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Conserved domains on  [gi|2620196322|ref|XP_001482475|]
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uncharacterized protein PGUG_05495 [Meyerozyma guilliermondii ATCC 6260]

Protein Classification

cytochrome b5 reductase family protein( domain architecture ID 10153046)

cytochrome b5 reductase family protein such as NADH-cytochrome b5 reductase that catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor; the cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes

CATH:  3.40.50.80
EC:  1.-.-.-
Gene Ontology:  GO:0016491
PubMed:  19997042

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 50-294 2.29e-105

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: 306.42  E-value: 2.29e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  50 LKLKKSWDVSSNTRHFVFELKSPEDVSGLVTASCLMTKFVTaKGNNVIRPYTPVSDVDQKGTIDFVIKKYDGGKMSTHFH 129
Cdd:cd06183     1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPD-DGEQVVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYLH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 130 GLKEGDTVSFKGPIVKWKWEPNQ-FQSIALIGGGTGITPLYQLLHEITKNPEDKTKVKLFYGNLTEEDILIKKELDDIAE 208
Cdd:cd06183    80 SLKPGDTVEIRGPFGKFEYKPNGkVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKISLLYANRTEEDILLREELDELAK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 209 KHKDQVSITYFVDKASANWKGETGHIDKEFLQSNLP-GPSKDSKVFVCGPPGLYKalsgvkvsptdqGEVTGVLAELGYT 287
Cdd:cd06183   160 KHPDRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPpPPSEDTLVLVCGPPPMIE------------GAVKGLLKELGYK 227


                  ....*..
gi 2620196322 288 KENVYKF 294
Cdd:cd06183   228 KDNVFKF 234
 
Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 50-294 2.29e-105

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: 306.42  E-value: 2.29e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  50 LKLKKSWDVSSNTRHFVFELKSPEDVSGLVTASCLMTKFVTaKGNNVIRPYTPVSDVDQKGTIDFVIKKYDGGKMSTHFH 129
Cdd:cd06183     1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPD-DGEQVVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYLH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 130 GLKEGDTVSFKGPIVKWKWEPNQ-FQSIALIGGGTGITPLYQLLHEITKNPEDKTKVKLFYGNLTEEDILIKKELDDIAE 208
Cdd:cd06183    80 SLKPGDTVEIRGPFGKFEYKPNGkVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKISLLYANRTEEDILLREELDELAK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 209 KHKDQVSITYFVDKASANWKGETGHIDKEFLQSNLP-GPSKDSKVFVCGPPGLYKalsgvkvsptdqGEVTGVLAELGYT 287
Cdd:cd06183   160 KHPDRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPpPPSEDTLVLVCGPPPMIE------------GAVKGLLKELGYK 227


                  ....*..
gi 2620196322 288 KENVYKF 294
Cdd:cd06183   228 KDNVFKF 234
PLN02252 PLN02252
nitrate reductase [NADPH]
 46-294 9.79e-60

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 204.14  E-value: 9.79e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  46 EWIDLKLKKSWDVSSNTRHFVFELKSPEDVSGLVTASCLmtkFVTAK--GNNVIRPYTPVSDVDQKGTIDFVIKKY---- 119
Cdd:PLN02252  633 EKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHV---FLCATinGKLCMRAYTPTSSDDEVGHFELVIKVYfknv 709

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 120 -----DGGKMSTHFHGLKEGDTVSFKGPIVKWKW----------EPNQFQSIALIGGGTGITPLYQLLHEITKNPEDKTK 184
Cdd:PLN02252  710 hpkfpNGGLMSQYLDSLPIGDTIDVKGPLGHIEYagrgsflvngKPKFAKKLAMLAGGTGITPMYQVIQAILRDPEDKTE 789

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 185 VKLFYGNLTEEDILIKKELDDIAEKHKDQVSITYFVDK-ASANWKGETGHIDKEFLQSNLPGPSKDSKVFVCGPPGLYka 263
Cdd:PLN02252  790 MSLVYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQvKREGWKYSVGRVTEAMLREHLPEGGDETLALMCGPPPMI-- 867

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2620196322 264 lsgvkvsptdQGEVTGVLAELGYTKENVYKF 294
Cdd:PLN02252  868 ----------EFACQPNLEKMGYDKDSILVF 888
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 158-263 2.04e-34

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: 120.83  E-value: 2.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 158 LIGGGTGITPLYQLLHEITKNPEDKTKVKLFYGNLTEEDILIKKELDDIAEKHKDQVSITYFVDKASANWKGETGHIDKE 237
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKDPTQVVLVFGNRNEDDILYREELDELAEKHPGRLTVVYVVSRPEAGWTGGKGRVQDA 80

                          90       100
                  ....*....|....*....|....*.
gi 2620196322 238 FLQSNLPGPSKDSKVFVCGPPGLYKA 263
Cdd:pfam00175  81 LLEDHLSLPDEETHVYVCGPPGMIKA 106
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
45-292 4.85e-31

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 115.66  E-value: 4.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  45 DEWIDLKLKKSWDVSSNTRHFVFElksPEDVSGLVTasclmtkF---------VTAKGNNVIRPYTPVSDVDQkGTIDFV 115
Cdd:COG1018     1 AGFRPLRVVEVRRETPDVVSFTLE---PPDGAPLPR-------FrpgqfvtlrLPIDGKPLRRAYSLSSAPGD-GRLEIT 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 116 IKKYDGGKMSTHFH-GLKEGDTVSFKGPIVKWKWEPNQFQSIALIGGGTGITPLYQLLHEITKNpEDKTKVKLFYGNLTE 194
Cdd:COG1018    70 VKRVPGGGGSNWLHdHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLAR-GPFRPVTLVYGARSP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 195 EDILIKKELDDIAEKHkDQVSITYFVDKASAnwkGETGHIDKEFLQSNLPGPSkDSKVFVCGPPGLYKAlsgvkvsptdq 274
Cdd:COG1018   149 ADLAFRDELEALAARH-PRLRLHPVLSREPA---GLQGRLDAELLAALLPDPA-DAHVYLCGPPPMMEA----------- 212

                         250
                  ....*....|....*...
gi 2620196322 275 geVTGVLAELGYTKENVY 292
Cdd:COG1018   213 --VRAALAELGVPEERIH 228
 
Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 50-294 2.29e-105

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: 306.42  E-value: 2.29e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  50 LKLKKSWDVSSNTRHFVFELKSPEDVSGLVTASCLMTKFVTaKGNNVIRPYTPVSDVDQKGTIDFVIKKYDGGKMSTHFH 129
Cdd:cd06183     1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPD-DGEQVVRPYTPISPDDDKGYFDLLIKIYPGGKMSQYLH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 130 GLKEGDTVSFKGPIVKWKWEPNQ-FQSIALIGGGTGITPLYQLLHEITKNPEDKTKVKLFYGNLTEEDILIKKELDDIAE 208
Cdd:cd06183    80 SLKPGDTVEIRGPFGKFEYKPNGkVKHIGMIAGGTGITPMLQLIRAILKDPEDKTKISLLYANRTEEDILLREELDELAK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 209 KHKDQVSITYFVDKASANWKGETGHIDKEFLQSNLP-GPSKDSKVFVCGPPGLYKalsgvkvsptdqGEVTGVLAELGYT 287
Cdd:cd06183   160 KHPDRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPpPPSEDTLVLVCGPPPMIE------------GAVKGLLKELGYK 227


                  ....*..
gi 2620196322 288 KENVYKF 294
Cdd:cd06183   228 KDNVFKF 234
PLN02252 PLN02252
nitrate reductase [NADPH]
 46-294 9.79e-60

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 204.14  E-value: 9.79e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  46 EWIDLKLKKSWDVSSNTRHFVFELKSPEDVSGLVTASCLmtkFVTAK--GNNVIRPYTPVSDVDQKGTIDFVIKKY---- 119
Cdd:PLN02252  633 EKIPCRLVEKISLSHDVRLFRFALPSEDHVLGLPVGKHV---FLCATinGKLCMRAYTPTSSDDEVGHFELVIKVYfknv 709

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 120 -----DGGKMSTHFHGLKEGDTVSFKGPIVKWKW----------EPNQFQSIALIGGGTGITPLYQLLHEITKNPEDKTK 184
Cdd:PLN02252  710 hpkfpNGGLMSQYLDSLPIGDTIDVKGPLGHIEYagrgsflvngKPKFAKKLAMLAGGTGITPMYQVIQAILRDPEDKTE 789

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 185 VKLFYGNLTEEDILIKKELDDIAEKHKDQVSITYFVDK-ASANWKGETGHIDKEFLQSNLPGPSKDSKVFVCGPPGLYka 263
Cdd:PLN02252  790 MSLVYANRTEDDILLREELDRWAAEHPDRLKVWYVVSQvKREGWKYSVGRVTEAMLREHLPEGGDETLALMCGPPPMI-- 867

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2620196322 264 lsgvkvsptdQGEVTGVLAELGYTKENVYKF 294
Cdd:PLN02252  868 ----------EFACQPNLEKMGYDKDSILVF 888
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 45-294 1.90e-54

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 178.87  E-value: 1.90e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  45 DEWIDLKLKKSWDVSSNTRHFVFELKSPEDVSGLVTA-----SCLMTKfvTAKGNNVIRPYTPVSDVDQKGTIDFVIKKY 119
Cdd:PTZ00319   31 DMFQHFKLIKKTEVTHDTFIFRFALHSPTQRLGLPIGqhivfRCDCTT--PGKPETVQHSYTPISSDDEKGYVDFLIKVY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 120 ---------DGGKMSTHFHGLKEGDTVSFKGPIVKWKWEPNQFQSI---------------ALIGGGTGITPLYQLLHEI 175
Cdd:PTZ00319  109 fkgvhpsfpNGGRLSQHLYHMKLGDKIEMRGPVGKFEYLGNGTYTVhkgkgglktmhvdafAMIAGGTGITPMLQIIHAI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 176 TKNPEDKTKVKLFYGNLTEEDILIKKELDDIAEkhKDQVSITYFVDK-ASANWKGETGHIDKEFLQSNLPGPS------K 248
Cdd:PTZ00319  189 KKNKEDRTKVFLVYANQTEDDILLRKELDEAAK--DPRFHVWYTLDReATPEWKYGTGYVDEEMLRAHLPVPDpqnsgiK 266

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2620196322 249 DSKVFVCGPPglykalsgvkvsPTDQGEVTGVLAELGYTKENVYKF 294
Cdd:PTZ00319  267 KVMALMCGPP------------PMLQMAVKPNLEKIGYTADNMFTF 300
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
 98-294 2.88e-38

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 137.36  E-value: 2.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  98 RPYTPVSDVDQKGTIDFVIKKYDGGKMSTHFHGLKEGDTVSFKGPIVKWKWEPNQFQSIALIGGGTGITPLYQLL-HEIT 176
Cdd:PTZ00274  104 RFYTPVTANHTKGYFDIIVKRKKDGLMTNHLFGMHVGDKLLFRSVTFKIQYRPNRWKHVGMIAGGTGFTPMLQIIrHSLT 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 177 KNPE----DKTKVKLFYGNLTEEDILIKKELDDIAEKHKDQVSITYFVDKA--SANWKGETGHIDKEFLQSNLPGPSKDS 250
Cdd:PTZ00274  184 EPWDsgevDRTKLSFLFCNRTERHILLKGLFDDLARRYSNRFKVYYTIDQAvePDKWNHFLGYVTKEMVRRTMPAPEEKK 263

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2620196322 251 K-VFVCGPPGLYKAL------------SGVKVSP--TDQGEVT---GVLAELGYTKENVYKF 294
Cdd:PTZ00274  264 KiIMLCGPDQLLNHVagtpmgtmssmsSGMNIQPmaPDLNNLVslgGILGELGYDNDDVYRF 325
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 47-286 3.83e-36

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: 129.31  E-value: 3.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  47 WIDLKLKKSWDVSSNTRHFVFelkspeDVSGLVTASCLMTKFVTAK-----GNNVIRPYTPVSDVDQKGTIDFVIKKYDG 121
Cdd:cd06217     1 WRVLRVTEIIQETPTVKTFRL------AVPDGVPPPFLAGQHVDLRltaidGYTAQRSYSIASSPTQRGRVELTVKRVPG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 122 GKMSTHFHG-LKEGDTVSFKGPIVKWKWEPNQFQSIALIGGGTGITPLYQLLHEITKNpEDKTKVKLFYGNLTEEDILIK 200
Cdd:cd06217    75 GEVSPYLHDeVKVGDLLEVRGPIGTFTWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDL-GWPVPFRLLYSARTAEDVIFR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 201 KELDDIAEKHKD-QVSITYfVDKASANWKGETGHIDKEFLQSnLPGPSKDSKVFVCGPPGLYkalsgvkvsptdqGEVTG 279
Cdd:cd06217   154 DELEQLARRHPNlHVTEAL-TRAAPADWLGPAGRITADLIAE-LVPPLAGRRVYVCGPPAFV-------------EAATR 218


                  ....*..
gi 2620196322 280 VLAELGY 286
Cdd:cd06217   219 LLLELGV 225
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 92-265 9.12e-36

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: 127.95  E-value: 9.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  92 KGNNVIRPYTPVSDVDQKGTIDFVIKKYDGGKMSTHFHGLKEGDTVSFKGPIVKWKWEPNQFQSIALIGGGTGITPLYQL 171
Cdd:cd00322    36 DGRGLRRAYSIASSPDEEGELELTVKIVPGGPFSAWLHDLKPGDEVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSM 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 172 LHEITKNpEDKTKVKLFYGNLTEEDILIKKELDDIAEKHKDQVSITYFvDKASANWKGETGHIDKEFLQSNLPGPSKDSK 251
Cdd:cd00322   116 LRHLAAD-KPGGEITLLYGARTPADLLFLDELEELAKEGPNFRLVLAL-SRESEAKLGPGGRIDREAEILALLPDDSGAL 193

                         170
                  ....*....|....
gi 2620196322 252 VFVCGPPGLYKALS 265
Cdd:cd00322   194 VYICGPPAMAKAVR 207
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 158-263 2.04e-34

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: 120.83  E-value: 2.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 158 LIGGGTGITPLYQLLHEITKNPEDKTKVKLFYGNLTEEDILIKKELDDIAEKHKDQVSITYFVDKASANWKGETGHIDKE 237
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKDPTQVVLVFGNRNEDDILYREELDELAEKHPGRLTVVYVVSRPEAGWTGGKGRVQDA 80

                          90       100
                  ....*....|....*....|....*.
gi 2620196322 238 FLQSNLPGPSKDSKVFVCGPPGLYKA 263
Cdd:pfam00175  81 LLEDHLSLPDEETHVYVCGPPGMIKA 106
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 99-292 2.32e-33

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: 122.33  E-value: 2.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  99 PYTPVSDVDQKGTIDFVIKKYdgGKMSTHFHGLKEGDTVSFKGPIVKWkWEPNQFQ--SIALIGGGTGITPLYQLLHEIT 176
Cdd:cd06221    45 PISISSDPTRRGPLELTIRRV--GRVTEALHELKPGDTVGLRGPFGNG-FPVEEMKgkDLLLVAGGLGLAPLRSLINYIL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 177 KNPEDKTKVKLFYGNLTEEDILIKKELDDIAEKHKDQVSITyfVDKASANWKGETGHIDKEFLQsnLPGPSKDSKVFVCG 256
Cdd:cd06221   122 DNREDYGKVTLLYGARTPEDLLFKEELKEWAKRSDVEVILT--VDRAEEGWTGNVGLVTDLLPE--LTLDPDNTVAIVCG 197

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2620196322 257 PPGLYKAlsgvkvsptdqgeVTGVLAELGYTKENVY 292
Cdd:cd06221   198 PPIMMRF-------------VAKELLKLGVPEEQIW 220
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
45-292 4.85e-31

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 115.66  E-value: 4.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  45 DEWIDLKLKKSWDVSSNTRHFVFElksPEDVSGLVTasclmtkF---------VTAKGNNVIRPYTPVSDVDQkGTIDFV 115
Cdd:COG1018     1 AGFRPLRVVEVRRETPDVVSFTLE---PPDGAPLPR-------FrpgqfvtlrLPIDGKPLRRAYSLSSAPGD-GRLEIT 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 116 IKKYDGGKMSTHFH-GLKEGDTVSFKGPIVKWKWEPNQFQSIALIGGGTGITPLYQLLHEITKNpEDKTKVKLFYGNLTE 194
Cdd:COG1018    70 VKRVPGGGGSNWLHdHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLAR-GPFRPVTLVYGARSP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 195 EDILIKKELDDIAEKHkDQVSITYFVDKASAnwkGETGHIDKEFLQSNLPGPSkDSKVFVCGPPGLYKAlsgvkvsptdq 274
Cdd:COG1018   149 ADLAFRDELEALAARH-PRLRLHPVLSREPA---GLQGRLDAELLAALLPDPA-DAHVYLCGPPPMMEA----------- 212

                         250
                  ....*....|....*...
gi 2620196322 275 geVTGVLAELGYTKENVY 292
Cdd:COG1018   213 --VRAALAELGVPEERIH 228
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
49-148 6.80e-31

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 111.13  E-value: 6.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  49 DLKLKKSWDVSSNTRHFVFELKSPEDVSGLVTASCLMTKfVTAKGNNVIRPYTPVSDVDQKGTIDFVIKKYDGGKMSTHF 128
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQHLFLR-LPIDGELVIRSYTPISSDDDKGYLELLVKVYPGGKMSQYL 79

                          90       100
                  ....*....|....*....|
gi 2620196322 129 HGLKEGDTVSFKGPIVKWKW 148
Cdd:pfam00970  80 DELKIGDTIDFKGPLGRFEY 99
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 98-292 2.37e-25

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 101.09  E-value: 2.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  98 RPYTPVSDVDQKGTIDFVIKKYdgGKMSTHFHGLKEGDTVSFKGPIvkWK-WE-PNQFQSIALIGGGTGITPLYQLLHEI 175
Cdd:COG0543    43 RPFSIASAPREDGTIELHIRVV--GKGTRALAELKPGDELDVRGPL--GNgFPlEDSGRPVLLVAGGTGLAPLRSLAEAL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 176 TKNPEdktKVKLFYGNLTEEDILIKKELDDIAEkhkdqVSITYFVDkasANWKGETGHIDKEFLQsnLPGPSKDSKVFVC 255
Cdd:COG0543   119 LARGR---RVTLYLGARTPEDLYLLDELEALAD-----FRVVVTTD---DGWYGRKGFVTDALKE--LLAEDSGDDVYAC 185

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2620196322 256 GPPGLYKAlsgvkvsptdqgeVTGVLAELGYTKENVY 292
Cdd:COG0543   186 GPPPMMKA-------------VAELLLERGVPPERIY 209
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 93-293 2.77e-23

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: 95.35  E-value: 2.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  93 GNNVIRPYTPVSDVDQKGTIDFVIKKYDGGKMSTHFH-GLKEGDTVSFKGPIVKWKWEPNQFQSIALIGGGTGITPLYQL 171
Cdd:cd06215    42 GETVYRAYTLSSSPSRPDSLSITVKRVPGGLVSNWLHdNLKVGDELWASGPAGEFTLIDHPADKLLLLSAGSGITPMMSM 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 172 LHEITKNPEDkTKVKLFYGNLTEEDILIKKELDDIAEKHkDQVSITYFV-DKASANWKGETGHIDKEFLQsNLPGPSKDS 250
Cdd:cd06215   122 ARWLLDTRPD-ADIVFIHSARSPADIIFADELEELARRH-PNFRLHLILeQPAPGAWGGYRGRLNAELLA-LLVPDLKER 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2620196322 251 KVFVCGPPGLYKAlsgvkvsptdqgeVTGVLAELGYTKENVYK 293
Cdd:cd06215   199 TVFVCGPAGFMKA-------------VKSLLAELGFPMSRFHQ 228
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 54-294 8.63e-23

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: 96.86  E-value: 8.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  54 KSWD--VSSNT------RHFVFELKSPEDV-------------------SGLVTASCLMTKFVTAKGNNVIRPYTPVSDV 106
Cdd:COG2871   130 KKWEatVVSNEnvttfiKELVLELPEGEEIdfkagqyiqievppyevdfKDFDIPEEEKFGLFDKNDEEVTRAYSMANYP 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 107 DQKGTIDFVIK------KYDGGKMSTHFHGLKEGDTVSFKGP------------IVkwkwepnqfqsiaLIGGGTGITPL 168
Cdd:COG2871   210 AEKGIIELNIRiatppmDVPPGIGSSYIFSLKPGDKVTISGPygefflrdsdreMV-------------FIGGGAGMAPL 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 169 YQLLHEITKNPEDKTKVKLFYGNLTEEDILIKKELDDIAEKHKDqvsITYFV----DKASANWKGETGHIDKEFLQ---S 241
Cdd:COG2871   277 RSHIFDLLERGKTDRKITFWYGARSLRELFYLEEFRELEKEHPN---FKFHPalsePLPEDNWDGETGFIHEVLYEnylK 353

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2620196322 242 NLPGPSkDSKVFVCGPPGLYKAlsgvkvsptdqgeVTGVLAELGYTKENVY--KF 294
Cdd:COG2871   354 DHPAPE-DCEAYLCGPPPMIDA-------------VIKMLDDLGVEEENIYfdDF 394
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 63-294 1.91e-22

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate.


Pssm-ID: 99808 [Multi-domain]  Cd Length: 232  Bit Score: 93.16  E-value: 1.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  63 RHFVFELKSPEDVsglvtasclmtKF-------VTAKGNNVIRPYTPVSDVDQKGTIDFVIKKYDGGKMSTHF-HGLKEG 134
Cdd:cd06212    16 RRLRLRLEEPEPI-----------KFfagqyvdITVPGTEETRSFSMANTPADPGRLEFIIKKYPGGLFSSFLdDGLAVG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 135 DTVSFKGPIVKWKWEPNQFQSIALIGGGTGITPLYQLLHEITKNPEDKTkVKLFYGNLTEEDILIKKELDDIAEKHKDQV 214
Cdd:cd06212    85 DPVTVTGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDMAASGSDRP-VRFFYGARTARDLFYLEEIAALGEKIPDFT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 215 SITYFVDK-ASANWKGETGHIdKEFLQSNLPGpSKDSKVFVCGPPGLYKAlsgvkvsptdqgeVTGVLAELGYTKENVY- 292
Cdd:cd06212   164 FIPALSESpDDEGWSGETGLV-TEVVQRNEAT-LAGCDVYLCGPPPMIDA-------------ALPVLEMSGVPPDQIFy 228


                  ...
gi 2620196322 293 -KF 294
Cdd:cd06212   229 dKF 231
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 88-293 2.91e-20

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: 87.21  E-value: 2.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  88 FVTAK----GNNVIRPY---TPVSDvdqkGTIDFVIKKYDGGKMSTHFHG-LKEGDTV---SFKGPIVkWKWEPNQfQSI 156
Cdd:cd06214    38 FLTLRvpidGEEVRRSYsicSSPGD----DELRITVKRVPGGRFSNWANDeLKAGDTLevmPPAGRFT-LPPLPGA-RHY 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 157 ALIGGGTGITP----LYQLLHEitknpEDKTKVKLFYGNLTEEDILIKKELDDIAEKHKDQVSITYFVDKASANWKGETG 232
Cdd:cd06214   112 VLFAAGSGITPvlsiLKTALAR-----EPASRVTLVYGNRTEASVIFREELADLKARYPDRLTVIHVLSREQGDPDLLRG 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2620196322 233 HIDKEFLQ---SNLPGPSKDSKVFVCGPPGLYKAlsgvkvsptdqgeVTGVLAELGYTKENVYK 293
Cdd:cd06214   187 RLDAAKLNallKNLLDATEFDEAFLCGPEPMMDA-------------VEAALLELGVPAERIHR 237
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
88-264 7.79e-20

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 88.80  E-value: 7.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  88 FVTAKGNNVIR---PYTPVSDVDQKGTIDFVIKkyDGGKMSTHFHGLKEGDTVSFKGP-----IVKWKWEPNQfqsiALI 159
Cdd:COG4097   251 FLRFDGSPFWEeahPFSISSAPGGDGRLRFTIK--ALGDFTRRLGRLKPGTRVYVEGPygrftFDRRDTAPRQ----VWI 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 160 GGGTGITPLYQLLHEITKNPEDKTKVKLFYGNLTEEDILIKKELDDIAEKHKDqVSITYFVDkasanwkGETGHIDKEFL 239
Cdd:COG4097   325 AGGIGITPFLALLRALAARPGDQRPVDLFYCVRDEEDAPFLEELRALAARLAG-LRLHLVVS-------DEDGRLTAERL 396

                         170       180
                  ....*....|....*....|....*
gi 2620196322 240 QSNLPGPSkDSKVFVCGPPGLYKAL 264
Cdd:COG4097   397 RRLVPDLA-EADVFFCGPPGMMDAL 420
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 58-292 2.44e-19

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: 84.70  E-value: 2.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  58 VSSNTRHFVFELKSPEDVSGLVtasclmtKFVTAK-------GNNVIRPYTPVSDVDQKGTIDFVIKKYDGGKMSTHF-H 129
Cdd:cd06210    12 VSSNVVRLRLQPDDAEGAGIAA-------EFVPGQfveieipGTDTRRSYSLANTPNWDGRLEFLIRLLPGGAFSTYLeT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 130 GLKEGDTVSFKGPIVKWKWEPNQFQSIALIGGGTGITPLYQLLHEITKNpEDKTKVKLFYGNLTEEDILIKKELDDIAEK 209
Cdd:cd06210    85 RAKVGQRLNLRGPLGAFGLRENGLRPRWFVAGGTGLAPLLSMLRRMAEW-GEPQEARLFFGVNTEAELFYLDELKRLADS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 210 HKdQVSITYFVDKASANWKGETGHIdKEFLQSNLPGPSKDSKVFVCGPPGLYKAlsgvkvsptdqgeVTGVLAELGYTKE 289
Cdd:cd06210   164 LP-NLTVRICVWRPGGEWEGYRGTV-VDALREDLASSDAKPDIYLCGPPGMVDA-------------AFAAAREAGVPDE 228


                  ...
gi 2620196322 290 NVY 292
Cdd:cd06210   229 QVY 231
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 43-273 3.66e-19

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: 84.53  E-value: 3.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  43 GGDEWIDLKLKKSWDVSSNTRHFVFElksPEDVSGLVTAsclmtK---FVTAK------GNNVIRPYTpVSDVDQKGTID 113
Cdd:cd06184     2 GWRGFRPFVVARKVAESEDITSFYLE---PADGGPLPPF-----LpgqYLSVRvklpglGYRQIRQYS-LSDAPNGDYYR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 114 FVIKKYDGGKMSTHFHG-LKEGDTV-------SF------KGPIVkwkwepnqfqsiaLIGGGTGITPLYQLLHEITKNp 179
Cdd:cd06184    73 ISVKREPGGLVSNYLHDnVKVGDVLevsapagDFvldeasDRPLV-------------LISAGVGITPMLSMLEALAAE- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 180 EDKTKVKLFYGNLTEEDILIKKELDDIAEKHkDQVSITYFVDKASANWKGE----TGHIDKEFLQSNLPGPskDSKVFVC 255
Cdd:cd06184   139 GPGRPVTFIHAARNSAVHAFRDELEELAARL-PNLKLHVFYSEPEAGDREEdydhAGRIDLALLRELLLPA--DADFYLC 215

                         250       260
                  ....*....|....*....|..
gi 2620196322 256 GPPG----LYKALSGVKVSPTD 273
Cdd:cd06184   216 GPVPfmqaVREGLKALGVPAER 237
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 57-274 2.09e-18

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: 81.92  E-value: 2.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  57 DVSSNTRHFVFELKSPedvsglvtASCLMTKFVTAK--GNNVIRPYTPVSDVDQKGTIDFVIKKYDGGKMSTH-FHGLKE 133
Cdd:cd06190     6 ELTHDVAEFRFALDGP--------ADFLPGQYALLAlpGVEGARAYSMANLANASGEWEFIIKRKPGGAASNAlFDNLEP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 134 GDTVSFKGPIVKWKWEPNQFQSIALIGGGTGITPLYQLL-HEITKNPEDKTKVKLFYGNLTEEDILIKKELDDiAEKHKD 212
Cdd:cd06190    78 GDELELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILrGAARSPYLSDRPVDLFYGGRTPSDLCALDELSA-LVALGA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 213 QVSITYFV----DKASANWKGETGHIdKEFLQSNLPGPSKDSKVFVCGPPGLYKA----LSGVKVSPTDQ 274
Cdd:cd06190   157 RLRVTPAVsdagSGSAAGWDGPTGFV-HEVVEATLGDRLAEFEFYFAGPPPMVDAvqrmLMIEGVVPFDQ 225
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 98-291 3.77e-18

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: 81.13  E-value: 3.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  98 RPYTPVSDVDQKgTIDFVIKKY-DGGKMSTHFHGLKEGDTV---------SFKGPIVkwkwepnqfqsiaLIGGGTGITP 167
Cdd:cd06196    48 RPFTFTSLPEDD-VLEFVIKSYpDHDGVTEQLGRLQPGDTLliedpwgaiEYKGPGV-------------FIAGGAGITP 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 168 LYQLLHEITKNPEDKTKvKLFYGNLTEEDILIKKELDdiaekHKDQVSITYFVDKASANwKGETGHIDKEFLQSNLpgPS 247
Cdd:cd06196   114 FIAILRDLAAKGKLEGN-TLIFANKTEKDIILKDELE-----KMLGLKFINVVTDEKDP-GYAHGRIDKAFLKQHV--TD 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2620196322 248 KDSKVFVCGPPGLYKAlsgvkvsptdqgeVTGVLAELGYTKENV 291
Cdd:cd06196   185 FNQHFYVCGPPPMEEA-------------INGALKELGVPEDSI 215
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 93-291 1.33e-17

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 82.90  E-value: 1.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322   93 GNNVIRPYTPVSDVDQKGTIDfVIKKYDGGKMSTHFHGLKEGDTVSFK---GPIVKWKWEPNQF-------QSIALIGGG 162
Cdd:PTZ00306   962 GQQLIGYYSPITLPDDLGVIS-ILARGDKGTLKEWISALRPGDSVEMKacgGLRIERRPADKQFvfrghviRKLALIAGG 1040

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  163 TGITPLYQLLHEITKNP--EDKTKVKLFYGNLTEEDILIKKELDDIAEKHKDQVSITYFVDKASANWKGETGHIDKEFLQ 240
Cdd:PTZ00306  1041 TGVAPMLQIIRAALKKPyvDSIESIRLIYAAEDVSELTYRELLESYRKENPGKFKCHFVLNNPPEGWTDGVGFVDRALLQ 1120

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2620196322  241 SNLPGPSKDSKVFVCGPPGLykalsgvkvsptdQGEVTGVLAELGYTKENV 291
Cdd:PTZ00306  1121 SALQPPSKDLLVAICGPPVM-------------QRAVKADLLALGYNMELV 1158
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 98-260 4.30e-17

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: 78.81  E-value: 4.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  98 RPYTPVSDVDQK-GTIDFVIKKYDGGKMSTHFHG-LKEGDTVSFKGPIVKWKWEPNQFQSIALIGGGTGITPLYQLLHEI 175
Cdd:cd06216    65 RSYSLSSSPTQEdGTITLTVKAQPDGLVSNWLVNhLAPGDVVELSQPQGDFVLPDPLPPRLLLIAAGSGITPVMSMLRTL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 176 TKNPEdKTKVKLFYGNLTEEDILIKKELDDIAEKHKdQVSITYFVDKAsanwkGETGHIDKEFLQsNLPGPSKDSKVFVC 255
Cdd:cd06216   145 LARGP-TADVVLLYYARTREDVIFADELRALAAQHP-NLRLHLLYTRE-----ELDGRLSAAHLD-AVVPDLADRQVYAC 216


                  ....*
gi 2620196322 256 GPPGL 260
Cdd:cd06216   217 GPPGF 221
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 98-263 4.71e-17

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: 78.02  E-value: 4.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  98 RPYTPVSDVDQKGTIDFVIKKYDGGKMSTH-FHGLKEGDTVSFKGP----IVKwkwePNQFQSIALIGGGTGITPLYQLL 172
Cdd:cd06187    42 RAYSPANPPNEDGEIEFHVRAVPGGRVSNAlHDELKVGDRVRLSGPygtfYLR----RDHDRPVLCIAGGTGLAPLRAIV 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 173 HEITKNPEDKtKVKLFYGNLTEEDILIKKELDDIAEKHkDQVSITYFVDKASANWKGETGHIdKEFLQSNLPGPSkDSKV 252
Cdd:cd06187   118 EDALRRGEPR-PVHLFFGARTERDLYDLEGLLALAARH-PWLRVVPVVSHEEGAWTGRRGLV-TDVVGRDGPDWA-DHDI 193

                         170
                  ....*....|.
gi 2620196322 253 FVCGPPGLYKA 263
Cdd:cd06187   194 YICGPPAMVDA 204
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 89-266 1.04e-16

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: 77.18  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  89 VTAKGNNVIRPYTpVSDVDQKGTIDFVIKKYDGGKMSTHFH-GLKEGDTVSFKGPIVKWKWEPNQFQSIALIGGGTGITP 167
Cdd:cd06191    38 LDFDGEELRRCYS-LCSSPAPDEISITVKRVPGGRVSNYLReHIQPGMTVEVMGPQGHFVYQPQPPGRYLLVAAGSGITP 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 168 LYQLLHEiTKNPEDKTKVKLFYGNLTEEDILIKKELDDIAEKHKD-QVSITYFVDKASANWKGETGHIDKEFLQSNLPgP 246
Cdd:cd06191   117 LMAMIRA-TLQTAPESDFTLIHSARTPADMIFAQELRELADKPQRlRLLCIFTRETLDSDLLHGRIDGEQSLGAALIP-D 194

                         170       180
                  ....*....|....*....|
gi 2620196322 247 SKDSKVFVCGPPGLYKALSG 266
Cdd:cd06191   195 RLEREAFICGPAGMMDAVET 214
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 89-264 1.24e-16

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: 77.36  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  89 VTAKGNNVIRPYTPVSDVDQKGTIDFVIKKYDGGKMSTHFHG-LKEGDTVSFKGPIVKWKWEPNQFQSIALIGGGTGITP 167
Cdd:cd06211    44 LQAPGYEGTRAFSIASSPSDAGEIELHIRLVPGGIATTYVHKqLKEGDELEISGPYGDFFVRDSDQRPIIFIAGGSGLSS 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 168 LYQLLHEITkNPEDKTKVKLFYGNLTEEDILIKKELDDIAEKHKDqvsiTYFVDKASA-----NWKGETGHIDkEFLQSN 242
Cdd:cd06211   124 PRSMILDLL-ERGDTRKITLFFGARTRAELYYLDEFEALEKDHPN----FKYVPALSReppesNWKGFTGFVH-DAAKKH 197

                         170       180
                  ....*....|....*....|..
gi 2620196322 243 LPGPSKDSKVFVCGPPGLYKAL 264
Cdd:cd06211   198 FKNDFRGHKAYLCGPPPMIDAC 219
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 96-291 1.42e-16

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: 77.73  E-value: 1.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  96 VIRPYTPVSDVDQKGTIDFVIK-------KYDG--GKMSTHFHGLKEGDTVSFKGPIvkwkwepnQFQSI-------ALI 159
Cdd:cd06188    85 VSRAYSLANYPAEEGELKLNVRiatpppgNSDIppGIGSSYIFNLKPGDKVTASGPF--------GEFFIkdtdremVFI 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 160 GGGTGITPLYQLLHEITKNPEDKTKVKLFYGNLTEEDILIKKELDDIAEKHKDqvsITYFV----DKASANWKGETGHID 235
Cdd:cd06188   157 GGGAGMAPLRSHIFHLLKTLKSKRKISFWYGARSLKELFYQEEFEALEKEFPN---FKYHPvlsePQPEDNWDGYTGFIH 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2620196322 236 KEFLQ---SNLPGPsKDSKVFVCGPPGLYKAlsgvkvsptdqgeVTGVLAELGYTKENV 291
Cdd:cd06188   234 QVLLEnylKKHPAP-EDIEFYLCGPPPMNSA-------------VIKMLDDLGVPRENI 278
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 99-292 3.55e-16

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 76.77  E-value: 3.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  99 PYTPVSDVDQKGTIDFVIKKydGGKMSTHFHGLKEGDTVSFKGPIVKW----KWEPnqfQSIALIGGGTGITPLYQLLHE 174
Cdd:PRK08345   55 PISICSSPTRKGFFELCIRR--AGRVTTVIHRLKEGDIVGVRGPYGNGfpvdEMEG---MDLLLIAGGLGMAPLRSVLLY 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 175 ITKNPEDKTKVKLFYGNLTEEDILIKKELDDI---AEKHKDQVSITYFVDKASANW--KGETGHIDKEFLQSNLPGPS-- 247
Cdd:PRK08345  130 AMDNRWKYGNITLIYGAKYYEDLLFYDELIKDlaeAENVKIIQSVTRDPEWPGCHGlpQGFIERVCKGVVTDLFREANtd 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2620196322 248 -KDSKVFVCGPPGLYKAlsgvkvsptdqgevtgVLAEL---GYTKENVY 292
Cdd:PRK08345  210 pKNTYAAICGPPVMYKF----------------VFKELinrGYRPERIY 242
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 58-264 3.97e-14

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: 70.27  E-value: 3.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  58 VSSNTRH----FVFELKSPEDVsglvtASCLMTKFVTAKGNNVIRPYTP----VSDVD-QKGTIDFVIKKYDGG--KMST 126
Cdd:cd06218     1 VLSNREIaddiYRLVLEAPEIA-----AAAKPGQFVMLRVPDGSDPLLRrpisIHDVDpEEGTITLLYKVVGKGtrLLSE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 127 hfhgLKEGDTVSFKGPI-----VKWKWEPnqfqsIALIGGGTGITPLYQLLHEITKNPedkTKVKLFYGNLTEEDILIKK 201
Cdd:cd06218    76 ----LKAGDELDVLGPLgngfdLPDDDGK-----VLLVGGGIGIAPLLFLAKQLAERG---IKVTVLLGFRSADDLFLVE 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2620196322 202 ELddiaEKHKDQVSITyfVDKASANWKGETGHIDKEFLQSNlpgpsKDSKVFVCGPPGLYKAL 264
Cdd:cd06218   144 EF----EALGAEVYVA--TDDGSAGTKGFVTDLLKELLAEA-----RPDVVYACGPEPMLKAV 195
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 89-292 4.46e-14

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: 70.03  E-value: 4.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  89 VTAKGNNVIRPYTPVSDVDQKGTIDFVIKKYDGGKMSTH-FHGLKEGDTVSFKGPIVKWKWEPNQfQSIALIGGGTGITP 167
Cdd:cd06213    36 LTLPGLPAARSYSFANAPQGDGQLSFHIRKVPGGAFSGWlFGADRTGERLTVRGPFGDFWLRPGD-APILCIAGGSGLAP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 168 LYQLLHEITKNpEDKTKVKLFYGNLTEEDILIKKELDDIAEKHKDQVSityFV-----DKASANWKGETG----HIDKEF 238
Cdd:cd06213   115 ILAILEQARAA-GTKRDVTLLFGARTQRDLYALDEIAAIAARWRGRFR---FIpvlseEPADSSWKGARGlvteHIAEVL 190

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2620196322 239 LQsnlpgpskDSKVFVCGPPGLYKAlsgvkvsptdqgeVTGVLAELGYTKENVY 292
Cdd:cd06213   191 LA--------ATEAYLCGPPAMIDA-------------AIAVLRALGIAREHIH 223
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 98-263 4.86e-14

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: 69.89  E-value: 4.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  98 RPYTPVSDVDQKGTIDFVIKKYDGGKMSTH-FHGLKEGDTVSFKGPIVKWKWEPNQFQSIALIGGGTGITPLYQLLHEIT 176
Cdd:cd06189    42 RPFSIASAPHEDGEIELHIRAVPGGSFSDYvFEELKENGLVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 177 KNpEDKTKVKLFYGNLTEEDILIKKELDDIAEKHKDqvsITYF--VDKASANWKGETGHIDkEFLQSNLPGPSkDSKVFV 254
Cdd:cd06189   122 AQ-GSKRPIHLYWGARTEEDLYLDELLEAWAEAHPN---FTYVpvLSEPEEGWQGRTGLVH-EAVLEDFPDLS-DFDVYA 195


                  ....*....
gi 2620196322 255 CGPPGLYKA 263
Cdd:cd06189   196 CGSPEMVYA 204
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 93-294 4.10e-12

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


Pssm-ID: 99805 [Multi-domain]  Cd Length: 228  Bit Score: 64.54  E-value: 4.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  93 GNNVIRPYTPVSDVDQkGTIDFVIKKYDGGKMSTHFHGL-KEGDTVSFKGPIVKWKWEPNQfQSIALIGGGTGITPLYQL 171
Cdd:cd06209    43 GTDETRSYSFSSAPGD-PRLEFLIRLLPGGAMSSYLRDRaQPGDRLTLTGPLGSFYLREVK-RPLLMLAGGTGLAPFLSM 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 172 LHEITKNPEDKtKVKLFYGNLTEEDILikkELDDIAEKHKDQVSITYFVDKASAN-WKGETGHIDKEFLQSNLPGPskDS 250
Cdd:cd06209   121 LDVLAEDGSAH-PVHLVYGVTRDADLV---ELDRLEALAERLPGFSFRTVVADPDsWHPRKGYVTDHLEAEDLNDG--DV 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2620196322 251 KVFVCGPPGLYKAlsgvkvsptdqgeVTGVLAELGYTKENVY--KF 294
Cdd:cd06209   195 DVYLCGPPPMVDA-------------VRSWLDEQGIEPANFYyeKF 227
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 98-264 7.02e-12

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: 63.44  E-value: 7.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  98 RPYTPVSDVDQKGTIDFVIKKYDGGKMSTH-FHGLKEGDTVSFKGPivkwkW------EPNQFQSIALIGGGTGITPLYQ 170
Cdd:cd06194    40 RSYSPTSLPDGDNELEFHIRRKPNGAFSGWlGEEARPGHALRLQGP-----FgqafyrPEYGEGPLLLVGAGTGLAPLWG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 171 LLHE-ITKNPEdkTKVKLFYGNLTEEDILIKKELDDIAEKHKdQVSITYFVDKASANwkGETGHIDKEFLQsnLPGPSKD 249
Cdd:cd06194   115 IARAaLRQGHQ--GEIRLVHGARDPDDLYLHPALLWLAREHP-NFRYIPCVSEGSQG--DPRVRAGRIAAH--LPPLTRD 187

                         170
                  ....*....|....*
gi 2620196322 250 SKVFVCGPPGLYKAL 264
Cdd:cd06194   188 DVVYLCGAPSMVNAV 202
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 93-288 2.53e-10

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: 59.50  E-value: 2.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  93 GNNVIRPYTPVSDVDQKgTIDFVIKKYDGGKMSTHFHGLKEGDTVSFKGPIV-----------KWKWepnqfqsiaLIGG 161
Cdd:cd06195    40 GKLVRRAYSIASAPYEE-NLEFYIILVPDGPLTPRLFKLKPGDTIYVGKKPTgfltldevppgKRLW---------LLAT 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 162 GTGITP-LYQLLHEITKNPEDKtkVKLFYGNLTEEDILIKKELDDIAEKHKDQVSITYFVDKASANWkGETGHIDkEFLQ 240
Cdd:cd06195   110 GTGIAPfLSMLRDLEIWERFDK--IVLVHGVRYAEELAYQDEIEALAKQYNGKFRYVPIVSREKENG-ALTGRIP-DLIE 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2620196322 241 S-------NLPGPSKDSKVFVCGPPGLYKalsgvkvsptdqgEVTGVLAELGYTK 288
Cdd:cd06195   186 SgeleehaGLPLDPETSHVMLCGNPQMID-------------DTQELLKEKGFSK 227
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 88-264 5.80e-10

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: 58.04  E-value: 5.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  88 FVT--AKGNNVIRPYTPVSDVDQKGTIDFVIKKY-DG-GKMSTHfhgLKEGDTVSFKGPIVKWKWEPNQFQSIaLIGGGT 163
Cdd:cd06198    30 FLRfdASGWEEPHPFTISSAPDPDGRLRFTIKALgDYtRRLAER---LKPGTRVTVEGPYGRFTFDDRRARQI-WIAGGI 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 164 GITPLYQLLHEITKNPEDKtKVKLFYGNLTEEDILIKKELDDIAEKHKDQVSItyfVDKASANWKGETGhidkefLQSNL 243
Cdd:cd06198   106 GITPFLALLEALAARGDAR-PVTLFYCVRDPEDAVFLDELRALAAAAGVVLHV---IDSPSDGRLTLEQ------LVRAL 175

                         170       180
                  ....*....|....*....|.
gi 2620196322 244 PGPSKDSKVFVCGPPGLYKAL 264
Cdd:cd06198   176 VPDLADADVWFCGPPGMADAL 196
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 89-204 3.38e-09

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: 56.57  E-value: 3.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  89 VTAKGNNVIRPYTPVSdVDQKGTIDFVIKKYDGGKMSTHFHGLKEGDTVsfKGPIvkwkwEPN-QFQ------SIALIGG 161
Cdd:cd06201    92 ILPPGSDVPRFYSLAS-SSSDGFLEICVRKHPGGLCSGYLHGLKPGDTI--KAFI-----RPNpSFRpakgaaPVILIGA 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2620196322 162 GTGITPLYQLLheitKNPEDKTKVKLFYGNLTEE-DILIKKELD 204
Cdd:cd06201   164 GTGIAPLAGFI----RANAARRPMHLYWGGRDPAsDFLYEDELD 203
PRK13289 PRK13289
NO-inducible flavohemoprotein;
93-294 5.09e-09

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 56.73  E-value: 5.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  93 GNNVIRPYTpVSDVDQKGTIDFVIKKYDGGKMSTHFH-GLKEGDTVSFKGPIVKWKWEPNQFQSIALIGGGTGITPLYQL 171
Cdd:PRK13289  201 EYQEIRQYS-LSDAPNGKYYRISVKREAGGKVSNYLHdHVNVGDVLELAAPAGDFFLDVASDTPVVLISGGVGITPMLSM 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 172 LHEITKNpEDKTKVKLFYGNLTEEDILIKKELDDIAEKHkDQVSITYF------VDKASANWKGEtGHIDKEFLQSNLpg 245
Cdd:PRK13289  280 LETLAAQ-QPKRPVHFIHAARNGGVHAFRDEVEALAARH-PNLKAHTWyrepteQDRAGEDFDSE-GLMDLEWLEAWL-- 354

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2620196322 246 PSKDSKVFVCGPPGLYKAlsgvkvsptdqgeVTGVLAELGYTKENV-YKF 294
Cdd:PRK13289  355 PDPDADFYFCGPVPFMQF-------------VAKQLLELGVPEERIhYEF 391
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 48-264 6.65e-09

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 55.26  E-value: 6.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  48 IDLKLKKSWDVSSNTRHFVFElkspedvsGLVTASCLMTKFVTAKGNNVI----RPYTpVSDVDqKGTIDFVIKKYdgGK 123
Cdd:PRK00054    5 ENMKIVENKEIAPNIYTLVLD--------GEKVFDMKPGQFVMVWVPGVEplleRPIS-ISDID-KNEITILYRKV--GE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 124 MSTHFHGLKEGDTVSFKGPIvkwkwePNQF------QSIALIGGGTGITPLYQLLHEITKNPEDktkVKLFYGNLTEEDI 197
Cdd:PRK00054   73 GTKKLSKLKEGDELDIRGPL------GNGFdleeigGKVLLVGGGIGVAPLYELAKELKKKGVE---VTTVLGARTKDEV 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2620196322 198 LIKKELDDIAEkhkdqVSITyfVDKASANWKGETGHIDKEFLqsnlpgpSKDSKVFVCGPPGLYKAL 264
Cdd:PRK00054  144 IFEEEFAKVGD-----VYVT--TDDGSYGFKGFVTDVLDELD-------SEYDAIYSCGPEIMMKKV 196
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
 131-270 1.21e-08

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 55.39  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 131 LKEGDTVSFKGPIVK---WKWEPNQfqSIALIGGGTGITPLYQLLHEITKNPEDKTKVK----LFYGNLTEEDILIKKEL 203
Cdd:PLN03115  192 LKPGAEVKITGPVGKemlMPKDPNA--TIIMLATGTGIAPFRSFLWKMFFEKHDDYKFNglawLFLGVPTSSSLLYKEEF 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2620196322 204 DDIAEKHKDQVSITYFVDKASANWKGETGHIDK---EFLQSNLPGPSKDSK-VFVCGPPGLYKALSGVKVS 270
Cdd:PLN03115  270 EKMKEKAPENFRLDFAVSREQTNAKGEKMYIQTrmaEYAEELWELLKKDNTyVYMCGLKGMEKGIDDIMVS 340
DHOD_e_trans_like1 cd06219
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 99-268 2.73e-08

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


Pssm-ID: 99815 [Multi-domain]  Cd Length: 248  Bit Score: 53.35  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  99 PYTpVSDVD-QKGTIDFVIKKydGGKMSTHFHGLKEGDTVS-FKGPIVKwKWEPNQFQSIALIGGGTGITPLYQLLHEIT 176
Cdd:cd06219    45 PLT-IADWDpEKGTITIVVQV--VGKSTRELATLEEGDKIHdVVGPLGK-PSEIENYGTVVFVGGGVGIAPIYPIAKALK 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 177 knpEDKTKVKLFYGNLTEEDILIKKELDDIAEKHkdqvsiTYFVDKASANWKGETGHIDKEFLQSNlpgpSKDSKVFVCG 256
Cdd:cd06219   121 ---EAGNRVITIIGARTKDLVILEDEFRAVSDEL------IITTDDGSYGEKGFVTDPLKELIESG----EKVDLVIAIG 187

                         170
                  ....*....|..
gi 2620196322 257 PPGLYKALSGVK 268
Cdd:cd06219   188 PPIMMKAVSELT 199
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 103-257 6.01e-08

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: 52.25  E-value: 6.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 103 VSDVDQKGTIdfVIKKYdgGKMSTHFHGLKEGDTVSFKGPIVKwKWEPNQfQSIALIGGGTGITPLYQLLHEITKnpedK 182
Cdd:cd06220    44 LSYIDGPNSI--TVKKV--GEATSALHDLKEGDKLGIRGPYGN-GFELVG-GKVLLIGGGIGIAPLAPLAERLKK----A 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2620196322 183 TKVKLFYGNLTEEDILIKKELDDIAEkhkdqVSITyfVDKASANWKGETGHIDKEFLQSNLpgpskdSKVFVCGP 257
Cdd:cd06220   114 ADVTVLLGARTKEELLFLDRLRKSDE-----LIVT--TDDGSYGFKGFVTDLLKELDLEEY------DAIYVCGP 175
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 125-230 6.11e-08

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: 52.71  E-value: 6.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 125 STHFHGLKEGDTVSFKGPIVKWKWEPNQFQS-IALIGGGTGITP----LYQLLHEITKNPEDKTKVKLFYGNLTEEDILI 199
Cdd:cd06208   106 SNYLCDLKPGDDVQITGPVGKTMLLPEDPNAtLIMIATGTGIAPfrsfLRRLFREKHADYKFTGLAWLFFGVPNSDSLLY 185

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2620196322 200 KKELDDIAEKHKDQVSITYFVDKASANWKGE 230
Cdd:cd06208   186 DDELEKYPKQYPDNFRIDYAFSREQKNADGG 216
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 99-260 1.50e-07

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: 50.77  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  99 PYTPVS-DVDQKGTIDFVIKKYDGgkMSTHFHGlkegDTVSFKGPIVKWKW-----------EPNQFQSIALIGGGTGIT 166
Cdd:cd06186    46 PFTIASsPEDEQDTLSLIIRAKKG--FTTRLLR----KALKSPGGGVSLKVlvegpygssseDLLSYDNVLLVAGGSGIT 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 167 PLYQLLHEITKNPEDKT---KVKLFYGNLTEEDIL-IKKELDDIAEkHKDQVSITYFVdkasanwkgetghidkeflqsn 242
Cdd:cd06186   120 FVLPILRDLLRRSSKTSrtrRVKLVWVVRDREDLEwFLDELRAAQE-LEVDGEIEIYV---------------------- 176

                         170
                  ....*....|....*...
gi 2620196322 243 lpgpskdSKVFVCGPPGL 260
Cdd:cd06186   177 -------TRVVVCGPPGL 187
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 65-265 1.94e-07

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 52.05  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  65 FVFELKSPedvsgLVTASCLMTKFVTA----KGNNVirPYTPVSDVDQKGTIDFVIKKYdgGKMSTHFHGLKEGDTVS-F 139
Cdd:PRK12778   15 FLLEIEAP-----LIAKSRKPGQFVIVrvgeKGERI--PLTIADADPEKGTITLVIQEV--GLSTTKLCELNEGDYITdV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 140 KGPIVKWKwEPNQFQSIALIGGGTGITPLYQLLHEITKNPEDKTKVklfYGNLTEEDILIKKELDDIAekhkDQVSITyf 219
Cdd:PRK12778   86 VGPLGNPS-EIENYGTVVCAGGGVGVAPMLPIVKALKAAGNRVITI---LGGRSKELIILEDEMRESS----DEVIIM-- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2620196322 220 VDKASANWKGETGHIDKEFLQSNlpgpSKDSKVFVCGPPGLYKALS 265
Cdd:PRK12778  156 TDDGSYGRKGLVTDGLEEVIKRE----TKVDKVFAIGPAIMMKFVC 197
PRK06222 PRK06222
sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein;
99-267 7.84e-07

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


Pssm-ID: 235747 [Multi-domain]  Cd Length: 281  Bit Score: 49.42  E-value: 7.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  99 PYTpVSDVD-QKGTIDFVIKKYdgGKMSTHFHGLKEGDTV-SFKGP------IVKWKwepnqfqSIALIGGGTGITPLY- 169
Cdd:PRK06222   46 PLT-IADYDrEKGTITIVFQAV--GKSTRKLAELKEGDSIlDVVGPlgkpseIEKFG-------TVVCVGGGVGIAPVYp 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 170 --QLLHEItknpedKTKVKLFYGNLTEEDILIKKELDDIAekhkDQVSITyfVDKASANWKGETGHIDKEFLQSnlpgPS 247
Cdd:PRK06222  116 iaKALKEA------GNKVITIIGARNKDLLILEDEMKAVS----DELYVT--TDDGSYGRKGFVTDVLKELLES----GK 179

                         170       180
                  ....*....|....*....|
gi 2620196322 248 KDSKVFVCGPPGLYKALSGV 267
Cdd:PRK06222  180 KVDRVVAIGPVIMMKFVAEL 199
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 103-264 6.87e-06

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: 46.17  E-value: 6.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 103 VSDVD-QKGTIDFVIKKYDGGkmSTHFHGLKEGDTVSFKGPIVKWKWEPNQFQSIALIGGGTGITPLYQLlheITKNPED 181
Cdd:cd06192    48 LAGVDpEEGTISLLVEIRGPK--TKLIAELKPGEKLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPI---AKKLAAN 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 182 KTKVKLFYGNLTEEDILIKKELddiaEKHKDQVSITyfVDKAsanWKGETGHIDKEFLQSNLpgpSKDSKVFVCGPPGLY 261
Cdd:cd06192   123 GNKVTVLAGAKKAKEEFLDEYF----ELPADVEIWT--TDDG---ELGLEGKVTDSDKPIPL---EDVDRIIVAGSDIMM 190


                  ...
gi 2620196322 262 KAL 264
Cdd:cd06192   191 KAV 193
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 124-284 1.23e-04

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: 42.71  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 124 MSTHF-HGLKEGDTVSFKGPIVKWKWEPNQFQS-IALIGGGTGITPLYQLLHE---ITKNPEDKTKVKLFYGNLT-EEDI 197
Cdd:cd06182    84 VCSNFlAGLQLGAKVTVFIRPAPSFRLPKDPTTpIIMVGPGTGIAPFRGFLQEraaLRANGKARGPAWLFFGCRNfASDY 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 198 LIKKELddiAEKHKDQVSITYFV--DKASANWKGETGHI---DKEFLQSNLpgpSKDSKVFVCGP-----PGLYKALSGV 267
Cdd:cd06182   164 LYREEL---QEALKDGALTRLDVafSREQAEPKVYVQDKlkeHAEELRRLL---NEGAHIYVCGDaksmaKDVEDALVKI 237

                         170
                  ....*....|....*..
gi 2620196322 268 kvsPTDQGEVTGVLAEL 284
Cdd:cd06182   238 ---IAKAGGVDESDAEE 251
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 116-258 1.76e-03

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 39.47  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 116 IKKYDGGKMSTH-FHGLKEGDTVSFKGPIVKW--KWEPNqfQSIALIGGGTGITPLYQLL-HEITKNpeDKTKVKLFYGN 191
Cdd:PRK07609  166 IRHMPGGVFTDHvFGALKERDILRIEGPLGTFflREDSD--KPIVLLASGTGFAPIKSIVeHLRAKG--IQRPVTLYWGA 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2620196322 192 LTEEDILikkeLDDIAEKHKDQVSITYFV-----DKASANWKGETGHIDKEFLQSnlpGPS-KDSKVFVCGPP 258
Cdd:PRK07609  242 RRPEDLY----LSALAEQWAEELPNFRYVpvvsdALDDDAWTGRTGFVHQAVLED---FPDlSGHQVYACGSP 307
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
153-265 3.26e-03

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 37.32  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 153 FQSIALIGGGTGITPLYQLLHEITKNP-EDKTKVKLFYGNLTEEDIL--IKKELDDIAEKHKDQVSITYFV--------- 220
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSkKLKTKKIKFYWVVRDLSSLewFKDVLNELEELKELNIEIHIYLtgeyeaeda 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2620196322 221 ---------DKASANWKGETGHID-----------KEFLQSNLPGPSKDS-KVFVCGPPGLYKALS 265
Cdd:pfam08030  81 sdqsdssirSENFDSLMNEVIGVDfvefhfgrpnwKEVLKDIAKQHPNGSiGVFSCGPPSLVDELR 146
PLN02631 PLN02631
ferric-chelate reductase
 99-183 4.66e-03

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 38.48  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322  99 PYTPVSDVD-QKGTIDFVIKKYDG--GKMSTHFHGLKEGDTVSFKGPIVKWKWEPNQFQSIALIGGGTGITPLYQLLHEI 175
Cdd:PLN02631  355 PFTITSSSNlEKDTLSVVIRRQGSwtQKLYTHLSSSIDSLEVSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIREL 434


                  ....*...
gi 2620196322 176 TKNPEDKT 183
Cdd:PLN02631  435 IFQSQNPS 442
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 122-203 8.02e-03

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: 37.25  E-value: 8.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2620196322 122 GKMSTHFHGLKEGDTV-------SFKGPivkwkwePNQFQSIALIGGGTGITPLYQLLHE---ITKNPEDKTKVKLFYGN 191
Cdd:cd06207   199 GLCSSYLAGLKVGQRVtvfikksSFKLP-------KDPKKPIIMVGPGTGLAPFRAFLQEraaLLAQGPEIGPVLLYFGC 271

                          90
                  ....*....|...
gi 2620196322 192 LTE-EDILIKKEL 203
Cdd:cd06207   272 RHEdKDYLYKEEL 284
 
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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