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Conserved domains on  [gi|169606282|ref|XP_001796561|]
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hypothetical protein SNOG_06179 [Parastagonospora nodorum SN15]

Protein Classification

NO-inducible flavohemoprotein( domain architecture ID 1001654)

NO-inducible flavohemoprotein such as nitric oxide dioxygenase, which catalyzes the conversion of NO, O2, and NAD(P)H to NO3-, NAD(P)+, and H+, and is involved NO detoxification and NO signaling

CATH:  1.10.490.10
EC:  1.14.12.17
Gene Ontology:  GO:0016491|GO:0008941|GO:0020037|GO:0051409|GO:0071949|GO:0019825
PubMed:  11751864|9724711|10922365

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13289 super family cl36224
NO-inducible flavohemoprotein;
4-409 1.24e-169

NO-inducible flavohemoprotein;


The actual alignment was detected with superfamily member PRK13289:

Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 480.45  E-value: 1.24e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   4 LSPSQVQIIKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVFNTTHQATGHQSRALAGALYAYAANIDNLGALSPALELI 83
Cdd:PRK13289   2 LSAQTIAIVKATVPLLEEHGEALTAHFYDRMFSHNPELKNIFNQSNQRNGDQPEALANAVLAYARNIDNLEALLPAVERI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  84 CHKHVSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLADIMIAKEEGLYKS----TPGWDGWKDFTIVR 159
Cdd:PRK13289  82 AQKHVSLQIKPEHYPIVGEHLLAAIREVLGDAATDEVLDAWGEAYGVLADVFIGREAEIYEEaaskPGGWRGWRDFRVVK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 160 KVAEsgSGEICSFYLKPKEAGvEVPVFKPGQYVSVNVRVEELdgGVWQARQYSLSDASGKGYLRISVKKEMGeareGYVS 239
Cdd:PRK13289 162 KVPE--SEVITSFYLEPVDGG-PVADFKPGQYLGVRLDPEGE--EYQEIRQYSLSDAPNGKYYRISVKREAG----GKVS 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 240 NILHGK-SEGDVVRVSHPFGDFFFDREesgENGPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGARDLNARAFKKD 318
Cdd:PRK13289 233 NYLHDHvNVGDVLELAAPAGDFFLDVA---SDTPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIHAARNGGVHAFRDE 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 319 VDTLVAANRNIRAVYFSSNPKEGEVEGQDYHIKGRVDMDKVGKDALFADNDqtqYFICGPTQFMLDVQAKLKSYGVPAER 398
Cdd:PRK13289 310 VEALAARHPNLKAHTWYREPTEQDRAGEDFDSEGLMDLEWLEAWLPDPDAD---FYFCGPVPFMQFVAKQLLELGVPEER 386

                        410
                 ....*....|.
gi 169606282 399 IKMELFGTGGV 409
Cdd:PRK13289 387 IHYEFFGPAKV 397
 
Name Accession Description Interval E-value
PRK13289 PRK13289
NO-inducible flavohemoprotein;
4-409 1.24e-169

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 480.45  E-value: 1.24e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   4 LSPSQVQIIKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVFNTTHQATGHQSRALAGALYAYAANIDNLGALSPALELI 83
Cdd:PRK13289   2 LSAQTIAIVKATVPLLEEHGEALTAHFYDRMFSHNPELKNIFNQSNQRNGDQPEALANAVLAYARNIDNLEALLPAVERI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  84 CHKHVSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLADIMIAKEEGLYKS----TPGWDGWKDFTIVR 159
Cdd:PRK13289  82 AQKHVSLQIKPEHYPIVGEHLLAAIREVLGDAATDEVLDAWGEAYGVLADVFIGREAEIYEEaaskPGGWRGWRDFRVVK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 160 KVAEsgSGEICSFYLKPKEAGvEVPVFKPGQYVSVNVRVEELdgGVWQARQYSLSDASGKGYLRISVKKEMGeareGYVS 239
Cdd:PRK13289 162 KVPE--SEVITSFYLEPVDGG-PVADFKPGQYLGVRLDPEGE--EYQEIRQYSLSDAPNGKYYRISVKREAG----GKVS 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 240 NILHGK-SEGDVVRVSHPFGDFFFDREesgENGPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGARDLNARAFKKD 318
Cdd:PRK13289 233 NYLHDHvNVGDVLELAAPAGDFFLDVA---SDTPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIHAARNGGVHAFRDE 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 319 VDTLVAANRNIRAVYFSSNPKEGEVEGQDYHIKGRVDMDKVGKDALFADNDqtqYFICGPTQFMLDVQAKLKSYGVPAER 398
Cdd:PRK13289 310 VEALAARHPNLKAHTWYREPTEQDRAGEDFDSEGLMDLEWLEAWLPDPDAD---FYFCGPVPFMQFVAKQLLELGVPEER 386

                        410
                 ....*....|.
gi 169606282 399 IKMELFGTGGV 409
Cdd:PRK13289 387 IHYEFFGPAKV 397
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 147-408 7.20e-108

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: 317.58  E-value: 7.20e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 147 PGWDGWKDFTIVRKVAESGsgEICSFYLKPKEaGVEVPVFKPGQYVSVNVRVEelDGGVWQARQYSLSDASGKGYLRISV 226
Cdd:cd06184    1 GGWRGFRPFVVARKVAESE--DITSFYLEPAD-GGPLPPFLPGQYLSVRVKLP--GLGYRQIRQYSLSDAPNGDYYRISV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 227 KKEmgeaREGYVSNILHG-KSEGDVVRVSHPFGDFFFDREEsgeNGPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIH 305
Cdd:cd06184   76 KRE----PGGLVSNYLHDnVKVGDVLEVSAPAGDFVLDEAS---DRPLVLISAGVGITPMLSMLEALAAEGPGRPVTFIH 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 306 GARDLNARAFKKDVDTLVAANRNIRAVYFSSNPKEGEVEgQDYHIKGRVDMDKVGKDALFADndqTQYFICGPTQFMLDV 385
Cdd:cd06184  149 AARNSAVHAFRDELEELAARLPNLKLHVFYSEPEAGDRE-EDYDHAGRIDLALLRELLLPAD---ADFYLCGPVPFMQAV 224

                        250       260
                 ....*....|....*....|...
gi 169606282 386 QAKLKSYGVPAERIKMELFGTGG 408
Cdd:cd06184  225 REGLKALGVPAERIHYEVFGPGE 247
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
150-402 1.29e-64

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 206.56  E-value: 1.29e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 150 DGWKDFTIVRKVAESGsgEICSFYLKPkEAGVEVPVFKPGQYVSVNVRVeeldGGVWQARQYSLSDASGKGYLRISVKKE 229
Cdd:COG1018    1 AGFRPLRVVEVRRETP--DVVSFTLEP-PDGAPLPRFRPGQFVTLRLPI----DGKPLRRAYSLSSAPGDGRLEITVKRV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 230 MGeareGYVSNILHGK-SEGDVVRVSHPFGDFFFDREESGengPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGAR 308
Cdd:COG1018   74 PG----GGGSNWLHDHlKVGDTLEVSGPRGDFVLDPEPAR---PLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGAR 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 309 DLNARAFKKDVDTLVAANRNIRAVYFSSNPKEGEvegqdyhiKGRVDMDKVgkDALFADNDQTQYFICGPTQFMLDVQAK 388
Cdd:COG1018  147 SPADLAFRDELEALAARHPRLRLHPVLSREPAGL--------QGRLDAELL--AALLPDPADAHVYLCGPPPMMEAVRAA 216

                        250
                 ....*....|....
gi 169606282 389 LKSYGVPAERIKME 402
Cdd:COG1018  217 LAELGVPEERIHFE 230
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 275-386 1.11e-11

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: 61.12  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  275 LISAGVGLTCLTSILNGLAAEQGS-RPVSWIHGARDLNARAFKKDVDTLVAAN-RNIRAVYFSSNPKEGevegqDYHIKG 352
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKDpTQVVLVFGNRNEDDILYREELDELAEKHpGRLTVVYVVSRPEAG-----WTGGKG 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 169606282  353 RVDmDKVGKDALFADNDQTQYFICGPTQFMLDVQ 386
Cdd:pfam00175  76 RVQ-DALLEDHLSLPDEETHVYVCGPPGMIKAVR 108
 
Name Accession Description Interval E-value
PRK13289 PRK13289
NO-inducible flavohemoprotein;
4-409 1.24e-169

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 480.45  E-value: 1.24e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   4 LSPSQVQIIKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVFNTTHQATGHQSRALAGALYAYAANIDNLGALSPALELI 83
Cdd:PRK13289   2 LSAQTIAIVKATVPLLEEHGEALTAHFYDRMFSHNPELKNIFNQSNQRNGDQPEALANAVLAYARNIDNLEALLPAVERI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  84 CHKHVSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLADIMIAKEEGLYKS----TPGWDGWKDFTIVR 159
Cdd:PRK13289  82 AQKHVSLQIKPEHYPIVGEHLLAAIREVLGDAATDEVLDAWGEAYGVLADVFIGREAEIYEEaaskPGGWRGWRDFRVVK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 160 KVAEsgSGEICSFYLKPKEAGvEVPVFKPGQYVSVNVRVEELdgGVWQARQYSLSDASGKGYLRISVKKEMGeareGYVS 239
Cdd:PRK13289 162 KVPE--SEVITSFYLEPVDGG-PVADFKPGQYLGVRLDPEGE--EYQEIRQYSLSDAPNGKYYRISVKREAG----GKVS 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 240 NILHGK-SEGDVVRVSHPFGDFFFDREesgENGPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGARDLNARAFKKD 318
Cdd:PRK13289 233 NYLHDHvNVGDVLELAAPAGDFFLDVA---SDTPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIHAARNGGVHAFRDE 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 319 VDTLVAANRNIRAVYFSSNPKEGEVEGQDYHIKGRVDMDKVGKDALFADNDqtqYFICGPTQFMLDVQAKLKSYGVPAER 398
Cdd:PRK13289 310 VEALAARHPNLKAHTWYREPTEQDRAGEDFDSEGLMDLEWLEAWLPDPDAD---FYFCGPVPFMQFVAKQLLELGVPEER 386

                        410
                 ....*....|.
gi 169606282 399 IKMELFGTGGV 409
Cdd:PRK13289 387 IHYEFFGPAKV 397
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 147-408 7.20e-108

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: 317.58  E-value: 7.20e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 147 PGWDGWKDFTIVRKVAESGsgEICSFYLKPKEaGVEVPVFKPGQYVSVNVRVEelDGGVWQARQYSLSDASGKGYLRISV 226
Cdd:cd06184    1 GGWRGFRPFVVARKVAESE--DITSFYLEPAD-GGPLPPFLPGQYLSVRVKLP--GLGYRQIRQYSLSDAPNGDYYRISV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 227 KKEmgeaREGYVSNILHG-KSEGDVVRVSHPFGDFFFDREEsgeNGPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIH 305
Cdd:cd06184   76 KRE----PGGLVSNYLHDnVKVGDVLEVSAPAGDFVLDEAS---DRPLVLISAGVGITPMLSMLEALAAEGPGRPVTFIH 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 306 GARDLNARAFKKDVDTLVAANRNIRAVYFSSNPKEGEVEgQDYHIKGRVDMDKVGKDALFADndqTQYFICGPTQFMLDV 385
Cdd:cd06184  149 AARNSAVHAFRDELEELAARLPNLKLHVFYSEPEAGDRE-EDYDHAGRIDLALLRELLLPAD---ADFYLCGPVPFMQAV 224

                        250       260
                 ....*....|....*....|...
gi 169606282 386 QAKLKSYGVPAERIKMELFGTGG 408
Cdd:cd06184  225 REGLKALGVPAERIHYEVFGPGE 247
FHb-globin cd08922
Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide ...
 4-143 2.33e-72

Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses. FlavoHb expression affects Aspergillus nidulans sexual development and mycotoxin production, and Dictyostelium discoideum development. This family also includes some single-domain goblins (SDgbs).


Pssm-ID: 381260  Cd Length: 140  Bit Score: 223.22  E-value: 2.33e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   4 LSPSQVQIIKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVFNTTHQATGHQSRALAGALYAYAANIDNLGALSPALELI 83
Cdd:cd08922    1 LSEETIAIVKATAPVLAEHGEEITTRFYKRMFAEHPELKNLFNMANQASGRQPKALAAAVLAYAANIDNLEVLLPAVERI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  84 CHKHVSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLADIMIAKEEGLY 143
Cdd:cd08922   81 AHKHVSLGVKPEHYPIVGEYLLEAIKEVLGDAATPEVLDAWAEAYGFLADILIEREKQLY 140
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
150-402 1.29e-64

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 206.56  E-value: 1.29e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 150 DGWKDFTIVRKVAESGsgEICSFYLKPkEAGVEVPVFKPGQYVSVNVRVeeldGGVWQARQYSLSDASGKGYLRISVKKE 229
Cdd:COG1018    1 AGFRPLRVVEVRRETP--DVVSFTLEP-PDGAPLPRFRPGQFVTLRLPI----DGKPLRRAYSLSSAPGDGRLEITVKRV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 230 MGeareGYVSNILHGK-SEGDVVRVSHPFGDFFFDREESGengPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGAR 308
Cdd:COG1018   74 PG----GGGSNWLHDHlKVGDTLEVSGPRGDFVLDPEPAR---PLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGAR 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 309 DLNARAFKKDVDTLVAANRNIRAVYFSSNPKEGEvegqdyhiKGRVDMDKVgkDALFADNDQTQYFICGPTQFMLDVQAK 388
Cdd:COG1018  147 SPADLAFRDELEALAARHPRLRLHPVLSREPAGL--------QGRLDAELL--AALLPDPADAHVYLCGPPPMMEAVRAA 216

                        250
                 ....*....|....
gi 169606282 389 LKSYGVPAERIKME 402
Cdd:COG1018  217 LAELGVPEERIHFE 230
FHP_Ae-globin-like cd14779
Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins; ...
 4-143 8.07e-59

Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins; Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb maintains Medicago truncatula-Sinorhizobium meliloti symbiosis. Alcaligenes eutrophus FHP contains a phospholipid-binding site.


Pssm-ID: 381287  Cd Length: 140  Bit Score: 188.42  E-value: 8.07e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   4 LSPSQVQIIKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVFNTTHQATGHQSRALAGALYAYAANIDNLGALSPALELI 83
Cdd:cd14779    1 LTEQQKDLVKATVPVLKEHGVALTKHFYQRMFEHNPELKNVFNMGHQESGKQQQALAMAVLAYAENIDDPEVLLPVLKLI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  84 CHKHVSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLADIMIAKEEGLY 143
Cdd:cd14779   81 AHKHVSLGIRAEQYPIVGEHLLASIKEVLGDAATDELISAWAAAYGQLADILIGMESKLY 140
HmpPa-globin-like cd14780
Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins; ...
 4-143 1.01e-56

Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins; Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. The physiological role of HmpPa is thought to be detoxification of NO under aerobic conditions.


Pssm-ID: 381288  Cd Length: 140  Bit Score: 183.04  E-value: 1.01e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   4 LSPSQVQIIKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVFNTTHQATGHQSRALAGALYAYAANIDNLGALSPALELI 83
Cdd:cd14780    1 LSPHQIAIIKATVPALEAHGEAITTHFYPLMFEEYPEVRALFNQAHQASGAQPRALANAVLAYARHIDRLEVLGGAVSLI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  84 CHKHVSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLADIMIAKEEGLY 143
Cdd:cd14780   81 VNKHVSLNILPEHYPIVGTCLLRAIREVLGDAATDEVIEAWGAAYQQLADLLIAAEEAVY 140
Yhb1-globin-like cd14777
Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains; ...
 4-143 7.48e-55

Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. S. cerevisiae Yhb1p has been shown to protect against nitrosative stress and to control ferric reductase activity; it may participate in regulating the activity of plasma membrane ferric reductase(s). Also included in this subfamily is Dictyostelium discoideum FlavoHb, the expression of which affects D. discoideum development.


Pssm-ID: 381285  Cd Length: 140  Bit Score: 177.92  E-value: 7.48e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   4 LSPSQVQIIKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVFNTTHQATGHQSRALAGALYAYAANIDNLGALSPALELI 83
Cdd:cd14777    1 LSEKTIQIVKSTVPVLKEKGTEITKRFYKRMFEEHPELLNIFNQTNQKKGLQQTALANTVYAAAKHIDNLEVILPVVKQI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  84 CHKHVSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLADIMIAKEEGLY 143
Cdd:cd14777   81 AHKHRALGVKPEHYPIVGENLLAAIKEVLGDAATDEILEAWEKAYGVIADVFIEVEKEMY 140
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
4-141 1.47e-52

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 171.88  E-value: 1.47e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   4 LSPSQVQIIKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVFNtthQATGHQSRALAGALYAYAANIDNLGALSPALELI 83
Cdd:COG1017    1 LSPETIALVKASFPLVAPHGEEITARFYERLFELHPELRPLFN---GDMGEQRKALAAALAAYARNLDNLEALLPALERL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 169606282  84 CHKHVSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLADIMIAKEEG 141
Cdd:COG1017   78 GRKHVSYGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLADVMIAAEAE 135
FHb-globin_1 cd14781
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 4-143 4.40e-49

Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. This subfamily may contain some single-domain goblins (SDgbs).


Pssm-ID: 381289  Cd Length: 139  Bit Score: 163.03  E-value: 4.40e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   4 LSPSQVQIIKSTVPVLAQHGEAITAKFYTDLLtANPSLKNVFNTTHQATGHQSRALAGALYAYAANIDNLGALSPALELI 83
Cdd:cd14781    1 LSPHTIAIVKATVPALEEHGVAITAAMYKRLF-EDPEIKALFNQAAQKSGEQPRALAGAILAYAKNIDNLGALGSAVERI 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  84 CHKHVSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLADIMIAKEEGLY 143
Cdd:cd14781   80 AQKHVGLHIKPEHYPHVATALLGAIKDVLGDAATDEVLEAWGEAYWFLADILINREKQLY 139
FHb-globin_3 cd14783
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 4-143 2.22e-45

Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways.


Pssm-ID: 271316  Cd Length: 140  Bit Score: 153.38  E-value: 2.22e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   4 LSPSQVQIIKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVFNTTHQATGHQSRALAGALYAYAANIDNLGALSPALELI 83
Cdd:cd14783    1 LSQKTIDIVKSTAPILEENGETLTRHFYKRMFEHNPEVKPFFNPAHQHSGSQQRALAAAICAYAANIDNLEVLGNAVELI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  84 CHKHVSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLADIMIAKEEGLY 143
Cdd:cd14783   81 AQKHASLGIKPEHYPIVGSNLLASIREVLGDAATDDIIEAWSEAYGFLADILIGREKQIY 140
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 168-402 9.64e-44

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: 152.22  E-value: 9.64e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 168 EICSFYLKPkeagVEVPVFKPGQYVSVNVRveelDGGVWQARQYSLSDASG-KGYLRISVKKemgeAREGYVSNILHGKS 246
Cdd:cd00322    9 DVRLFRLQL----PNGFSFKPGQYVDLHLP----GDGRGLRRAYSIASSPDeEGELELTVKI----VPGGPFSAWLHDLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 247 EGDVVRVSHPFGDFFFDREEsgeNGPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGARDLNARAFKKDVDTLVAAN 326
Cdd:cd00322   77 PGDEVEVSGPGGDFFLPLEE---SGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTPADLLFLDELEELAKEG 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169606282 327 RNIRAVYFSSNPKEGEVEGQDYHIKGRvdmdkvGKDALFADNDQTQYFICGPTQFMLDVQAKLKSYGVPAERIKME 402
Cdd:cd00322  154 PNFRLVLALSRESEAKLGPGGRIDREA------EILALLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
HmpEc-globin-like cd14776
Globin domain of Escherichia coli flavohemoglobin (Hmp) and related proteins; Flavohemoglobins ...
 4-143 1.54e-43

Globin domain of Escherichia coli flavohemoglobin (Hmp) and related proteins; Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. This subfamily includes Vibrio fischeri Hmp and E.coli Hmp. NO scavenging by flavoHb affects the swarming behavior of Escherichia coli, and protects against NO during initiation of the squid-Vibrio symbiosis. E.coli Hmp can catalyze the reduction of several alkylhydroperoxide substrates into their corresponding alcohols using NADH as an electron donor, and it has been suggested that it participates in the repair of the lipid membrane oxidative damage generated during oxidative/nitrosative stress.


Pssm-ID: 271309  Cd Length: 138  Bit Score: 148.77  E-value: 1.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   4 LSPSQVQIIKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVFNTTHQATGHQSRALAGALYAYAANIDNLGALSPALELI 83
Cdd:cd14776    1 LSAETIRIVKATIPLLAAAGPALTQHFYQRMLTHNPELKNIFNLAHQRTGRQPKALFDAVAAYAQNIRNLQALLPAVERI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  84 CHKHVSLFIQPAQYAIVGEFLLATMKTVLgaAATGEVLDAWGAAYWQLADIMIAKEEGLY 143
Cdd:cd14776   81 AQKHTSFNIQPEQYQIVGEHLLATIEELA--PPDKDVLAAWAKAYQFLADIFIDREGEIY 138
VtHb-like_SDgb cd14778
Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is ...
 4-143 2.84e-40

Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is homodimeric, and may both transport oxygen to terminal respiratory oxidases, and provide resistance to nitrosative stress. It has medium oxygen affinity and displays cooperative ligand-binding properties. VHb has biotechnological application, its expression in heterologous hosts (bacteria and plants) has improved growth and productivity under microaerobic conditions. Another member of this subfamily Campylobacter jejuni hemoglobin (Cgb) is monomeric, and plays a role in detoxifying NO. Along with a truncated globin Ctb, it is up-regulated by the transcription factor NssR in response to nitrosative stress.


Pssm-ID: 381286 [Multi-domain]  Cd Length: 140  Bit Score: 140.26  E-value: 2.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   4 LSPSQVQIIKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVFNTTHQATGHQSRALAGALYAYAANIDNLGALSPALELI 83
Cdd:cd14778    1 LDQQTIEIIKSTVPVLKEHGVEITTEFYKNMFTEYPEVRPMFDMEKQKSGEQPKALAMTVLAAAQNIENLEKIRPAVEKI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  84 CHKHVSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLADIMIAKEEGLY 143
Cdd:cd14778   81 GKTHVNLNVKPEHYPIVGACLLGAIKEVLGDTATDEILEAWEKAYGEIAKIFIDVEKKLY 140
FHb-globin_2 cd14782
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 4-143 5.15e-38

Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways.


Pssm-ID: 381290  Cd Length: 143  Bit Score: 134.45  E-value: 5.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   4 LSPSQVQIIKSTVPVLAQHGEAITAKFYTDLLTANPSL-KNVFNTTHQATGHQSRALAGALYAYAANI--DNLGALSPAL 80
Cdd:cd14782    1 LSAESAEVIRATLPVVGEHIEEITPLFYRRMFGEHPELlRNLFNRGNQASGEQQKALAASVAAFATHLvdPDAPPPDSVL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169606282  81 ELICHKHVSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLADIMIAKEEGLY 143
Cdd:cd14782   81 SRIAHKHASLGITPEQYTIVHRHLFAAIAEVLGAAVTPEVAAAWDEVYWLMADQLIATEARLY 143
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 156-405 5.33e-38

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: 137.29  E-value: 5.33e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 156 TIVRKVAESGsgEICSFYLKPKEAGVEVPVFKPGQYVSVNVRVeeldGGVWQARQYSLSDASGKGYLRISVKKEmgeaRE 235
Cdd:cd06214    5 TVAEVVRETA--DAVSITFDVPEELRDAFRYRPGQFLTLRVPI----DGEEVRRSYSICSSPGDDELRITVKRV----PG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 236 GYVSNILHGK-SEGDVVRVSHPFGDFFFDREESGENgpVVLISAGVGLTCLTSILN-GLAAEQGSRpVSWIHGARDLNAR 313
Cdd:cd06214   75 GRFSNWANDElKAGDTLEVMPPAGRFTLPPLPGARH--YVLFAAGSGITPVLSILKtALAREPASR-VTLVYGNRTEASV 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 314 AFKKDVDTLVAANRNIRAVYFSSNPKEGEVEGQdyhiKGRVDMDKVGK--DALFADNDQTQYFICGPTQFMLDVQAKLKS 391
Cdd:cd06214  152 IFREELADLKARYPDRLTVIHVLSREQGDPDLL----RGRLDAAKLNAllKNLLDATEFDEAFLCGPEPMMDAVEAALLE 227

                        250
                 ....*....|....
gi 169606282 392 YGVPAERIKMELFG 405
Cdd:cd06214  228 LGVPAERIHRELFT 241
FHb_fungal-globin cd19754
Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide ...
 4-143 6.05e-38

Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses. FlavoHb expression affects Aspergillus nidulans sexual development and mycotoxin production, and Dictyostelium discoideum development.


Pssm-ID: 381294  Cd Length: 141  Bit Score: 134.00  E-value: 6.05e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   4 LSPSQVQIIKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVFNTTHQATGHQSRALAGALYAYAANIDNLGALSPALELI 83
Cdd:cd19754    1 LTPAQIKIIKDSVPILESLGVKLTEKFYKYMLKRYPEVKPYFNETNQKLLRQPKILAFALLQYAKNIDDLTPLSGFVEQI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169606282  84 CHKHVSLFIQPAQYAIVGEFLLATMKTVLG-AAATGEVLDAWGAAYWQLADIMIAKEEGLY 143
Cdd:cd19754   81 VSKHVGLQVKPEHYPIVGECLIETMKELLPeAVATDEFIEAWTTAYGNLANILIDAEKKEY 141
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 152-404 3.13e-31

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


Pssm-ID: 99813 [Multi-domain]  Cd Length: 235  Bit Score: 119.29  E-value: 3.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 152 WKDFTIVRKVAESGSgeICSFYLKPkeAGVEVPVFKPGQYVsvNVRVEELDGgVWQARQYSL-SDASGKGYLRISVKKEM 230
Cdd:cd06217    1 WRVLRVTEIIQETPT--VKTFRLAV--PDGVPPPFLAGQHV--DLRLTAIDG-YTAQRSYSIaSSPTQRGRVELTVKRVP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 231 GeareGYVSNILHGK-SEGDVVRVSHPFGDFFFDREESGengPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGARD 309
Cdd:cd06217   74 G----GEVSPYLHDEvKVGDLLEVRGPIGTFTWNPLHGD---PVVLLAGGSGIVPLMSMIRYRRDLGWPVPFRLLYSART 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 310 LNARAFKKDVDTLVAANRNIRAVYFSSNPKEGEVEGqdyhIKGRVDMDKVGKdaLFADNDQTQYFICGPTQFMLDVQAKL 389
Cdd:cd06217  147 AEDVIFRDELEQLARRHPNLHVTEALTRAAPADWLG----PAGRITADLIAE--LVPPLAGRRVYVCGPPAFVEAATRLL 220

                        250
                 ....*....|....*
gi 169606282 390 KSYGVPAERIKMELF 404
Cdd:cd06217  221 LELGVPRDRIRTEAF 235
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 157-404 5.93e-30

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap 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: 115.78  E-value: 5.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 157 IVRKVAESGsgEICSFYLKPkeaGVEVPVFKPGQYVSVNVRVEeldgGVWQARQYSLS--DASGKGYLRISVKKemgeAR 234
Cdd:cd06216   22 VVAVRPETA--DMVTLTLRP---NRGWPGHRAGQHVRLGVEID----GVRHWRSYSLSssPTQEDGTITLTVKA----QP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 235 EGYVSNILHGKSE-GDVVRVSHPFGDFFFdreESGENGPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGARDLNAR 313
Cdd:cd06216   89 DGLVSNWLVNHLApGDVVELSQPQGDFVL---PDPLPPRLLLIAAGSGITPVMSMLRTLLARGPTADVVLLYYARTREDV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 314 AFKKDVDTLVAANRNIRAVYFSSnpkegevegqDYHIKGRVDMDKVgkDALFADNDQTQYFICGPTQFMLDVQAKLKSYG 393
Cdd:cd06216  166 IFADELRALAAQHPNLRLHLLYT----------REELDGRLSAAHL--DAVVPDLADRQVYACGPPGFLDAAEELLEAAG 233

                        250
                 ....*....|.
gi 169606282 394 VpAERIKMELF 404
Cdd:cd06216  234 L-ADRLHTERF 243
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 171-404 7.83e-27

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: 106.91  E-value: 7.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 171 SFYLKPKEAgvEVPVFKPGQYVSVNVrveELDGGVWQaRQYSLSDA-SGKGYLRISVKKEMGeareGYVSNILHGK-SEG 248
Cdd:cd06215   15 TFRFAAPDG--SLFAYKPGQFLTLEL---EIDGETVY-RAYTLSSSpSRPDSLSITVKRVPG----GLVSNWLHDNlKVG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 249 DVVRVSHPFGDFFFDReesGENGPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGARDLNARAFKKDVDTLVAANRN 328
Cdd:cd06215   85 DELWASGPAGEFTLID---HPADKLLLLSAGSGITPMMSMARWLLDTRPDADIVFIHSARSPADIIFADELEELARRHPN 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169606282 329 IRAVYfssNPKEGEvEGQDYHIKGRVDMDKVGkdALFADNDQTQYFICGPTQFMLDVQAKLKSYGVPAERIKMELF 404
Cdd:cd06215  162 FRLHL---ILEQPA-PGAWGGYRGRLNAELLA--LLVPDLKERTVFVCGPAGFMKAVKSLLAELGFPMSRFHQESF 231
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
155-404 3.61e-23

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 100.74  E-value: 3.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 155 FTIVRKVAESGSgeICSFYLKPKeaGVEVPVFKPGQYVSVNVrveELDGGVWQARQYSLSDASGK-GYLRISVKkemgeA 233
Cdd:COG4097  217 YRVESVEPEAGD--VVELTLRPE--GGRWLGHRAGQFAFLRF---DGSPFWEEAHPFSISSAPGGdGRLRFTIK-----A 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 234 REGYVSNILHGKsEGDVVRVSHPFGDFFFDREESGEngPVVLISAGVGLTCLTSILNGLAAEQGS-RPVSWIHGARDLNA 312
Cdd:COG4097  285 LGDFTRRLGRLK-PGTRVYVEGPYGRFTFDRRDTAP--RQVWIAGGIGITPFLALLRALAARPGDqRPVDLFYCVRDEED 361

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 313 RAFKKDVDTLVAANRNIRAVYFSSNPKegevegqdyhikGRVDMDKVGkdALFADNDQTQYFICGPTQFMLDVQAKLKSY 392
Cdd:COG4097  362 APFLEELRALAARLAGLRLHLVVSDED------------GRLTAERLR--RLVPDLAEADVFFCGPPGMMDALRRDLRAL 427

                        250
                 ....*....|..
gi 169606282 393 GVPAERIKMELF 404
Cdd:COG4097  428 GVPARRIHQERF 439
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 156-399 1.22e-22

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 96.09  E-value: 1.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 156 TIVRKVAESGsgEICSFYLKPKEAGVEvpvFKPGQYVsvNVRVEELDGgvwqARQYSLSDA-SGKGYLRISVKkemgeaR 234
Cdd:COG0543    1 KVVSVERLAP--DVYLLRLEAPLIALK---FKPGQFV--MLRVPGDGL----RRPFSIASApREDGTIELHIR------V 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 235 EGYVSNILHGKSEGDVVRVSHPFGDFFfDREESGenGPVVLISAGVGLTCLTSILNGLAAEQgsRPVSWIHGARDLNARA 314
Cdd:COG0543   64 VGKGTRALAELKPGDELDVRGPLGNGF-PLEDSG--RPVLLVAGGTGLAPLRSLAEALLARG--RRVTLYLGARTPEDLY 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 315 FKKDVDTLvaanRNIRAVYFSSNPKEGEvegqdyhiKGRVDmDKVgkDALFADNDQTQYFICGPTQFMLDVQAKLKSYGV 394
Cdd:COG0543  139 LLDELEAL----ADFRVVVTTDDGWYGR--------KGFVT-DAL--KELLAEDSGDDVYACGPPPMMKAVAELLLERGV 203


                 ....*
gi 169606282 395 PAERI 399
Cdd:COG0543  204 PPERI 208
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 186-404 1.30e-22

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: 95.67  E-value: 1.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 186 FKPGQYVSVNVRVEeldgGVWQARQYSLSDASGKGYLRISVKKEMGeareGYVSNILHGK-SEGDVVRVSHPFGDFFFDR 264
Cdd:cd06191   28 FRPGQHVTLKLDFD----GEELRRCYSLCSSPAPDEISITVKRVPG----GRVSNYLREHiQPGMTVEVMGPQGHFVYQP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 265 EESGengPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGARDLNARAFKKDVDTLVAANRNIRAVYFSSnpkegEVE 344
Cdd:cd06191  100 QPPG---RYLLVAAGSGITPLMAMIRATLQTAPESDFTLIHSARTPADMIFAQELRELADKPQRLRLLCIFT-----RET 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 345 GQDYHIKGRVDMDKVGKDALFADNDQTQYFICGPTQFMLDVQAKLKSYGVPAERIKMELF 404
Cdd:cd06191  172 LDSDLLHGRIDGEQSLGAALIPDRLEREAFICGPAGMMDAVETALKELGMPPERIHTERF 231
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 186-404 5.03e-22

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: 93.43  E-value: 5.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 186 FKPGQYVsvNVRVEELDGgvwQARQYSLSDA-SGKGYLRISVKKemgeAREGYVSNILHGKSE-GDVVRVSHPFGDFFFD 263
Cdd:cd06187   24 FWAGQYV--NVTVPGRPR---TWRAYSPANPpNEDGEIEFHVRA----VPGGRVSNALHDELKvGDRVRLSGPYGTFYLR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 264 REESGengPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGAR---DLnarafkKDVDTLV---AANRNIRAVYFSSN 337
Cdd:cd06187   95 RDHDR---PVLCIAGGTGLAPLRAIVEDALRRGEPRPVHLFFGARterDL------YDLEGLLalaARHPWLRVVPVVSH 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169606282 338 PkEGEVEGQDYHIKGRVdmdkvgkDALFADNDQTQYFICGPTQFMLDVQAKLKSYGVPAERIKMELF 404
Cdd:cd06187  166 E-EGAWTGRRGLVTDVV-------GRDGPDWADHDIYICGPPAMVDATVDALLARGAPPERIHFDKF 224
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 8-137 1.12e-19

Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a single-domain heme-containing protein isolated from Methylacidiphilum infernorum, an aerobic acidophilic and thermophilic methanotroph. M. infernorum grows optimally at pH 2.0 and 60C and its home is New Zealand's Hell's Gate geothermal park. The physiological role of HGbI has yet to be determined. It has an extremely strong resistance to auto-oxidation, and has fast oxygen-binding/slow release characteristics. Its CO on-rate is comparable to the O2 on-rate, and it is able to bind acetate with high affinity in the ferric state. The coordination of the heme iron changes in the ferrous form from pentacoordinate at low pH to predominantly hexacoordinate at high pH; in the ferric form, it is predominantly hexacoordinate at all pH.


Pssm-ID: 381269 [Multi-domain]  Cd Length: 128  Bit Score: 84.14  E-value: 1.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   8 QVQIIKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVFNTTHQATghQSRALAGALYAYAANIDNLGALSPALELICHKH 87
Cdd:cd12131    1 QIELVQQSFAKVEPIADEAAALFYERLFELDPELKPLFKGTDMEE--QGRKLMAMLVLVVKGLDDLEALLPALQDLGRRH 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 169606282  88 VSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLADIMIA 137
Cdd:cd12131   79 VKYGVKPEHYPLVGEALLWTLEEGLGDEWTPEVKQAWTDAYGILAGTMIE 128
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 153-404 4.73e-19

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: 85.45  E-value: 4.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 153 KDFTIVRKVAESGSGEICSFYLKPKEAgvEVPVFKPGQYVsvNVRVEELDGgvwqARQYSLSDA-SGKGYLRISVKKEMG 231
Cdd:cd06211    5 KDFEGTVVEIEDLTPTIKGVRLKLDEP--EEIEFQAGQYV--NLQAPGYEG----TRAFSIASSpSDAGEIELHIRLVPG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 232 EAREGYVSNILhgkSEGDVVRVSHPFGDFFFDREESGengPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGARDLN 311
Cdd:cd06211   77 GIATTYVHKQL---KEGDELEISGPYGDFFVRDSDQR---PIIFIAGGSGLSSPRSMILDLLERGDTRKITLFFGARTRA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 312 ARAFKKDVDTLVAANRNIRAV-YFSSNPKEGEVEGQdyhiKGRVDmDKVGKdalFADNDQTQY--FICGPTQfMLDVQAK 388
Cdd:cd06211  151 ELYYLDEFEALEKDHPNFKYVpALSREPPESNWKGF----TGFVH-DAAKK---HFKNDFRGHkaYLCGPPP-MIDACIK 221

                        250
                 ....*....|....*..
gi 169606282 389 -LKSYGVPAERIKMELF 404
Cdd:cd06211  222 tLMQGRLFERDIYYEKF 238
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 186-404 8.46e-18

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: 81.53  E-value: 8.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 186 FKPGQYVSVNVrveeLDGGVWQARQYSLSDAS-GKGYLRISVKkEMGEaregYVSNILHGKSEGDVVRVSHPFGDFFFDR 264
Cdd:cd06198   23 HRAGQFAFLRF----DASGWEEPHPFTISSAPdPDGRLRFTIK-ALGD----YTRRLAERLKPGTRVTVEGPYGRFTFDD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 265 EEsgenGPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGARDLNARAFkkdVDTLVAANRNIRAVYfssNPKEGEVE 344
Cdd:cd06198   94 RR----ARQIWIAGGIGITPFLALLEALAARGDARPVTLFYCVRDPEDAVF---LDELRALAAAAGVVL---HVIDSPSD 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 345 GQDYHIKGRvdmdkvgkDALFADNDQTQYFICGPTQFMLDVQAKLKSYGVPAERIKMELF 404
Cdd:cd06198  164 GRLTLEQLV--------RALVPDLADADVWFCGPPGMADALEKGLRALGVPARRFHYERF 215
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 157-403 1.05e-16

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: 79.19  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 157 IVRKVAESGSGEIcsFYLKPKEAGVEVPVFKPGQYVSVNVRveeldgGVWQArQYSL-SDASGKGYLRISVKkemgeaRE 235
Cdd:cd06221    1 IVEVVDETEDIKT--FTLRLEDDDEELFTFKPGQFVMLSLP------GVGEA-PISIsSDPTRRGPLELTIR------RV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 236 GYVSNILHGKSEGDVVRVSHPFGDFFFDREESGENgpVVLISAGVGLTCLTSILNGLAAEQGS-RPVSWIHGARDLNARA 314
Cdd:cd06221   66 GRVTEALHELKPGDTVGLRGPFGNGFPVEEMKGKD--LLLVAGGLGLAPLRSLINYILDNREDyGKVTLLYGARTPEDLL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 315 FKKDVDTlVAANRNIRAVYfssnpkegEVEGQDYHIKGRVDMDKVGKDALFADNDQTQYFICGPTQFMLDVQAKLKSYGV 394
Cdd:cd06221  144 FKEELKE-WAKRSDVEVIL--------TVDRAEEGWTGNVGLVTDLLPELTLDPDNTVAIVCGPPIMMRFVAKELLKLGV 214


                 ....*....
gi 169606282 395 PAERIKMEL 403
Cdd:cd06221  215 PEEQIWVSL 223
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 172-406 3.82e-16

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: 79.52  E-value: 3.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 172 FYLKPKEaGVEVPvFKPGQYVsvNVRVEELD-------------GGVWQA------RQYSL-SDASGKGYLRISVKKEMG 231
Cdd:COG2871  149 LVLELPE-GEEID-FKAGQYI--QIEVPPYEvdfkdfdipeeekFGLFDKndeevtRAYSMaNYPAEKGIIELNIRIATP 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 232 --EAREGYVSNILHGKSEGDVVRVSHPFGDFFFdREesgENGPVVLISAGVGLTCLTSILNGLAAEQGS-RPVSWIHGAR 308
Cdd:COG2871  225 pmDVPPGIGSSYIFSLKPGDKVTISGPYGEFFL-RD---SDREMVFIGGGAGMAPLRSHIFDLLERGKTdRKITFWYGAR 300

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 309 DLNARAFKKDVDTLVAANRNiravyFS-----SNPKEGEV-EGQdyhiKGRVdmDKVGKDALFADNDQT---QYFICGPT 379
Cdd:COG2871  301 SLRELFYLEEFRELEKEHPN-----FKfhpalSEPLPEDNwDGE----TGFI--HEVLYENYLKDHPAPedcEAYLCGPP 369

                        250       260
                 ....*....|....*....|....*...
gi 169606282 380 QfMLD-VQAKLKSYGVPAERIKMELFGT 406
Cdd:COG2871  370 P-MIDaVIKMLDDLGVEEENIYFDDFGG 396
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 158-405 1.36e-15

Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal.


Pssm-ID: 99782 [Multi-domain]  Cd Length: 211  Bit Score: 75.21  E-value: 1.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 158 VRKVAEsgsgEICSFYLKPkEAGVEVPVFKPGQYVSVNVRveelDGGVwqaRQYSL-SDASGKGYLRISVKKEmgEA-RE 235
Cdd:cd06185    3 IRDEAP----DIRSFELEA-PDGAPLPAFEPGAHIDVHLP----NGLV---RQYSLcGDPADRDRYRIAVLRE--PAsRG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 236 GyvSNILHGK-SEGDVVRVSHPFGDFFFDREEsgenGPVVLISAGVGLTCLTSILNGLAAEQgsRPVSWIHGARDLNARA 314
Cdd:cd06185   69 G--SRYMHELlRVGDELEVSAPRNLFPLDEAA----RRHLLIAGGIGITPILSMARALAARG--ADFELHYAGRSREDAA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 315 FkkdVDTLVAANRNIRAVYFSSnpkegevEGQdyhikgRVDMDkvgkdALFADNDQ-TQYFICGPTQFMLDVQAKLKSYG 393
Cdd:cd06185  141 F---LDELAALPGDRVHLHFDD-------EGG------RLDLA-----ALLAAPPAgTHVYVCGPEGMMDAVRAAAAALG 199

                        250
                 ....*....|..
gi 169606282 394 VPAERIKMELFG 405
Cdd:cd06185  200 WPEARLHFERFA 211
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 186-399 2.28e-15

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: 74.66  E-value: 2.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 186 FKPGQYVsvNVRVEELDGgvwqARQYSLSDA-SGKGYLRISVKKEMGeareGYVSNILHGKS-EGDVVRVSHPFGDFFFd 263
Cdd:cd06213   28 YKAGQYA--ELTLPGLPA----ARSYSFANApQGDGQLSFHIRKVPG----GAFSGWLFGADrTGERLTVRGPFGDFWL- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 264 REEsgeNGPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGAR---DLNArafkkdVDTLVAANRNIRAVY-----FS 335
Cdd:cd06213   97 RPG---DAPILCIAGGSGLAPILAILEQARAAGTKRDVTLLFGARtqrDLYA------LDEIAAIAARWRGRFrfipvLS 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169606282 336 SNPKEGEVEGQdyhiKGRVdMDKVGKDALfadnDQTQYFICGPTQfMLD-VQAKLKSYGVPAERI 399
Cdd:cd06213  168 EEPADSSWKGA----RGLV-TEHIAEVLL----AATEAYLCGPPA-MIDaAIAVLRALGIAREHI 222
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 186-403 2.89e-15

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 75.61  E-value: 2.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 186 FKPGQYVSVNVRveeldgGVWQARQYSLSDASGKGYLRISVKkemgeaREGYVSNILHGKSEGDVVRVSHPFGDFFFDRE 265
Cdd:PRK08345  38 FKPGQFVQVTIP------GVGEVPISICSSPTRKGFFELCIR------RAGRVTTVIHRLKEGDIVGVRGPYGNGFPVDE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 266 ESGENgpVVLISAGVGLTCLTSIL-----NGLAAEQgsrpVSWIHGARDLNARAFKKDVDTLVAANRNIRAvyFSSNPKE 340
Cdd:PRK08345 106 MEGMD--LLLIAGGLGMAPLRSVLlyamdNRWKYGN----ITLIYGAKYYEDLLFYDELIKDLAEAENVKI--IQSVTRD 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169606282 341 GEVEGQDYHIKGRVDMDKVGKDA-LFA----DNDQTQYFICGPTQFMLDVQAKLKSYGVPAERIKMEL 403
Cdd:PRK08345 178 PEWPGCHGLPQGFIERVCKGVVTdLFReantDPKNTYAAICGPPVMYKFVFKELINRGYRPERIYVTL 245
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 155-399 1.99e-14

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: 72.21  E-value: 1.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 155 FTIVRKVAESGSGEICSFYLKPKEagvEVPVFKPGQYVSVNVRVEELDggVwqARQYS-LSDASGKGYLRISVKKEmgea 233
Cdd:cd06183    1 FKLVSKEDISHDTRIFRFELPSPD---QVLGLPVGQHVELKAPDDGEQ--V--VRPYTpISPDDDKGYFDLLIKIY---- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 234 REGYVSNILHGKSEGDVVRVSHPFGDFFFDREESGENgpVVLISAGVGLTCLTSILNGLAAEQGSRP-VSWIHGARDLNA 312
Cdd:cd06183   70 PGGKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGKVKH--IGMIAGGTGITPMLQLIRAILKDPEDKTkISLLYANRTEED 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 313 RAFKKDVDTLVAANR-NIRAVYFSSNPKEGEVEGqdyhiKGRVDMDKVGKDALFADNDQTQYFICGPTQFM-LDVQAKLK 390
Cdd:cd06183  148 ILLREELDELAKKHPdRFKVHYVLSRPPEGWKGG-----VGFITKEMIKEHLPPPPSEDTLVLVCGPPPMIeGAVKGLLK 222


                 ....*....
gi 169606282 391 SYGVPAERI 399
Cdd:cd06183  223 ELGYKKDNV 231
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 186-399 7.41e-14

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: 70.44  E-value: 7.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 186 FKPGQYVSVNVRveelDGGVWqaRQYSLSDASGK-GYLRISVKKEMGeareGYVSNILHGK-SEGDVVRVSHPFGDFFFd 263
Cdd:cd06212   30 FFAGQYVDITVP----GTEET--RSFSMANTPADpGRLEFIIKKYPG----GLFSSFLDDGlAVGDPVTVTGPYGTCTL- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 264 REESgeNGPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGARDLNARAFKKDVDTLVAANRNIRAV-YFSSNPKEGE 342
Cdd:cd06212   99 RESR--DRPIVLIGGGSGMAPLLSLLRDMAASGSDRPVRFFYGARTARDLFYLEEIAALGEKIPDFTFIpALSESPDDEG 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 169606282 343 VEGQdyhiKGRVdMDKVgkDALFADNDQTQYFICGPTQfMLD-VQAKLKSYGVPAERI 399
Cdd:cd06212  177 WSGE----TGLV-TEVV--QRNEATLAGCDVYLCGPPP-MIDaALPVLEMSGVPPDQI 226
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 184-404 1.08e-13

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: 69.93  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 184 PVFKPGQYvsVNVRVEELDggvwQARQYSLSDASGKGYLRISVKKEMGeareGYVSNILHGKSE-GDVVRVSHPFGDFFF 262
Cdd:cd06209   29 LAFLPGQY--VNLQVPGTD----ETRSYSFSSAPGDPRLEFLIRLLPG----GAMSSYLRDRAQpGDRLTLTGPLGSFYL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 263 dREESgenGPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGAR---------DLNARAFKK---DVDTLVAANRnir 330
Cdd:cd06209   99 -REVK---RPLLMLAGGTGLAPFLSMLDVLAEDGSAHPVHLVYGVTrdadlveldRLEALAERLpgfSFRTVVADPD--- 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169606282 331 avyfSSNPKEGEVEGqdyHIkgrvdmdkvgKDALFADNDQTQYfICGPtQFMLD-VQAKLKSYGVPAERIKMELF 404
Cdd:cd06209  172 ----SWHPRKGYVTD---HL----------EAEDLNDGDVDVY-LCGP-PPMVDaVRSWLDEQGIEPANFYYEKF 227
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 185-405 1.29e-13

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: 69.97  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 185 VFKPGQYVSVnvRVEELDGgvwqARQYSLSD-ASGKGYLRISVKKEMGeareGYVSNILHGKSE-GDVVRVSHPFGDFFF 262
Cdd:cd06190   23 DFLPGQYALL--ALPGVEG----ARAYSMANlANASGEWEFIIKRKPG----GAASNALFDNLEpGDELELDGPYGLAYL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 263 dREESGenGPVVLISAGVGLTCLTSILNGLAAEQ--GSRPVSWIHGARDLNARAFKKDVDTLVAANRNIRAVYFSSNPKE 340
Cdd:cd06190   93 -RPDED--RDIVCIAGGSGLAPMLSILRGAARSPylSDRPVDLFYGGRTPSDLCALDELSALVALGARLRVTPAVSDAGS 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169606282 341 GEVEGQDYHiKGRVdmDKVGKDALFADNDQTQYFICGPTQfMLD-VQAKL-KSYGVPAERIKMELFG 405
Cdd:cd06190  170 GSAAGWDGP-TGFV--HEVVEATLGDRLAEFEFYFAGPPP-MVDaVQRMLmIEGVVPFDQIHFDRFV 232
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 169-404 1.90e-13

Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) provides a means of storing redox reaction energy via the transmembrane translocation of Na2+ ions. The C-terminal domain resembles ferredoxin:NADP+ oxidoreductase, and has NADH and FAD binding sites. (Na+-NQR) is distinct from H+-translocating NADH:quinone oxidoreductases and noncoupled NADH:quinone oxidoreductases. The NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain of this group typically contains an iron-sulfur cluster binding domain.


Pssm-ID: 99785 [Multi-domain]  Cd Length: 283  Bit Score: 70.03  E-value: 1.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 169 ICSFYLKPKEaGVEVPvFKPGQYVSVNVRVEEL----------------DGGVWQ---------ARQYSL-SDASGKGYL 222
Cdd:cd06188   24 IKELVLKLPS-GEEIA-FKAGGYIQIEIPAYEIayadfdvaekyradwdKFGLWQlvfkhdepvSRAYSLaNYPAEEGEL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 223 RISVK-----KEMGEAREGYVSNILHGKSEGDVVRVSHPFGDFFFDREESgengPVVLISAGVGLTCLTS-ILNGLAAEQ 296
Cdd:cd06188  102 KLNVRiatppPGNSDIPPGIGSSYIFNLKPGDKVTASGPFGEFFIKDTDR----EMVFIGGGAGMAPLRShIFHLLKTLK 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 297 GSRPVSWIHGARDLNARAFKKDVDTLVAANRNIRAVYFSSNPKEGEVE-GQDYHIKgRVDMDKVGKDaLFADNDqTQYFI 375
Cdd:cd06188  178 SKRKISFWYGARSLKELFYQEEFEALEKEFPNFKYHPVLSEPQPEDNWdGYTGFIH-QVLLENYLKK-HPAPED-IEFYL 254

                        250       260
                 ....*....|....*....|....*....
gi 169606282 376 CGPTQFMLDVQAKLKSYGVPAERIKMELF 404
Cdd:cd06188  255 CGPPPMNSAVIKMLDDLGVPRENIAFDDF 283
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 186-399 2.94e-13

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: 68.73  E-value: 2.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 186 FKPGQYVSVnvrveELDGGvwQARQYSL-SDASGKGYLRISVKKEMGEAregYVSNILHGKSEGDVVRVSHPFGDFFFdR 264
Cdd:cd06189   26 FLAGQYLDL-----LLDDG--DKRPFSIaSAPHEDGEIELHIRAVPGGS---FSDYVFEELKENGLVRIEGPLGDFFL-R 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 265 EESgeNGPVVLISAGVGLTCLTSILNGLAAEQGSRPVS--WihGARDLNARAFKKDVDTLVAANRNIRAVYFSSNPKege 342
Cdd:cd06189   95 EDS--DRPLILIAGGTGFAPIKSILEHLLAQGSKRPIHlyW--GARTEEDLYLDELLEAWAEAHPNFTYVPVLSEPE--- 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169606282 343 vEGQDYHIkGRVDmDKVGKDalFADNDQTQYFICGPTQFMLDVQAKLKSYGVPAERI 399
Cdd:cd06189  168 -EGWQGRT-GLVH-EAVLED--FPDLSDFDVYACGSPEMVYAARDDFVEKGLPEENF 219
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 186-399 1.05e-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: 66.91  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 186 FKPGQYVsvNVRVEeldGGVwqARQYSL-SDASGKGYLRISVKKEmgeaREGYVSNILHGKSE-GDVVRVSHPFGDFFFd 263
Cdd:cd06194   24 YLPGQYV--NLRRA---GGL--ARSYSPtSLPDGDNELEFHIRRK----PNGAFSGWLGEEARpGHALRLQGPFGQAFY- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 264 REESGEnGPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGARDLNARAFKKDVDTLVAANRNIRAVYFSSnpkegev 343
Cdd:cd06194   92 RPEYGE-GPLLLVGAGTGLAPLWGIARAALRQGHQGEIRLVHGARDPDDLYLHPALLWLAREHPNFRYIPCVS------- 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169606282 344 EGQDYHikGRVDMDKVGKDALFADNDQTQYfICGPTQFMLDVQAKLKSYGVPAERI 399
Cdd:cd06194  164 EGSQGD--PRVRAGRIAAHLPPLTRDDVVY-LCGAPSMVNAVRRRAFLAGAPMKRI 216
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 12-135 1.24e-12

myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) and single-domain globins: FHbs, Ngbs/neuroglobins, Cygb/cytoglobins, GbE/avian eye specific globin E, GbX/globin X, amphibian GbY/globin Y, Mb/myoglobin, HbA/hemoglobin-alpha, HbB/hemoglobin-beta, SDgbs/single-domain globins related to FHbs, and Adgb/androglobin. The M family exhibits the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments (named A through H). In Adgbs, the globin domain is split into two: helices C-H are followed by helices A-B and the two parts are separated by the IQ motif. Although rearranged, the globin domain of most Adgbs contains a number of conserved residues which play critical roles in heme-coordination and gas ligand binding. Adgbs have been omitted from this A-H helix cd.


Pssm-ID: 381254  Cd Length: 133  Bit Score: 64.78  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  12 IKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVFNTTHQATG---------HQSRALAGALYAYAANIDNLGALSPALEL 82
Cdd:cd01040    1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDLdlkgspefkAHAKRVVGALDSLIDNLDDPEALDALLRK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169606282  83 ICHKHVSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLADIM 135
Cdd:cd01040   81 LGKRHKRRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 275-386 1.11e-11

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: 61.12  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  275 LISAGVGLTCLTSILNGLAAEQGS-RPVSWIHGARDLNARAFKKDVDTLVAAN-RNIRAVYFSSNPKEGevegqDYHIKG 352
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKDpTQVVLVFGNRNEDDILYREELDELAEKHpGRLTVVYVVSRPEAG-----WTGGKG 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 169606282  353 RVDmDKVGKDALFADNDQTQYFICGPTQFMLDVQ 386
Cdd:pfam00175  76 RVQ-DALLEDHLSLPDEETHVYVCGPPGMIKAVR 108
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 186-400 2.49e-11

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: 63.35  E-value: 2.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 186 FKPGQYVSVNVRVEElDGGVWqaRQYSLSDASGKGYLRI-SVKKEMGEAregyvSNILHGKSEGDVVRVSH-PFGDFFFD 263
Cdd:cd06195   25 FQAGQFTKLGLPNDD-GKLVR--RAYSIASAPYEENLEFyIILVPDGPL-----TPRLFKLKPGDTIYVGKkPTGFLTLD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 264 REESGENgpVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGAR---DLnarAFKKDVDTLVAA-NRNIRAV-YFSSNP 338
Cdd:cd06195   97 EVPPGKR--LWLLATGTGIAPFLSMLRDLEIWERFDKIVLVHGVRyaeEL---AYQDEIEALAKQyNGKFRYVpIVSREK 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169606282 339 KEGEVEG--QDYHIKGRVDmDKVGkdaLFADNDQTQYFICGPTQFMLDVQAKLKSYGVPAERIK 400
Cdd:cd06195  172 ENGALTGriPDLIESGELE-EHAG---LPLDPETSHVMLCGNPQMIDDTQELLKEKGFSKNHRR 231
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 182-308 1.10e-09

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 59.50  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 182 EVPVFKPGQYVSVnvrveELDGGvwQARQYSLSDASGKG-YLRISVKKEMGEAREGYVSNILhgkSEGDVVRVSHPFGDF 260
Cdd:PRK07609 128 ERLQYLAGQYIEF-----ILKDG--KRRSYSIANAPHSGgPLELHIRHMPGGVFTDHVFGAL---KERDILRIEGPLGTF 197

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 169606282 261 FFdREESgeNGPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGAR 308
Cdd:PRK07609 198 FL-REDS--DKPIVLLASGTGFAPIKSIVEHLRAKGIQRPVTLYWGAR 242
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 186-402 3.12e-08

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: 53.78  E-value: 3.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 186 FKPGQYVSVnvrveELDGGVW--QARQYSLSDASGKGYLRISVKkemGEAREGYVSNILHGKSEGDVVRVSHPFGDFFFD 263
Cdd:cd06196   28 FTPGQATEV-----AIDKPGWrdEKRPFTFTSLPEDDVLEFVIK---SYPDHDGVTEQLGRLQPGDTLLIEDPWGAIEYK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 264 reesgenGPVVLISAGVGLTCLTSILNGLAAEQgsrpvswihgardlnarafKKDVDTLVAANRN----IRAVYFSSNPK 339
Cdd:cd06196  100 -------GPGVFIAGGAGITPFIAILRDLAAKG-------------------KLEGNTLIFANKTekdiILKDELEKMLG 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169606282 340 EGEV-----EGQDYHIKGRVDMDKVGKdaLFADNDQtQYFICGPTQFMLDVQAKLKSYGVPAERIKME 402
Cdd:cd06196  154 LKFInvvtdEKDPGYAHGRIDKAFLKQ--HVTDFNQ-HFYVCGPPPMEEAINGALKELGVPEDSIVFE 218
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 186-406 1.21e-07

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 53.17  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 186 FKPGQY--VSVNVRVEELdggvwqaRQYSLSDASGKG-YLRISVKKEMGEAREGYVSNILhgkSEGDVVRVSHPFGDFFF 262
Cdd:PRK10684  37 YRAGQYalVSIRNSAETL-------RAYTLSSTPGVSeFITLTVRRIDDGVGSQWLTRDV---KRGDYLWLSDAMGEFTC 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 263 DREESGEngpVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGARDLNARAFKKDVDTLVAANRNIRAVYFSsnpkegE 342
Cdd:PRK10684 107 DDKAEDK---YLLLAAGCGVTPIMSMRRWLLKNRPQADVQVIFNVRTPQDVIFADEWRQLKQRYPQLNLTLVA------E 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169606282 343 VEGQDYHIKGRVDMDKVGKDAlfadNDQTQY--FICGPTQFMLDVQAKLKSYGVPAERIKMELFGT 406
Cdd:PRK10684 178 NNATEGFIAGRLTRELLQQAV----PDLASRtvMTCGPAPYMDWVEQEVKALGVTADRFFKEKFFT 239
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 174-377 1.59e-07

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


Pssm-ID: 99798 [Multi-domain]  Cd Length: 289  Bit Score: 52.33  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 174 LKPKEAGVEVPVFKPGQYVSVnvrveeLDGGVWQARQYSLSDASGKGYLRISVKKEMGeareGYVSNILHGKSEGDVVRV 253
Cdd:cd06201   72 AKRKLSGKGLPSFEAGDLLGI------LPPGSDVPRFYSLASSSSDGFLEICVRKHPG----GLCSGYLHGLKPGDTIKA 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 254 S---HPfgDFFFDREESgengPVVLISAGVGLTCLTSILNGLAAEqgsRPVSWIHGARDLNARA-FKKDVDTLVAANRnI 329
Cdd:cd06201  142 FirpNP--SFRPAKGAA----PVILIGAGTGIAPLAGFIRANAAR---RPMHLYWGGRDPASDFlYEDELDQYLADGR-L 211

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 169606282 330 RAVY--FSSNPKEGEVegQDyhiKGRVDMDKVGKDAlfadNDQTQYFICG 377
Cdd:cd06201  212 TQLHtaFSRTPDGAYV--QD---RLRADAERLRRLI----EDGAQIMVCG 252
Mb-like_oxidoreductase cd19753
Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This ...
 12-135 1.60e-07

Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This subfamily is composed of uncharacterized proteins containing an N-terminal myoglobin-like (M family globin) domain and a C-terminal oxygenase reductase FAD/NADH binding domain belonging to the ferredoxin reductase (FNR) family and is usually part of multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. The domain architecture of this subfamily is similar to flavohemoglobins, which function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses.


Pssm-ID: 381293 [Multi-domain]  Cd Length: 121  Bit Score: 49.55  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  12 IKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVF--NTTHQ------ATGHqsralagalyaYAANIDNLGALSPALELI 83
Cdd:cd19753    1 LRASLAAVEDGPDELARRFYARLFAEAPELRDLFpaDMDAQrdrlarALTH-----------VVENLDDPDGLVPFLAQL 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 169606282  84 CHKHVSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLADIM 135
Cdd:cd19753   70 GRDHRKYGVAPEHYPAVGAALLAALRHFAGEAWTPELEAAWAEAYTLIAGVM 121
Globin pfam00042
Globin;
28-135 2.62e-07

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 48.82  E-value: 2.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   28 AKFYTDLLTANPSLKNVFNTTHQATG---------HQSRALAGALYAYAANIDNLGALSPALELICHKHV-SLFIQPAQY 97
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRFEKSADdlkgspkfkAHGKKVLAALGEAVKHLDDLAALNAALKKLGARHKeKRGVDPANF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 169606282   98 AIVGEFLLATMKTVLGaAATGEVLDAWGAAYWQLADIM 135
Cdd:pfam00042  81 KLFGEALLVVLAEHLG-EFTPETKAAWDKALDVIAAAL 117
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 186-397 4.17e-07

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: 50.71  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 186 FKPGQYVSVNVR-VEELdggvwqarQYSLSDASGKgyLRISVKKeMGEAREGyvsniLHGKSEGDVVRVSHPFGDFFfdr 264
Cdd:cd06220   24 FKPGQFVMVWVPgVDEI--------PMSLSYIDGP--NSITVKK-VGEATSA-----LHDLKEGDKLGIRGPYGNGF--- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 265 eeSGENGPVVLISAGVGLTCLTSIlnglaaeqgsrpvswihgARDLNARAfkkDVDTLVAANRNIRAVYFSSNPKEGEV- 343
Cdd:cd06220   85 --ELVGGKVLLIGGGIGIAPLAPL------------------AERLKKAA---DVTVLLGARTKEELLFLDRLRKSDELi 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 344 ---EGQDYHIKGRVDmdkvgkdALFADNDQTQY---FICGPTQFMLDVQAKLKSYGVPAE 397
Cdd:cd06220  142 vttDDGSYGFKGFVT-------DLLKELDLEEYdaiYVCGPEIMMYKVLEILDERGVRAQ 194
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 176-404 4.57e-07

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: 50.42  E-value: 4.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 176 PKEAGVEVPvFKPGQYVSVNVRveelDGGVWqaRQYSLSDASG-KGYLRISVKKEMGeareGYVSNIL-HGKSEGDVVRV 253
Cdd:cd06210   26 AEGAGIAAE-FVPGQFVEIEIP----GTDTR--RSYSLANTPNwDGRLEFLIRLLPG----GAFSTYLeTRAKVGQRLNL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 254 SHPFGDFFFdREESGenGPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHGARDLNARAFKKDVDTLVAANRNIRAVY 333
Cdd:cd06210   95 RGPLGAFGL-RENGL--RPRWFVAGGTGLAPLLSMLRRMAEWGEPQEARLFFGVNTEAELFYLDELKRLADSLPNLTVRI 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169606282 334 FSSNPkEGEVEGQdyhiKGRVdmdkvgKDALFADNDQTQ----YFICGPTQFMLDVQAKLKSYGVPAERIKMELF 404
Cdd:cd06210  172 CVWRP-GGEWEGY----RGTV------VDALREDLASSDakpdIYLCGPPGMVDAAFAAAREAGVPDEQVYLEKF 235
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 156-402 6.59e-06

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 47.17  E-value: 6.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 156 TIVRKVAESGSgeICSFYLKpkeaGVEVPVFKPGQYVSVNVR-VEELDGgvwqaRQYSLSDAsGKGYLRISVKKEmGEAr 234
Cdd:PRK00054   8 KIVENKEIAPN--IYTLVLD----GEKVFDMKPGQFVMVWVPgVEPLLE-----RPISISDI-DKNEITILYRKV-GEG- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 235 egyvSNILHGKSEGDVVRVSHPFGDfFFDREESGENgpVVLISAGVGLTCLTSIlnglaAEQgsrpvswihgardlnARA 314
Cdd:PRK00054  74 ----TKKLSKLKEGDELDIRGPLGN-GFDLEEIGGK--VLLVGGGIGVAPLYEL-----AKE---------------LKK 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 315 FKKDVDTLVAAnRNIRAVYFSSNPKE-GEV----EGQDYHIKGRV--DMDKVGK--DALFAdndqtqyfiCGPTQFMLDV 385
Cdd:PRK00054 127 KGVEVTTVLGA-RTKDEVIFEEEFAKvGDVyvttDDGSYGFKGFVtdVLDELDSeyDAIYS---------CGPEIMMKKV 196

                        250
                 ....*....|....*..
gi 169606282 386 QAKLKSYGVPAErIKME 402
Cdd:PRK00054 197 VEILKEKKVPAY-VSLE 212
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 159-402 1.98e-05

NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. 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: 45.79  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 159 RKVAESGSGEICsFYLKPKEAGVEVPVFKPGQYVsvnvrveeldgGVW-----QARQYSLS----DASGKGYL---RISV 226
Cdd:cd06182    6 RKLTPPDSPRST-RHLEFDLSGNSVLKYQPGDHL-----------GVIppnplQPRYYSIAsspdVDPGEVHLcvrVVSY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 227 KKEMGEAREGYVSNILHGKSEGDVVRVSHPFGDFFfdREESGENGPVVLISAGVGLTCLTSILNGLAAEQ---------- 296
Cdd:cd06182   74 EAPAGRIRKGVCSNFLAGLQLGAKVTVFIRPAPSF--RLPKDPTTPIIMVGPGTGIAPFRGFLQERAALRangkargpaw 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 297 ---GSRpvswiHGARDLnarAFKKDVDTLVAANRNIRAVY-FSSNPKEGEVEGQDyhikgrvdmdKVGKDALF---ADND 369
Cdd:cd06182  152 lffGCR-----NFASDY---LYREELQEALKDGALTRLDVaFSREQAEPKVYVQD----------KLKEHAEElrrLLNE 213

                        250       260       270
                 ....*....|....*....|....*....|....
gi 169606282 370 QTQYFICGPTQFML-DVQAKLksYGVPAERIKME 402
Cdd:cd06182  214 GAHIYVCGDAKSMAkDVEDAL--VKIIAKAGGVD 245
fre PRK08051
FMN reductase; Validated
 173-362 6.93e-05

FMN reductase; Validated


Pssm-ID: 236142 [Multi-domain]  Cd Length: 232  Bit Score: 44.07  E-value: 6.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 173 YLKPkeagvEVPV-FKPGQYVsvNVRVEELDggvwqARQYSL-SDASGKGY--LRISvkkemGEAREGYVSNILHGKSEG 248
Cdd:PRK08051  21 RLVP-----EAPFsFRAGQYL--MVVMGEKD-----KRPFSIaSTPREKGFieLHIG-----ASELNLYAMAVMERILKD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 249 DVVRVSHPFGDFFFdREESgeNGPVVLISAGVGLTCLTSILNGLAAEQGSRPVS--WihGARDLNARAFKKDVDTLVAAN 326
Cdd:PRK08051  84 GEIEVDIPHGDAWL-REES--ERPLLLIAGGTGFSYARSILLTALAQGPNRPITlyW--GGREEDHLYDLDELEALALKH 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169606282 327 RNIRA---VYFSSNP---KEGEV-----------EGQDYHIKGRVDMDKVGKD 362
Cdd:PRK08051 159 PNLHFvpvVEQPEEGwqgKTGTVltavmqdfgslAEYDIYIAGRFEMAKIARE 211
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
154-262 7.22e-05

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 41.41  E-value: 7.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282  154 DFTIVRKVAESGSGEICSFYLKPKEAGVEVPvfkPGQYVSVNVRVEelDGGVWqaRQYS-LSDASGKGYLRISVKKEMGe 232
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLP---VGQHLFLRLPID--GELVI--RSYTpISSDDDKGYLELLVKVYPG- 72

                          90       100       110
                  ....*....|....*....|....*....|
gi 169606282  233 areGYVSNILHGKSEGDVVRVSHPFGDFFF 262
Cdd:pfam00970  73 ---GKMSQYLDELKIGDTIDFKGPLGRFEY 99
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
186-310 4.23e-04

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 42.04  E-value: 4.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 186 FKPGQYVSVNVRveelDGGVWqaRQYSLSDASGKG-YLRISVKKEMGeareGYVSNILHGKSE-GDVVRVSHPFGDFFFD 263
Cdd:PRK11872 137 FLPGQYARLQIP----GTDDW--RSYSFANRPNATnQLQFLIRLLPD----GVMSNYLRERCQvGDEILFEAPLGAFYLR 206

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 169606282 264 REESgengPVVLISAGVGLTCLTSILNGLAAEQGSRPVSWIHG---ARDL 310
Cdd:PRK11872 207 EVER----PLVFVAGGTGLSAFLGMLDELAEQGCSPPVHLYYGvrhAADL 252
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 159-391 8.44e-04

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: 40.77  E-value: 8.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 159 RKVAESGSGEICSF---------YLKPKEAGVeVPvfkPGqyvsvnvrVEELDGGVWQARQYSLS-----DASGKGYLRI 224
Cdd:cd06208   18 RLTGPDAPGEVCHIvidhggklpYLEGQSIGI-IP---PG--------TDAKNGKPHKLRLYSIAssrygDDGDGKTLSL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 225 SVKK------EMGEAREGYVSNILHGKSEGDVVRVSHPFGDFFFDREEsgENGPVVLISAGVGLTCLTSILNGL----AA 294
Cdd:cd06208   86 CVKRlvytdpETDETKKGVCSNYLCDLKPGDDVQITGPVGKTMLLPED--PNATLIMIATGTGIAPFRSFLRRLfrekHA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282 295 EQGSRPVSW-IHGARDLNARAFKKDVDTLVAAN-RNIRAVY-FSSNPKEGevEGQDYHIKgrvdmDKVG--KDALFA--D 367
Cdd:cd06208  164 DYKFTGLAWlFFGVPNSDSLLYDDELEKYPKQYpDNFRIDYaFSREQKNA--DGGKMYVQ-----DRIAeyAEEIWNllD 236

                        250       260
                 ....*....|....*....|....
gi 169606282 368 NDQTQYFICGPTQFMLDVQAKLKS 391
Cdd:cd06208  237 KDNTHVYICGLKGMEPGVDDALTS 260
class1-2_nsHbs_Lbs cd08923
Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related ...
 4-139 8.44e-04

Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related proteins; Class1 nsHbs include the dimeric hexacoordinate Trema tomentosa nsHb and the dimeric hexacoordinate nsHb from monocot barley. Also belonging to this family is ParaHb, a dimeric pentacoordinate Hb from the root nodules of Parasponia andersonii, a non-legume capable of symbiotic nitrogen fixation. ParaHb is unusual in that it has different heme redox potentials for each subunit; it may have evolved from class1 nsHbs. Lbs are pentacoordinate, and facilitate the diffusion of O2 to the respiring Rhizobium bacteroids within root nodules. They may have evolved from class 2 nonsymbiotic hemoglobins (class2 nsHb).


Pssm-ID: 381261  Cd Length: 147  Bit Score: 39.40  E-value: 8.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169606282   4 LSPSQVQIIKSTVPVLAQHGEAITAKFYTDLLTANPSLKNVFN---------------TTHQA--------TGHQSRaLA 60
Cdd:cd08923    1 FTEKQEALVKSSWEVLKKNIPQLSLRFFLLILEIAPAAKDMFSflkdsdeipennpklKAHAMkvfkmtceSAIQLR-KK 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169606282  61 GALYAYAANIDNLGALspalelichkHVSLFIQPAQYAIVGEFLLATMKTVLGAAATGEVLDAWGAAYWQLAdIMIAKE 139
Cdd:cd08923   80 GKVVVADTTLKRLGSV----------HLKKGVADPHFEVVKEALLKTIKEAVGDKWSEEMKCAWGEAYDQLA-AAIKKE 147
 
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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