQPadaSRNLVLIAGGVGINPLLSILRHAAdllrEQANKRNgyeigtIKLFYSAKNTSELLFKKNILDLVNEFP 209
Cdd:PRK13289  252 GDFFLDVAS---DTPVVLISGGVGITPMLSMLETLA----AQQPKRP------VHFIHAARNGGVHAFRDEVEALAARHP 318

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1210675834 210 ekiacSLHVT---KQTTQINAELKPYITEGRITEKEIRDHI-SKETLFYICGPPPMTDFFSKQLENNHVPKEHICFE 282
Cdd:PRK13289  319 -----NLKAHtwyREPTEQDRAGEDFDSEGLMDLEWLEAWLpDPDADFYFCGPVPFMQFVAKQLLELGVPEERIHYE 390
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 48-279 3.05e-15

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: 72.97  E-value: 3.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  48 SPSVKSLRLLVaDQDFSFKAGQWVDFFIPGVSVVGgFSICSSPRlleQERVIELAVKytnhppaLWVHNTCT------LD 121
Cdd:cd06189    10 NDDVYRVRLKP-PAPLDFLAGQYLDLLLDDGDKRP-FSIASAPH---EDGEIELHIR-------AVPGGSFSdyvfeeLK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 122 CEVAVRV---GGEFFFDPqpaDASRNLVLIAGGVGINPLLSILRHaadlLREQANKRNgyeigtIKLFYSAKNTSELLFk 198
Cdd:cd06189    78 ENGLVRIegpLGDFFLRE---DSDRPLILIAGGTGFAPIKSILEH----LLAQGSKRP------IHLYWGARTEEDLYL- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 199 knildlvNEFPEKIACS---LHVTKQTTQINAElkPYITEGRITEKEIRDHIS-KETLFYICGPPPMTDFFSKQLENNHV 274
Cdd:cd06189   144 -------DELLEAWAEAhpnFTYVPVLSEPEEG--WQGRTGLVHEAVLEDFPDlSDFDVYACGSPEMVYAARDDFVEKGL 214


                  ....*
gi 1210675834 275 PKEHI 279
Cdd:cd06189   215 PEENF 219
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 146-282 8.53e-14

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: 68.81  E-value: 8.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 146 VLIAGGVGINPLLSILRhaaDLLREQANKRNgyeigtiKLFYSAKNTSELLFKKNILDLVNEfpekiACSLHVTKQTTQi 225
Cdd:cd06196   103 VFIAGGAGITPFIAILR---DLAAKGKLEGN-------TLIFANKTEKDIILKDELEKMLGL-----KFINVVTDEKDP- 166

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1210675834 226 naelkPYITeGRITEKEIRDHISKET-LFYICGPPPMTDFFSKQLENNHVPKEHICFE 282
Cdd:cd06196   167 -----GYAH-GRIDKAFLKQHVTDFNqHFYVCGPPPMEEAINGALKELGVPEDSIVFE 218
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 54-279 1.22e-13

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: 68.49  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  54 LRLLVA-DQDFSFKAGQWVDFFIPGVSVVGGFSICSSPRlleQERVIELAVKytnHPPA----LWVHNTCTLDCEVAVRV 128
Cdd:cd06213    16 VRLTVQlDRPIAYKAGQYAELTLPGLPAARSYSFANAPQ---GDGQLSFHIR---KVPGgafsGWLFGADRTGERLTVRG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 129 -GGEFFFdpQPADASrnLVLIAGGVGINPLLSILRHAadllREQANKRNgyeigtIKLFYSAKnTSELLFKkniLDlvne 207
Cdd:cd06213    90 pFGDFWL--RPGDAP--ILCIAGGSGLAPILAILEQA----RAAGTKRD------VTLLFGAR-TQRDLYA---LD---- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 208 fpekiacSLHVTKQTTQINAELKPYITE-----------GRITEKeIRDHISKETLFYICGPPPMTDFFSKQLENNHVPK 276
Cdd:cd06213   148 -------EIAAIAARWRGRFRFIPVLSEepadsswkgarGLVTEH-IAEVLLAATEAYLCGPPAMIDAAIAVLRALGIAR 219


                  ...
gi 1210675834 277 EHI 279
Cdd:cd06213   220 EHI 222
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 47-263 1.42e-13

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap 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: 68.79  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  47 ESPSVKSLRLLVADQDFSFKAGQWVDFFIP--GVSVVGGFSICSSPRllEQERVIELAVKytNHPPAL---WVHNtctld 121
Cdd:cd06216    28 ETADMVTLTLRPNRGWPGHRAGQHVRLGVEidGVRHWRSYSLSSSPT--QEDGTITLTVK--AQPDGLvsnWLVN----- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 122 cevAVRVG---------GEFFF-DPQPADasrnLVLIAGGVGINPLLSILRhaaDLLREQankrngyEIGTIKLFYSAKN 191
Cdd:cd06216    99 ---HLAPGdvvelsqpqGDFVLpDPLPPR----LLLIAAGSGITPVMSMLR---TLLARG-------PTADVVLLYYART 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1210675834 192 TSELLFKKNILDLVNEFPekiacSLHVTKQTTQinAELKPYITEGRIteKEIrDHISKETLFYICGPPPMTD 263
Cdd:cd06216   162 REDVIFADELRALAAQHP-----NLRLHLLYTR--EELDGRLSAAHL--DAV-VPDLADRQVYACGPPGFLD 223
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 48-283 5.29e-13

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: 67.71  E-value: 5.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  48 SPSVKSLRL-LVADQDFSFKAGQWVDFFIPGVS-------------------------------VVGGFSICSSPrllEQ 95
Cdd:cd06188    21 ATFIKELVLkLPSGEEIAFKAGGYIQIEIPAYEiayadfdvaekyradwdkfglwqlvfkhdepVSRAYSLANYP---AE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  96 ERVIELAVKYTNHPPAL----------WVHNTCTLDcevAVRVGG--EFFFDPqpaDASRNLVLIAGGVGINPLLSILRH 163
Cdd:cd06188    98 EGELKLNVRIATPPPGNsdippgigssYIFNLKPGD---KVTASGpfGEFFIK---DTDREMVFIGGGAGMAPLRSHIFH 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 164 aadLLREQANKRNgyeigtIKLFYSAKNTSELLFKKNILDLVNEFPEkiaCSLHVTKQTTQINAELKPYIteGRITEKEI 243
Cdd:cd06188   172 ---LLKTLKSKRK------ISFWYGARSLKELFYQEEFEALEKEFPN---FKYHPVLSEPQPEDNWDGYT--GFIHQVLL 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1210675834 244 ----RDHISKETL-FYICGPPPMTDFFSKQLENNHVPKEHICFEK 283
Cdd:cd06188   238 enylKKHPAPEDIeFYLCGPPPMNSAVIKMLDDLGVPRENIAFDD 282
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 48-283 1.44e-12

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


Pssm-ID: 99805 [Multi-domain]  Cd Length: 228  Bit Score: 65.69  E-value: 1.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  48 SPSVKSLRL-LVADQDFSFKAGQWVDFFIPGVSVVGGFSICSSPrlleQERVIELAVKytNHPPAL---WVHNTCTLDCE 123
Cdd:cd06209    13 SDSTIGLTLeLDEAGALAFLPGQYVNLQVPGTDETRSYSFSSAP----GDPRLEFLIR--LLPGGAmssYLRDRAQPGDR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 124 VAVRvG--GEFFFDPQPadasRNLVLIAGGVGINPLLSILrhaaDLLREQANKRngyeigTIKLFYSAKNTSELlFKkni 201
Cdd:cd06209    87 LTLT-GplGSFYLREVK----RPLLMLAGGTGLAPFLSML----DVLAEDGSAH------PVHLVYGVTRDADL-VE--- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 202 LDLVNEFPEKI-ACSLHVTKQTTQINAELKPYITEGrITEKEIRDhisKETLFYICGPPPMTDFFSKQLENNHVPKEHIC 280
Cdd:cd06209   148 LDRLEALAERLpGFSFRTVVADPDSWHPRKGYVTDH-LEAEDLND---GDVDVYLCGPPPMVDAVRSWLDEQGIEPANFY 223


                  ...
gi 1210675834 281 FEK 283
Cdd:cd06209   224 YEK 226
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 39-284 5.84e-12

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: 64.08  E-value: 5.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  39 AKVCGAASESPSVKSLRLLVADQD-FSFKAGQWVDF--FIPGVSVVGGFSICSSPRLLEqervIELAVKYTnhPPAL--- 112
Cdd:cd06191     1 LRVAEVRSETPDAVTIVFAVPGPLqYGFRPGQHVTLklDFDGEELRRCYSLCSSPAPDE----ISITVKRV--PGGRvsn 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 113 WVHNTCTLDCEVAVRVG-GEFFFDPQPAdasRNLVLIAGGVGINPLLSILRHAADLLREQankrngyeigTIKLFYSAKN 191
Cdd:cd06191    75 YLREHIQPGMTVEVMGPqGHFVYQPQPP---GRYLLVAAGSGITPLMAMIRATLQTAPES----------DFTLIHSART 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 192 TSELLFKKNILDLVNEfPEKIACSLHVTKQTTQINAELKPYITEGRITEKEIRDHISKETlfYICGPPPMTDFFSKQLEN 271
Cdd:cd06191   142 PADMIFAQELRELADK-PQRLRLLCIFTRETLDSDLLHGRIDGEQSLGAALIPDRLEREA--FICGPAGMMDAVETALKE 218

                         250
                  ....*....|...
gi 1210675834 272 NHVPKEHICFEKW 284
Cdd:cd06191   219 LGMPPERIHTERF 231
PLN02252 PLN02252
nitrate reductase [NADPH]
 130-264 7.73e-12

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 65.47  E-value: 7.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 130 GEFFFDPQPADASRnLVLIAGGVGINPLLSILRHAadlLREQANKRngyeigTIKLFYSAKNTSELLFKKNILDLVNEFP 209
Cdd:PLN02252  747 GSFLVNGKPKFAKK-LAMLAGGTGITPMYQVIQAI---LRDPEDKT------EMSLVYANRTEDDILLREELDRWAAEHP 816

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1210675834 210 EKiacsLHVTKQTTQINAELKPYITeGRITEKEIRDHI---SKETLFYICGPPPMTDF 264
Cdd:PLN02252  817 DR----LKVWYVVSQVKREGWKYSV-GRVTEAMLREHLpegGDETLALMCGPPPMIEF 869
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 36-283 1.29e-10

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


Pssm-ID: 99806  Cd Length: 236  Bit Score: 60.05  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  36 VSAAKVCGAASESPSVKSLRL-----LVADQDFSFKAGQWVDFFIPGVSVVGGFSICSSP----RLleqERVIELAvkyt 106
Cdd:cd06210     1 VREAEIVAVDRVSSNVVRLRLqpddaEGAGIAAEFVPGQFVEIEIPGTDTRRSYSLANTPnwdgRL---EFLIRLL---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 107 nhpPALWVHNTCTLDCEVAVRVG-----GEFFFDpqpADASRNLVLIAGGVGINPLLSILRHAAdllREQANkrngyeiG 181
Cdd:cd06210    74 ---PGGAFSTYLETRAKVGQRLNlrgplGAFGLR---ENGLRPRWFVAGGTGLAPLLSMLRRMA---EWGEP-------Q 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 182 TIKLFYSAKNTSELLFKKNILDLVNEFPekiacslhvtkQTTQINAELKPYIT-EG-RITEKEI-RDHISKETL---FYI 255
Cdd:cd06210   138 EARLFFGVNTEAELFYLDELKRLADSLP-----------NLTVRICVWRPGGEwEGyRGTVVDAlREDLASSDAkpdIYL 206

                         250       260
                  ....*....|....*....|....*...
gi 1210675834 256 CGPPPMTDFFSKQLENNHVPKEHICFEK 283
Cdd:cd06210   207 CGPPGMVDAAFAAAREAGVPDEQVYLEK 234
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 48-279 2.00e-10

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


Pssm-ID: 99791 [Multi-domain]  Cd Length: 222  Bit Score: 59.20  E-value: 2.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  48 SPSVKSLRLLVaDQDFSFKAGQWVDFFIPGVsVVGGFSICSSPrllEQERVIELAVK-YTNHPPALWVHNTCTLDCEVAV 126
Cdd:cd06194     8 SPDVLRVRLEP-DRPLPYLPGQYVNLRRAGG-LARSYSPTSLP---DGDNELEFHIRrKPNGAFSGWLGEEARPGHALRL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 127 R--VGGEFFFDPQPADasrNLVLIAGGVGINPLLSILRHAadLLREQAnkrngyeiGTIKLFYSAKNTSELLFKKNILDL 204
Cdd:cd06194    83 QgpFGQAFYRPEYGEG---PLLLVGAGTGLAPLWGIARAA--LRQGHQ--------GEIRLVHGARDPDDLYLHPALLWL 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1210675834 205 VNEFPEkiacsLHVTKQTTQiNAELKPYITEGRITEKEIrdHISKETLFYICGPPPMTDFFSKQLENNHVPKEHI 279
Cdd:cd06194   150 AREHPN-----FRYIPCVSE-GSQGDPRVRAGRIAAHLP--PLTRDDVVYLCGAPSMVNAVRRRAFLAGAPMKRI 216
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 84-162 2.20e-10

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: 59.33  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  84 FSICSSPRLLEQERVIELAVKY----TNHppaLWVHNTCTLDCEVAVRV---GGEFFFDPQPADASRNLVLIAGGVGINP 156
Cdd:cd06197    63 FTVSSAPPHDPATDEFEITVRKkgpvTGF---LFQVARRLREQGLEVPVlgvGGEFTLSLPGEGAERKMVWIAGGVGITP 139


                  ....*.
gi 1210675834 157 LLSILR 162
Cdd:cd06197   140 FLAMLR 145
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 138-278 6.93e-10

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: 58.49  E-value: 6.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 138 PADASRNLVLIAGGVGINPLLSILRHaadLLREQANKRNgyEIGTIKLFYSAKNTSELLFKKNILDLVNEFPEKIACSLH 217
Cdd:cd06208   131 PEDPNATLIMIATGTGIAPFRSFLRR---LFREKHADYK--FTGLAWLFFGVPNSDSLLYDDELEKYPKQYPDNFRIDYA 205

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1210675834 218 VTKQTTQINAElKPYITEgRITE--KEIRDHISKE-TLFYICG----PPPMTDFFSKQLENNHVPKEH 278
Cdd:cd06208   206 FSREQKNADGG-KMYVQD-RIAEyaEEIWNLLDKDnTHVYICGlkgmEPGVDDALTSVAEGGLAWEEF 271
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 53-283 1.51e-09

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


Pssm-ID: 99792 [Multi-domain]  Cd Length: 241  Bit Score: 57.19  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  53 SLRLlVADQDFSFKAGQWVDFFIP---GVSVVGGFSICSSPrlleQERVIELAVKYTNHPPA---LWvhntctldcevAV 126
Cdd:cd06195    14 SFRV-TRDIPFRFQAGQFTKLGLPnddGKLVRRAYSIASAP----YEENLEFYIILVPDGPLtprLF-----------KL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 127 RVGGEFFFDPQPA--------DASRNLVLIAGGVGINPLLSILRHAADLLREQankrngyeigTIKLFYSAKNTSELLFk 198
Cdd:cd06195    78 KPGDTIYVGKKPTgfltldevPPGKRLWLLATGTGIAPFLSMLRDLEIWERFD----------KIVLVHGVRYAEELAY- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 199 kniLDLVNEFPEKIACSLHVTKQTTQinaELKPYITEGRITE----KEIRDHI-----SKETLFYICGPPPMTDFFSKQL 269
Cdd:cd06195   147 ---QDEIEALAKQYNGKFRYVPIVSR---EKENGALTGRIPDliesGELEEHAglpldPETSHVMLCGNPQMIDDTQELL 220

                         250       260
                  ....*....|....*....|
gi 1210675834 270 ENN----HVPKE--HICFEK 283
Cdd:cd06195   221 KEKgfskNHRRKpgNITVEK 240
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 47-282 5.13e-09

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: 55.18  E-value: 5.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  47 ESPSVKSLRLLVADQDF--SFKAGQWVDffipgVSVVGGF----SICSSPRllEQERViELAVKytnHPPA-----LWVH 115
Cdd:cd06185     6 EAPDIRSFELEAPDGAPlpAFEPGAHID-----VHLPNGLvrqySLCGDPA--DRDRY-RIAVL---REPAsrggsRYMH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 116 NTCTLDCEVAVRVGGEFFfdPQPADASRNlVLIAGGVGINPLLSILRHAAdllREQANkrngYEigtikLFYSAKNTSEL 195
Cdd:cd06185    75 ELLRVGDELEVSAPRNLF--PLDEAARRH-LLIAGGIGITPILSMARALA---ARGAD----FE-----LHYAGRSREDA 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 196 LFkkniLDLVNEFPEKiACSLHVTKQTTQINAElkpyitegritekEIRDHISKETLFYICGPPPMTDFFSKQLENNHVP 275
Cdd:cd06185   140 AF----LDELAALPGD-RVHLHFDDEGGRLDLA-------------ALLAAPPAGTHVYVCGPEGMMDAVRAAAAALGWP 201


                  ....*..
gi 1210675834 276 KEHICFE 282
Cdd:cd06185   202 EARLHFE 208
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 61-282 1.29e-08

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: 53.85  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  61 QDFSFKAGQWVdfFI--PGVSVVGG---FSICSSPRLLEQErvIELAVK----YTNHppaLWVHNTCTLDCEVAVRVgge 131
Cdd:cd06186    21 KPFKWKPGQHV--YLnfPSLLSFWQshpFTIASSPEDEQDT--LSLIIRakkgFTTR---LLRKALKSPGGGVSLKV--- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 132 fFFD------PQPADASRNLVLIAGGVGINPLLSILRhaaDLLREQANKRNgyeIGTIKLFYSAKNTSELLFKKNILDLV 205
Cdd:cd06186    91 -LVEgpygssSEDLLSYDNVLLVAGGSGITFVLPILR---DLLRRSSKTSR---TRRVKLVWVVRDREDLEWFLDELRAA 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1210675834 206 NEFPEKIACSLHVTKqttqinaelkpyitegritekeirdhisketlFYICGPPPMTDFFSKQLENNHVPKEHICFE 282
Cdd:cd06186   164 QELEVDGEIEIYVTR--------------------------------VVVCGPPGLVDDVRNAVAKKGGTGVEFHEE 208
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
143-268 2.31e-08

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 51.96  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 143 RNLVLIAGGVGINPLLSILRHAADLLREQANKRngyeigtIKLFYSAKNTSEL-LFKKNILDLVNEFPEKIACSLHVT-- 219
Cdd:pfam08030   2 ENVLLVAGGIGITPFISILKDLGNKSKKLKTKK-------IKFYWVVRDLSSLeWFKDVLNELEELKELNIEIHIYLTge 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1210675834 220 -------------KQTTQINAELKPYITEGRIT------------EKEIRDHISKETLFYICGPPPMTDFFSKQ 268
Cdd:pfam08030  75 yeaedasdqsdssIRSENFDSLMNEVIGVDFVEfhfgrpnwkevlKDIAKQHPNGSIGVFSCGPPSLVDELRNL 148
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 143-261 2.22e-07

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 52.09  E-value: 2.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  143 RNLVLIAGGVGINPLLSILRHAadllreqANKRNGYEIGTIKLFYSAKNTSELLFKKNILDLVNEFPEKIACSLHVTKQT 222
Cdd:PTZ00306  1032 RKLALIAGGTGVAPMLQIIRAA-------LKKPYVDSIESIRLIYAAEDVSELTYRELLESYRKENPGKFKCHFVLNNPP 1104

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1210675834  223 TQinaelkpyITE--GRITEKEIRDHI---SKETLFYICGPPPM 261
Cdd:PTZ00306  1105 EG--------WTDgvGFVDRALLQSALqppSKDLLVAICGPPVM 1140
BenC NF040810
benzoate 1,2-dioxygenase electron transfer component BenC;
48-283 6.09e-07

benzoate 1,2-dioxygenase electron transfer component BenC;


Pssm-ID: 468751 [Multi-domain]  Cd Length: 333  Bit Score: 49.82  E-value: 6.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  48 SPSVKSLRL-LVADQDFSFKAGQWVDFFIPGVSVVGGFSICSSPrlleQERVIELAVKytNHPPAL---WVHNTCtldce 123
Cdd:NF040810  116 SDSTIELSLdLDDDAALAFLPGQYVNIQVPGTGQTRSYSFSSLP----GAREASFLIR--NVPGGLmssYLTERA----- 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 124 vavRVG---------GEFFFdpqpADASRNLVLIAGGVGINPLLSILRHaadlLREQANKRngyeigTIKLFYSAKNTse 194
Cdd:NF040810  185 ---KPGdrlsltgplGSFYL----REVTRPLLMLAGGTGLAPFLSMLEV----LAEQGSEQ------PVHLIYGVTRD-- 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 195 llfkkniLDLV-----NEFPEKIAcslHVTKQTTQINAE----LKPYITegritekeirDHISKETL------FYICGPP 259
Cdd:NF040810  246 -------ADLVeverlEAFAARLP---NFTFRTCVADAAsahpRKGYVT----------QHIEAEWLndgdvdVYLCGPP 305

                         250       260
                  ....*....|....*....|....
gi 1210675834 260 PMTDFFSKQLENNHVPKEHICFEK 283
Cdd:NF040810  306 PMVDAVRGWFREQGITPASFHYEK 329
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 47-283 1.49e-06

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 48.94  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  47 ESPSVKSLRLLvaDQDF-SFKAGQWVDffipgVSVVG------GFSICSSPRLleqERVIELAVK-YTNHPPALWVHNTc 118
Cdd:PRK10684   20 ETPDVWTISLI--CHDFyPYRAGQYAL-----VSIRNsaetlrAYTLSSTPGV---SEFITLTVRrIDDGVGSQWLTRD- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 119 tldcevaVRVG---------GEFFFDPQPADasrNLVLIAGGVGINPLLSILRHaadLL--REQANkrngyeigtIKLFY 187
Cdd:PRK10684   89 -------VKRGdylwlsdamGEFTCDDKAED---KYLLLAAGCGVTPIMSMRRW---LLknRPQAD---------VQVIF 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 188 SAKNTSELLFKKNILDLVNEFPEkiacsLHVTkqttqINAELK--PYITEGRITEKEIRDH---ISKETLFyICGPPPMT 262
Cdd:PRK10684  147 NVRTPQDVIFADEWRQLKQRYPQ-----LNLT-----LVAENNatEGFIAGRLTRELLQQAvpdLASRTVM-TCGPAPYM 215

                         250       260
                  ....*....|....*....|.
gi 1210675834 263 DFFSKQLENNHVPKEHICFEK 283
Cdd:PRK10684  216 DWVEQEVKALGVTADRFFKEK 236
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 133-283 3.07e-06

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: 47.16  E-value: 3.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 133 FFDPqpaDASRNLVLIAGGVGINPLLsilrHAADLLREQANKrngyeigtIKLFYSAKNTSELLfkknildLVNEFpEKI 212
Cdd:cd06218    92 FDLP---DDDGKVLLVGGGIGIAPLL----FLAKQLAERGIK--------VTVLLGFRSADDLF-------LVEEF-EAL 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1210675834 213 ACSLHVTkqTTQINAELKPYITEgrITEKEIRDhiSKETLFYICGPPPMTDFFSKQLENNHVPKEhICFEK 283
Cdd:cd06218   149 GAEVYVA--TDDGSAGTKGFVTD--LLKELLAE--ARPDVVYACGPEPMLKAVAELAAERGVPCQ-VSLEE 212
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 43-258 4.46e-06

NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal ferredoxin reducatase (FNR)- like FAD and NAD binding module, an FMN-binding domain, and an additional conecting domain (inserted within the FAD binding region) that orients the FNR and FMN binding domains. 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: 99779 [Multi-domain]  Cd Length: 267  Bit Score: 46.95  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  43 GAASESPSVKSLRLLVAD----QDFSFKAGQWVDFFIPGVSVVGGFSICSSPRllEQERVIELAVKYTNHPPALWVHNT- 117
Cdd:cd06182     6 RKLTPPDSPRSTRHLEFDlsgnSVLKYQPGDHLGVIPPNPLQPRYYSIASSPD--VDPGEVHLCVRVVSYEAPAGRIRKg 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 118 ------CTLD----CEVAVRVGGEFFFdpqPADASRNLVLIAGGVGINPLLSILRHAAdllreqANKRNGYEIGTIKLFY 187
Cdd:cd06182    84 vcsnflAGLQlgakVTVFIRPAPSFRL---PKDPTTPIIMVGPGTGIAPFRGFLQERA------ALRANGKARGPAWLFF 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1210675834 188 SAKN-TSELLFKKNIldlvNEFPEKIACS-LHVTKQTTQinAELKPYITEgRITE--KEIRDHISKETLFYICGP 258
Cdd:cd06182   155 GCRNfASDYLYREEL----QEALKDGALTrLDVAFSREQ--AEPKVYVQD-KLKEhaEELRRLLNEGAHIYVCGD 222
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 47-261 6.33e-06

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 46.40  E-value: 6.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  47 ESPSVKSLRLlVADQDFSFKAGQWVDFFIPGVSVVGG--FSICssprlleqervielavkYTNHppalwvhntctLDCEV 124
Cdd:PRK00054   15 IAPNIYTLVL-DGEKVFDMKPGQFVMVWVPGVEPLLErpISIS-----------------DIDK-----------NEITI 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 125 AVRVGGEF---FFDPQPAD----------------ASRNLVLIAGGVGINPLLSIlrhaADLLREqankrNGYEIGTIkl 185
Cdd:PRK00054   66 LYRKVGEGtkkLSKLKEGDeldirgplgngfdleeIGGKVLLVGGGIGVAPLYEL----AKELKK-----KGVEVTTV-- 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1210675834 186 fYSAKNTSELLFKKnildlvnEFPEkiACSLHVTKQTTQinaelkpYITEGRITEKeIRDHISKETLFYICGPPPM 261
Cdd:PRK00054  135 -LGARTKDEVIFEE-------EFAK--VGDVYVTTDDGS-------YGFKGFVTDV-LDELDSEYDAIYSCGPEIM 192
fre PRK08051
FMN reductase; Validated
 56-167 7.54e-06

FMN reductase; Validated


Pssm-ID: 236142 [Multi-domain]  Cd Length: 232  Bit Score: 46.00  E-value: 7.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  56 LLVADQDFSFKAGQWvdffipgVSVVGG------FSICSSPRlleQERVIELavkytnHPPALwVHNTCT------LDCE 123
Cdd:PRK08051   21 RLVPEAPFSFRAGQY-------LMVVMGekdkrpFSIASTPR---EKGFIEL------HIGAS-ELNLYAmavmerILKD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1210675834 124 VAVRV---GGEFFFDpqpADASRNLVLIAGGVGINPLLSILRHAADL 167
Cdd:PRK08051   84 GEIEVdipHGDAWLR---EESERPLLLIAGGTGFSYARSILLTALAQ 127
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
38-279 1.45e-05

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 45.49  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  38 AAKVCGAASESPSVKSLRLLvADQDFSFKAGQWVDFFIPGvSVVGGFSICSSPrllEQERVIELAVKyTNHPPALwvhnt 117
Cdd:PRK05713   93 PARVVALDWLGGDVLRLRLE-PERPLRYRAGQHLVLWTAG-GVARPYSLASLP---GEDPFLEFHID-CSRPGAF----- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 118 ctldCEVAVRV------------GGEFFFDPQPADasRNLVLIAGGVGINPLLSILRHAAdllreqankRNGYEiGTIKL 185
Cdd:PRK05713  162 ----CDAARQLqvgdllrlgelrGGALHYDPDWQE--RPLWLLAAGTGLAPLWGILREAL---------RQGHQ-GPIRL 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 186 FYSAKNTSELLFKKNILDLVNEFPEkIACSLHVTKQTTQINAELKPyitegritekeirdhISKETLFYICGPPPMTDFF 265
Cdd:PRK05713  226 LHLARDSAGHYLAEPLAALAGRHPQ-LSVELVTAAQLPAALAELRL---------------VSRQTMALLCGSPASVERF 289

                         250
                  ....*....|....
gi 1210675834 266 SKQLENNHVPKEHI 279
Cdd:PRK05713  290 ARRLYLAGLPRNQL 303
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
141-284 2.43e-05

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 45.12  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 141 ASRNLVLIAGGVGINPLLSILrhaaDLLREQANKRngyeigTIKLFYSAKNTSELLFKKNIldlvNEFPEKIAcslhvtk 220
Cdd:PRK11872  208 VERPLVFVAGGTGLSAFLGML----DELAEQGCSP------PVHLYYGVRHAADLCELQRL----AAYAERLP------- 266

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1210675834 221 qttqiNAELKPYITE---------GRITEKEIRDHISKETL-FYICGPPPMTDFFSKQLENNHVPKEHICFEKW 284
Cdd:PRK11872  267 -----NFRYHPVVSKasadwqgkrGYIHEHFDKAQLRDQAFdMYLCGPPPMVEAVKQWLDEQALENYRLYYEKF 335
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 147-271 7.82e-05

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 43.28  E-value: 7.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 147 LIAGGVGINPLLSILRhaadllreqANKRNGYEIGTIKLFYSAKNTSELLFKKNILDLVNEFPEKIACSLhvTKQTTqin 226
Cdd:PTZ00319  171 MIAGGTGITPMLQIIH---------AIKKNKEDRTKVFLVYANQTEDDILLRKELDEAAKDPRFHVWYTL--DREAT--- 236

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1210675834 227 AELKpyITEGRITEKEIRDHI---------SKETLFYICGPPPMTDFFSK-QLEN 271
Cdd:PTZ00319  237 PEWK--YGTGYVDEEMLRAHLpvpdpqnsgIKKVMALMCGPPPMLQMAVKpNLEK 289
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
 65-257 1.13e-04

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 43.07  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  65 FKAGQWVDFFIPGVSVVGG------FSICSS-PRLLEQERVIELAVK---YTNHPPALwVHNTCT---------LDCEVA 125
Cdd:PLN03115  123 YREGQSIGVIPDGIDKNGKphklrlYSIASSaLGDFGDSKTVSLCVKrlvYTNDQGEI-VKGVCSnflcdlkpgAEVKIT 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 126 VRVGGEFFFdpqPADASRNLVLIAGGVGINPLLSIlrhaadLLREQANKRNGYEI-GTIKLFYSAKNTSELLFKKNILDL 204
Cdd:PLN03115  202 GPVGKEMLM---PKDPNATIIMLATGTGIAPFRSF------LWKMFFEKHDDYKFnGLAWLFLGVPTSSSLLYKEEFEKM 272

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1210675834 205 VNEFPEKIACSLHVTKQTTQINAElKPYItEGRITE--KEIRDHISKE-TLFYICG 257
Cdd:PLN03115  273 KEKAPENFRLDFAVSREQTNAKGE-KMYI-QTRMAEyaEELWELLKKDnTYVYMCG 326
PLN02292 PLN02292
ferric-chelate reductase
 124-246 2.01e-04

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 42.55  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 124 VAVRVGGEFffDPQPADASRN--LVLIAGGVGINPLLSILRhaaDLLreQANKRNGYEIGTIKLFYSAKNTSELlfkkNI 201
Cdd:PLN02292  413 LAVSVEGPY--GPASTDFLRHesLVMVSGGSGITPFISIIR---DLI--YTSSTETCKIPKITLICAFKNSSDL----SM 481

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1210675834 202 LDLVnefpekIACSLHVTKQTTQINAELKPYITEGRITEKEIRDH 246
Cdd:PLN02292  482 LDLI------LPTSGLETELSSFIDIQIKAFVTREKEAGVKESTG 520
PLN02631 PLN02631
ferric-chelate reductase
 84-273 2.28e-04

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 42.34  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  84 FSICSSPRLlEQERVIELAVKYTNHPPALWVHNTCTLDcevAVRVGGEFFFDPQPADASRN--LVLIAGGVGINPLLSIL 161
Cdd:PLN02631  356 FTITSSSNL-EKDTLSVVIRRQGSWTQKLYTHLSSSID---SLEVSTEGPYGPNSFDVSRHnsLILVSGGSGITPFISVI 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 162 RhaaDLLREQANKRNgyEIGTIKLFYSAKNTSELLFkkniLDLVneFPEKIACSlhvtkQTTQINAELKPYITEGRITEK 241
Cdd:PLN02631  432 R---ELIFQSQNPST--KLPDVLLVCSFKHYHDLAF----LDLI--FPLDISVS-----DISRLNLRIEAYITREDKKPE 495

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1210675834 242 EIRDHISKETLFYicGPPPMTDFFSKQLENNH 273
Cdd:PLN02631  496 TTDDHRLLQTKWF--KPQPLDSPISPVLGPNN 525
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 24-252 2.43e-04

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 42.53  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  24 LRNKGSSPFTSIVSAAKVCGAASESPSVKSLRLLVADQDFSFKAgqwvdffIPGVSVVG--GFSICSSPRLleQERVIEL 101
Cdd:PLN02844  305 LRIVQSRPETCILSARLFPCKAIELVLPKDPGLKYAPTSVIFMK-------IPSISRFQwhPFSITSSSNI--DDHTMSV 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 102 AVK----YTNhppALWVHNTCTLDCE------VAVRVGGEFffDPQPADASR--NLVLIAGGVGINPLLSILRHAAdllr 169
Cdd:PLN02844  376 IIKceggWTN---SLYNKIQAELDSEtnqmncIPVAIEGPY--GPASVDFLRydSLLLVAGGIGITPFLSILKEIA---- 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 170 eqANKRNGYEIGT-IKLFYSAKNTSELlfkkNILDLVNefpekiacSLHVTKQTTQINAELKPYITEGRITEKEIRDHIS 248
Cdd:PLN02844  447 --SQSSSRYRFPKrVQLIYVVKKSQDI----CLLNPIS--------SLLLNQSSNQLNLKLKVFVTQEEKPNATLRELLN 512


                  ....
gi 1210675834 249 KETL 252
Cdd:PLN02844  513 QFSQ 516
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
 84-257 2.58e-04

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


Pssm-ID: 99800 [Multi-domain]  Cd Length: 398  Bit Score: 41.92  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834  84 FSICSSPRllEQERVIELAVKYTNHP-PAL---WVHNTCTLDCEVAVRVggEFFFDPQ------PADASRNLVLIAGGVG 153
Cdd:cd06203   177 YSIASSPL--EGPGKLRFIFSVVEFPaKGLctsWLESLCLSASSHGVKV--PFYLRSSsrfrlpPDDLRRPIIMVGPGTG 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 154 INPLLSILRHAADLLREQANKrngyEIGTIKLFYSAKNTSE-LLFKKNILDLVNefpEKIACSLHVTKQTTQINAELKPY 232
Cdd:cd06203   253 VAPFLGFLQHREKLKESHTET----VFGEAWLFFGCRHRDRdYLFRDELEEFLE---EGILTRLIVAFSRDENDGSTPKY 325

                         170       180
                  ....*....|....*....|....*...
gi 1210675834 233 ITEGrITE--KEIRDHISKE-TLFYICG 257
Cdd:cd06203   326 VQDK-LEErgKKLVDLLLNSnAKIYVCG 352
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 142-280 8.89e-04

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


Pssm-ID: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 40.00  E-value: 8.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 142 SRNLVLIAGGVGINPLLSILRHaadlLREQANKrngyeigtIKLFYSAKntsellfKKNILDLVNEFPEkiacSLHVTKQ 221
Cdd:cd06192    97 GGTVLLVAGGIGLAPLLPIAKK----LAANGNK--------VTVLAGAK-------KAKEEFLDEYFEL----PADVEIW 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1210675834 222 TTqinaELKPYITEGRITEKEIRDHISKETLFYICGPPPMTDFFSKQLENNHVPKEHIC 280
Cdd:cd06192   154 TT----DDGELGLEGKVTDSDKPIPLEDVDRIIVAGSDIMMKAVVEALDEWLQLIKASV 208
DHOD_e_trans_like1 cd06219
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 144-267 3.26e-03

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


Pssm-ID: 99815 [Multi-domain]  Cd Length: 248  Bit Score: 38.33  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210675834 144 NLVLIAGGVGINPLLSILRHaadlLREQankrnGYEIGTIKLFYSAkntsELLFkknildLVNEFpEKIACSLHVTkqTT 223
Cdd:cd06219    99 TVVFVGGGVGIAPIYPIAKA----LKEA-----GNRVITIIGARTK----DLVI------LEDEF-RAVSDELIIT--TD 156

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1210675834 224 QINAELKPYITEGRiteKEIRDHISKETLFYICGPPPMTDFFSK 267
Cdd:cd06219   157 DGSYGEKGFVTDPL---KELIESGEKVDLVIAIGPPIMMKAVSE 197
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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