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Conserved domains on  [gi|767924570|ref|XP_011532532|]
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oxidoreductase NAD-binding domain-containing protein 1 isoform X1 [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 ...
 148-382 2.26e-56

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: 2.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 148 SPSVKSLRLlVADQDFSFKAGQWVDFFIP--GVSVVGGFSICSSPrllEQERVIELAVK-YTNHPPALWVHNTCtLDCEV 224
Cdd:cd00322    7 TDDVRLFRL-QLPNGFSFKPGQYVDLHLPgdGRGLRRAYSIASSP---DEEGELELTVKiVPGGPFSAWLHDLK-PGDEV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 225 AVRVGGEFFFdpQPADASRNLVLIAGGVGINPLLSILRHAADLLreqankrngyEIGTIKLFYSAKNTSELLFKKNILDL 304
Cdd:cd00322   82 EVSGPGGDFF--LPLEESGPVVLIAGGIGITPFRSMLRHLAADK----------PGGEITLLYGARTPADLLFLDELEEL 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767924570 305 VNEFPekiaCSLHVTKQTTQINAELKPYITEGRITEKEIRDHISKETLFYICGPPPMTDFFSKQLENNHVPKEHICFE 382
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 ...
 148-382 2.26e-56

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: 2.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 148 SPSVKSLRLlVADQDFSFKAGQWVDFFIP--GVSVVGGFSICSSPrllEQERVIELAVK-YTNHPPALWVHNTCtLDCEV 224
Cdd:cd00322    7 TDDVRLFRL-QLPNGFSFKPGQYVDLHLPgdGRGLRRAYSIASSP---DEEGELELTVKiVPGGPFSAWLHDLK-PGDEV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 225 AVRVGGEFFFdpQPADASRNLVLIAGGVGINPLLSILRHAADLLreqankrngyEIGTIKLFYSAKNTSELLFKKNILDL 304
Cdd:cd00322   82 EVSGPGGDFF--LPLEESGPVVLIAGGIGITPFRSMLRHLAADK----------PGGEITLLYGARTPADLLFLDELEEL 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767924570 305 VNEFPekiaCSLHVTKQTTQINAELKPYITEGRITEKEIRDHISKETLFYICGPPPMTDFFSKQLENNHVPKEHICFE 382
Cdd:cd00322  150 AKEGP----NFRLVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
139-383 7.12e-39

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 138.77  E-value: 7.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 139 AKVCGAASESPSVKSLRLLVAD--QDFSFKAGQWVDFFIP--GVSVVGGFSICSSPRlleqERVIELAVKYTNHPPA-LW 213
Cdd:COG1018    6 LRVVEVRRETPDVVSFTLEPPDgaPLPRFRPGQFVTLRLPidGKPLRRAYSLSSAPG----DGRLEITVKRVPGGGGsNW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 214 VHNTctldcevaVRVG---------GEFFFDPQPAdasRNLVLIAGGVGINPLLSILRHaadLLREQANKRngyeigtIK 284
Cdd:COG1018   82 LHDH--------LKVGdtlevsgprGDFVLDPEPA---RPLLLIAGGIGITPFLSMLRT---LLARGPFRP-------VT 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 285 LFYSAKNTSELLFKKNILDLVNEFPekiacSLHVTKQTTQINAELkpyitEGRITEKEIRDHIS--KETLFYICGPPPMT 362
Cdd:COG1018  141 LVYGARSPADLAFRDELEALAARHP-----RLRLHPVLSREPAGL-----QGRLDAELLAALLPdpADAHVYLCGPPPMM 210

                        250       260
                 ....*....|....*....|.
gi 767924570 363 DFFSKQLENNHVPKEHICFEK 383
Cdd:COG1018  211 EAVRAALAELGVPEERIHFER 231
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 161-379 1.31e-18

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 85.24  E-value: 1.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 161 QDFSFKAGQWVDFFIPGVSVVGgFSICSSPRlleQERVIELAVKYTNHPPALwVHNTCTLDCeVAVR--VGGEFffdpqP 238
Cdd:PRK08345  34 ESFTFKPGQFVQVTIPGVGEVP-ISICSSPT---RKGFFELCIRRAGRVTTV-IHRLKEGDI-VGVRgpYGNGF-----P 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 239 ADA--SRNLVLIAGGVGINPLLSILRHAADllreqankrNGYEIGTIKLFYSAKNTSELLFKKNILDLVNEfPEKIACSL 316
Cdd:PRK08345 103 VDEmeGMDLLLIAGGLGMAPLRSVLLYAMD---------NRWKYGNITLIYGAKYYEDLLFYDELIKDLAE-AENVKIIQ 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767924570 317 HVTKQT---TQINAELK--PYITEGRITEKEIRDHIS-KETLFYICGPPPMTDFFSKQLENNHVPKEHI 379
Cdd:PRK08345 173 SVTRDPewpGCHGLPQGfiERVCKGVVTDLFREANTDpKNTYAAICGPPVMYKFVFKELINRGYRPERI 241
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 247-367 2.05e-15

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: 2.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570  247 LIAGGVGINPLLSILRHaadLLREQANKRNgyeigtIKLFYSAKNTSELLFKKNILDLVNEFPEKiacsLHVTKQTTQIN 326
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRA---ILEDPKDPTQ------VVLVFGNRNEDDILYREELDELAEKHPGR----LTVVYVVSRPE 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767924570  327 AElkPYITEGRITEKEIRDHISK---ETLFYICGPPPMTDFFSK 367
Cdd:pfam00175  68 AG--WTGGKGRVQDALLEDHLSLpdeETHVYVCGPPGMIKAVRK 109
BenC NF040810
benzoate 1,2-dioxygenase electron transfer component BenC;
148-383 1.14e-06

benzoate 1,2-dioxygenase electron transfer component BenC;


Pssm-ID: 468751 [Multi-domain]  Cd Length: 333  Bit Score: 49.82  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 148 SPSVKSLRL-LVADQDFSFKAGQWVDFFIPGVSVVGGFSICSSPrlleQERVIELAVKytNHPPAL---WVHNTCtldce 223
Cdd:NF040810 116 SDSTIELSLdLDDDAALAFLPGQYVNIQVPGTGQTRSYSFSSLP----GAREASFLIR--NVPGGLmssYLTERA----- 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 224 vavRVG---------GEFFFdpqpADASRNLVLIAGGVGINPLLSILRHaadlLREQANKRngyeigTIKLFYSAKNTse 294
Cdd:NF040810 185 ---KPGdrlsltgplGSFYL----REVTRPLLMLAGGTGLAPFLSMLEV----LAEQGSEQ------PVHLIYGVTRD-- 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 295 llfkkniLDLV-----NEFPEKIAcslHVTKQTTQINAE----LKPYITegritekeirDHISKETL------FYICGPP 359
Cdd:NF040810 246 -------ADLVeverlEAFAARLP---NFTFRTCVADAAsahpRKGYVT----------QHIEAEWLndgdvdVYLCGPP 305

                        250       260
                 ....*....|....*....|....
gi 767924570 360 PMTDFFSKQLENNHVPKEHICFEK 383
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 ...
 148-382 2.26e-56

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: 2.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 148 SPSVKSLRLlVADQDFSFKAGQWVDFFIP--GVSVVGGFSICSSPrllEQERVIELAVK-YTNHPPALWVHNTCtLDCEV 224
Cdd:cd00322    7 TDDVRLFRL-QLPNGFSFKPGQYVDLHLPgdGRGLRRAYSIASSP---DEEGELELTVKiVPGGPFSAWLHDLK-PGDEV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 225 AVRVGGEFFFdpQPADASRNLVLIAGGVGINPLLSILRHAADLLreqankrngyEIGTIKLFYSAKNTSELLFKKNILDL 304
Cdd:cd00322   82 EVSGPGGDFF--LPLEESGPVVLIAGGIGITPFRSMLRHLAADK----------PGGEITLLYGARTPADLLFLDELEEL 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767924570 305 VNEFPekiaCSLHVTKQTTQINAELKPYITEGRITEKEIRDHISKETLFYICGPPPMTDFFSKQLENNHVPKEHICFE 382
Cdd:cd00322  150 AKEGP----NFRLVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
139-383 7.12e-39

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 138.77  E-value: 7.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 139 AKVCGAASESPSVKSLRLLVAD--QDFSFKAGQWVDFFIP--GVSVVGGFSICSSPRlleqERVIELAVKYTNHPPA-LW 213
Cdd:COG1018    6 LRVVEVRRETPDVVSFTLEPPDgaPLPRFRPGQFVTLRLPidGKPLRRAYSLSSAPG----DGRLEITVKRVPGGGGsNW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 214 VHNTctldcevaVRVG---------GEFFFDPQPAdasRNLVLIAGGVGINPLLSILRHaadLLREQANKRngyeigtIK 284
Cdd:COG1018   82 LHDH--------LKVGdtlevsgprGDFVLDPEPA---RPLLLIAGGIGITPFLSMLRT---LLARGPFRP-------VT 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 285 LFYSAKNTSELLFKKNILDLVNEFPekiacSLHVTKQTTQINAELkpyitEGRITEKEIRDHIS--KETLFYICGPPPMT 362
Cdd:COG1018  141 LVYGARSPADLAFRDELEALAARHP-----RLRLHPVLSREPAGL-----QGRLDAELLAALLPdpADAHVYLCGPPPMM 210

                        250       260
                 ....*....|....*....|.
gi 767924570 363 DFFSKQLENNHVPKEHICFEK 383
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 ...
 139-384 1.85e-30

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: 1.85e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 139 AKVCGAASESPSVKSLRLLVADQD-FSFKAGQWVDFF---IPGVSVVGGFSICSSPrllEQERVIELAVKytnHPPALWV 214
Cdd:cd06217    4 LRVTEIIQETPTVKTFRLAVPDGVpPPFLAGQHVDLRltaIDGYTAQRSYSIASSP---TQRGRVELTVK---RVPGGEV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 215 HNTCTlDCevaVRVG---------GEFFFDPQPADasrNLVLIAGGVGINPLLSILRHaadlLREQANKRNgyeigtIKL 285
Cdd:cd06217   78 SPYLH-DE---VKVGdllevrgpiGTFTWNPLHGD---PVVLLAGGSGIVPLMSMIRY----RRDLGWPVP------FRL 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 286 FYSAKNTSELLFKKNILDLVNEFPekiacSLHVTKQTTQInaelKPYIT---EGRIT----EKEIRDHISKEtlFYICGP 358
Cdd:cd06217  141 LYSARTAEDVIFRDELEQLARRHP-----NLHVTEALTRA----APADWlgpAGRITadliAELVPPLAGRR--VYVCGP 209

                        250       260
                 ....*....|....*....|....*.
gi 767924570 359 PPMTDFFSKQLENNHVPKEHICFEKW 384
Cdd:cd06217  210 PAFVEAATRLLLELGVPRDRIRTEAF 235
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 161-382 6.60e-27

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: 6.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 161 QDFSFKAGQWVDFFIP--GVSVVGGFSICSSPrlleQERVIELAVK------YTNhppalWVHNTctldcevaVRVG--- 229
Cdd:cd06214   29 DAFRYRPGQFLTLRVPidGEEVRRSYSICSSP----GDDELRITVKrvpggrFSN-----WANDE--------LKAGdtl 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 230 ------GEFFFDPQPADasRNLVLIAGGVGINPLLSILRHAadLLREQAnkrngyeiGTIKLFYSAKNTSELLFKKNILD 303
Cdd:cd06214   92 evmppaGRFTLPPLPGA--RHYVLFAAGSGITPVLSILKTA--LAREPA--------SRVTLVYGNRTEASVIFREELAD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 304 LVNEFPEKiaCSL-HVTKQTTQINAELKPYITEGRITEKEIRDHISKE-TLFYICGPPPMTDFFSKQLENNHVPKEHICF 381
Cdd:cd06214  160 LKARYPDR--LTViHVLSREQGDPDLLRGRLDAAKLNALLKNLLDATEfDEAFLCGPEPMMDAVEAALLELGVPAERIHR 237


                 .
gi 767924570 382 E 382
Cdd:cd06214  238 E 238
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 133-382 7.11e-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: 101.87  E-value: 7.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 133 REIVSAAKVcgaaSESPSVKSLRLLVADQDF--SFKAGQW--VDFFIPGVS--VVGGFSICSSPRllEQERVIelAVKY- 205
Cdd:cd06184    7 RPFVVARKV----AESEDITSFYLEPADGGPlpPFLPGQYlsVRVKLPGLGyrQIRQYSLSDAPN--GDYYRI--SVKRe 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 206 -----TNhppalWVHNTctldcevaVRVG---------GEFFFDPqpaDASRNLVLIAGGVGINPLLSILRHAAdllrEQ 271
Cdd:cd06184   79 pgglvSN-----YLHDN--------VKVGdvlevsapaGDFVLDE---ASDRPLVLISAGVGITPMLSMLEALA----AE 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 272 ANKRNgyeigtIKLFYSAKNTSELLFKKNILDLVNEFPekiACSLHVTKQTTQINAELKPYITEGRITEKEIRDH-ISKE 350
Cdd:cd06184  139 GPGRP------VTFIHAARNSAVHAFRDELEELAARLP---NLKLHVFYSEPEAGDREEDYDHAGRIDLALLRELlLPAD 209

                        250       260       270
                 ....*....|....*....|....*....|..
gi 767924570 351 TLFYICGPPPMTDFFSKQLENNHVPKEHICFE 382
Cdd:cd06184  210 ADFYLCGPVPFMQAVREGLKALGVPAERIHYE 241
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 147-379 8.23e-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: 8.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 147 ESPSVKSLRLLVADQDFSFKAGQWVDFFIPGVSVVGGFSICSSPRlleQERVIELAVK----YTNhppalWVHNTCTLDc 222
Cdd:COG0543    8 LAPDVYLLRLEAPLIALKFKPGQFVMLRVPGDGLRRPFSIASAPR---EDGTIELHIRvvgkGTR-----ALAELKPGD- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 223 EVAVRvG--GEFFfdpQPADASRNLVLIAGGVGINPLLSILRHAADLLREqankrngyeigtIKLFYSAKNTSELLFKKN 300
Cdd:COG0543   79 ELDVR-GplGNGF---PLEDSGRPVLLVAGGTGLAPLRSLAEALLARGRR------------VTLYLGARTPEDLYLLDE 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 301 ILDLVNefpekiaCSLHVTkqttqinAELKPYITEGRITEKeIRDHI--SKETLFYICGPPPMTDFFSKQLENNHVPKEH 378
Cdd:COG0543  143 LEALAD-------FRVVVT-------TDDGWYGRKGFVTDA-LKELLaeDSGDDVYACGPPPMMKAVAELLLERGVPPER 207


                 .
gi 767924570 379 I 379
Cdd:COG0543  208 I 208
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 138-383 8.83e-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: 8.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 138 AAKVCGAASESPSVKSLRL-LVADQDFSFKAGQWVDFFIPGVSVVGGFSICSSPRlleQERVIELAVKytNHPPALWvhn 216
Cdd:cd06212    2 VGTVVAVEALTHDIRRLRLrLEEPEPIKFFAGQYVDITVPGTEETRSFSMANTPA---DPGRLEFIIK--KYPGGLF--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 217 TCTLDCEVA----VRVGGEF--FFDPQPADasRNLVLIAGGVGINPLLSILRHAAdllrEQANKRngyeigTIKLFYSAK 290
Cdd:cd06212   74 SSFLDDGLAvgdpVTVTGPYgtCTLRESRD--RPIVLIGGGSGMAPLLSLLRDMA----ASGSDR------PVRFFYGAR 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 291 NTSELLFKKNILDLVNEFP--EKIACSLHVTKQtTQINAElKPYITE--GRiTEKEIRDHISketlfYICGPPPMTDFFS 366
Cdd:cd06212  142 TARDLFYLEEIAALGEKIPdfTFIPALSESPDD-EGWSGE-TGLVTEvvQR-NEATLAGCDV-----YLCGPPPMIDAAL 213

                        250
                 ....*....|....*..
gi 767924570 367 KQLENNHVPKEHICFEK 383
Cdd:cd06212  214 PVLEMSGVPPDQIFYDK 230
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
138-382 1.12e-22

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 98.81  E-value: 1.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 138 AAKVCGAASESPSVKSLRL-LVADQDFSFKAGQ--WVDFFIPGVSVvGG--FSICSSPrllEQERVIELAVK----YTNh 208
Cdd:COG4097  216 PYRVESVEPEAGDVVELTLrPEGGRWLGHRAGQfaFLRFDGSPFWE-EAhpFSISSAP---GGDGRLRFTIKalgdFTR- 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 209 ppalwvhntcTLDcevAVRVG---------GEFFFDPqpADASRNLVLIAGGVGINPLLSILRHAADLLREQAnkrngye 279
Cdd:COG4097  291 ----------RLG---RLKPGtrvyvegpyGRFTFDR--RDTAPRQVWIAGGIGITPFLALLRALAARPGDQR------- 348

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 280 igTIKLFYSAKNTSELLFKKNILDLVNEFPekiacslhvtkqttqiNAELKPYIT--EGRITEKEIRDHIS--KETLFYI 355
Cdd:COG4097  349 --PVDLFYCVRDEEDAPFLEELRALAARLA----------------GLRLHLVVSdeDGRLTAERLRRLVPdlAEADVFF 410

                        250       260
                 ....*....|....*....|....*..
gi 767924570 356 CGPPPMTDFFSKQLENNHVPKEHICFE 382
Cdd:COG4097  411 CGPPGMMDALRRDLRALGVPARRIHQE 437
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 148-383 3.49e-21

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


Pssm-ID: 99807  Cd Length: 238  Bit Score: 91.23  E-value: 3.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 148 SPSVKSLRL-LVADQDFSFKAGQWVDFFIPGVSVVGGFSICSSPRlleQERVIELAVKYTnhPPALwvhntCTLDCEVAV 226
Cdd:cd06211   18 TPTIKGVRLkLDEPEEIEFQAGQYVNLQAPGYEGTRAFSIASSPS---DAGEIELHIRLV--PGGI-----ATTYVHKQL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 227 RVG---------GEFFFDPQpadASRNLVLIAGGVGINPLLSILRHaadlLREQANKRNgyeigtIKLFYSAKNTSELLF 297
Cdd:cd06211   88 KEGdeleisgpyGDFFVRDS---DQRPIIFIAGGSGLSSPRSMILD----LLERGDTRK------ITLFFGARTRAELYY 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 298 KKNILDLVNEFPE-KIACSLHVTKQTTQINAElKPYITE--GRITEKEIRDHISketlfYICGPPPMTDFFSKQLENNHV 374
Cdd:cd06211  155 LDEFEALEKDHPNfKYVPALSREPPESNWKGF-TGFVHDaaKKHFKNDFRGHKA-----YLCGPPPMIDACIKTLMQGRL 228


                 ....*....
gi 767924570 375 PKEHICFEK 383
Cdd:cd06211  229 FERDIYYEK 237
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 148-383 1.48e-19

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: 89.15  E-value: 1.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 148 SPSVKSLRL-LVADQDFSFKAGQWVDFFIPGV-----------------------SVVGGFSICSSPrllEQERVIELAV 203
Cdd:COG2871  143 TTFIKELVLeLPEGEEIDFKAGQYIQIEVPPYevdfkdfdipeeekfglfdkndeEVTRAYSMANYP---AEKGIIELNI 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 204 KY----TNHPPAL---WVHNtctldcevaVRVG---------GEFFFDpqpaDASRNLVLIAGGVGINPLLSILRhaaDL 267
Cdd:COG2871  220 RIatppMDVPPGIgssYIFS---------LKPGdkvtisgpyGEFFLR----DSDREMVFIGGGAGMAPLRSHIF---DL 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 268 LREQANKRNgyeigtIKLFYSAKNTSELLFKKNILDLVNEFPekiacslhvtkqttqiNAELKPYITE-----------G 336
Cdd:COG2871  284 LERGKTDRK------ITFWYGARSLRELFYLEEFRELEKEHP----------------NFKFHPALSEplpednwdgetG 341

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767924570 337 RIT----EKEIRDHISKE-TLFYICGPPPMTDFFSKQLENNHVPKEHICFEK 383
Cdd:COG2871  342 FIHevlyENYLKDHPAPEdCEAYLCGPPPMIDAVIKMLDDLGVEEENIYFDD 393
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 147-382 4.71e-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: 4.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 147 ESPSVKSLRLLVADQDFSFKAGQ--WVDFFIPGVSVVGGFSICSSPRlleQERVIELAVK----YTNhppalwvhntcTL 220
Cdd:cd06198    5 EVRPTTTLTLEPRGPALGHRAGQfaFLRFDASGWEEPHPFTISSAPD---PDGRLRFTIKalgdYTR-----------RL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 221 DCEVAV--RV---G--GEFFFDpqpaDASRNLVLIAGGVGINPLLSILRHAADllreqankrnGYEIGTIKLFYSAKNTS 293
Cdd:cd06198   71 AERLKPgtRVtveGpyGRFTFD----DRRARQIWIAGGIGITPFLALLEALAA----------RGDARPVTLFYCVRDPE 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 294 ELLFkkniLDLVNEFPEKIACSLHVtkqttqINAELKPYITEGRITEKEIRDHisKETLFYICGPPPMTDFFSKQLENNH 373
Cdd:cd06198  137 DAVF----LDELRALAAAAGVVLHV------IDSPSDGRLTLEQLVRALVPDL--ADADVWFCGPPGMADALEKGLRALG 204


                 ....*....
gi 767924570 374 VPKEHICFE 382
Cdd:cd06198  205 VPARRFHYE 213
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 161-379 1.31e-18

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 85.24  E-value: 1.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 161 QDFSFKAGQWVDFFIPGVSVVGgFSICSSPRlleQERVIELAVKYTNHPPALwVHNTCTLDCeVAVR--VGGEFffdpqP 238
Cdd:PRK08345  34 ESFTFKPGQFVQVTIPGVGEVP-ISICSSPT---RKGFFELCIRRAGRVTTV-IHRLKEGDI-VGVRgpYGNGF-----P 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 239 ADA--SRNLVLIAGGVGINPLLSILRHAADllreqankrNGYEIGTIKLFYSAKNTSELLFKKNILDLVNEfPEKIACSL 316
Cdd:PRK08345 103 VDEmeGMDLLLIAGGLGMAPLRSVLLYAMD---------NRWKYGNITLIYGAKYYEDLLFYDELIKDLAE-AENVKIIQ 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767924570 317 HVTKQT---TQINAELK--PYITEGRITEKEIRDHIS-KETLFYICGPPPMTDFFSKQLENNHVPKEHI 379
Cdd:PRK08345 173 SVTRDPewpGCHGLPQGfiERVCKGVVTDLFREANTDpKNTYAAICGPPVMYKFVFKELINRGYRPERI 241
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 146-379 1.42e-18

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: 1.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 146 SESPSVKSLRLLVADQD---FSFKAGQWVDFFIPGVsvvgG---FSICSSPrllEQERVIELAVK----YTNhppALwvH 215
Cdd:cd06221    6 DETEDIKTFTLRLEDDDeelFTFKPGQFVMLSLPGV----GeapISISSDP---TRRGPLELTIRrvgrVTE---AL--H 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 216 NTCTLDCeVAVRvgGEF---FfdPQPADASRNLVLIAGGVGINPLLSILRHAADllreqankrNGYEIGTIKLFYSAKNT 292
Cdd:cd06221   74 ELKPGDT-VGLR--GPFgngF--PVEEMKGKDLLLVAGGLGLAPLRSLINYILD---------NREDYGKVTLLYGARTP 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 293 SELLFKKNIldlvnefpEKIACSLHVTKQTTQINAELKPYITEGRITEkEIRDHI--SKETLFYICGPPPMTDFFSKQLE 370
Cdd:cd06221  140 EDLLFKEEL--------KEWAKRSDVEVILTVDRAEEGWTGNVGLVTD-LLPELTldPDNTVAIVCGPPIMMRFVAKELL 210


                 ....*....
gi 767924570 371 NNHVPKEHI 379
Cdd:cd06221  211 KLGVPEEQI 219
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 147-361 1.59e-18

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: 1.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 147 ESPSVKSLRLLVADQD-FSFKAGQWV--DFFIPGVSVVGGFSICSSPrllEQERVIELAVKYTnhPPAL---WVHNTCTL 220
Cdd:cd06215    9 ETPDVKTFRFAAPDGSlFAYKPGQFLtlELEIDGETVYRAYTLSSSP---SRPDSLSITVKRV--PGGLvsnWLHDNLKV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 221 DCEVAVR-VGGEFFFDPQPADasrNLVLIAGGVGINPLLSILRHAADlLREQANkrngyeigtIKLFYSAKNTSELLFKK 299
Cdd:cd06215   84 GDELWASgPAGEFTLIDHPAD---KLLLLSAGSGITPMMSMARWLLD-TRPDAD---------IVFIHSARSPADIIFAD 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767924570 300 NILDLVNEFPEkiaCSLHVTKQTTQINAELKPyitEGRITEKEIRDHIS--KETLFYICGPPPM 361
Cdd:cd06215  151 ELEELARRHPN---FRLHLILEQPAPGAWGGY---RGRLNAELLALLVPdlKERTVFVCGPAGF 208
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 230-364 3.78e-16

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


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 76.84  E-value: 3.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 230 GEFFFDPQpaDASRNLVLIAGGVGINPLLSILRHAADllreqankrNGYEIGTIKLFYSAKNTSELLFKKNILDLVNEFP 309
Cdd:cd06183   94 GKFEYKPN--GKVKHIGMIAGGTGITPMLQLIRAILK---------DPEDKTKISLLYANRTEEDILLREELDELAKKHP 162

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767924570 310 EKIACSLHVTKQTTQINAElkpyitEGRITEKEIRDHI----SKETLFYICGPPPMTDF 364
Cdd:cd06183  163 DRFKVHYVLSRPPEGWKGG------VGFITKEMIKEHLppppSEDTLVLVCGPPPMIEG 215
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 148-384 8.23e-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: 8.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 148 SPSVKSLRLlVADQDFSFKAGQWVDFFIPGV-SVVGGFSICSSPRlleQERVIELAVKytnHPPALWVhnTCTLDCEVAV 226
Cdd:cd06187    8 THDIAVVRL-QLDQPLPFWAGQYVNVTVPGRpRTWRAYSPANPPN---EDGEIEFHVR---AVPGGRV--SNALHDELKV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 227 ----RVG---GEFFFDPqpaDASRNLVLIAGGVGINPLLSILRhaaDLLREQANKRngyeigtIKLFYSAKNTSELLFKK 299
Cdd:cd06187   79 gdrvRLSgpyGTFYLRR---DHDRPVLCIAGGTGLAPLRAIVE---DALRRGEPRP-------VHLFFGARTERDLYDLE 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 300 NILDLVNEFPEkiacsLHVTKQTTQINAELKPYitEGRITEKEIRDHiskETL----FYICGPPPMTDFFSKQLENNHVP 375
Cdd:cd06187  146 GLLALAARHPW-----LRVVPVVSHEEGAWTGR--RGLVTDVVGRDG---PDWadhdIYICGPPAMVDATVDALLARGAP 215


                 ....*....
gi 767924570 376 KEHICFEKW 384
Cdd:cd06187  216 PERIHFDKF 224
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 247-367 2.05e-15

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: 2.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570  247 LIAGGVGINPLLSILRHaadLLREQANKRNgyeigtIKLFYSAKNTSELLFKKNILDLVNEFPEKiacsLHVTKQTTQIN 326
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRA---ILEDPKDPTQ------VVLVFGNRNEDDILYREELDELAEKHPGR----LTVVYVVSRPE 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767924570  327 AElkPYITEGRITEKEIRDHISK---ETLFYICGPPPMTDFFSK 367
Cdd:pfam00175  68 AG--WTGGKGRVQDALLEDHLSLpdeETHVYVCGPPGMIKAVRK 109
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 164-383 2.38e-15

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: 2.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 164 SFKAGQWVDFFIPGVSVVGGFSICSSPrllEQERVIELAVKytnHPP--ALwvhnTCTL--DCEVAVRVG-----GEFFF 234
Cdd:cd06190   23 DFLPGQYALLALPGVEGARAYSMANLA---NASGEWEFIIK---RKPggAA----SNALfdNLEPGDELEldgpyGLAYL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 235 DPqpaDASRNLVLIAGGVGINPLLSILRHAAdllreqankRNGYEIG-TIKLFYSAKNTSELLFkkniLDLVNEFPEKIA 313
Cdd:cd06190   93 RP---DEDRDIVCIAGGSGLAPMLSILRGAA---------RSPYLSDrPVDLFYGGRTPSDLCA----LDELSALVALGA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767924570 314 cSLHVTKQTTQINAELKPYIT--EGRITEkEIRDHIS---KETLFYICGPPPMTDFFSKQLENNH-VPKEHICFEK 383
Cdd:cd06190  157 -RLRVTPAVSDAGSGSAAGWDgpTGFVHE-VVEATLGdrlAEFEFYFAGPPPMVDAVQRMLMIEGvVPFDQIHFDR 230
PRK13289 PRK13289
NO-inducible flavohemoprotein;
230-382 4.59e-15

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 75.99  E-value: 4.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 230 GEFFFDPQPadaSRNLVLIAGGVGINPLLSILRHAAdllrEQANKRNgyeigtIKLFYSAKNTSELLFKKNILDLVNEFP 309
Cdd:PRK13289 252 GDFFLDVAS---DTPVVLISGGVGITPMLSMLETLA----AQQPKRP------VHFIHAARNGGVHAFRDEVEALAARHP 318

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767924570 310 ekiacSLHVT---KQTTQINAELKPYITEGRITEKEIRDHI-SKETLFYICGPPPMTDFFSKQLENNHVPKEHICFE 382
Cdd:PRK13289 319 -----NLKAHtwyREPTEQDRAGEDFDSEGLMDLEWLEAWLpDPDADFYFCGPVPFMQFVAKQLLELGVPEERIHYE 390
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 139-379 5.34e-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: 73.35  E-value: 5.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 139 AKVCGAASESPSVKSLRLLVaDQDFSFKAGQWVDFFIPGVSVVGgFSICSSPRlleQERVIELAVKytnhppaLWVHNTC 218
Cdd:cd06189    1 CKVESIEPLNDDVYRVRLKP-PAPLDFLAGQYLDLLLDDGDKRP-FSIASAPH---EDGEIELHIR-------AVPGGSF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 219 T------LDCEVAVRV---GGEFFFDPqpaDASRNLVLIAGGVGINPLLSILRHaadlLREQANKRNgyeigtIKLFYSA 289
Cdd:cd06189   69 SdyvfeeLKENGLVRIegpLGDFFLRE---DSDRPLILIAGGTGFAPIKSILEH----LLAQGSKRP------IHLYWGA 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 290 KNTSELLFkknildlvNEFPEKIACS---LHVTKQTTQINAElkPYITEGRITEKEIRDHIS-KETLFYICGPPPMTDFF 365
Cdd:cd06189  136 RTEEDLYL--------DELLEAWAEAhpnFTYVPVLSEPEEG--WQGRTGLVHEAVLEDFPDlSDFDVYACGSPEMVYAA 205

                        250
                 ....*....|....
gi 767924570 366 SKQLENNHVPKEHI 379
Cdd:cd06189  206 RDDFVEKGLPEENF 219
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 246-382 2.03e-13

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: 2.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 246 VLIAGGVGINPLLSILRhaaDLLREQANKRNgyeigtiKLFYSAKNTSELLFKKNILDLVNEfpekiACSLHVTKQTTQi 325
Cdd:cd06196  103 VFIAGGAGITPFIAILR---DLAAKGKLEGN-------TLIFANKTEKDIILKDELEKMLGL-----KFINVVTDEKDP- 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767924570 326 naelkPYITeGRITEKEIRDHISKET-LFYICGPPPMTDFFSKQLENNHVPKEHICFE 382
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 ...
 154-379 2.88e-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: 2.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 154 LRLLVA-DQDFSFKAGQWVDFFIPGVSVVGGFSICSSPRlleQERVIELAVKytnHPPA----LWVHNTCTLDCEVAVRV 228
Cdd:cd06213   16 VRLTVQlDRPIAYKAGQYAELTLPGLPAARSYSFANAPQ---GDGQLSFHIR---KVPGgafsGWLFGADRTGERLTVRG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 229 -GGEFFFdpQPADASrnLVLIAGGVGINPLLSILRHAadllREQANKRNgyeigtIKLFYSAKnTSELLFKkniLDlvne 307
Cdd:cd06213   90 pFGDFWL--RPGDAP--ILCIAGGSGLAPILAILEQA----RAAGTKRD------VTLLFGAR-TQRDLYA---LD---- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 308 fpekiacSLHVTKQTTQINAELKPYITE-----------GRITEKeIRDHISKETLFYICGPPPMTDFFSKQLENNHVPK 376
Cdd:cd06213  148 -------EIAAIAARWRGRFRFIPVLSEepadsswkgarGLVTEH-IAEVLLAATEAYLCGPPAMIDAAIAVLRALGIAR 219


                 ...
gi 767924570 377 EHI 379
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 ...
 147-363 3.42e-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: 3.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 147 ESPSVKSLRLLVADQDFSFKAGQWVDFFIP--GVSVVGGFSICSSPRllEQERVIELAVKytNHPPAL---WVHNtctld 221
Cdd:cd06216   28 ETADMVTLTLRPNRGWPGHRAGQHVRLGVEidGVRHWRSYSLSSSPT--QEDGTITLTVK--AQPDGLvsnWLVN----- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 222 cevAVRVG---------GEFFF-DPQPADasrnLVLIAGGVGINPLLSILRhaaDLLREQankrngyEIGTIKLFYSAKN 291
Cdd:cd06216   99 ---HLAPGdvvelsqpqGDFVLpDPLPPR----LLLIAAGSGITPVMSMLR---TLLARG-------PTADVVLLYYART 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767924570 292 TSELLFKKNILDLVNEFPekiacSLHVTKQTTQinAELKPYITEGRIteKEIrDHISKETLFYICGPPPMTD 363
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) ...
 148-383 5.67e-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: 68.48  E-value: 5.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 148 SPSVKSLRL-LVADQDFSFKAGQWVDFFIPGVS-------------------------------VVGGFSICSSPrllEQ 195
Cdd:cd06188   21 ATFIKELVLkLPSGEEIAFKAGGYIQIEIPAYEiayadfdvaekyradwdkfglwqlvfkhdepVSRAYSLANYP---AE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 196 ERVIELAVKYTNHPPAL----------WVHNtctLDCEVAVRVGG--EFFFDPqpaDASRNLVLIAGGVGINPLLSILRH 263
Cdd:cd06188   98 EGELKLNVRIATPPPGNsdippgigssYIFN---LKPGDKVTASGpfGEFFIK---DTDREMVFIGGGAGMAPLRSHIFH 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 264 aadLLREQANKRNgyeigtIKLFYSAKNTSELLFKKNILDLVNEFPEkiaCSLHVTKQTTQINAELKPYIteGRITEKEI 343
Cdd:cd06188  172 ---LLKTLKSKRK------ISFWYGARSLKELFYQEEFEALEKEFPN---FKYHPVLSEPQPEDNWDGYT--GFIHQVLL 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 767924570 344 ----RDHISKETL-FYICGPPPMTDFFSKQLENNHVPKEHICFEK 383
Cdd:cd06188  238 enylKKHPAPEDIeFYLCGPPPMNSAVIKMLDDLGVPRENIAFDD 282
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 148-383 3.18e-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: 3.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 148 SPSVKSLRL-LVADQDFSFKAGQWVDFFIPGVSVVGGFSICSSPrlleQERVIELAVKytNHPPAL---WVHNTCTLDCE 223
Cdd:cd06209   13 SDSTIGLTLeLDEAGALAFLPGQYVNLQVPGTDETRSYSFSSAP----GDPRLEFLIR--LLPGGAmssYLRDRAQPGDR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 224 VAVRvG--GEFFFDPQPadasRNLVLIAGGVGINPLLSILrhaaDLLREQANKRngyeigTIKLFYSAKNTSELlFKkni 301
Cdd:cd06209   87 LTLT-GplGSFYLREVK----RPLLMLAGGTGLAPFLSML----DVLAEDGSAH------PVHLVYGVTRDADL-VE--- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 302 LDLVNEFPEKI-ACSLHVTKQTTQINAELKPYITEGrITEKEIRDhisKETLFYICGPPPMTDFFSKQLENNHVPKEHIC 380
Cdd:cd06209  148 LDRLEALAERLpGFSFRTVVADPDSWHPRKGYVTDH-LEAEDLND---GDVDVYLCGPPPMVDAVRSWLDEQGIEPANFY 223


                 ...
gi 767924570 381 FEK 383
Cdd:cd06209  224 YEK 226
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 139-384 1.23e-11

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: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 139 AKVCGAASESPSVKSLRLLVADQD-FSFKAGQWVDF--FIPGVSVVGGFSICSSPRLLEqervIELAVKYTnhPPAL--- 212
Cdd:cd06191    1 LRVAEVRSETPDAVTIVFAVPGPLqYGFRPGQHVTLklDFDGEELRRCYSLCSSPAPDE----ISITVKRV--PGGRvsn 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 213 WVHNTCTLDCEVAVRVG-GEFFFDPQPAdasRNLVLIAGGVGINPLLSILRHAADLLREQankrngyeigTIKLFYSAKN 291
Cdd:cd06191   75 YLREHIQPGMTVEVMGPqGHFVYQPQPP---GRYLLVAAGSGITPLMAMIRATLQTAPES----------DFTLIHSART 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 292 TSELLFKKNILDLVNEfPEKIACSLHVTKQTTQINAELKPYITEGRITEKEIRDHISKETlfYICGPPPMTDFFSKQLEN 371
Cdd:cd06191  142 PADMIFAQELRELADK-PQRLRLLCIFTRETLDSDLLHGRIDGEQSLGAALIPDRLEREA--FICGPAGMMDAVETALKE 218

                        250
                 ....*....|...
gi 767924570 372 NHVPKEHICFEKW 384
Cdd:cd06191  219 LGMPPERIHTERF 231
PLN02252 PLN02252
nitrate reductase [NADPH]
 230-364 2.31e-11

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 65.47  E-value: 2.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 230 GEFFFDPQPADASRnLVLIAGGVGINPLLSILRHAadlLREQANKRngyeigTIKLFYSAKNTSELLFKKNILDLVNEFP 309
Cdd:PLN02252 747 GSFLVNGKPKFAKK-LAMLAGGTGITPMYQVIQAI---LRDPEDKT------EMSLVYANRTEDDILLREELDRWAAEHP 816

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767924570 310 EKiacsLHVTKQTTQINAELKPYITeGRITEKEIRDHI---SKETLFYICGPPPMTDF 364
Cdd:PLN02252 817 DR----LKVWYVVSQVKREGWKYSV-GRVTEAMLREHLpegGDETLALMCGPPPMIEF 869
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 136-383 2.54e-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: 2.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 136 VSAAKVCGAASESPSVKSLRL-----LVADQDFSFKAGQWVDFFIPGVSVVGGFSICSSP----RLleqERVIELAvkyt 206
Cdd:cd06210    1 VREAEIVAVDRVSSNVVRLRLqpddaEGAGIAAEFVPGQFVEIEIPGTDTRRSYSLANTPnwdgRL---EFLIRLL---- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 207 nhpPALWVHNTCTLDCEVAVRVG-----GEFFFDpqpADASRNLVLIAGGVGINPLLSILRHAAdllREQANkrngyeiG 281
Cdd:cd06210   74 ---PGGAFSTYLETRAKVGQRLNlrgplGAFGLR---ENGLRPRWFVAGGTGLAPLLSMLRRMA---EWGEP-------Q 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 282 TIKLFYSAKNTSELLFKKNILDLVNEFPekiacslhvtkQTTQINAELKPYIT-EG-RITEKEI-RDHISKETL---FYI 355
Cdd:cd06210  138 EARLFFGVNTEAELFYLDELKRLADSLP-----------NLTVRICVWRPGGEwEGyRGTVVDAlREDLASSDAkpdIYL 206

                        250       260
                 ....*....|....*....|....*...
gi 767924570 356 CGPPPMTDFFSKQLENNHVPKEHICFEK 383
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 ...
 148-379 3.83e-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: 3.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 148 SPSVKSLRLLVaDQDFSFKAGQWVDFFIPGVsVVGGFSICSSPrllEQERVIELAVK-YTNHPPALWVHNTCTLDCEVAV 226
Cdd:cd06194    8 SPDVLRVRLEP-DRPLPYLPGQYVNLRRAGG-LARSYSPTSLP---DGDNELEFHIRrKPNGAFSGWLGEEARPGHALRL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 227 R--VGGEFFFDPQPADasrNLVLIAGGVGINPLLSILRHAadLLREQAnkrngyeiGTIKLFYSAKNTSELLFKKNILDL 304
Cdd:cd06194   83 QgpFGQAFYRPEYGEG---PLLLVGAGTGLAPLWGIARAA--LRQGHQ--------GEIRLVHGARDPDDLYLHPALLWL 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767924570 305 VNEFPEkiacsLHVTKQTTQiNAELKPYITEGRITEKEIrdHISKETLFYICGPPPMTDFFSKQLENNHVPKEHI 379
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) ...
 184-262 4.18e-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: 4.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 184 FSICSSPRLLEQERVIELAVKY----TNHppaLWVHNTCTLDCEVAVRV---GGEFFFDPQPADASRNLVLIAGGVGINP 256
Cdd:cd06197   63 FTVSSAPPHDPATDEFEITVRKkgpvTGF---LFQVARRLREQGLEVPVlgvGGEFTLSLPGEGAERKMVWIAGGVGITP 139


                 ....*.
gi 767924570 257 LLSILR 262
Cdd:cd06197  140 FLAMLR 145
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 238-378 1.40e-09

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: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 238 PADASRNLVLIAGGVGINPLLSILRHaadLLREQANKRNgyEIGTIKLFYSAKNTSELLFKKNILDLVNEFPEKIACSLH 317
Cdd:cd06208  131 PEDPNATLIMIATGTGIAPFRSFLRR---LFREKHADYK--FTGLAWLFFGVPNSDSLLYDDELEKYPKQYPDNFRIDYA 205

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767924570 318 VTKQTTQINAElKPYITEgRITE--KEIRDHISKE-TLFYICG----PPPMTDFFSKQLENNHVPKEH 378
Cdd:cd06208  206 FSREQKNADGG-KMYVQD-RIAEyaEEIWNLLDKDnTHVYICGlkgmEPGVDDALTSVAEGGLAWEEF 271
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 153-383 2.56e-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: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 153 SLRLlVADQDFSFKAGQWVDFFIP---GVSVVGGFSICSSPrlleQERVIELAVKYTNHPPA---LWvhntctldcevAV 226
Cdd:cd06195   14 SFRV-TRDIPFRFQAGQFTKLGLPnddGKLVRRAYSIASAP----YEENLEFYIILVPDGPLtprLF-----------KL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 227 RVGGEFFFDPQPA--------DASRNLVLIAGGVGINPLLSILRHAADLLREQankrngyeigTIKLFYSAKNTSELLFk 298
Cdd:cd06195   78 KPGDTIYVGKKPTgfltldevPPGKRLWLLATGTGIAPFLSMLRDLEIWERFD----------KIVLVHGVRYAEELAY- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 299 kniLDLVNEFPEKIACSLHVTKQTTQinaELKPYITEGRITE----KEIRDHI-----SKETLFYICGPPPMTDFFSKQL 369
Cdd:cd06195  147 ---QDEIEALAKQYNGKFRYVPIVSR---EKENGALTGRIPDliesGELEEHAglpldPETSHVMLCGNPQMIDDTQELL 220

                        250       260
                 ....*....|....*....|
gi 767924570 370 ENN----HVPKE--HICFEK 383
Cdd:cd06195  221 KEKgfskNHRRKpgNITVEK 240
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 147-382 9.08e-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: 9.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 147 ESPSVKSLRLLVADQDF--SFKAGQWVDffipgVSVVGGF----SICSSPRllEQERViELAVKytnHPPA-----LWVH 215
Cdd:cd06185    6 EAPDIRSFELEAPDGAPlpAFEPGAHID-----VHLPNGLvrqySLCGDPA--DRDRY-RIAVL---REPAsrggsRYMH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 216 NTCTLDCEVAVRVGGEFFfdPQPADASRNlVLIAGGVGINPLLSILRHAAdllREQANkrngYEigtikLFYSAKNTSEL 295
Cdd:cd06185   75 ELLRVGDELEVSAPRNLF--PLDEAARRH-LLIAGGIGITPILSMARALA---ARGAD----FE-----LHYAGRSREDA 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 296 LFkkniLDLVNEFPEKiACSLHVTKQTTQINAElkpyitegritekEIRDHISKETLFYICGPPPMTDFFSKQLENNHVP 375
Cdd:cd06185  140 AF----LDELAALPGD-RVHLHFDDEGGRLDLA-------------ALLAAPPAGTHVYVCGPEGMMDAVRAAAAALGWP 201


                 ....*..
gi 767924570 376 KEHICFE 382
Cdd:cd06185  202 EARLHFE 208
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 161-382 1.13e-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: 54.62  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 161 QDFSFKAGQWVdfFI--PGVSVVGG---FSICSSPRLLEQErvIELAVK----YTNHppaLWVHNTCTLDCEVAVRVgge 231
Cdd:cd06186   21 KPFKWKPGQHV--YLnfPSLLSFWQshpFTIASSPEDEQDT--LSLIIRakkgFTTR---LLRKALKSPGGGVSLKV--- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 232 fFFD------PQPADASRNLVLIAGGVGINPLLSILRhaaDLLREQANKRNgyeIGTIKLFYSAKNTSELLFKKNILDLV 305
Cdd:cd06186   91 -LVEgpygssSEDLLSYDNVLLVAGGSGITFVLPILR---DLLRRSSKTSR---TRRVKLVWVVRDREDLEWFLDELRAA 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767924570 306 NEFPEKIACSLHVTKqttqinaelkpyitegritekeirdhisketlFYICGPPPMTDFFSKQLENNHVPKEHICFE 382
Cdd:cd06186  164 QELEVDGEIEIYVTR--------------------------------VVVCGPPGLVDDVRNAVAKKGGTGVEFHEE 208
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
243-368 3.83e-08

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 51.96  E-value: 3.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570  243 RNLVLIAGGVGINPLLSILRHAADLLREQANKRngyeigtIKLFYSAKNTSEL-LFKKNILDLVNEFPEKIACSLHVT-- 319
Cdd:pfam08030   2 ENVLLVAGGIGITPFISILKDLGNKSKKLKTKK-------IKFYWVVRDLSSLeWFKDVLNELEELKELNIEIHIYLTge 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767924570  320 -------------KQTTQINAELKPYITEGRIT------------EKEIRDHISKETLFYICGPPPMTDFFSKQ 368
Cdd:pfam08030  75 yeaedasdqsdssIRSENFDSLMNEVIGVDFVEfhfgrpnwkevlKDIAKQHPNGSIGVFSCGPPSLVDELRNL 148
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 243-361 4.79e-07

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 52.09  E-value: 4.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570  243 RNLVLIAGGVGINPLLSILRHAadllreqANKRNGYEIGTIKLFYSAKNTSELLFKKNILDLVNEFPEKIACSLHVTKQT 322
Cdd:PTZ00306 1032 RKLALIAGGTGVAPMLQIIRAA-------LKKPYVDSIESIRLIYAAEDVSELTYRELLESYRKENPGKFKCHFVLNNPP 1104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767924570  323 TQinaelkpyITE--GRITEKEIRDHI---SKETLFYICGPPPM 361
Cdd:PTZ00306 1105 EG--------WTDgvGFVDRALLQSALqppSKDLLVAICGPPVM 1140
BenC NF040810
benzoate 1,2-dioxygenase electron transfer component BenC;
148-383 1.14e-06

benzoate 1,2-dioxygenase electron transfer component BenC;


Pssm-ID: 468751 [Multi-domain]  Cd Length: 333  Bit Score: 49.82  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 148 SPSVKSLRL-LVADQDFSFKAGQWVDFFIPGVSVVGGFSICSSPrlleQERVIELAVKytNHPPAL---WVHNTCtldce 223
Cdd:NF040810 116 SDSTIELSLdLDDDAALAFLPGQYVNIQVPGTGQTRSYSFSSLP----GAREASFLIR--NVPGGLmssYLTERA----- 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 224 vavRVG---------GEFFFdpqpADASRNLVLIAGGVGINPLLSILRHaadlLREQANKRngyeigTIKLFYSAKNTse 294
Cdd:NF040810 185 ---KPGdrlsltgplGSFYL----REVTRPLLMLAGGTGLAPFLSMLEV----LAEQGSEQ------PVHLIYGVTRD-- 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 295 llfkkniLDLV-----NEFPEKIAcslHVTKQTTQINAE----LKPYITegritekeirDHISKETL------FYICGPP 359
Cdd:NF040810 246 -------ADLVeverlEAFAARLP---NFTFRTCVADAAsahpRKGYVT----------QHIEAEWLndgdvdVYLCGPP 305

                        250       260
                 ....*....|....*....|....
gi 767924570 360 PMTDFFSKQLENNHVPKEHICFEK 383
Cdd:NF040810 306 PMVDAVRGWFREQGITPASFHYEK 329
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 147-383 3.50e-06

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 48.55  E-value: 3.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 147 ESPSVKSLRLLvaDQDF-SFKAGQWVDffipgVSVVG------GFSICSSPRLleqERVIELAVK-YTNHPPALWVHNTc 218
Cdd:PRK10684  20 ETPDVWTISLI--CHDFyPYRAGQYAL-----VSIRNsaetlrAYTLSSTPGV---SEFITLTVRrIDDGVGSQWLTRD- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 219 tldcevaVRVG---------GEFFFDPQPADasrNLVLIAGGVGINPLLSILRHaadLL--REQANkrngyeigtIKLFY 287
Cdd:PRK10684  89 -------VKRGdylwlsdamGEFTCDDKAED---KYLLLAAGCGVTPIMSMRRW---LLknRPQAD---------VQVIF 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 288 SAKNTSELLFKKNILDLVNEFPEkiacsLHVTkqttqINAELK--PYITEGRITEKEIRDH---ISKETLFyICGPPPMT 362
Cdd:PRK10684 147 NVRTPQDVIFADEWRQLKQRYPQ-----LNLT-----LVAENNatEGFIAGRLTRELLQQAvpdLASRTVM-TCGPAPYM 215

                        250       260
                 ....*....|....*....|.
gi 767924570 363 DFFSKQLENNHVPKEHICFEK 383
Cdd:PRK10684 216 DWVEQEVKALGVTADRFFKEK 236
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 233-383 5.20e-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: 5.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 233 FFDPqpaDASRNLVLIAGGVGINPLLsilrHAADLLREQANKrngyeigtIKLFYSAKNTSELLfkknildLVNEFpEKI 312
Cdd:cd06218   92 FDLP---DDDGKVLLVGGGIGIAPLL----FLAKQLAERGIK--------VTVLLGFRSADDLF-------LVEEF-EAL 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767924570 313 ACSLHVTkqTTQINAELKPYITEgrITEKEIRDhiSKETLFYICGPPPMTDFFSKQLENNHVPKEhICFEK 383
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 ...
 143-358 7.66e-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: 7.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 143 GAASESPSVKSLRLLVAD----QDFSFKAGQWVDFFIPGVSVVGGFSICSSPRllEQERVIELAVKYTNHPPALWVHNT- 217
Cdd:cd06182    6 RKLTPPDSPRSTRHLEFDlsgnSVLKYQPGDHLGVIPPNPLQPRYYSIASSPD--VDPGEVHLCVRVVSYEAPAGRIRKg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 218 ------CTLD----CEVAVRVGGEFFFdpqPADASRNLVLIAGGVGINPLLSILRHAAdllreqANKRNGYEIGTIKLFY 287
Cdd:cd06182   84 vcsnflAGLQlgakVTVFIRPAPSFRL---PKDPTTPIIMVGPGTGIAPFRGFLQERA------ALRANGKARGPAWLFF 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767924570 288 SAKN-TSELLFKKNIldlvNEFPEKIACS-LHVTKQTTQinAELKPYITEgRITE--KEIRDHISKETLFYICGP 358
Cdd:cd06182  155 GCRNfASDYLYREEL----QEALKDGALTrLDVAFSREQ--AEPKVYVQD-KLKEhaEELRRLLNEGAHIYVCGD 222
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 147-361 1.07e-05

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 46.40  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 147 ESPSVKSLRLlVADQDFSFKAGQWVDFFIPGVSVVGG--FSICssprlleqervielavkYTNHppalwvhntctLDCEV 224
Cdd:PRK00054  15 IAPNIYTLVL-DGEKVFDMKPGQFVMVWVPGVEPLLErpISIS-----------------DIDK-----------NEITI 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 225 AVRVGGEF---FFDPQPAD----------------ASRNLVLIAGGVGINPLLSIlrhaADLLREqankrNGYEIGTIkl 285
Cdd:PRK00054  66 LYRKVGEGtkkLSKLKEGDeldirgplgngfdleeIGGKVLLVGGGIGVAPLYEL----AKELKK-----KGVEVTTV-- 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767924570 286 fYSAKNTSELLFKKnildlvnEFPEkiACSLHVTKQTTQinaelkpYITEGRITEKeIRDHISKETLFYICGPPPM 361
Cdd:PRK00054 135 -LGARTKDEVIFEE-------EFAK--VGDVYVTTDDGS-------YGFKGFVTDV-LDELDSEYDAIYSCGPEIM 192
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
138-379 2.53e-05

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 45.49  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 138 AAKVCGAASESPSVKSLRLLvADQDFSFKAGQWVDFFIPGvSVVGGFSICSSPrllEQERVIELAVKyTNHPPALwvhnt 217
Cdd:PRK05713  93 PARVVALDWLGGDVLRLRLE-PERPLRYRAGQHLVLWTAG-GVARPYSLASLP---GEDPFLEFHID-CSRPGAF----- 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 218 ctldCEVAVRV------------GGEFFFDPQPADasRNLVLIAGGVGINPLLSILRHAAdllreqankRNGYEiGTIKL 285
Cdd:PRK05713 162 ----CDAARQLqvgdllrlgelrGGALHYDPDWQE--RPLWLLAAGTGLAPLWGILREAL---------RQGHQ-GPIRL 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 286 FYSAKNTSELLFKKNILDLVNEFPEkIACSLHVTKQTTQINAELKPyitegritekeirdhISKETLFYICGPPPMTDFF 365
Cdd:PRK05713 226 LHLARDSAGHYLAEPLAALAGRHPQ-LSVELVTAAQLPAALAELRL---------------VSRQTMALLCGSPASVERF 289

                        250
                 ....*....|....
gi 767924570 366 SKQLENNHVPKEHI 379
Cdd:PRK05713 290 ARRLYLAGLPRNQL 303
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
241-384 4.28e-05

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 45.12  E-value: 4.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 241 ASRNLVLIAGGVGINPLLSILrhaaDLLREQANKRngyeigTIKLFYSAKNTSELLFKKNIldlvNEFPEKIAcslhvtk 320
Cdd:PRK11872 208 VERPLVFVAGGTGLSAFLGML----DELAEQGCSP------PVHLYYGVRHAADLCELQRL----AAYAERLP------- 266

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767924570 321 qttqiNAELKPYITE---------GRITEKEIRDHISKETL-FYICGPPPMTDFFSKQLENNHVPKEHICFEKW 384
Cdd:PRK11872 267 -----NFRYHPVVSKasadwqgkrGYIHEHFDKAQLRDQAFdMYLCGPPPMVEAVKQWLDEQALENYRLYYEKF 335
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 247-371 1.33e-04

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 43.28  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 247 LIAGGVGINPLLSILRhaadllreqANKRNGYEIGTIKLFYSAKNTSELLFKKNILDLVNEFPEKIACSLhvTKQTTqin 326
Cdd:PTZ00319 171 MIAGGTGITPMLQIIH---------AIKKNKEDRTKVFLVYANQTEDDILLRKELDEAAKDPRFHVWYTL--DREAT--- 236

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767924570 327 AELKpyITEGRITEKEIRDHI---------SKETLFYICGPPPMTDFFSK-QLEN 371
Cdd:PTZ00319 237 PEWK--YGTGYVDEEMLRAHLpvpdpqnsgIKKVMALMCGPPPMLQMAVKpNLEK 289
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
 165-357 1.96e-04

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 43.07  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 165 FKAGQWVDFFIPGVSVVGG------FSICSS-PRLLEQERVIELAVK---YTNHPPALwVHNTCT---------LDCEVA 225
Cdd:PLN03115 123 YREGQSIGVIPDGIDKNGKphklrlYSIASSaLGDFGDSKTVSLCVKrlvYTNDQGEI-VKGVCSnflcdlkpgAEVKIT 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 226 VRVGGEFFFdpqPADASRNLVLIAGGVGINPLLSIlrhaadLLREQANKRNGYEI-GTIKLFYSAKNTSELLFKKNILDL 304
Cdd:PLN03115 202 GPVGKEMLM---PKDPNATIIMLATGTGIAPFRSF------LWKMFFEKHDDYKFnGLAWLFLGVPTSSSLLYKEEFEKM 272

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767924570 305 VNEFPEKIACSLHVTKQTTQINAElKPYItEGRITE--KEIRDHISKE-TLFYICG 357
Cdd:PLN03115 273 KEKAPENFRLDFAVSREQTNAKGE-KMYI-QTRMAEyaEELWELLKKDnTYVYMCG 326
PLN02631 PLN02631
ferric-chelate reductase
 184-373 3.06e-04

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 42.72  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 184 FSICSSPRLlEQERVIELAVKYTNHPPALWVHNTCTLDcevAVRVGGEFFFDPQPADASRN--LVLIAGGVGINPLLSIL 261
Cdd:PLN02631 356 FTITSSSNL-EKDTLSVVIRRQGSWTQKLYTHLSSSID---SLEVSTEGPYGPNSFDVSRHnsLILVSGGSGITPFISVI 431

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 262 RhaaDLLREQANKRNgyEIGTIKLFYSAKNTSELLFkkniLDLVneFPEKIACSlhvtkQTTQINAELKPYITEGRITEK 341
Cdd:PLN02631 432 R---ELIFQSQNPST--KLPDVLLVCSFKHYHDLAF----LDLI--FPLDISVS-----DISRLNLRIEAYITREDKKPE 495

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767924570 342 EIRDHISKETLFYicGPPPMTDFFSKQLENNH 373
Cdd:PLN02631 496 TTDDHRLLQTKWF--KPQPLDSPISPVLGPNN 525
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
 184-357 4.95e-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: 4.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 184 FSICSSPRllEQERVIELAVKYTNHP-PAL---WVHNTCTLDCEVAVRVggEFFFDPQ------PADASRNLVLIAGGVG 253
Cdd:cd06203  177 YSIASSPL--EGPGKLRFIFSVVEFPaKGLctsWLESLCLSASSHGVKV--PFYLRSSsrfrlpPDDLRRPIIMVGPGTG 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 254 INPLLSILRHAADLLREQANKrngyEIGTIKLFYSAKNTSE-LLFKKNILDLVNefpEKIACSLHVTKQTTQINAELKPY 332
Cdd:cd06203  253 VAPFLGFLQHREKLKESHTET----VFGEAWLFFGCRHRDRdYLFRDELEEFLE---EGILTRLIVAFSRDENDGSTPKY 325

                        170       180
                 ....*....|....*....|....*...
gi 767924570 333 ITEGrITE--KEIRDHISKE-TLFYICG 357
Cdd:cd06203  326 VQDK-LEErgKKLVDLLLNSnAKIYVCG 352
PLN02292 PLN02292
ferric-chelate reductase
 224-346 6.09e-04

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 41.78  E-value: 6.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 224 VAVRVGGEFffDPQPADASRN--LVLIAGGVGINPLLSILRhaaDLLreQANKRNGYEIGTIKLFYSAKNTSELlfkkNI 301
Cdd:PLN02292 413 LAVSVEGPY--GPASTDFLRHesLVMVSGGSGITPFISIIR---DLI--YTSSTETCKIPKITLICAFKNSSDL----SM 481

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767924570 302 LDLVnefpekIACSLHVTKQTTQINAELKPYITEGRITEKEIRDH 346
Cdd:PLN02292 482 LDLI------LPTSGLETELSSFIDIQIKAFVTREKEAGVKESTG 520
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 184-352 7.08e-04

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 41.76  E-value: 7.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 184 FSICSSPRLleQERVIELAVK----YTNhppALWVHNTCTLDCE------VAVRVGGEFffDPQPADASR--NLVLIAGG 251
Cdd:PLN02844 360 FSITSSSNI--DDHTMSVIIKceggWTN---SLYNKIQAELDSEtnqmncIPVAIEGPY--GPASVDFLRydSLLLVAGG 432

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 252 VGINPLLSILRHAAdllreqANKRNGYEIGT-IKLFYSAKNTSELlfkkNILDLVNefpekiacSLHVTKQTTQINAELK 330
Cdd:PLN02844 433 IGITPFLSILKEIA------SQSSSRYRFPKrVQLIYVVKKSQDI----CLLNPIS--------SLLLNQSSNQLNLKLK 494

                        170       180
                 ....*....|....*....|..
gi 767924570 331 PYITEGRITEKEIRDHISKETL 352
Cdd:PLN02844 495 VFVTQEEKPNATLRELLNQFSQ 516
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 242-380 1.60e-03

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


Pssm-ID: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 39.62  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 242 SRNLVLIAGGVGINPLLSILRHaadlLREQANKrngyeigtIKLFYSAKntsellfKKNILDLVNEFPEkiacSLHVTKQ 321
Cdd:cd06192   97 GGTVLLVAGGIGLAPLLPIAKK----LAANGNK--------VTVLAGAK-------KAKEEFLDEYFEL----PADVEIW 153

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767924570 322 TTqinaELKPYITEGRITEKEIRDHISKETLFYICGPPPMTDFFSKQLENNHVPKEHIC 380
Cdd:cd06192  154 TT----DDGELGLEGKVTDSDKPIPLEDVDRIIVAGSDIMMKAVVEALDEWLQLIKASV 208
DHOD_e_trans_like1 cd06219
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 244-367 5.19e-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: 5.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767924570 244 NLVLIAGGVGINPLLSILRHaadlLREQankrnGYEIGTIKLFYSAkntsELLFkknildLVNEFpEKIACSLHVTkqTT 323
Cdd:cd06219   99 TVVFVGGGVGIAPIYPIAKA----LKEA-----GNRVITIIGARTK----DLVI------LEDEF-RAVSDELIIT--TD 156

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767924570 324 QINAELKPYITEGRiteKEIRDHISKETLFYICGPPPMTDFFSK 367
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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