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Conserved domains on  [gi|1796985942|gb|QHG88711|]
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ferredoxin--NADP reductase [Xanthomonas cucurbitae]

Protein Classification

ferredoxin--NADP reductase( domain architecture ID 10153094)

ferredoxin--NADP reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin

EC:  1.18.1.2
Gene Ontology:  GO:0004324
SCOP:  4003770|4002840

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
8-245 8.54e-74

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: 224.75  E-value: 8.54e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   8 KLVDRRMLAPTvaHCQFVRDDGQPLDFQPGQFIQIHFAAADGTPTKRSYSLATIHDHalgpgEAVDIAVSFVPGGSATAL 87
Cdd:cd06195     1 TVLKRRDWTDD--LFSFRVTRDIPFRFQAGQFTKLGLPNDDGKLVRRAYSIASAPYE-----ENLEFYIILVPDGPLTPR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  88 FEGLEIGDPLQAS-GPYGRFCLQAGDHNQRYVLIATGTGVTPYRSMLPLLaeAIASRSVQVVLLQGARTPAELLYGDDFR 166
Cdd:cd06195    74 LFKLKPGDTIYVGkKPTGFLTLDEVPPGKRLWLLATGTGIAPFLSMLRDL--EIWERFDKIVLVHGVRYAEELAYQDEIE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 167 AFAQAH-PQFRYLPCLSRELPAPAHadvrHGYVQQHLAE--------IAPDASTDIAYLCGNPDMVDACAEALKAAGLP- 236
Cdd:cd06195   152 ALAKQYnGKFRYVPIVSREKENGAL----TGRIPDLIESgeleehagLPLDPETSHVMLCGNPQMIDDTQELLKEKGFSk 227
                         250
                  ....*....|....
gi 1796985942 237 -----NAQIRREKY 245
Cdd:cd06195   228 nhrrkPGNITVEKY 241
 
Name Accession Description Interval E-value
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
8-245 8.54e-74

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: 224.75  E-value: 8.54e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   8 KLVDRRMLAPTvaHCQFVRDDGQPLDFQPGQFIQIHFAAADGTPTKRSYSLATIHDHalgpgEAVDIAVSFVPGGSATAL 87
Cdd:cd06195     1 TVLKRRDWTDD--LFSFRVTRDIPFRFQAGQFTKLGLPNDDGKLVRRAYSIASAPYE-----ENLEFYIILVPDGPLTPR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  88 FEGLEIGDPLQAS-GPYGRFCLQAGDHNQRYVLIATGTGVTPYRSMLPLLaeAIASRSVQVVLLQGARTPAELLYGDDFR 166
Cdd:cd06195    74 LFKLKPGDTIYVGkKPTGFLTLDEVPPGKRLWLLATGTGIAPFLSMLRDL--EIWERFDKIVLVHGVRYAEELAYQDEIE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 167 AFAQAH-PQFRYLPCLSRELPAPAHadvrHGYVQQHLAE--------IAPDASTDIAYLCGNPDMVDACAEALKAAGLP- 236
Cdd:cd06195   152 ALAKQYnGKFRYVPIVSREKENGAL----TGRIPDLIESgeleehagLPLDPETSHVMLCGNPQMIDDTQELLKEKGFSk 227
                         250
                  ....*....|....
gi 1796985942 237 -----NAQIRREKY 245
Cdd:cd06195   228 nhrrkPGNITVEKY 241
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
5-244 4.90e-64

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 199.63  E-value: 4.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   5 FPLKLVDRRMLAPTVAHCQFVRDDGQPL-DFQPGQFIQIHFAAaDGTPTKRSYSLATIHDHalgpgEAVDIAVSFVPGGS 83
Cdd:COG1018     4 RPLRVVEVRRETPDVVSFTLEPPDGAPLpRFRPGQFVTLRLPI-DGKPLRRAYSLSSAPGD-----GRLEITVKRVPGGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  84 AT-ALFEGLEIGDPLQASGPYGRFCLQAgDHNQRYVLIATGTGVTPYRSMLPLLAEAiaSRSVQVVLLQGARTPAELLYG 162
Cdd:COG1018    78 GSnWLHDHLKVGDTLEVSGPRGDFVLDP-EPARPLLLIAGGIGITPFLSMLRTLLAR--GPFRPVTLVYGARSPADLAFR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 163 DDFRAFAQAHPQFRYLPCLSRElpapahADVRHGYV-QQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQIR 241
Cdd:COG1018   155 DELEALAARHPRLRLHPVLSRE------PAGLQGRLdAELLAALLPDPADAHVYLCGPPPMMEAVRAALAELGVPEERIH 228

                  ...
gi 1796985942 242 REK 244
Cdd:COG1018   229 FER 231
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
13-251 3.38e-28

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 109.58  E-value: 3.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  13 RMLAPTVAHCQFVRDD----------GQPLDFQPGQFIQIHFAaaDGTptKRSYSLATihdhALGPGEAVDIAVSFVPGG 82
Cdd:PRK07609  101 KKLPCRVASLERVAGDvmrlklrlpaTERLQYLAGQYIEFILK--DGK--RRSYSIAN----APHSGGPLELHIRHMPGG 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  83 -SATALFEGLEIGDPLQASGPYGRFCLqAGDHNQRYVLIATGTGVTPYRSMLPLLAEAIASRsvQVVLLQGARTPAELlY 161
Cdd:PRK07609  173 vFTDHVFGALKERDILRIEGPLGTFFL-REDSDKPIVLLASGTGFAPIKSIVEHLRAKGIQR--PVTLYWGARRPEDL-Y 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 162 GDDF-RAFAQAHPQFRYLPCLSRELPAPAHADvRHGYVQQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQI 240
Cdd:PRK07609  249 LSALaEQWAEELPNFRYVPVVSDALDDDAWTG-RTGFVHQAVLEDFPDLSGHQVYACGSPVMVYAARDDFVAAGLPAEEF 327
                         250
                  ....*....|.
gi 1796985942 241 RREKYVSSAPS 251
Cdd:PRK07609  328 FADAFTYAADL 338
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
119-228 2.72e-20

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: 83.08  E-value: 2.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 119 LIATGTGVTPYRSMLPLLAEAiASRSVQVVLLQGARTPAELLYGDDFRAFAQAHP-QFRYLPCLSRELPAPAHadvRHGY 197
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILED-PKDPTQVVLVFGNRNEDDILYREELDELAEKHPgRLTVVYVVSRPEAGWTG---GKGR 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1796985942 198 VQQHLAE---IAPDASTDIaYLCGNPDMVDACAE 228
Cdd:pfam00175  77 VQDALLEdhlSLPDEETHV-YVCGPPGMIKAVRK 109
 
Name Accession Description Interval E-value
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
8-245 8.54e-74

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: 224.75  E-value: 8.54e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   8 KLVDRRMLAPTvaHCQFVRDDGQPLDFQPGQFIQIHFAAADGTPTKRSYSLATIHDHalgpgEAVDIAVSFVPGGSATAL 87
Cdd:cd06195     1 TVLKRRDWTDD--LFSFRVTRDIPFRFQAGQFTKLGLPNDDGKLVRRAYSIASAPYE-----ENLEFYIILVPDGPLTPR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  88 FEGLEIGDPLQAS-GPYGRFCLQAGDHNQRYVLIATGTGVTPYRSMLPLLaeAIASRSVQVVLLQGARTPAELLYGDDFR 166
Cdd:cd06195    74 LFKLKPGDTIYVGkKPTGFLTLDEVPPGKRLWLLATGTGIAPFLSMLRDL--EIWERFDKIVLVHGVRYAEELAYQDEIE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 167 AFAQAH-PQFRYLPCLSRELPAPAHadvrHGYVQQHLAE--------IAPDASTDIAYLCGNPDMVDACAEALKAAGLP- 236
Cdd:cd06195   152 ALAKQYnGKFRYVPIVSREKENGAL----TGRIPDLIESgeleehagLPLDPETSHVMLCGNPQMIDDTQELLKEKGFSk 227
                         250
                  ....*....|....
gi 1796985942 237 -----NAQIRREKY 245
Cdd:cd06195   228 nhrrkPGNITVEKY 241
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
5-244 4.90e-64

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 199.63  E-value: 4.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   5 FPLKLVDRRMLAPTVAHCQFVRDDGQPL-DFQPGQFIQIHFAAaDGTPTKRSYSLATIHDHalgpgEAVDIAVSFVPGGS 83
Cdd:COG1018     4 RPLRVVEVRRETPDVVSFTLEPPDGAPLpRFRPGQFVTLRLPI-DGKPLRRAYSLSSAPGD-----GRLEITVKRVPGGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  84 AT-ALFEGLEIGDPLQASGPYGRFCLQAgDHNQRYVLIATGTGVTPYRSMLPLLAEAiaSRSVQVVLLQGARTPAELLYG 162
Cdd:COG1018    78 GSnWLHDHLKVGDTLEVSGPRGDFVLDP-EPARPLLLIAGGIGITPFLSMLRTLLAR--GPFRPVTLVYGARSPADLAFR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 163 DDFRAFAQAHPQFRYLPCLSRElpapahADVRHGYV-QQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQIR 241
Cdd:COG1018   155 DELEALAARHPRLRLHPVLSRE------PAGLQGRLdAELLAALLPDPADAHVYLCGPPPMMEAVRAALAELGVPEERIH 228

                  ...
gi 1796985942 242 REK 244
Cdd:COG1018   229 FER 231
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
4-245 5.72e-50

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: 163.65  E-value: 5.72e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   4 QFPLKLVDRRMLAPTVAHCQFVRDDGQPLDFQPGQFIQIHfaaADGTPTKRSYSLATihdhalGPGEA--VDIAVSFVPG 81
Cdd:cd06211     6 DFEGTVVEIEDLTPTIKGVRLKLDEPEEIEFQAGQYVNLQ---APGYEGTRAFSIAS------SPSDAgeIELHIRLVPG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  82 GSATA-LFEGLEIGDPLQASGPYGRFCLQAGDhNQRYVLIATGTGVTPYRSMLPLLAEAIASRsvQVVLLQGARTPAELL 160
Cdd:cd06211    77 GIATTyVHKQLKEGDELEISGPYGDFFVRDSD-QRPIIFIAGGSGLSSPRSMILDLLERGDTR--KITLFFGARTRAELY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 161 YGDDFRAFAQAHPQFRYLPCLSRELPAPAHADVRhGYVQQHLAE-IAPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQ 239
Cdd:cd06211   154 YLDEFEALEKDHPNFKYVPALSREPPESNWKGFT-GFVHDAAKKhFKNDFRGHKAYLCGPPPMIDACIKTLMQGRLFERD 232

                  ....*.
gi 1796985942 240 IRREKY 245
Cdd:cd06211   233 IYYEKF 238
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
10-243 6.42e-49

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: 160.69  E-value: 6.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  10 VDRRMLAPTVAHcqFVRDDGQPLDFQPGQFIQIHFAAaDGTPTKRSYSLAtihDHALGPGEaVDIAVSFVPGGSATALFE 89
Cdd:cd00322     1 VATEDVTDDVRL--FRLQLPNGFSFKPGQYVDLHLPG-DGRGLRRAYSIA---SSPDEEGE-LELTVKIVPGGPFSAWLH 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  90 GLEIGDPLQASGPYGRFCLQAGDhNQRYVLIATGTGVTPYRSMLPLLAEAIASRsvQVVLLQGARTPAELLYGDDFRAFA 169
Cdd:cd00322    74 DLKPGDEVEVSGPGGDFFLPLEE-SGPVVLIAGGIGITPFRSMLRHLAADKPGG--EITLLYGARTPADLLFLDELEELA 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1796985942 170 QAHPQFRYLPCLSRELPAPAHADVRHGYVQQHLAEIaPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQIRRE 243
Cdd:cd00322   151 KEGPNFRLVLALSRESEAKLGPGGRIDREAEILALL-PDDSGALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
8-247 1.59e-44

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: 154.25  E-value: 1.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   8 KLVDRRMLAPTVAHCQFVRDDGQPLDFQPGQFIQIH-------FAAAD-------------GTPTKRSYSLATIhdhalg 67
Cdd:COG2871   135 TVVSNENVTTFIKELVLELPEGEEIDFKAGQYIQIEvppyevdFKDFDipeeekfglfdknDEEVTRAYSMANY------ 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  68 PGEA------VDIAVSF--VPGGSATALFEGLEIGDPLQASGPYGRFCLQagDHNQRYVLIATGTGVTPYRSML-PLLAE 138
Cdd:COG2871   209 PAEKgiielnIRIATPPmdVPPGIGSSYIFSLKPGDKVTISGPYGEFFLR--DSDREMVFIGGGAGMAPLRSHIfDLLER 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 139 AIASRsvQVVLLQGARTPAELLYGDDFRAFAQAHPQFRYLPCLSRELPAPAHADVRhGYVQQHLAE---IAPDASTDI-A 214
Cdd:COG2871   287 GKTDR--KITFWYGARSLRELFYLEEFRELEKEHPNFKFHPALSEPLPEDNWDGET-GFIHEVLYEnylKDHPAPEDCeA 363
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1796985942 215 YLCGNPDMVDACAEALKAAGLPNAQIRREKYVS 247
Cdd:COG2871   364 YLCGPPPMIDAVIKMLDDLGVEEENIYFDDFGG 396
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
30-245 2.02e-44

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: 148.90  E-value: 2.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  30 QPLDFQPGQFIQIHFaaaDGTP-TKRSYSLATihdhALGPGEAVDIAVSFVPGGSAT-ALFEGLEIGDPLQASGPYGRFC 107
Cdd:cd06187    20 QPLPFWAGQYVNVTV---PGRPrTWRAYSPAN----PPNEDGEIEFHVRAVPGGRVSnALHDELKVGDRVRLSGPYGTFY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 108 LQaGDHNQRYVLIATGTGVTPYRSMLPLLAEAIASRSVQVVLlqGARTPAELLYGDDFRAFAQAHPQFRYLPCLSRElpa 187
Cdd:cd06187    93 LR-RDHDRPVLCIAGGTGLAPLRAIVEDALRRGEPRPVHLFF--GARTERDLYDLEGLLALAARHPWLRVVPVVSHE--- 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1796985942 188 PAHADVRHGYVQQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQIRREKY 245
Cdd:cd06187   167 EGAWTGRRGLVTDVVGRDGPDWADHDIYICGPPAMVDATVDALLARGAPPERIHFDKF 224
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
27-246 1.01e-41

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: 142.47  E-value: 1.01e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  27 DDGQPLDFQPGQFIQIhfaAADGTPTKRSYSLATIHDHalgPGEaVDIAVSFVPGGS-ATALFEGLEIGDPLQASGPYGR 105
Cdd:cd06212    23 EEPEPIKFFAGQYVDI---TVPGTEETRSFSMANTPAD---PGR-LEFIIKKYPGGLfSSFLDDGLAVGDPVTVTGPYGT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 106 FCLQAGDHnQRYVLIATGTGVTPYRSMLPLLAEAIASRSVqvVLLQGARTPAELLYGDDFRAFAQAHPQFRYLPCLSREL 185
Cdd:cd06212    96 CTLRESRD-RPIVLIGGGSGMAPLLSLLRDMAASGSDRPV--RFFYGARTARDLFYLEEIAALGEKIPDFTFIPALSESP 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1796985942 186 PAPAHaDVRHGYV----QQHLAEIapdASTDiAYLCGNPDMVDACAEALKAAGLPNAQIRREKYV 246
Cdd:cd06212   173 DDEGW-SGETGLVtevvQRNEATL---AGCD-VYLCGPPPMIDAALPVLEMSGVPPDQIFYDKFT 232
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
5-245 1.46e-41

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: 142.02  E-value: 1.46e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   5 FPLKLVDRRMLAPTVAHCQFVRDDGQPLDFQPGQFIQIHFAAADGTPTKRSYSLA---TIHDHalgpgeaVDIAVSFVPG 81
Cdd:cd06217     2 RVLRVTEIIQETPTVKTFRLAVPDGVPPPFLAGQHVDLRLTAIDGYTAQRSYSIAsspTQRGR-------VELTVKRVPG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  82 GSATA-LFEGLEIGDPLQASGPYGRFCLQAGdHNQRYVLIATGTGVTPYRSMLPLLAEaiASRSVQVVLLQGARTPAELL 160
Cdd:cd06217    75 GEVSPyLHDEVKVGDLLEVRGPIGTFTWNPL-HGDPVVLLAGGSGIVPLMSMIRYRRD--LGWPVPFRLLYSARTAEDVI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 161 YGDDFRAFAQAHPQFRYLPCLSRELPApahadVRHGYVQQ----HLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLP 236
Cdd:cd06217   152 FRDELEQLARRHPNLHVTEALTRAAPA-----DWLGPAGRitadLIAELVPPLAGRRVYVCGPPAFVEAATRLLLELGVP 226

                  ....*....
gi 1796985942 237 NAQIRREKY 245
Cdd:cd06217   227 RDRIRTEAF 235
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
7-243 5.26e-39

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: 135.41  E-value: 5.26e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   7 LKLVDRRMLAPTVAHCQFVRDDGQPLDFQPGQFIQIHFAAaDGTPTKRSYSLATihdhalGPGE--AVDIAVSFVPGGSA 84
Cdd:cd06215     1 LRCVKIIQETPDVKTFRFAAPDGSLFAYKPGQFLTLELEI-DGETVYRAYTLSS------SPSRpdSLSITVKRVPGGLV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  85 TA-LFEGLEIGDPLQASGPYGRFCLQAGDhNQRYVLIATGTGVTPYRSMLPLLAeaiASRS-VQVVLLQGARTPAELLYG 162
Cdd:cd06215    74 SNwLHDNLKVGDELWASGPAGEFTLIDHP-ADKLLLLSAGSGITPMMSMARWLL---DTRPdADIVFIHSARSPADIIFA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 163 DDFRAFAQAHPQFRYLPCLSRelPAPAHADVRHGYV-QQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQIR 241
Cdd:cd06215   150 DELEELARRHPNFRLHLILEQ--PAPGAWGGYRGRLnAELLALLVPDLKERTVFVCGPAGFMKAVKSLLAELGFPMSRFH 227

                  ..
gi 1796985942 242 RE 243
Cdd:cd06215   228 QE 229
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
8-247 2.96e-38

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 133.83  E-value: 2.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   8 KLVDRRMLAPTVAHcqF-VRDDGQPLDFQPGQFIQIHfaaADGTPTKRSYSLATIHDhalgPGEAVDIAVSFVpgGSATA 86
Cdd:COG0543     1 KVVSVERLAPDVYL--LrLEAPLIALKFKPGQFVMLR---VPGDGLRRPFSIASAPR----EDGTIELHIRVV--GKGTR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  87 LFEGLEIGDPLQASGPYGRFClQAGDHNQRYVLIATGTGVTPyrsmLPLLAEAIASRSVQVVLLQGARTPAELLYGDDFR 166
Cdd:COG0543    70 ALAELKPGDELDVRGPLGNGF-PLEDSGRPVLLVAGGTGLAP----LRSLAEALLARGRRVTLYLGARTPEDLYLLDELE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 167 AFAQahpqFRYLpCLSRElpapaHADVRHGYVQQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQIrrekYV 246
Cdd:COG0543   145 ALAD----FRVV-VTTDD-----GWYGRKGFVTDALKELLAEDSGDDVYACGPPPMMKAVAELLLERGVPPERI----YV 210

                  .
gi 1796985942 247 S 247
Cdd:COG0543   211 S 211
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
13-246 1.99e-37

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: 131.18  E-value: 1.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  13 RMLAPTVAHCQFVRDDGQPLDFQPGQFIQIhfaAADGTPTKRSYSLATihdhalGPGEAvdiAVSF----VPGGS-ATAL 87
Cdd:cd06209    10 ERLSDSTIGLTLELDEAGALAFLPGQYVNL---QVPGTDETRSYSFSS------APGDP---RLEFlirlLPGGAmSSYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  88 FEGLEIGDPLQASGPYGRFCLQAGDHNQryVLIATGTGVTPYRSMLPLLAEAiaSRSVQVVLLQGARTPAELLYGDDFRA 167
Cdd:cd06209    78 RDRAQPGDRLTLTGPLGSFYLREVKRPL--LMLAGGTGLAPFLSMLDVLAED--GSAHPVHLVYGVTRDADLVELDRLEA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 168 FAQAHPQFRYLPCLSRelpaPAHADVRHGYVQQHL-AEIAPDASTDIaYLCGNPDMVDACAEALKAAGLPNAQIRREKYV 246
Cdd:cd06209   154 LAERLPGFSFRTVVAD----PDSWHPRKGYVTDHLeAEDLNDGDVDV-YLCGPPPMVDAVRSWLDEQGIEPANFYYEKFT 228
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
7-245 1.87e-35

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: 126.10  E-value: 1.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   7 LKLVDRRMLAPTVAHCQFVRDDGQPLDFQPGQFIQIHfAAADGTPTKRSYSLATihdhALGPGEaVDIAVSFVPGGSATA 86
Cdd:cd06191     1 LRVAEVRSETPDAVTIVFAVPGPLQYGFRPGQHVTLK-LDFDGEELRRCYSLCS----SPAPDE-ISITVKRVPGGRVSN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  87 -LFEGLEIGDPLQASGPYGRFCLQAGDHnQRYVLIATGTGVTPYRSMLPllAEAIASRSVQVVLLQGARTPAELLYGDDF 165
Cdd:cd06191    75 yLREHIQPGMTVEVMGPQGHFVYQPQPP-GRYLLVAAGSGITPLMAMIR--ATLQTAPESDFTLIHSARTPADMIFAQEL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 166 RAFAQAHPQFRYLPCLSRELPAPAHADVRHGYVQQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQIRREKY 245
Cdd:cd06191   152 RELADKPQRLRLLCIFTRETLDSDLLHGRIDGEQSLGAALIPDRLEREAFICGPAGMMDAVETALKELGMPPERIHTERF 231
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
30-240 3.49e-35

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: 125.35  E-value: 3.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  30 QPLDFQPGQFIQIHFAAADgtptKRSYSLATIHDHalgpGEAVDIAVSFVPGGS-ATALFEGLEIGDPLQASGPYGRFCL 108
Cdd:cd06189    22 APLDFLAGQYLDLLLDDGD----KRPFSIASAPHE----DGEIELHIRAVPGGSfSDYVFEELKENGLVRIEGPLGDFFL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 109 QAGDHNQRyVLIATGTGVTPYRSMLpllAEAIASRSVQ-VVLLQGARTPAELLYGDDFRAFAQAHPQFRYLPCLSRelpA 187
Cdd:cd06189    94 REDSDRPL-ILIAGGTGFAPIKSIL---EHLLAQGSKRpIHLYWGARTEEDLYLDELLEAWAEAHPNFTYVPVLSE---P 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1796985942 188 PAHADVRHGYVQQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQI 240
Cdd:cd06189   167 EEGWQGRTGLVHEAVLEDFPDLSDFDVYACGSPEMVYAARDDFVEKGLPEENF 219
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
32-246 2.59e-34

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: 123.42  E-value: 2.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  32 LDFQPGQFIQIHfAAADGTPTKRSYSL-ATIHDHALGpgeavdIAVSFVPGGSA-TALFEGLEIGDPLQASGPYGRFCLQ 109
Cdd:cd06214    31 FRYRPGQFLTLR-VPIDGEEVRRSYSIcSSPGDDELR------ITVKRVPGGRFsNWANDELKAGDTLEVMPPAGRFTLP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 110 AGDHNQRYVLIATGTGVTPyrsMLPLLAEAIA-SRSVQVVLLQGARTPAELLYGDDFRAFAQAHP-QFRYLPCLSRElpa 187
Cdd:cd06214   104 PLPGARHYVLFAAGSGITP---VLSILKTALArEPASRVTLVYGNRTEASVIFREELADLKARYPdRLTVIHVLSRE--- 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1796985942 188 PAHADVRHGYVQQHLAE-----IAPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQIRREKYV 246
Cdd:cd06214   178 QGDPDLLRGRLDAAKLNallknLLDATEFDEAFLCGPEPMMDAVEAALLELGVPAERIHRELFT 241
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
24-243 1.00e-32

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: 119.58  E-value: 1.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  24 FVRDDGQPL-DFQPGQFIQIHFAAAD-GTPTKRSYSLATihdhalGPGEA-VDIAVSFVPGGSA-TALFEGLEIGDPLQA 99
Cdd:cd06184    26 LEPADGGPLpPFLPGQYLSVRVKLPGlGYRQIRQYSLSD------APNGDyYRISVKREPGGLVsNYLHDNVKVGDVLEV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 100 SGPYGRFCLQAgDHNQRYVLIATGTGVTPYRSMLPLLAEAIASRsvQVVLLQGARTPAELLYGDDFRAFAQAHPQFRYLP 179
Cdd:cd06184   100 SAPAGDFVLDE-ASDRPLVLISAGVGITPMLSMLEALAAEGPGR--PVTFIHAARNSAVHAFRDELEELAARLPNLKLHV 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1796985942 180 CLSRELPAPAHADVRH-GYVQQH-LAEIAPDASTDIaYLCGNPDMVDACAEALKAAGLPNAQIRRE 243
Cdd:cd06184   177 FYSEPEAGDREEDYDHaGRIDLAlLRELLLPADADF-YLCGPVPFMQAVREGLKALGVPAERIHYE 241
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
9-240 1.72e-32

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: 118.14  E-value: 1.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   9 LVDRRMLAPTVAHCQFVRDdgQPLDFQPGQFIQIHFAaadGTPTkRSYSLAtihdhaLGPGEAVDIA--VSFVPGGSAT- 85
Cdd:cd06194     1 VVSLQRLSPDVLRVRLEPD--RPLPYLPGQYVNLRRA---GGLA-RSYSPT------SLPDGDNELEfhIRRKPNGAFSg 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  86 ALFEGLEIGDPLQASGPYGRFCLQAGDHNQRYVLIATGTGVTPyrsMLPLLAEAIAS-RSVQVVLLQGARTPAELLYGDD 164
Cdd:cd06194    69 WLGEEARPGHALRLQGPFGQAFYRPEYGEGPLLLVGAGTGLAP---LWGIARAALRQgHQGEIRLVHGARDPDDLYLHPA 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1796985942 165 FRAFAQAHPQFRYLPCLSRELPAPAHADVRHGYVQQHlaeiaPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQI 240
Cdd:cd06194   146 LLWLAREHPNFRYIPCVSEGSQGDPRVRAGRIAAHLP-----PLTRDDVVYLCGAPSMVNAVRRRAFLAGAPMKRI 216
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
9-246 9.26e-32

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: 116.58  E-value: 9.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   9 LVDRRMLAPTVAhcQFVRDDGQPLDFQPGQFIQIHFAAADGTptkRSYSLAtihDHALGPGEaVDIAVSFVPGGSAT-AL 87
Cdd:cd06190     1 LVDVRELTHDVA--EFRFALDGPADFLPGQYALLALPGVEGA---RAYSMA---NLANASGE-WEFIIKRKPGGAASnAL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  88 FEGLEIGDPLQASGPYGRFCLQAgDHNQRYVLIATGTGVTPyrsMLPLLAEAIASRSV---QVVLLQGARTPAELLYGDD 164
Cdd:cd06190    72 FDNLEPGDELELDGPYGLAYLRP-DEDRDIVCIAGGSGLAP---MLSILRGAARSPYLsdrPVDLFYGGRTPSDLCALDE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 165 FRAFAQAHPQFRYLPCLSRELPAP-AHADVRHGYVQQHLAEIAPDASTD-IAYLCGNPDMVDACAEALKAAGLPNA-QIR 241
Cdd:cd06190   148 LSALVALGARLRVTPAVSDAGSGSaAGWDGPTGFVHEVVEATLGDRLAEfEFYFAGPPPMVDAVQRMLMIEGVVPFdQIH 227

                  ....*
gi 1796985942 242 REKYV 246
Cdd:cd06190   228 FDRFV 232
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
4-236 1.35e-31

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap 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: 116.56  E-value: 1.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   4 QFPLKLVDRRMLAPTVAHCQFvRDDGQPLDFQPGQFIQIHFAAaDGTPTKRSYSLATIHDHAlgpGEAVDIAVSFVPGGS 83
Cdd:cd06216    17 ELRARVVAVRPETADMVTLTL-RPNRGWPGHRAGQHVRLGVEI-DGVRHWRSYSLSSSPTQE---DGTITLTVKAQPDGL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  84 AT-ALFEGLEIGDPLQASGPYGRFCLQAGDHnQRYVLIATGTGVTPYRSMLPLLAEAIASRsvQVVLLQGARTPAELLYG 162
Cdd:cd06216    92 VSnWLVNHLAPGDVVELSQPQGDFVLPDPLP-PRLLLIAAGSGITPVMSMLRTLLARGPTA--DVVLLYYARTREDVIFA 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1796985942 163 DDFRAFAQAHPQFRYLPCLSRElpapaHADVRHGYvqQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLP 236
Cdd:cd06216   169 DELRALAAQHPNLRLHLLYTRE-----ELDGRLSA--AHLDAVVPDLADRQVYACGPPGFLDAAEELLEAAGLA 235
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
30-245 1.71e-31

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: 115.87  E-value: 1.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  30 QPLDFQPGQFIQIhfaAADGTPTKRSYSLATihdhALGPGEAVDIAVSFVPGGSAT-ALFEGLEIGDPLQASGPYGRFCL 108
Cdd:cd06213    24 RPIAYKAGQYAEL---TLPGLPAARSYSFAN----APQGDGQLSFHIRKVPGGAFSgWLFGADRTGERLTVRGPFGDFWL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 109 QAGDhnQRYVLIATGTGVTPYRSMLpllAEAIASRSVQ-VVLLQGARTPAELLYGDDFRAFAQA-HPQFRYLPCLSRElp 186
Cdd:cd06213    97 RPGD--APILCIAGGSGLAPILAIL---EQARAAGTKRdVTLLFGARTQRDLYALDEIAAIAARwRGRFRFIPVLSEE-- 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1796985942 187 aPAHADV--RHGYVQQHLAEIAPDASTdiAYLCGNPDMVDACAEALKAAGLPNAQIRREKY 245
Cdd:cd06213   170 -PADSSWkgARGLVTEHIAEVLLAATE--AYLCGPPAMIDAAIAVLRALGIAREHIHADRF 227
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
27-241 9.41e-31

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: 115.09  E-value: 9.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  27 DDGQPLDFQPGQFIQIHFAAADGT----------------------------PTKRSYSLATiHDHALG----------- 67
Cdd:cd06188    32 PSGEEIAFKAGGYIQIEIPAYEIAyadfdvaekyradwdkfglwqlvfkhdePVSRAYSLAN-YPAEEGelklnvriatp 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  68 PGEAVDIAvsfvPGGSATALFeGLEIGDPLQASGPYGRFCLQAGDHNQryVLIATGTGVTPYRSMLPLLAEAIASRSvQV 147
Cdd:cd06188   111 PPGNSDIP----PGIGSSYIF-NLKPGDKVTASGPFGEFFIKDTDREM--VFIGGGAGMAPLRSHIFHLLKTLKSKR-KI 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 148 VLLQGARTPAELLYGDDFRAFAQAHPQFRYLPCLSRELPAPAHaDVRHGYVQQHLAEI---APDASTDIA-YLCGNPDMV 223
Cdd:cd06188   183 SFWYGARSLKELFYQEEFEALEKEFPNFKYHPVLSEPQPEDNW-DGYTGFIHQVLLENylkKHPAPEDIEfYLCGPPPMN 261
                         250
                  ....*....|....*...
gi 1796985942 224 DACAEALKAAGLPNAQIR 241
Cdd:cd06188   262 SAVIKMLDDLGVPRENIA 279
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
13-251 3.38e-28

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 109.58  E-value: 3.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  13 RMLAPTVAHCQFVRDD----------GQPLDFQPGQFIQIHFAaaDGTptKRSYSLATihdhALGPGEAVDIAVSFVPGG 82
Cdd:PRK07609  101 KKLPCRVASLERVAGDvmrlklrlpaTERLQYLAGQYIEFILK--DGK--RRSYSIAN----APHSGGPLELHIRHMPGG 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  83 -SATALFEGLEIGDPLQASGPYGRFCLqAGDHNQRYVLIATGTGVTPYRSMLPLLAEAIASRsvQVVLLQGARTPAELlY 161
Cdd:PRK07609  173 vFTDHVFGALKERDILRIEGPLGTFFL-REDSDKPIVLLASGTGFAPIKSIVEHLRAKGIQR--PVTLYWGARRPEDL-Y 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 162 GDDF-RAFAQAHPQFRYLPCLSRELPAPAHADvRHGYVQQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQI 240
Cdd:PRK07609  249 LSALaEQWAEELPNFRYVPVVSDALDDDAWTG-RTGFVHQAVLEDFPDLSGHQVYACGSPVMVYAARDDFVAAGLPAEEF 327
                         250
                  ....*....|.
gi 1796985942 241 RREKYVSSAPS 251
Cdd:PRK07609  328 FADAFTYAADL 338
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
14-246 1.33e-27

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: 105.89  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  14 MLAPTVAHCQFVRDD----GQPLDFQPGQFIQIHFAaadGTPTKRSYSLATIHDHAlgpGEaVDIAVSFVPGGS-ATALF 88
Cdd:cd06210    11 RVSSNVVRLRLQPDDaegaGIAAEFVPGQFVEIEIP---GTDTRRSYSLANTPNWD---GR-LEFLIRLLPGGAfSTYLE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  89 EGLEIGDPLQASGPYGRFCLQAGDHNQRYvLIATGTGVTPYRSMLPLLAEAiaSRSVQVVLLQGARTPAELLYGDDFRAF 168
Cdd:cd06210    84 TRAKVGQRLNLRGPLGAFGLRENGLRPRW-FVAGGTGLAPLLSMLRRMAEW--GEPQEARLFFGVNTEAELFYLDELKRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 169 AQAHPQFRYLPCLSRelpAPAHADVRHGYVQQHLAE--IAPDASTDIaYLCGNPDMVDACAEALKAAGLPNAQIRREKYV 246
Cdd:cd06210   161 ADSLPNLTVRICVWR---PGGEWEGYRGTVVDALREdlASSDAKPDI-YLCGPPGMVDAAFAAAREAGVPDEQVYLEKFL 236
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
4-245 7.49e-27

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 107.67  E-value: 7.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   4 QFPLKLVDRRMLAPTVAHCQFVRDDGQPLDFQPGQFiqiHFAAADGTPTKRS---YSLATihdhalGPGEAVDIAVSFVP 80
Cdd:COG4097   214 RHPYRVESVEPEAGDVVELTLRPEGGRWLGHRAGQF---AFLRFDGSPFWEEahpFSISS------APGGDGRLRFTIKA 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  81 GGSATALFEGLEIGDPLQASGPYGRFCLQAGDHNQRYVLIATGTGVTPYRSMLPLLAEAIASRsVQVVLLQGARTPAELL 160
Cdd:COG4097   285 LGDFTRRLGRLKPGTRVYVEGPYGRFTFDRRDTAPRQVWIAGGIGITPFLALLRALAARPGDQ-RPVDLFYCVRDEEDAP 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 161 YGDDFRAFAQAHPQFRYLPCLSRElpapahadvrHGYV-QQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQ 239
Cdd:COG4097   364 FLEELRALAARLAGLRLHLVVSDE----------DGRLtAERLRRLVPDLAEADVFFCGPPGMMDALRRDLRALGVPARR 433

                  ....*.
gi 1796985942 240 IRREKY 245
Cdd:COG4097   434 IHQERF 439
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
7-240 2.25e-24

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: 97.25  E-value: 2.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   7 LKLVDRRMLAPTVAHCQFVRDDG-QPLDFQPGQFIQIHfAAADGTPTKRSYSLATIHDHalgPGEaVDIAVSFVPGGSAT 85
Cdd:cd06183     1 FKLVSKEDISHDTRIFRFELPSPdQVLGLPVGQHVELK-APDDGEQVVRPYTPISPDDD---KGY-FDLLIKIYPGGKMS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  86 ALFEGLEIGDPLQASGPYGRFCLQAGDHNQRYVLIATGTGVTPyrsMLPLLAEAIASRS--VQVVLLQGARTPAELLYGD 163
Cdd:cd06183    76 QYLHSLKPGDTVEIRGPFGKFEYKPNGKVKHIGMIAGGTGITP---MLQLIRAILKDPEdkTKISLLYANRTEEDILLRE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 164 DFRAFAQAHP-QFRYLPCLSRElpaPAHADVRHGYV-QQHLAEIAPDASTD--IAYLCGNPDMVD-ACAEALKAAGLPNA 238
Cdd:cd06183   153 ELDELAKKHPdRFKVHYVLSRP---PEGWKGGVGFItKEMIKEHLPPPPSEdtLVLVCGPPPMIEgAVKGLLKELGYKKD 229

                  ..
gi 1796985942 239 QI 240
Cdd:cd06183   230 NV 231
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
10-243 4.33e-24

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: 95.63  E-value: 4.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  10 VDRRMLAPTVAHCQFVRDDGQPL-DFQPGQFIQIHFaaadGTPTKRSYSLatihdhaLGPGEAVD---IAVSFVP---GG 82
Cdd:cd06185     1 VRIRDEAPDIRSFELEAPDGAPLpAFEPGAHIDVHL----PNGLVRQYSL-------CGDPADRDryrIAVLREPasrGG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  83 SAtALFEGLEIGDPLQASGPYGRFCLQAGDhnQRYVLIATGTGVTPYRSMlpllAEAIASRSVQVVLLQGARTPAELLYG 162
Cdd:cd06185    70 SR-YMHELLRVGDELEVSAPRNLFPLDEAA--RRHLLIAGGIGITPILSM----ARALAARGADFELHYAGRSREDAAFL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 163 DDFRAFAQAHPQFrylpclsrelpapaHADVRHG--YVQQHLAEIAPDAStdiAYLCGNPDMVDACAEALKAAGLPNAQI 240
Cdd:cd06185   143 DELAALPGDRVHL--------------HFDDEGGrlDLAALLAAPPAGTH---VYVCGPEGMMDAVRAAAAALGWPEARL 205

                  ...
gi 1796985942 241 RRE 243
Cdd:cd06185   206 HFE 208
PRK13289 PRK13289
NO-inducible flavohemoprotein;
24-243 7.00e-22

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 93.32  E-value: 7.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  24 FVRDDGQPL-DFQPGQFIQIHFAAADGTPTK-RSYSLAtihdhALGPGEAVDIAVSFVPGGSATA-LFEGLEIGDPLQAS 100
Cdd:PRK13289  174 LEPVDGGPVaDFKPGQYLGVRLDPEGEEYQEiRQYSLS-----DAPNGKYYRISVKREAGGKVSNyLHDHVNVGDVLELA 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 101 GPYGRFCLQAgDHNQRYVLIATGTGVTPYRSMLPLLAEAIASRsvQVVLLQGARTPAELLYGDDFRAFAQAHPQFRYLPC 180
Cdd:PRK13289  249 APAGDFFLDV-ASDTPVVLISGGVGITPMLSMLETLAAQQPKR--PVHFIHAARNGGVHAFRDEVEALAARHPNLKAHTW 325
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1796985942 181 LSRELPAPAHADVRH--GYV-QQHLAEIAPDASTDiAYLCGNPDMVDACAEALKAAGLPNAQIRRE 243
Cdd:PRK13289  326 YREPTEQDRAGEDFDseGLMdLEWLEAWLPDPDAD-FYFCGPVPFMQFVAKQLLELGVPEERIHYE 390
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
9-247 1.16e-21

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: 90.36  E-value: 1.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   9 LVDRRMLAPTVAHCQFVRDDGQ--PLDFQPGQFIQIH-FAAADGT------PTKRSYSLATIHdhALGPgeavdiaVSfv 79
Cdd:cd06221     1 IVEVVDETEDIKTFTLRLEDDDeeLFTFKPGQFVMLSlPGVGEAPisissdPTRRGPLELTIR--RVGR-------VT-- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  80 pggsaTALFEgLEIGDPLQASGPYGR-FCLQAG-DHNqrYVLIATGTGVTPYRSmlpLLAEAIASRSV--QVVLLQGART 155
Cdd:cd06221    70 -----EALHE-LKPGDTVGLRGPFGNgFPVEEMkGKD--LLLVAGGLGLAPLRS---LINYILDNREDygKVTLLYGART 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 156 PAELLYGDDFRAFAQaHPQFRYLPCLSRelpAPAHADVRHGYVQQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGL 235
Cdd:cd06221   139 PEDLLFKEELKEWAK-RSDVEVILTVDR---AEEGWTGNVGLVTDLLPELTLDPDNTVAIVCGPPIMMRFVAKELLKLGV 214
                         250
                  ....*....|..
gi 1796985942 236 PNAQIrrekYVS 247
Cdd:cd06221   215 PEEQI----WVS 222
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
28-249 1.75e-21

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 91.34  E-value: 1.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  28 DGQPLDFQPGQFIQIHFAaadGTPTKRSYSLAtihdHALGPGEAVDIAVSFVPGGS-ATALFEGLEIGDPLQASGPYGRF 106
Cdd:PRK11872  131 HGRQLDFLPGQYARLQIP---GTDDWRSYSFA----NRPNATNQLQFLIRLLPDGVmSNYLRERCQVGDEILFEAPLGAF 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 107 CLQagdHNQR-YVLIATGTGVTPYRSMLPLLAEAIASRSVQvvLLQGARTPAELLYGDDFRAFAQAHPQFRYLPCLSRel 185
Cdd:PRK11872  204 YLR---EVERpLVFVAGGTGLSAFLGMLDELAEQGCSPPVH--LYYGVRHAADLCELQRLAAYAERLPNFRYHPVVSK-- 276
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1796985942 186 pAPAHADVRHGYVQQHL--AEIApDASTDIaYLCGNPDMVDACAEALKAAGLPNAQIRREKYVSSA 249
Cdd:PRK11872  277 -ASADWQGKRGYIHEHFdkAQLR-DQAFDM-YLCGPPPMVEAVKQWLDEQALENYRLYYEKFTQSN 339
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
22-233 1.21e-20

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: 88.15  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  22 CQFVRDDGQPLDFQPGQFIQI---HFAAADGTPTK-RSYSLATIHDHALGPGEAVDIAVSFVPG----------GSATAL 87
Cdd:cd06208    29 CHIVIDHGGKLPYLEGQSIGIippGTDAKNGKPHKlRLYSIASSRYGDDGDGKTLSLCVKRLVYtdpetdetkkGVCSNY 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  88 FEGLEIGDPLQASGPYGRFCLQAGDHNQRYVLIATGTGVTPYRSML-PLLAEAIASRSVQ--VVLLQGARTPAELLYGDD 164
Cdd:cd06208   109 LCDLKPGDDVQITGPVGKTMLLPEDPNATLIMIATGTGIAPFRSFLrRLFREKHADYKFTglAWLFFGVPNSDSLLYDDE 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1796985942 165 FRAFAQAHP-QFRYLPCLSRElpaPAHADVRHGYVQQHLAEIAP-------DASTDIaYLCGNPDMVDACAEALKAA 233
Cdd:cd06208   189 LEKYPKQYPdNFRIDYAFSRE---QKNADGGKMYVQDRIAEYAEeiwnlldKDNTHV-YICGLKGMEPGVDDALTSV 261
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
25-243 2.50e-20

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: 86.16  E-value: 2.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  25 VRDDGQPLDFQPGQFIQIHFAAADGT---PtkrsYSLATIHDH---------ALGPGEAvdiavsfvpggsatALFEGLE 92
Cdd:cd06198    14 LEPRGPALGHRAGQFAFLRFDASGWEephP----FTISSAPDPdgrlrftikALGDYTR--------------RLAERLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  93 IGDPLQASGPYGRFCLQAGDHNQryVLIATGTGVTPYRSMLPLLAEAIASRsvQVVLLQGARTPAELLYGDDFRAFAQAH 172
Cdd:cd06198    76 PGTRVTVEGPYGRFTFDDRRARQ--IWIAGGIGITPFLALLEALAARGDAR--PVTLFYCVRDPEDAVFLDELRALAAAA 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1796985942 173 pQFRYLPCLSRELPAPAHADVRHGYVqqhlaeiaPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQIRRE 243
Cdd:cd06198   152 -GVVLHVIDSPSDGRLTLEQLVRALV--------PDLADADVWFCGPPGMADALEKGLRALGVPARRFHYE 213
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
119-228 2.72e-20

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: 83.08  E-value: 2.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 119 LIATGTGVTPYRSMLPLLAEAiASRSVQVVLLQGARTPAELLYGDDFRAFAQAHP-QFRYLPCLSRELPAPAHadvRHGY 197
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILED-PKDPTQVVLVFGNRNEDDILYREELDELAEKHPgRLTVVYVVSRPEAGWTG---GKGR 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1796985942 198 VQQHLAE---IAPDASTDIaYLCGNPDMVDACAE 228
Cdd:pfam00175  77 VQDALLEdhlSLPDEETHV-YVCGPPGMIKAVRK 109
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
35-236 2.22e-19

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99814 [Multi-domain]  Cd Length: 246  Bit Score: 84.13  E-value: 2.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  35 QPGQFIQIHFAAADGTPTKRSYSlatIHDhALGPGEAVDIAVSFVpgGSATALFEGLEIGDPLQASGPYGR-FCLQAGDh 113
Cdd:cd06218    26 KPGQFVMLRVPDGSDPLLRRPIS---IHD-VDPEEGTITLLYKVV--GKGTRLLSELKAGDELDVLGPLGNgFDLPDDD- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 114 nQRYVLIATGTGVTPyrsmLPLLAEAIASRSVQVVLLQGARTPAELLYGDDFRAFAqahpqfrylpclsrelpapahADV 193
Cdd:cd06218    99 -GKVLLVGGGIGIAP----LLFLAKQLAERGIKVTVLLGFRSADDLFLVEEFEALG---------------------AEV 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1796985942 194 R----------HGYVQQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLP 236
Cdd:cd06218   153 YvatddgsagtKGFVTDLLKELLAEARPDVVYACGPEPMLKAVAELAAERGVP 205
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
1-245 2.83e-15

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 72.98  E-value: 2.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   1 MPVQFPLKLVDRRMLAPTVAhcQFVRDDGQPLDFQPGQFIqiHFAAADGTPT-KRSYSLATIHDHALGpgeavdIAVSFV 79
Cdd:PRK00054    1 MMKPENMKIVENKEIAPNIY--TLVLDGEKVFDMKPGQFV--MVWVPGVEPLlERPISISDIDKNEIT------ILYRKV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  80 pgGSATALFEGLEIGDPLQASGPYGR-FCLQAGDhnQRYVLIATGTGVTPyrsMLPLlAEAIASRSVQVVLLQGARTPAE 158
Cdd:PRK00054   71 --GEGTKKLSKLKEGDELDIRGPLGNgFDLEEIG--GKVLLVGGGIGVAP---LYEL-AKELKKKGVEVTTVLGARTKDE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 159 LLYGDDFRAFAQAHpqfrylpclsrelpaPAHADV---RHGYVQQHLAEIapDASTDIAYLCGNPDMVDACAEALKAAGL 235
Cdd:PRK00054  143 VIFEEEFAKVGDVY---------------VTTDDGsygFKGFVTDVLDEL--DSEYDAIYSCGPEIMMKKVVEILKEKKV 205
                         250
                  ....*....|
gi 1796985942 236 PnAQIRREKY 245
Cdd:PRK00054  206 P-AYVSLERR 214
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
13-246 8.11e-14

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 68.43  E-value: 8.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  13 RMLAPTVAhcQFVRDDgqPLDFQPGQFIQIHFAAADGTPTKRSYslatihdhalGPGEAvDIAVSFVpgGSATALFEGLE 92
Cdd:cd06220     7 IDETPTVK--TFVFDW--DFDFKPGQFVMVWVPGVDEIPMSLSY----------IDGPN-SITVKKV--GEATSALHDLK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  93 IGDPLQASGPYGR-FCLQAGdhnqRYVLIATGTGVTPyrsMLPLLAEaiASRSVQVVLLQGARTPAELLYGDDFRAFAQA 171
Cdd:cd06220    70 EGDKLGIRGPYGNgFELVGG----KVLLIGGGIGIAP---LAPLAER--LKKAADVTVLLGARTKEELLFLDRLRKSDEL 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1796985942 172 HpqfrylpclsrelpaPAHAD---VRHGYVQQHLAEIAPDaSTDIAYLCGNPDMVDACAEALKAAGLPnAQIRREKYV 246
Cdd:cd06220   141 I---------------VTTDDgsyGFKGFVTDLLKELDLE-EYDAIYVCGPEIMMYKVLEILDERGVR-AQFSLERYM 201
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
94-231 1.65e-13

ferredoxin--NADP+ reductase; Provisional


Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 68.59  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  94 GDPLQASGPYGR-FCLQAGDHNQRYVLIATGTGVTPYRSMLP-LLAEAIASRSV--QVVLLQGARTPAELLYGDDFRAFA 169
Cdd:PLN03116  135 GDKVQITGPSGKvMLLPEEDPNATHIMVATGTGIAPFRGFLRrMFMEDVPAFKFggLAWLFLGVANSDSLLYDDEFERYL 214
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1796985942 170 QAHP-QFRYLPCLSRElpapaHADVRHG--YVQQHLAEIAP------DASTDIaYLCGNPDMVDACAEALK 231
Cdd:PLN03116  215 KDYPdNFRYDYALSRE-----QKNKKGGkmYVQDKIEEYSDeifkllDNGAHI-YFCGLKGMMPGIQDTLK 279
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
16-245 3.39e-13

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 68.20  E-value: 3.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  16 APTVAHCQFVRDDGQPldFQPGQFIQIHFAAADgtPTKRSYSLATihdhalGPGEA--VDIAVSFVPGG-SATALFEGLE 92
Cdd:PRK10684   21 TPDVWTISLICHDFYP--YRAGQYALVSIRNSA--ETLRAYTLSS------TPGVSefITLTVRRIDDGvGSQWLTRDVK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  93 IGDPLQASGPYGRF-CLQAGDhnQRYVLIATGTGVTPYRSMLPLLAEAIASRSVQVVLlqGARTPAELLYGDDFRAFAQA 171
Cdd:PRK10684   91 RGDYLWLSDAMGEFtCDDKAE--DKYLLLAAGCGVTPIMSMRRWLLKNRPQADVQVIF--NVRTPQDVIFADEWRQLKQR 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1796985942 172 HPQFRylpclsreLPAPAHADVRHGYV-----QQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQIRREKY 245
Cdd:PRK10684  167 YPQLN--------LTLVAENNATEGFIagrltRELLQQAVPDLASRTVMTCGPAPYMDWVEQEVKALGVTADRFFKEKF 237
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
7-243 3.35e-11

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: 61.10  E-value: 3.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   7 LKLVDRRMLAPTVAHCQFVRDDGqpLDFQPGQfiQIHFA-AADG-TPTKRSYSLATIhdhalgPGEAVdiaVSFV----P 80
Cdd:cd06196     3 VTLLSIEPVTHDVKRLRFDKPEG--YDFTPGQ--ATEVAiDKPGwRDEKRPFTFTSL------PEDDV---LEFViksyP 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  81 G-GSATALFEGLEIGDPLQASGPYGRFclqagdhnqRY----VLIATGTGVTPYRSMLPLLAEAIASRSVQvvLLQGART 155
Cdd:cd06196    70 DhDGVTEQLGRLQPGDTLLIEDPWGAI---------EYkgpgVFIAGGAGITPFIAILRDLAAKGKLEGNT--LIFANKT 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 156 PAELLYGDDFRAFaqahPQFRYLPCLSRElPAPAHAdvrHGYV-QQHLAEIAPDAStDIAYLCGNPDMVDACAEALKAAG 234
Cdd:cd06196   139 EKDIILKDELEKM----LGLKFINVVTDE-KDPGYA---HGRIdKAFLKQHVTDFN-QHFYVCGPPPMEEAINGALKELG 209

                  ....*....
gi 1796985942 235 LPNAQIRRE 243
Cdd:cd06196   210 VPEDSIVFE 218
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
33-234 2.24e-09

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


Pssm-ID: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 56.18  E-value: 2.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  33 DFQPGQFIQIHFAAADGTpTKRSYSLATIHdhalgpGEAVDIAVSFVPGGSATALFEGLEIGDPLQASGPYGR-FCLqaG 111
Cdd:cd06192    24 LFRPGQFVFLRNFESPGL-ERIPLSLAGVD------PEEGTISLLVEIRGPKTKLIAELKPGEKLDVMGPLGNgFEG--P 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 112 DHNQRYVLIATGTGVTPyrsMLPlLAEAIASRSVQVVLLQGARTPAELLYGDDFRAFAQAHpqfrYLPCLSRELPAPAHA 191
Cdd:cd06192    95 KKGGTVLLVAGGIGLAP---LLP-IAKKLAANGNKVTVLAGAKKAKEEFLDEYFELPADVE----IWTTDDGELGLEGKV 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1796985942 192 DVrhgyvqqhLAEIAPDASTDIAYLCGNPDMVDACAEALKAAG 234
Cdd:cd06192   167 TD--------SDKPIPLEDVDRIIVAGSDIMMKAVVEALDEWL 201
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
16-234 4.18e-09

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: 55.42  E-value: 4.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  16 APTVAHCQFVRDDGQPLDFQPGQFIQIHFaaaDGTPTKRSYSLATIHDHALGPgeaVDIAVSFVPG---------GSATA 86
Cdd:cd06182    14 PRSTRHLEFDLSGNSVLKYQPGDHLGVIP---PNPLQPRYYSIASSPDVDPGE---VHLCVRVVSYeapagrirkGVCSN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  87 LFEGLEIGDPLQASGPYGRFCLQAGDHNQRYVLIATGTGVTPYRSML---PLLAEAIASRSvQVVLLQGARTPAE-LLYG 162
Cdd:cd06182    88 FLAGLQLGAKVTVFIRPAPSFRLPKDPTTPIIMVGPGTGIAPFRGFLqerAALRANGKARG-PAWLFFGCRNFASdYLYR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 163 DDFRAFAQAHPQFRYLPCLSRElpaPAHADVrhgYVQQHLAEIApDASTDI------AYLCGN-----PDMVDACAEALK 231
Cdd:cd06182   167 EELQEALKDGALTRLDVAFSRE---QAEPKV---YVQDKLKEHA-EELRRLlnegahIYVCGDaksmaKDVEDALVKIIA 239

                  ...
gi 1796985942 232 AAG 234
Cdd:cd06182   240 KAG 242
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
6-106 7.20e-09

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 51.81  E-value: 7.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   6 PLKLVDRRMLAPTVAHCQF-VRDDGQPLDFQPGQFIQIHfAAADGTPTKRSYSLATiHDHALGpgeAVDIAVSFVPGGSA 84
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFaLPHPDQVLGLPVGQHLFLR-LPIDGELVIRSYTPIS-SDDDKG---YLELLVKVYPGGKM 75
                          90       100
                  ....*....|....*....|..
gi 1796985942  85 TALFEGLEIGDPLQASGPYGRF 106
Cdd:pfam00970  76 SQYLDELKIGDTIDFKGPLGRF 97
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
34-222 1.13e-08

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 55.01  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  34 FQPGQFIQIHFAAAD--GTPTK-RSYSLATIHDHALGPGEAVDIAV----------SFVPGGSATALFEgLEIGDPLQAS 100
Cdd:PLN03115  123 YREGQSIGVIPDGIDknGKPHKlRLYSIASSALGDFGDSKTVSLCVkrlvytndqgEIVKGVCSNFLCD-LKPGAEVKIT 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 101 GPYGRFCLQAGDHNQRYVLIATGTGVTPYRSML-PLLAEAIASRSVQVV--LLQGARTPAELLYGDDFRAFAQAHPQ-FR 176
Cdd:PLN03115  202 GPVGKEMLMPKDPNATIIMLATGTGIAPFRSFLwKMFFEKHDDYKFNGLawLFLGVPTSSSLLYKEEFEKMKEKAPEnFR 281
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1796985942 177 YLPCLSRElpaPAHADVRHGYVQQHLAEIAPD------ASTDIAYLCGNPDM 222
Cdd:PLN03115  282 LDFAVSRE---QTNAKGEKMYIQTRMAEYAEElwellkKDNTYVYMCGLKGM 330
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
54-223 5.29e-08

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: 52.71  E-value: 5.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  54 RSYSLATIHdhALGPGEAVDI--AVSFVPGGSATALFEGL-----EIGDPLQASG-PYGRFCLQAGDHNQRYVLIATGTG 125
Cdd:cd06203   175 RPYSIASSP--LEGPGKLRFIfsVVEFPAKGLCTSWLESLclsasSHGVKVPFYLrSSSRFRLPPDDLRRPIIMVGPGTG 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 126 VTPYRSMLPLLAEAIASRS----VQVVLLQGARTPAE-LLYGDDFRAFAQAHPQFRYLPCLSRELPAPAHadvrHGYVQ- 199
Cdd:cd06203   253 VAPFLGFLQHREKLKESHTetvfGEAWLFFGCRHRDRdYLFRDELEEFLEEGILTRLIVAFSRDENDGST----PKYVQd 328
                         170       180
                  ....*....|....*....|....*....
gi 1796985942 200 ---QHLAEIAP--DASTDIAYLCGNPDMV 223
Cdd:cd06203   329 kleERGKKLVDllLNSNAKIYVCGDAKGM 357
fre PRK08051
FMN reductase; Validated
30-225 7.52e-08

FMN reductase; Validated


Pssm-ID: 236142 [Multi-domain]  Cd Length: 232  Bit Score: 51.78  E-value: 7.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  30 QPLDFQPGQFIQIHFAAADgtptKRSYSLAT---------IH----DHALGPGEAVDiavsfvpggsatALFEGLEIgdp 96
Cdd:PRK08051   26 APFSFRAGQYLMVVMGEKD----KRPFSIAStprekgfieLHigasELNLYAMAVME------------RILKDGEI--- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  97 lQASGPYGRFCLQAGDHNQRyVLIATGTGVTPYRSMLpllaEAIASRS--VQVVLLQGARTPAELLYGDDFRAFAQAHPQ 174
Cdd:PRK08051   87 -EVDIPHGDAWLREESERPL-LLIAGGTGFSYARSIL----LTALAQGpnRPITLYWGGREEDHLYDLDELEALALKHPN 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1796985942 175 FRYLPCLsrELPaPAHADVRHGYV-QQHLAEIAPDASTDIaYLCGNPDMVDA 225
Cdd:PRK08051  161 LHFVPVV--EQP-EEGWQGKTGTVlTAVMQDFGSLAEYDI-YIAGRFEMAKI 208
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
2-230 1.12e-07

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99798 [Multi-domain]  Cd Length: 289  Bit Score: 51.56  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   2 PVQFPLKLVDRRML-----APTV-----AHCQFVRDDGQPlDFQPGQFIQIhfaAADGTPTKRSYSLATIHDHalgpgEA 71
Cdd:cd06201    43 PRTKALELVERKDYgaavqAPTAilrfkPAKRKLSGKGLP-SFEAGDLLGI---LPPGSDVPRFYSLASSSSD-----GF 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  72 VDIAVSFVPGGSATALFEGLEIGDPLQAS-GPYGRFCLQAGDHNqrYVLIATGTGVTPYRSMLpllaEAIASRsVQVVLL 150
Cdd:cd06201   114 LEICVRKHPGGLCSGYLHGLKPGDTIKAFiRPNPSFRPAKGAAP--VILIGAGTGIAPLAGFI----RANAAR-RPMHLY 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 151 QGARTPA-ELLYGDDFRAFAQAHP--QFRYlpCLSRElPAPAhadvrhgYVQQHLAEIAPDASTDIA-----YLCGNPDM 222
Cdd:cd06201   187 WGGRDPAsDFLYEDELDQYLADGRltQLHT--AFSRT-PDGA-------YVQDRLRADAERLRRLIEdgaqiMVCGSRAM 256

                  ....*...
gi 1796985942 223 VDACAEAL 230
Cdd:cd06201   257 AQGVAAVL 264
PLN02252 PLN02252
nitrate reductase [NADPH]
77-240 1.81e-07

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 51.60  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  77 SFVPGGSATALFEGLEIGDPLQASGPYGRFcLQAG------DHNQRYV----LIATGTGVTPyrsMLPLLAEAIASR--S 144
Cdd:PLN02252  712 KFPNGGLMSQYLDSLPIGDTIDVKGPLGHI-EYAGrgsflvNGKPKFAkklaMLAGGTGITP---MYQVIQAILRDPedK 787
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 145 VQVVLLQGARTPAELLYGDDFRAFAQAHP-QFRYLPCLSRelPAPAHADVRHGYV-----QQHLAEIAPDAstdIAYLCG 218
Cdd:PLN02252  788 TEMSLVYANRTEDDILLREELDRWAAEHPdRLKVWYVVSQ--VKREGWKYSVGRVteamlREHLPEGGDET---LALMCG 862
                         170       180
                  ....*....|....*....|...
gi 1796985942 219 NPDMV-DACAEALKAAGLPNAQI 240
Cdd:PLN02252  863 PPPMIeFACQPNLEKMGYDKDSI 885
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
30-240 5.42e-07

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 49.72  E-value: 5.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  30 QPLDFQPGQfiqiHFAAADGTPTKRSYSLATI---------HDHALGPGEAVDIAvsfvpggsatalfEGLEIGDPLQAS 100
Cdd:PRK05713  115 RPLRYRAGQ----HLVLWTAGGVARPYSLASLpgedpflefHIDCSRPGAFCDAA-------------RQLQVGDLLRLG 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 101 GPYGRFCLQAGDHNQR-YVLIATGTGVTPyrsMLPLLAEAI-ASRSVQVVLLQGARTPAELLYGDDFRAFAQAHPQfryl 178
Cdd:PRK05713  178 ELRGGALHYDPDWQERpLWLLAAGTGLAP---LWGILREALrQGHQGPIRLLHLARDSAGHYLAEPLAALAGRHPQ---- 250
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1796985942 179 pcLSRELPAPAHadvrhgyVQQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQI 240
Cdd:PRK05713  251 --LSVELVTAAQ-------LPAALAELRLVSRQTMALLCGSPASVERFARRLYLAGLPRNQL 303
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
2-234 5.78e-06

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 46.36  E-value: 5.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942   2 PVQF-PLKLVDRRmlapTVAHCQFV-----RDDGQPLDFQPGQfiQIHFAAADGTPTK-----RSYSLATIHDHaLGpge 70
Cdd:PTZ00319   30 PDMFqHFKLIKKT----EVTHDTFIfrfalHSPTQRLGLPIGQ--HIVFRCDCTTPGKpetvqHSYTPISSDDE-KG--- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  71 AVDIAV---------SFVPGGSATALFEGLEIGDPLQASGPYGRF--------CLQAG------DHNQRYVLIATGTGVT 127
Cdd:PTZ00319  100 YVDFLIkvyfkgvhpSFPNGGRLSQHLYHMKLGDKIEMRGPVGKFeylgngtyTVHKGkgglktMHVDAFAMIAGGTGIT 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 128 PYRSMLPLLAEAIASRSvQVVLLQGARTPAELLYGDDFRAFAQaHPQFRYLPCLSRELPAPAHADVrhGYV-----QQHL 202
Cdd:PTZ00319  180 PMLQIIHAIKKNKEDRT-KVFLVYANQTEDDILLRKELDEAAK-DPRFHVWYTLDREATPEWKYGT--GYVdeemlRAHL 255
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1796985942 203 AEIAPDASTD---IAYLCGNPDMV-DACAEALKAAG 234
Cdd:PTZ00319  256 PVPDPQNSGIkkvMALMCGPPPMLqMAVKPNLEKIG 291
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
54-232 4.77e-05

NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99803 [Multi-domain]  Cd Length: 382  Bit Score: 43.80  E-value: 4.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  54 RSYSLATIHDHAlgpGEAVDIAVSFV----PGGS-----ATALFEGLEIGDPLqasgpygRFCLQAG------DHNQRYV 118
Cdd:cd06207   165 RYYSISSSPLKN---PNEVHLLVSLVswktPSGRsryglCSSYLAGLKVGQRV-------TVFIKKSsfklpkDPKKPII 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 119 LIATGTGVTPYRSMLPLLAEAIA--SRSVQVVLLQGARTPA-ELLYGDDFRAFAQAHPQFRYLPCLSRELPAPAhadvrh 195
Cdd:cd06207   235 MVGPGTGLAPFRAFLQERAALLAqgPEIGPVLLYFGCRHEDkDYLYKEELEEYEKSGVLTTLGTAFSRDQPKKV------ 308
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1796985942 196 gYVQ----QHLAEIA----PDAStdIAYLCGN-----PDMVDACAEALKA 232
Cdd:cd06207   309 -YVQdlirENSDLVYqlleEGAG--VIYVCGStwkmpPDVQEAFEEILKK 355
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
34-240 8.58e-05

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 42.87  E-value: 8.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  34 FQPGQFIQIHFAAAD-------GTPTKRSYslatihdhalgpgeaVDIAVSFVpgGSATALFEGLEIGDPLQASGPYGR- 105
Cdd:PRK08345   38 FKPGQFVQVTIPGVGevpisicSSPTRKGF---------------FELCIRRA--GRVTTVIHRLKEGDIVGVRGPYGNg 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 106 FCLQAGDhNQRYVLIATGTGVTPYRSmlpLLAEAIASRSV--QVVLLQGARTPAELLYGDDFRAFAQAHPQFRYLPCLSR 183
Cdd:PRK08345  101 FPVDEME-GMDLLLIAGGLGMAPLRS---VLLYAMDNRWKygNITLIYGAKYYEDLLFYDELIKDLAEAENVKIIQSVTR 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1796985942 184 ELPAPAH--------ADVRHGYVQQHLAEIAPDASTDIAYLCGNPDMVDACAEALKAAGLPNAQI 240
Cdd:PRK08345  177 DPEWPGChglpqgfiERVCKGVVTDLFREANTDPKNTYAAICGPPVMYKFVFKELINRGYRPERI 241
bifunctional_CYPOR cd06206
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ...
54-235 7.18e-04

These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase (CYPOR). NADPH cytochrome p450 reductase serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99802 [Multi-domain]  Cd Length: 384  Bit Score: 40.32  E-value: 7.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  54 RSYSLATihDHALGPGEAvDIAVSFV--PGGSATALFEG--------LEIGDPLQAS--GPYGRFCLQAgDHNQRYVLIA 121
Cdd:cd06206   162 RQYSISS--SPLVDPGHA-TLTVSVLdaPALSGQGRYRGvassylssLRPGDSIHVSvrPSHSAFRPPS-DPSTPLIMIA 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 122 TGTGVTPYRSMLPLLAEAIASRSVQ--VVLLQGARTP-AELLYGDDFRAFAQA-----HPQFrylpclSRelpapaHADV 193
Cdd:cd06206   238 AGTGLAPFRGFLQERAALLAQGRKLapALLFFGCRHPdHDDLYRDELEEWEAAgvvsvRRAY------SR------PPGG 305
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1796985942 194 RHGYVQQHLAEIAPD-----ASTDIAYLCGNPDMVDACAEALKAAGL 235
Cdd:cd06206   306 GCRYVQDRLWAEREEvwelwEQGARVYVCGDGRMAPGVREVLKRIYA 352
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
35-144 2.12e-03

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: 38.05  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942  35 QPGQFIQIHFAAADGtPTKRsyslatIHDHALGPGEavdiavsfvPGGSATALFEGleigdplqasgPYGRFCLQAGDHn 114
Cdd:cd06186    55 DEQDTLSLIIRAKKG-FTTR------LLRKALKSPG---------GGVSLKVLVEG-----------PYGSSSEDLLSY- 106
                          90       100       110
                  ....*....|....*....|....*....|
gi 1796985942 115 QRYVLIATGTGVTPyrsMLPLLAEAIASRS 144
Cdd:cd06186   107 DNVLLVAGGSGITF---VLPILRDLLRRSS 133
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
136-235 6.93e-03

TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria; TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria. The Tor respiratory system is consists of three proteins (TorC, TorA, and TorD) and is induced in the presence of TMAO. The TMAO control is tightly regulated by three proteins: TorS, TorT, and TorR. Thus, the disruption of any of these proteins can abolish the Tor respiratory induction. TorT shares homology with the sugar-binding domain of the type 1 periplasmic binding proteins. The members of TorT-like family bind TMAO or related compounds and are predicted to be involved in signal transduction and/or substrate transport.


Pssm-ID: 380529 [Multi-domain]  Cd Length: 269  Bit Score: 37.18  E-value: 6.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796985942 136 LAEAIASRSVQVVLLQGARTP--AELLYgDDFRAFAQAHpqfrylpclSRELPAPAHADVRHGyVQQHLAEIAPDASTDI 213
Cdd:cd06306   116 LVEHHPGKPVKVAWFPGPAGAgwAEDRE-KGFKEALAGS---------NVEIVATKYGDTGKA-VQLNLVEDALQAHPDI 184
                          90       100
                  ....*....|....*....|..
gi 1796985942 214 AYLCGNPDMVDACAEALKAAGL 235
Cdd:cd06306   185 DYIVGNAVAAEAAVGALREAGL 206
 
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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