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Conserved domains on  [gi|16130477|ref|NP_417047|]
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nitric oxide dioxygenase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

NO-inducible flavohemoprotein( domain architecture ID 11486532)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13289 PRK13289
NO-inducible flavohemoprotein;
1-396 0e+00

NO-inducible flavohemoprotein;


:

Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 759.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477    1 MLDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRNGDQREALFNAIAAYASNIENLPALLPAVEK 80
Cdd:PRK13289   1 MLSAQTIAIVKATVPLLEEHGEALTAHFYDRMFSHNPELKNIFNQSNQRNGDQPEALANAVLAYARNIDNLEALLPAVER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   81 IAQKHTSFQIKPEQYNIVGEHLLATLDEMFS--PGQEVLDAWGKAYGVLANVFINREAEIYNENASKAGGWEGTRDFRIV 158
Cdd:PRK13289  81 IAQKHVSLQIKPEHYPIVGEHLLAAIREVLGdaATDEVLDAWGEAYGVLADVFIGREAEIYEEAASKPGGWRGWRDFRVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  159 AKTPRSALITSFELEPVDGGAVAEYRPGQYLGVWLKPEGFPHQEIRQYSLTRKPDGKGYRIAVKREEGGQVSNWLHNHAN 238
Cdd:PRK13289 161 KKVPESEVITSFYLEPVDGGPVADFKPGQYLGVRLDPEGEEYQEIRQYSLSDAPNGKYYRISVKREAGGKVSNYLHDHVN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  239 VGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKELGQSLPRF 318
Cdd:PRK13289 241 VGDVLELAAPAGDFFLDVASDTPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIHAARNGGVHAFRDEVEALAARHPNL 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130477  319 TAHTWYRQPSEADRAKGQFDSEGLMDLSKLEGAFSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIHYECFGPHKVL 396
Cdd:PRK13289 321 KAHTWYREPTEQDRAGEDFDSEGLMDLEWLEAWLPDPDADFYFCGPVPFMQFVAKQLLELGVPEERIHYEFFGPAKVL 398
 
Name Accession Description Interval E-value
PRK13289 PRK13289
NO-inducible flavohemoprotein;
1-396 0e+00

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 759.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477    1 MLDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRNGDQREALFNAIAAYASNIENLPALLPAVEK 80
Cdd:PRK13289   1 MLSAQTIAIVKATVPLLEEHGEALTAHFYDRMFSHNPELKNIFNQSNQRNGDQPEALANAVLAYARNIDNLEALLPAVER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   81 IAQKHTSFQIKPEQYNIVGEHLLATLDEMFS--PGQEVLDAWGKAYGVLANVFINREAEIYNENASKAGGWEGTRDFRIV 158
Cdd:PRK13289  81 IAQKHVSLQIKPEHYPIVGEHLLAAIREVLGdaATDEVLDAWGEAYGVLADVFIGREAEIYEEAASKPGGWRGWRDFRVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  159 AKTPRSALITSFELEPVDGGAVAEYRPGQYLGVWLKPEGFPHQEIRQYSLTRKPDGKGYRIAVKREEGGQVSNWLHNHAN 238
Cdd:PRK13289 161 KKVPESEVITSFYLEPVDGGPVADFKPGQYLGVRLDPEGEEYQEIRQYSLSDAPNGKYYRISVKREAGGKVSNYLHDHVN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  239 VGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKELGQSLPRF 318
Cdd:PRK13289 241 VGDVLELAAPAGDFFLDVASDTPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIHAARNGGVHAFRDEVEALAARHPNL 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130477  319 TAHTWYRQPSEADRAKGQFDSEGLMDLSKLEGAFSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIHYECFGPHKVL 396
Cdd:PRK13289 321 KAHTWYREPTEQDRAGEDFDSEGLMDLEWLEAWLPDPDADFYFCGPVPFMQFVAKQLLELGVPEERIHYEFFGPAKVL 398
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
147-393 2.71e-132

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: 379.21  E-value: 2.71e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 147 GGWEGTRDFRIVAKTPRSALITSFELEPVDGGAVAEYRPGQYLGVWLKPEGFPHQEIRQYSLTRKPDGKGYRIAVKREEG 226
Cdd:cd06184   1 GGWRGFRPFVVARKVAESEDITSFYLEPADGGPLPPFLPGQYLSVRVKLPGLGYRQIRQYSLSDAPNGDYYRISVKREPG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 227 GQVSNWLHNHANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFAD 306
Cdd:cd06184  81 GLVSNYLHDNVKVGDVLEVSAPAGDFVLDEASDRPLVLISAGVGITPMLSMLEALAAEGPGRPVTFIHAARNSAVHAFRD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 307 EVKELGQSLPRFTAHTWYRQPSEADRAkGQFDSEGLMDLSKLEGAFSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIH 386
Cdd:cd06184 161 ELEELAARLPNLKLHVFYSEPEAGDRE-EDYDHAGRIDLALLRELLLPADADFYLCGPVPFMQAVREGLKALGVPAERIH 239

                ....*..
gi 16130477 387 YECFGPH 393
Cdd:cd06184 240 YEVFGPG 246
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
150-388 6.72e-85

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 257.80  E-value: 6.72e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 150 EGTRDFRIVAKTPRSALITSFELEPVDGGAVAEYRPGQYLGVWLKPEGFPHqeIRQYSLTRKPDGKGYRIAVKREEGGQV 229
Cdd:COG1018   1 AGFRPLRVVEVRRETPDVVSFTLEPPDGAPLPRFRPGQFVTLRLPIDGKPL--RRAYSLSSAPGDGRLEITVKRVPGGGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 230 SNWLHNHANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVK 309
Cdd:COG1018  79 SNWLHDHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGARSPADLAFRDELE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 310 ELGQSLPRFTAHTWYRQPSEADRakgqfdseGLMDLSKLEGAFSDPT-MQFYLCGPVGFMQFTAKQLVDLGVKQENIHYE 388
Cdd:COG1018 159 ALAARHPRLRLHPVLSREPAGLQ--------GRLDAELLAALLPDPAdAHVYLCGPPPMMEAVRAALAELGVPEERIHFE 230
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
264-373 3.28e-24

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: 95.79  E-value: 3.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   264 LISAGVGQTPMLAMLDTLAK-AGHTAQVNWFHAAENGDVHAFADEVKELGQSLPRftAHTWYRQPSEADraKGQFDSEGL 342
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEdPKDPTQVVLVFGNRNEDDILYREELDELAEKHPG--RLTVVYVVSRPE--AGWTGGKGR 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 16130477   343 MDLSKLEGAFS--DPTMQFYLCGPVGFMQFTAK 373
Cdd:pfam00175  77 VQDALLEDHLSlpDEETHVYVCGPPGMIKAVRK 109
 
Name Accession Description Interval E-value
PRK13289 PRK13289
NO-inducible flavohemoprotein;
1-396 0e+00

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 759.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477    1 MLDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRNGDQREALFNAIAAYASNIENLPALLPAVEK 80
Cdd:PRK13289   1 MLSAQTIAIVKATVPLLEEHGEALTAHFYDRMFSHNPELKNIFNQSNQRNGDQPEALANAVLAYARNIDNLEALLPAVER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   81 IAQKHTSFQIKPEQYNIVGEHLLATLDEMFS--PGQEVLDAWGKAYGVLANVFINREAEIYNENASKAGGWEGTRDFRIV 158
Cdd:PRK13289  81 IAQKHVSLQIKPEHYPIVGEHLLAAIREVLGdaATDEVLDAWGEAYGVLADVFIGREAEIYEEAASKPGGWRGWRDFRVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  159 AKTPRSALITSFELEPVDGGAVAEYRPGQYLGVWLKPEGFPHQEIRQYSLTRKPDGKGYRIAVKREEGGQVSNWLHNHAN 238
Cdd:PRK13289 161 KKVPESEVITSFYLEPVDGGPVADFKPGQYLGVRLDPEGEEYQEIRQYSLSDAPNGKYYRISVKREAGGKVSNYLHDHVN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  239 VGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKELGQSLPRF 318
Cdd:PRK13289 241 VGDVLELAAPAGDFFLDVASDTPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIHAARNGGVHAFRDEVEALAARHPNL 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130477  319 TAHTWYRQPSEADRAKGQFDSEGLMDLSKLEGAFSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIHYECFGPHKVL 396
Cdd:PRK13289 321 KAHTWYREPTEQDRAGEDFDSEGLMDLEWLEAWLPDPDADFYFCGPVPFMQFVAKQLLELGVPEERIHYEFFGPAKVL 398
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
147-393 2.71e-132

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: 379.21  E-value: 2.71e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 147 GGWEGTRDFRIVAKTPRSALITSFELEPVDGGAVAEYRPGQYLGVWLKPEGFPHQEIRQYSLTRKPDGKGYRIAVKREEG 226
Cdd:cd06184   1 GGWRGFRPFVVARKVAESEDITSFYLEPADGGPLPPFLPGQYLSVRVKLPGLGYRQIRQYSLSDAPNGDYYRISVKREPG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 227 GQVSNWLHNHANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFAD 306
Cdd:cd06184  81 GLVSNYLHDNVKVGDVLEVSAPAGDFVLDEASDRPLVLISAGVGITPMLSMLEALAAEGPGRPVTFIHAARNSAVHAFRD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 307 EVKELGQSLPRFTAHTWYRQPSEADRAkGQFDSEGLMDLSKLEGAFSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIH 386
Cdd:cd06184 161 ELEELAARLPNLKLHVFYSEPEAGDRE-EDYDHAGRIDLALLRELLLPADADFYLCGPVPFMQAVREGLKALGVPAERIH 239

                ....*..
gi 16130477 387 YECFGPH 393
Cdd:cd06184 240 YEVFGPG 246
HmpEc-globin-like cd14776
Globin domain of Escherichia coli flavohemoglobin (Hmp) and related proteins; Flavohemoglobins ...
2-139 5.72e-88

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: 262.40  E-value: 5.72e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   2 LDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRNGDQREALFNAIAAYASNIENLPALLPAVEKI 81
Cdd:cd14776   1 LSAETIRIVKATIPLLAAAGPALTQHFYQRMLTHNPELKNIFNLAHQRTGRQPKALFDAVAAYAQNIRNLQALLPAVERI 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16130477  82 AQKHTSFQIKPEQYNIVGEHLLATLDEMFSPGQEVLDAWGKAYGVLANVFINREAEIY 139
Cdd:cd14776  81 AQKHTSFNIQPEQYQIVGEHLLATIEELAPPDKDVLAAWAKAYQFLADIFIDREGEIY 138
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
150-388 6.72e-85

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 257.80  E-value: 6.72e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 150 EGTRDFRIVAKTPRSALITSFELEPVDGGAVAEYRPGQYLGVWLKPEGFPHqeIRQYSLTRKPDGKGYRIAVKREEGGQV 229
Cdd:COG1018   1 AGFRPLRVVEVRRETPDVVSFTLEPPDGAPLPRFRPGQFVTLRLPIDGKPL--RRAYSLSSAPGDGRLEITVKRVPGGGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 230 SNWLHNHANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVK 309
Cdd:COG1018  79 SNWLHDHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLARGPFRPVTLVYGARSPADLAFRDELE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 310 ELGQSLPRFTAHTWYRQPSEADRakgqfdseGLMDLSKLEGAFSDPT-MQFYLCGPVGFMQFTAKQLVDLGVKQENIHYE 388
Cdd:COG1018 159 ALAARHPRLRLHPVLSREPAGLQ--------GRLDAELLAALLPDPAdAHVYLCGPPPMMEAVRAALAELGVPEERIHFE 230
FHb-globin cd08922
Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide ...
2-139 9.28e-74

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: 226.30  E-value: 9.28e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   2 LDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRNGDQREALFNAIAAYASNIENLPALLPAVEKI 81
Cdd:cd08922   1 LSEETIAIVKATAPVLAEHGEEITTRFYKRMFAEHPELKNLFNMANQASGRQPKALAAAVLAYAANIDNLEVLLPAVERI 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  82 AQKHTSFQIKPEQYNIVGEHLLATLDEMFSP--GQEVLDAWGKAYGVLANVFINREAEIY 139
Cdd:cd08922  81 AHKHVSLGVKPEHYPIVGEYLLEAIKEVLGDaaTPEVLDAWAEAYGFLADILIEREKQLY 140
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
2-137 2.52e-62

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 196.53  E-value: 2.52e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   2 LDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNqrnGDQREALFNAIAAYASNIENLPALLPAVEKI 81
Cdd:COG1017   1 LSPETIALVKASFPLVAPHGEEITARFYERLFELHPELRPLFNGDM---GEQRKALAAALAAYARNLDNLEALLPALERL 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16130477  82 AQKHTSFQIKPEQYNIVGEHLLATLDEMFSPG--QEVLDAWGKAYGVLANVFINREAE 137
Cdd:COG1017  78 GRKHVSYGVKPEHYPIVGEALLAALREVLGDAwtPEVAAAWAEAYGLLADVMIAAEAE 135
FHP_Ae-globin-like cd14779
Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins; ...
2-139 9.65e-60

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: 190.34  E-value: 9.65e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   2 LDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRNGDQREALFNAIAAYASNIENLPALLPAVEKI 81
Cdd:cd14779   1 LTEQQKDLVKATVPVLKEHGVALTKHFYQRMFEHNPELKNVFNMGHQESGKQQQALAMAVLAYAENIDDPEVLLPVLKLI 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  82 AQKHTSFQIKPEQYNIVGEHLLATLDEMFS--PGQEVLDAWGKAYGVLANVFINREAEIY 139
Cdd:cd14779  81 AHKHVSLGIRAEQYPIVGEHLLASIKEVLGdaATDELISAWAAAYGQLADILIGMESKLY 140
Yhb1-globin-like cd14777
Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains; ...
2-139 8.76e-57

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: 182.54  E-value: 8.76e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   2 LDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRNGDQREALFNAIAAYASNIENLPALLPAVEKI 81
Cdd:cd14777   1 LSEKTIQIVKSTVPVLKEKGTEITKRFYKRMFEEHPELLNIFNQTNQKKGLQQTALANTVYAAAKHIDNLEVILPVVKQI 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  82 AQKHTSFQIKPEQYNIVGEHLLATLDEMF--SPGQEVLDAWGKAYGVLANVFINREAEIY 139
Cdd:cd14777  81 AHKHRALGVKPEHYPIVGENLLAAIKEVLgdAATDEILEAWEKAYGVIADVFIEVEKEMY 140
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
158-388 1.72e-56

Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99778 [Multi-domain]  Cd Length: 223  Bit Score: 184.96  E-value: 1.72e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 158 VAKTPRSALITSFELEPVDGgavAEYRPGQYLGVWLKPEGFPhqEIRQYSLTRKPDGKGY-RIAVKREEGGQVSNWLHNH 236
Cdd:cd00322   1 VATEDVTDDVRLFRLQLPNG---FSFKPGQYVDLHLPGDGRG--LRRAYSIASSPDEEGElELTVKIVPGGPFSAWLHDL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 237 AnVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKELGQSLP 316
Cdd:cd00322  76 K-PGDEVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGARTPADLLFLDELEELAKEGP 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130477 317 RFTAHTWYRQPSEADRAKGQFDSEGLMDLSKLegaFSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIHYE 388
Cdd:cd00322 155 NFRLVLALSRESEAKLGPGGRIDREAEILALL---PDDSGALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
FHb-globin_3 cd14783
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
2-139 3.84e-56

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: 181.12  E-value: 3.84e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   2 LDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRNGDQREALFNAIAAYASNIENLPALLPAVEKI 81
Cdd:cd14783   1 LSQKTIDIVKSTAPILEENGETLTRHFYKRMFEHNPEVKPFFNPAHQHSGSQQRALAAAICAYAANIDNLEVLGNAVELI 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  82 AQKHTSFQIKPEQYNIVGEHLLATLDEMFSPG--QEVLDAWGKAYGVLANVFINREAEIY 139
Cdd:cd14783  81 AQKHASLGIKPEHYPIVGSNLLASIREVLGDAatDDIIEAWSEAYGFLADILIGREKQIY 140
VtHb-like_SDgb cd14778
Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is ...
2-139 1.21e-49

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: 164.14  E-value: 1.21e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   2 LDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRNGDQREALFNAIAAYASNIENLPALLPAVEKI 81
Cdd:cd14778   1 LDQQTIEIIKSTVPVLKEHGVEITTEFYKNMFTEYPEVRPMFDMEKQKSGEQPKALAMTVLAAAQNIENLEKIRPAVEKI 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  82 AQKHTSFQIKPEQYNIVGEHLLATLDEMF--SPGQEVLDAWGKAYGVLANVFINREAEIY 139
Cdd:cd14778  81 GKTHVNLNVKPEHYPIVGACLLGAIKEVLgdTATDEILEAWEKAYGEIAKIFIDVEKKLY 140
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
156-390 4.10e-49

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: 166.25  E-value: 4.10e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 156 RIVAKTPRSALITSFELEPvdGGAVAEYRPGQYLGVWLKPEGFPHQeiRQYSLTRKPDGKG--YRIAVKREEGGQVSNWL 233
Cdd:cd06216  21 RVVAVRPETADMVTLTLRP--NRGWPGHRAGQHVRLGVEIDGVRHW--RSYSLSSSPTQEDgtITLTVKAQPDGLVSNWL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 234 HNHANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKELGQ 313
Cdd:cd06216  97 VNHLAPGDVVELSQPQGDFVLPDPLPPRLLLIAAGSGITPVMSMLRTLLARGPTADVVLLYYARTREDVIFADELRALAA 176
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130477 314 SLPRFTAHTWYRQpseaDRAKGQFDSEglmDLSKLEGAFSDptMQFYLCGPVGFMQFTAKQLVDLGVkQENIHYECF 390
Cdd:cd06216 177 QHPNLRLHLLYTR----EELDGRLSAA---HLDAVVPDLAD--RQVYACGPPGFLDAAEELLEAAGL-ADRLHTERF 243
HmpPa-globin-like cd14780
Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins; ...
2-139 3.21e-46

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: 155.31  E-value: 3.21e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   2 LDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRNGDQREALFNAIAAYASNIENLPALLPAVEKI 81
Cdd:cd14780   1 LSPHQIAIIKATVPALEAHGEAITTHFYPLMFEEYPEVRALFNQAHQASGAQPRALANAVLAYARHIDRLEVLGGAVSLI 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  82 AQKHTSFQIKPEQYNIVGEHLLATLDEMFSPG--QEVLDAWGKAYGVLANVFINREAEIY 139
Cdd:cd14780  81 VNKHVSLNILPEHYPIVGTCLLRAIREVLGDAatDEVIEAWGAAYQQLADLLIAAEEAVY 140
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
149-390 1.24e-45

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: 156.98  E-value: 1.24e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 149 WEGTRDFRivaktprsalitSFELEPVDGgAVAEYRPGQYLGVWLKPEGFPHQeiRQYSLTRKP-DGKGYRIAVKREEGG 227
Cdd:cd06215   7 IQETPDVK------------TFRFAAPDG-SLFAYKPGQFLTLELEIDGETVY--RAYTLSSSPsRPDSLSITVKRVPGG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 228 QVSNWLHNHANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADE 307
Cdd:cd06215  72 LVSNWLHDNLKVGDELWASGPAGEFTLIDHPADKLLLLSAGSGITPMMSMARWLLDTRPDADIVFIHSARSPADIIFADE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 308 VKELGQSLPRFTAHTWYRQPSEaDRAKGQfdsEGLMDLSKLEGAFSD-PTMQFYLCGPVGFMQFTAKQLVDLGVKQENIH 386
Cdd:cd06215 152 LEELARRHPNFRLHLILEQPAP-GAWGGY---RGRLNAELLALLVPDlKERTVFVCGPAGFMKAVKSLLAELGFPMSRFH 227

                ....
gi 16130477 387 YECF 390
Cdd:cd06215 228 QESF 231
FHb-globin_1 cd14781
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
2-139 3.23e-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. This subfamily may contain some single-domain goblins (SDgbs).


Pssm-ID: 381289  Cd Length: 139  Bit Score: 152.63  E-value: 3.23e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   2 LDAQTIATVKATIPLLVETGPKLTAHFYDRMFThNPELKEIFNMSNQRNGDQREALFNAIAAYASNIENLPALLPAVEKI 81
Cdd:cd14781   1 LSPHTIAIVKATVPALEEHGVAITAAMYKRLFE-DPEIKALFNQAAQKSGEQPRALAGAILAYAKNIDNLGALGSAVERI 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  82 AQKHTSFQIKPEQYNIVGEHLLATLDEMF--SPGQEVLDAWGKAYGVLANVFINREAEIY 139
Cdd:cd14781  80 AQKHVGLHIKPEHYPHVATALLGAIKDVLgdAATDEVLEAWGEAYWFLADILINREKQLY 139
FHb_fungal-globin cd19754
Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide ...
3-139 1.29e-41

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: 143.25  E-value: 1.29e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   3 DAQtIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRNGDQREALFNAIAAYASNIENLPALLPAVEKIA 82
Cdd:cd19754   3 PAQ-IKIIKDSVPILESLGVKLTEKFYKYMLKRYPEVKPYFNETNQKLLRQPKILAFALLQYAKNIDDLTPLSGFVEQIV 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  83 QKHTSFQIKPEQYNIVGEHLLATLDEMFSPG---QEVLDAWGKAYGVLANVFINREAEIY 139
Cdd:cd19754  82 SKHVGLQVKPEHYPIVGECLIETMKELLPEAvatDEFIEAWTTAYGNLANILIDAEKKEY 141
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
149-390 2.27e-40

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: 143.18  E-value: 2.27e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 149 WEGTRDFRIVAKTPRsalITSFELEPVDGGaVAEYRPGQYLGVWLKPE-GFPHQeiRQYSLTRKPDGKG-YRIAVKREEG 226
Cdd:cd06217   1 WRVLRVTEIIQETPT---VKTFRLAVPDGV-PPPFLAGQHVDLRLTAIdGYTAQ--RSYSIASSPTQRGrVELTVKRVPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 227 GQVSNWLHNHANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAEN-GDVhAFA 305
Cdd:cd06217  75 GEVSPYLHDEVKVGDLLEVRGPIGTFTWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVPFRLLYSARTaEDV-IFR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 306 DEVKELGQSLPRFTAHTWYRQPSEADR--AKGQFDsegLMDLSKLEGafSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQE 383
Cdd:cd06217 154 DELEQLARRHPNLHVTEALTRAAPADWlgPAGRIT---ADLIAELVP--PLAGRRVYVCGPPAFVEAATRLLLELGVPRD 228

                ....*..
gi 16130477 384 NIHYECF 390
Cdd:cd06217 229 RIRTEAF 235
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
156-391 3.90e-39

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: 139.99  E-value: 3.90e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 156 RIVAKTPRSALITsFELEPVDGGAVAeYRPGQYLGVWLKPEGfphQEI-RQYSLTRKPDGKGYRIAVKREEGGQVSNWLH 234
Cdd:cd06214   8 EVVRETADAVSIT-FDVPEELRDAFR-YRPGQFLTLRVPIDG---EEVrRSYSICSSPGDDELRITVKRVPGGRFSNWAN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 235 NHANVGDVVKLVAPAGDFFMAV-ADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAaeNGDVHA--FADEVKEL 311
Cdd:cd06214  83 DELKAGDTLEVMPPAGRFTLPPlPGARHYVLFAAGSGITPVLSILKTALAREPASRVTLVYG--NRTEASviFREELADL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 312 G-QSLPRFTAHTWY-RQPSEADRAKGQFDSEGLMDLSKLEGAFSDPTmQFYLCGPVGFMQFTAKQLVDLGVKQENIHYEC 389
Cdd:cd06214 161 KaRYPDRLTVIHVLsREQGDPDLLRGRLDAAKLNALLKNLLDATEFD-EAFLCGPEPMMDAVEAALLELGVPAERIHREL 239

                ..
gi 16130477 390 FG 391
Cdd:cd06214 240 FT 241
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
156-391 9.83e-37

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: 132.61  E-value: 9.83e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 156 RIVAKTPRsalITSFELEPVDGGAVAEYRPGQYLGVWLkPEGFphqeIRQYSLTRKP-DGKGYRIAVKREE---GGqvSN 231
Cdd:cd06185   2 RIRDEAPD---IRSFELEAPDGAPLPAFEPGAHIDVHL-PNGL----VRQYSLCGDPaDRDRYRIAVLREPasrGG--SR 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 232 WLHNHANVGDVVKLVAPAGDFFMaVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDvhAFADEVKEL 311
Cdd:cd06185  72 YMHELLRVGDELEVSAPRNLFPL-DEAARRHLLIAGGIGITPILSMARALAARGADFELHYAGRSREDA--AFLDELAAL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 312 gqslprftahtwyrqpsEADRAKGQFDSEG-LMDLSKLEGAfSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIHYECF 390
Cdd:cd06185 149 -----------------PGDRVHLHFDDEGgRLDLAALLAA-PPAGTHVYVCGPEGMMDAVRAAAAALGWPEARLHFERF 210

                .
gi 16130477 391 G 391
Cdd:cd06185 211 A 211
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
175-390 2.06e-33

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: 124.56  E-value: 2.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 175 VDGGAVAEYRPGQYLGVWLKPEGFPHQeiRQYSLTRKPDGKGYRIAVKREEGGQVSNWLHNHANVGDVVKLVAPAGDFFM 254
Cdd:cd06191  20 VPGPLQYGFRPGQHVTLKLDFDGEELR--RCYSLCSSPAPDEISITVKRVPGGRVSNYLREHIQPGMTVEVMGPQGHFVY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 255 AVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKELGQSLPRF-TAHTWYRQPSEADRA 333
Cdd:cd06191  98 QPQPPGRYLLVAAGSGITPLMAMIRATLQTAPESDFTLIHSARTPADMIFAQELRELADKPQRLrLLCIFTRETLDSDLL 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16130477 334 KGQFDSEglMDLSKLeGAFSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIHYECF 390
Cdd:cd06191 178 HGRIDGE--QSLGAA-LIPDRLEREAFICGPAGMMDAVETALKELGMPPERIHTERF 231
FHb-globin_2 cd14782
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
2-139 5.84e-32

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: 117.88  E-value: 5.84e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   2 LDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHNPEL-KEIFNMSNQRNGDQREALFNAIAAYASNI--ENLPALLPAV 78
Cdd:cd14782   1 LSAESAEVIRATLPVVGEHIEEITPLFYRRMFGEHPELlRNLFNRGNQASGEQQKALAASVAAFATHLvdPDAPPPDSVL 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130477  79 EKIAQKHTSFQIKPEQYNIVGEHLLAT----LDEMFSPgqEVLDAWGKAYGVLANVFINREAEIY 139
Cdd:cd14782  81 SRIAHKHASLGITPEQYTIVHRHLFAAiaevLGAAVTP--EVAAAWDEVYWLMADQLIATEARLY 143
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
157-390 1.88e-28

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: 111.15  E-value: 1.88e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 157 IVAKTPRSALITSFELEPVDGgavAEYRPGQYLGVwlkpeGFPHQEI--RQYSLTRKPDGKGyRIA--VKREEGGQVSNW 232
Cdd:cd06187   1 VVSVERLTHDIAVVRLQLDQP---LPFWAGQYVNV-----TVPGRPRtwRAYSPANPPNEDG-EIEfhVRAVPGGRVSNA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 233 LHNHANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAEN-GDVHAfADEVKEL 311
Cdd:cd06187  72 LHDELKVGDRVRLSGPYGTFYLRRDHDRPVLCIAGGTGLAPLRAIVEDALRRGEPRPVHLFFGARTeRDLYD-LEGLLAL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 312 GQSLPRFTAH-TWYRQPSEADRAKGQFDSEGLMDLSKLEGAfsdptmQFYLCGPVGFMQFTAKQLVDLGVKQENIHYECF 390
Cdd:cd06187 151 AARHPWLRVVpVVSHEEGAWTGRRGLVTDVVGRDGPDWADH------DIYICGPPAMVDATVDALLARGAPPERIHFDKF 224
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
156-390 4.49e-26

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: 105.10  E-value: 4.49e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 156 RIVAKTPRsalITSFELEpVDGGAVAEYRPGQYLGVWLKP-EGFphqeiRQYSLTRKPDGKGY-RIAVKREEGGQVSNWL 233
Cdd:cd06211  13 EIEDLTPT---IKGVRLK-LDEPEEIEFQAGQYVNLQAPGyEGT-----RAFSIASSPSDAGEiELHIRLVPGGIATTYV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 234 HNHANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKELGQ 313
Cdd:cd06211  84 HKQLKEGDELEISGPYGDFFVRDSDQRPIIFIAGGSGLSSPRSMILDLLERGDTRKITLFFGARTRAELYYLDEFEALEK 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130477 314 SLPRFTAHTWYRQPSEADRAKGQ--FDSEGLMDLskLEGAFSDptMQFYLCGPVGFMQFTAKQLVDLGVKQENIHYECF 390
Cdd:cd06211 164 DHPNFKYVPALSREPPESNWKGFtgFVHDAAKKH--FKNDFRG--HKAYLCGPPPMIDACIKTLMQGRLFERDIYYEKF 238
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
170-390 6.19e-26

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: 104.21  E-value: 6.19e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 170 FELEpVDGGAVAEYRPGQYlgVWLKPEGFphQEIRQYSLTRKPDGKGYRIAVKREEGGQVSNWLHNHANVGDVVKLVAPA 249
Cdd:cd06209  19 LTLE-LDEAGALAFLPGQY--VNLQVPGT--DETRSYSFSSAPGDPRLEFLIRLLPGGAMSSYLRDRAQPGDRLTLTGPL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 250 GDFFMAvADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDvHAFA-DEVKELGQSLPRFTAHTWYRQPS 328
Cdd:cd06209  94 GSFYLR-EVKRPLLMLAGGTGLAPFLSMLDVLAEDGSAHPVHLVYGVTRDA-DLVElDRLEALAERLPGFSFRTVVADPD 171
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130477 329 EADRAKGqFDSEGLMDlskleGAFSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIHYECF 390
Cdd:cd06209 172 SWHPRKG-YVTDHLEA-----EDLNDGDVDVYLCGPPPMVDAVRSWLDEQGIEPANFYYEKF 227
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
264-373 3.28e-24

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: 95.79  E-value: 3.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   264 LISAGVGQTPMLAMLDTLAK-AGHTAQVNWFHAAENGDVHAFADEVKELGQSLPRftAHTWYRQPSEADraKGQFDSEGL 342
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEdPKDPTQVVLVFGNRNEDDILYREELDELAEKHPG--RLTVVYVVSRPE--AGWTGGKGR 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 16130477   343 MDLSKLEGAFS--DPTMQFYLCGPVGFMQFTAK 373
Cdd:pfam00175  77 VQDALLEDHLSlpDEETHVYVCGPPGMIKAVRK 109
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
156-388 2.05e-23

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 98.01  E-value: 2.05e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 156 RIVAKTPRSALITSFELEPVDGGAvaEYRPGQYLGVWLKPEGFPhqeiRQYSLTRKPDGKGY-RIAVKREegGQVSNWLH 234
Cdd:COG0543   1 KVVSVERLAPDVYLLRLEAPLIAL--KFKPGQFVMLRVPGDGLR----RPFSIASAPREDGTiELHIRVV--GKGTRALA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 235 nHANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHtaQVNWFHAAENGDVHAFADEVKELGQs 314
Cdd:COG0543  73 -ELKPGDELDVRGPLGNGFPLEDSGRPVLLVAGGTGLAPLRSLAEALLARGR--RVTLYLGARTPEDLYLLDELEALAD- 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130477 315 lprFTAHTwyrqpSEADRAKGQ--FDSEGLMDLSKLEGAFsdptmQFYLCGPVGFMQFTAKQLVDLGVKQENIHYE 388
Cdd:COG0543 149 ---FRVVV-----TTDDGWYGRkgFVTDALKELLAEDSGD-----DVYACGPPPMMKAVAELLLERGVPPERIYVS 211
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
6-133 6.93e-23

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: 93.00  E-value: 6.93e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   6 TIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRngDQREALFNAIAAYASNIENLPALLPAVEKIAQKH 85
Cdd:cd12131   1 QIELVQQSFAKVEPIADEAAALFYERLFELDPELKPLFKGTDME--EQGRKLMAMLVLVVKGLDDLEALLPALQDLGRRH 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 16130477  86 TSFQIKPEQYNIVGEHLLATLDEM----FSPgqEVLDAWGKAYGVLANVFIN 133
Cdd:cd12131  79 VKYGVKPEHYPLVGEALLWTLEEGlgdeWTP--EVKQAWTDAYGILAGTMIE 128
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
149-392 4.81e-22

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 96.86  E-value: 4.81e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 149 WEGTrdfrIVAKTPRSALITSFELEPVDGGAVaEYRPGQY----------------------LGVWLKPEGfphQEIRQY 206
Cdd:COG2871 132 WEAT----VVSNENVTTFIKELVLELPEGEEI-DFKAGQYiqievppyevdfkdfdipeeekFGLFDKNDE---EVTRAY 203
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 207 SLTRKPDGKGY-----RIAVKREE--GGQVSNWLHNhANVGDVVKLVAPAGDFFMAvADDTPVTLISAGVGQTPMLAMLD 279
Cdd:COG2871 204 SMANYPAEKGIielniRIATPPMDvpPGIGSSYIFS-LKPGDKVTISGPYGEFFLR-DSDREMVFIGGGAGMAPLRSHIF 281
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 280 TLAKAGHTAQ-VNWFHAAENGDVHAFADEVKELGQSLPRFTAHTWYRQPSEADRAKGQ--FDSEGLMD-LSKLEGAFSDp 355
Cdd:COG2871 282 DLLERGKTDRkITFWYGARSLRELFYLEEFRELEKEHPNFKFHPALSEPLPEDNWDGEtgFIHEVLYEnYLKDHPAPED- 360
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 16130477 356 tMQFYLCGPVGFMQFTAKQLVDLGVKQENIHYECFGP 392
Cdd:COG2871 361 -CEAYLCGPPPMIDAVIKMLDDLGVEEENIYFDDFGG 396
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
157-390 6.98e-22

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


Pssm-ID: 99808 [Multi-domain]  Cd Length: 232  Bit Score: 93.16  E-value: 6.98e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 157 IVAKTPRSALITSFELEpVDGGAVAEYRPGQYLGVWLkPEGFPHqeiRQYSLTRKPDGKGY-RIAVKREEGGQVSNWLHN 235
Cdd:cd06212   5 VVAVEALTHDIRRLRLR-LEEPEPIKFFAGQYVDITV-PGTEET---RSFSMANTPADPGRlEFIIKKYPGGLFSSFLDD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 236 HANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKELGQSL 315
Cdd:cd06212  80 GLAVGDPVTVTGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDMAASGSDRPVRFFYGARTARDLFYLEEIAALGEKI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 316 PRFT-----AHTWyrqPSEADRAKGQFDSEGLMD-LSKLEGAfsdptmQFYLCGPVGFMQFTAKQLVDLGVKQENIHYEC 389
Cdd:cd06212 160 PDFTfipalSESP---DDEGWSGETGLVTEVVQRnEATLAGC------DVYLCGPPPMIDAALPVLEMSGVPPDQIFYDK 230

                .
gi 16130477 390 F 390
Cdd:cd06212 231 F 231
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
155-390 3.89e-21

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 94.57  E-value: 3.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 155 FRIVAKTPRSALITSFELEPVDGGAvAEYRPGQYlgVWLKPEGFPHqeIRQ---YSLTRKPDGKGY-RIAVKreEGGQVS 230
Cdd:COG4097 217 YRVESVEPEAGDVVELTLRPEGGRW-LGHRAGQF--AFLRFDGSPF--WEEahpFSISSAPGGDGRlRFTIK--ALGDFT 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 231 NWLHNHAnVGDVVKLVAPAGDFFMAVADDTP-VTLISAGVGQTPMLAMLDTLAKAGHTAQ-VNWFHAAENGDVHAFADEV 308
Cdd:COG4097 290 RRLGRLK-PGTRVYVEGPYGRFTFDRRDTAPrQVWIAGGIGITPFLALLRALAARPGDQRpVDLFYCVRDEEDAPFLEEL 368
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 309 KELGQSLPRFTAHTWyrqpseADRAKGQFDSEGLMDLS-KLEGAfsdptmQFYLCGPVGFMQFTAKQLVDLGVKQENIHY 387
Cdd:COG4097 369 RALAARLAGLRLHLV------VSDEDGRLTAERLRRLVpDLAEA------DVFFCGPPGMMDALRRDLRALGVPARRIHQ 436

                ...
gi 16130477 388 ECF 390
Cdd:COG4097 437 ERF 439
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
156-390 1.26e-19

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: 86.98  E-value: 1.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 156 RIVAKTPRSALITSFELE---PVdggavaEYRPGQYlgVWLKPEGFPhqEIRQYSLTRKPDGKG-YRIAVKREEGGQVSN 231
Cdd:cd06213   4 TIVAQERLTHDIVRLTVQldrPI------AYKAGQY--AELTLPGLP--AARSYSFANAPQGDGqLSFHIRKVPGGAFSG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 232 WLHNHANVGDVVKLVAPAGDFFMAVAdDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNW-FHAAENGDVHAFaDEVKE 310
Cdd:cd06213  74 WLFGADRTGERLTVRGPFGDFWLRPG-DAPILCIAGGSGLAPILAILEQARAAGTKRDVTLlFGARTQRDLYAL-DEIAA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 311 LGQS-LPRFT-----AHtwyrQPSEAD--RAKGQFDSEglmdLSKLEGafsdPTMQFYLCGPVGFMQFTAKQLVDLGVKQ 382
Cdd:cd06213 152 IAARwRGRFRfipvlSE----EPADSSwkGARGLVTEH----IAEVLL----AATEAYLCGPPAMIDAAIAVLRALGIAR 219

                ....*...
gi 16130477 383 ENIHYECF 390
Cdd:cd06213 220 EHIHADRF 227
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
159-390 9.67e-19

NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 84.23  E-value: 9.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 159 AKTPRSALITSFELEPvdGGAVAEYRPGQYlgVWLKpegFPHQEIRQ---YSLTRKPDGKG-YRIAVKreEGGQVSNWLH 234
Cdd:cd06198   1 ARVTEVRPTTTLTLEP--RGPALGHRAGQF--AFLR---FDASGWEEphpFTISSAPDPDGrLRFTIK--ALGDYTRRLA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 235 NHANVGDVVKLVAPAGDFFMAVADDtPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKELGQS 314
Cdd:cd06198  72 ERLKPGTRVTVEGPYGRFTFDDRRA-RQIWIAGGIGITPFLALLEALAARGDARPVTLFYCVRDPEDAVFLDELRALAAA 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130477 315 LpRFTAHtwyrqPSEADRAKGQFDSEGLMDLSKLEGAFSdptmqFYLCGPVGFMQFTAKQLVDLGVKQENIHYECF 390
Cdd:cd06198 151 A-GVVLH-----VIDSPSDGRLTLEQLVRALVPDLADAD-----VWFCGPPGMADALEKGLRALGVPARRFHYERF 215
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
157-386 4.15e-18

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: 82.32  E-value: 4.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 157 IVAKTPRSALITSFELEPvdgGAVAEYRPGQYLGVWLkpEGFPhqeIRQYSLTRKPDGKGY-RIAVKREEGGQVSNWLHN 235
Cdd:cd06194   1 VVSLQRLSPDVLRVRLEP---DRPLPYLPGQYVNLRR--AGGL---ARSYSPTSLPDGDNElEFHIRRKPNGAFSGWLGE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 236 HANVGDVVKLVAPAGD-FFMAVADDTPVTLISAGVGQTPMLAML-DTLAkAGHTAQVNWFHAAENGDVHAFADEVKELGQ 313
Cdd:cd06194  73 EARPGHALRLQGPFGQaFYRPEYGEGPLLLVGAGTGLAPLWGIArAALR-QGHQGEIRLVHGARDPDDLYLHPALLWLAR 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130477 314 SLPRFTahtwYRQPSEADRAKGQFDSEGLMDLSKLEgafSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIH 386
Cdd:cd06194 152 EHPNFR----YIPCVSEGSQGDPRVRAGRIAAHLPP---LTRDDVVYLCGAPSMVNAVRRRAFLAGAPMKRIY 217
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
141-390 4.33e-18

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: 83.51  E-value: 4.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 141 ENASKAGGWEGTRdfriVAKTPRSALITSFELEPVDGGAVaEYRPGQYLGV---------------------WLKPEGFP 199
Cdd:cd06188   2 EEVLGAKKWECTV----ISNDNVATFIKELVLKLPSGEEI-AFKAGGYIQIeipayeiayadfdvaekyradWDKFGLWQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 200 HQEI------RQYSLTRKPDGKG-----YRIAV--KREEG---GQVSNWLHNHAnVGDVVKLVAPAGDFFMAvADDTPVT 263
Cdd:cd06188  77 LVFKhdepvsRAYSLANYPAEEGelklnVRIATppPGNSDippGIGSSYIFNLK-PGDKVTASGPFGEFFIK-DTDREMV 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 264 LISAGVGQTPMLAMLDTLAKAGHTAQ-VNWFHAAENGDVHAFADEVKELGQSLPRFTAHTWYRQPSEADRAKGQ--FDSE 340
Cdd:cd06188 155 FIGGGAGMAPLRSHIFHLLKTLKSKRkISFWYGARSLKELFYQEEFEALEKEFPNFKYHPVLSEPQPEDNWDGYtgFIHQ 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 16130477 341 GLMD--LSKLEGafsDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIHYECF 390
Cdd:cd06188 235 VLLEnyLKKHPA---PEDIEFYLCGPPPMNSAVIKMLDDLGVPRENIAFDDF 283
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
10-131 1.09e-17

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: 78.65  E-value: 1.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  10 VKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRNGD---------QREALFNAIAAYASNIENLPALLPAVEK 80
Cdd:cd01040   1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDLDlkgspefkaHAKRVVGALDSLIDNLDDPEALDALLRK 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 16130477  81 IAQKHTSFQIKPEQYNIVGEHLLATLDEMFSPGQ--EVLDAWGKAYGVLANVF 131
Cdd:cd01040  81 LGKRHKRRGVTPEHFEVFGEALLETLEEVLGEAFtpEVEAAWRKLLDYIANAI 133
Globin pfam00042
Globin;
26-130 5.37e-17

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 76.17  E-value: 5.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477    26 AHFYDRMFTHNPELKEIFN---------MSNQRNGDQREALFNAIAAYASNIENLPALLPAVEKIAQKH-TSFQIKPEQY 95
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPrfeksaddlKGSPKFKAHGKKVLAALGEAVKHLDDLAALNAALKKLGARHkEKRGVDPANF 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 16130477    96 NIVGEHLLATLDEMFSP-GQEVLDAWGKAYGVLANV 130
Cdd:pfam00042  81 KLFGEALLVVLAEHLGEfTPETKAAWDKALDVIAAA 116
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
152-390 5.67e-17

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: 79.69  E-value: 5.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 152 TRDFRIVAKTPRSALITSFELEPVD---GGAVAEYRPGQYLGVWLkpegfPHQEI-RQYSLTRKPDGKG---YRIAVKre 224
Cdd:cd06210   1 VREAEIVAVDRVSSNVVRLRLQPDDaegAGIAAEFVPGQFVEIEI-----PGTDTrRSYSLANTPNWDGrleFLIRLL-- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 225 EGGQVSNWLHNHANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAF 304
Cdd:cd06210  74 PGGAFSTYLETRAKVGQRLNLRGPLGAFGLRENGLRPRWFVAGGTGLAPLLSMLRRMAEWGEPQEARLFFGVNTEAELFY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 305 ADEVKELGQSLPRFTAHTWYRQPSEadrakgqfDSEGL----MDL--SKLEGAFSDPTMqfYLCGPVGFMQFTAKQLVDL 378
Cdd:cd06210 154 LDELKRLADSLPNLTVRICVWRPGG--------EWEGYrgtvVDAlrEDLASSDAKPDI--YLCGPPGMVDAAFAAAREA 223
                       250
                ....*....|..
gi 16130477 379 GVKQENIHYECF 390
Cdd:cd06210 224 GVPDEQVYLEKF 235
Mb-like_oxidoreductase cd19753
Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This ...
10-130 5.86e-17

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: 76.51  E-value: 5.86e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  10 VKATIPLLVETGPKLTAHFYDRMFTHNPELKEIF--NMSNQRngdqrEALFNAIAAYASNIENLPALLPAVEKIAQKHTS 87
Cdd:cd19753   1 LRASLAAVEDGPDELARRFYARLFAEAPELRDLFpaDMDAQR-----DRLARALTHVVENLDDPDGLVPFLAQLGRDHRK 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 16130477  88 FQIKPEQYNIVGEHLLATLDEMFSPG--QEVLDAWGKAYGVLANV 130
Cdd:cd19753  76 YGVAPEHYPAVGAALLAALRHFAGEAwtPELEAAWAEAYTLIAGV 120
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
155-386 4.12e-16

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


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 76.84  E-value: 4.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 155 FRIVAKTPRS--ALITSFELEPVDggAVAEYRPGQYLGVWLKPEGFPHqeIRQYSLTRKPDGKGY-RIAVKREEGGQVSN 231
Cdd:cd06183   1 FKLVSKEDIShdTRIFRFELPSPD--QVLGLPVGQHVELKAPDDGEQV--VRPYTPISPDDDKGYfDLLIKIYPGGKMSQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 232 WLHNhANVGDVVKLVAPAGDF----FMAVADdtpVTLISAGVGQTPMLAMLDTLAKA-GHTAQVNWFHAAEN-GDVhAFA 305
Cdd:cd06183  77 YLHS-LKPGDTVEIRGPFGKFeykpNGKVKH---IGMIAGGTGITPMLQLIRAILKDpEDKTKISLLYANRTeEDI-LLR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 306 DEVKELGQSLP-RFTAHTWYRQPSEADRAKGQFDSEGLmdLSKLEGAFSDPTMQFYLCGPVGFMQFTAKQ-LVDLGVKQE 383
Cdd:cd06183 152 EELDELAKKHPdRFKVHYVLSRPPEGWKGGVGFITKEM--IKEHLPPPPSEDTLVLVCGPPPMIEGAVKGlLKELGYKKD 229

                ...
gi 16130477 384 NIH 386
Cdd:cd06183 230 NVF 232
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
183-392 5.66e-16

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 78.21  E-value: 5.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  183 YRPGQYLGVWLKpeGFPHQeIRQYSLTRKPDGKGY-RIAVKREEGGQVSNWLHNHANVGDVVKLVAPAGDFFMAVADDTP 261
Cdd:PRK10684  37 YRAGQYALVSIR--NSAET-LRAYTLSSTPGVSEFiTLTVRRIDDGVGSQWLTRDVKRGDYLWLSDAMGEFTCDDKAEDK 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  262 VTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKELGQSLPRFTAHTWYRQPSEADRAKGQFDSEG 341
Cdd:PRK10684 114 YLLLAAGCGVTPIMSMRRWLLKNRPQADVQVIFNVRTPQDVIFADEWRQLKQRYPQLNLTLVAENNATEGFIAGRLTREL 193
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16130477  342 LMdlsKLEGAFSDPTMQfyLCGPVGFMQFTAKQLVDLGVKQENIHYECFGP 392
Cdd:PRK10684 194 LQ---QAVPDLASRTVM--TCGPAPYMDWVEQEVKALGVTADRFFKEKFFT 239
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
157-386 2.40e-14

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: 72.25  E-value: 2.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 157 IVAKTPRSALITSFELEPVDG-GAVAEYRPGQYLGVWLKPEG-FPhqeirqYSLTRKPDGKGY-RIAVKREegGQVSNWL 233
Cdd:cd06221   1 IVEVVDETEDIKTFTLRLEDDdEELFTFKPGQFVMLSLPGVGeAP------ISISSDPTRRGPlELTIRRV--GRVTEAL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 234 HNhANVGDVVKLVAPAGDFF-MAVADDTPVTLISAGVGQTPMLA-MLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKEL 311
Cdd:cd06221  73 HE-LKPGDTVGLRGPFGNGFpVEEMKGKDLLLVAGGLGLAPLRSlINYILDNREDYGKVTLLYGARTPEDLLFKEELKEW 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130477 312 GQSlPRFTAHTwyrqpsEADRAKGQFDSE-GLMDLSKLEGAFSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIH 386
Cdd:cd06221 152 AKR-SDVEVIL------TVDRAEEGWTGNvGLVTDLLPELTLDPDNTVAIVCGPPIMMRFVAKELLKLGVPEEQIW 220
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
181-391 3.06e-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: 68.82  E-value: 3.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 181 AEYRPGQYlgVWLKPEGFPHQeiRQYSLTRKPDGKG-YRIAVKREEGGQVSNWLHNHANVGDVVKLVAPAGDFFMAVADD 259
Cdd:cd06190  22 ADFLPGQY--ALLALPGVEGA--RAYSMANLANASGeWEFIIKRKPGGAASNALFDNLEPGDELELDGPYGLAYLRPDED 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 260 TPVTLISAGVGQTPMLAMLDTLAKAGHTA--QVNWFHAAENGDVHAFADEVKELGQSLPRFTAHTWYRQPSEADRAKGQF 337
Cdd:cd06190  98 RDIVCIAGGSGLAPMLSILRGAARSPYLSdrPVDLFYGGRTPSDLCALDELSALVALGARLRVTPAVSDAGSGSAAGWDG 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16130477 338 DSEGLMDLskLEGAFSDPTMQ--FYLCGPVGFMQFTAKQLVDLG-VKQENIHYECFG 391
Cdd:cd06190 178 PTGFVHEV--VEATLGDRLAEfeFYFAGPPPMVDAVQRMLMIEGvVPFDQIHFDRFV 232
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
156-390 1.59e-12

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: 66.42  E-value: 1.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 156 RIVAKTPRSALITSFELEPvdgGAVAEYRPGQYLGVWLkPEGFPhqeiRQYSLTRKP-DGKGYRIAVKREEGGQVSNWLH 234
Cdd:cd06189   2 KVESIEPLNDDVYRVRLKP---PAPLDFLAGQYLDLLL-DDGDK----RPFSIASAPhEDGEIELHIRAVPGGSFSDYVF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 235 NHANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKELGQS 314
Cdd:cd06189  74 EELKENGLVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQGSKRPIHLYWGARTEEDLYLDELLEAWAEA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 315 LPRFTAHtwyrqPSEADRAKGQFDSEG------LMDLSKLEGAfsdptmQFYLCGPVGFMQFTAKQLVDLGVKQENIHYE 388
Cdd:cd06189 154 HPNFTYV-----PVLSEPEEGWQGRTGlvheavLEDFPDLSDF------DVYACGSPEMVYAARDDFVEKGLPEENFFSD 222

                ..
gi 16130477 389 CF 390
Cdd:cd06189 223 AF 224
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
175-391 3.70e-12

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 66.69  E-value: 3.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  175 VDGGAVAE---YRPGQYlgVWLKPEGfpHQEIRQYSLTRKP-DGKGYRIAVKREEGGQVSNWLHNHANVGDVVKLVAPAG 250
Cdd:PRK11872 126 LDASAHGRqldFLPGQY--ARLQIPG--TDDWRSYSFANRPnATNQLQFLIRLLPDGVMSNYLRERCQVGDEILFEAPLG 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  251 DFFMAVAdDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWF----HAA---ENGDVHAFAdevkelgQSLPRFTAHTW 323
Cdd:PRK11872 202 AFYLREV-ERPLVFVAGGTGLSAFLGMLDELAEQGCSPPVHLYygvrHAAdlcELQRLAAYA-------ERLPNFRYHPV 273
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130477  324 YRQPSEADRAKGQFDSEGLmDLSKLegafSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIHYECFG 391
Cdd:PRK11872 274 VSKASADWQGKRGYIHEHF-DKAQL----RDQAFDMYLCGPPPMVEAVKQWLDEQALENYRLYYEKFT 336
SiR_like1 cd06200
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
178-308 1.03e-08

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: 99797  Cd Length: 245  Bit Score: 55.36  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 178 GAVAEYRPGQYLgvwlkpegfPHqeiRQYSLTRKPDGKGYRIAVKRE---EG--GQVSNWLHNHANVGDVVKLVAPAGDF 252
Cdd:cd06200  35 GDIAEIGPRHPL---------PH---REYSIASLPADGALELLVRQVrhaDGglGLGSGWLTRHAPIGASVALRLRENPG 102
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16130477 253 FMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHtaQVNWFHAAENGDVH--AFADEV 308
Cdd:cd06200 103 FHLPDDGRPLILIGNGTGLAGLRSHLRARARAGR--HRNWLLFGERQAAHdfFCREEL 158
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
182-388 1.73e-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: 54.55  E-value: 1.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 182 EYRPGQYLGVWLKPEGFpHQEIRQYSLTRKPDGKGYRIAVK-REEGGQVSNWLHNHANvGDVVKLVAPAGdffmAVADDT 260
Cdd:cd06196  27 DFTPGQATEVAIDKPGW-RDEKRPFTFTSLPEDDVLEFVIKsYPDHDGVTEQLGRLQP-GDTLLIEDPWG----AIEYKG 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 261 PVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHA-AENGDVhAFADEVKELGQSlpRFTaHTWYRQPSEaDRAKGQFDS 339
Cdd:cd06196 101 PGVFIAGGAGITPFIAILRDLAAKGKLEGNTLIFAnKTEKDI-ILKDELEKMLGL--KFI-NVVTDEKDP-GYAHGRIDK 175
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 16130477 340 EGLMDLsklegaFSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIHYE 388
Cdd:cd06196 176 AFLKQH------VTDFNQHFYVCGPPPMEEAINGALKELGVPEDSIVFE 218
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
175-388 3.97e-08

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: 53.72  E-value: 3.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 175 VDGGAVAEYRPGQY--LGVwLKPEGFPHQeiRQYSLTRKPDGKGYRIAVKREEGGQVSNWLHnHANVGDVVKLVAPAGDF 252
Cdd:cd06195  17 VTRDIPFRFQAGQFtkLGL-PNDDGKLVR--RAYSIASAPYEENLEFYIILVPDGPLTPRLF-KLKPGDTIYVGKKPTGF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 253 FmaVADDTP----VTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKELGQSL-PRFTAHTWYRQP 327
Cdd:cd06195  93 L--TLDEVPpgkrLWLLATGTGIAPFLSMLRDLEIWERFDKIVLVHGVRYAEELAYQDEIEALAKQYnGKFRYVPIVSRE 170
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130477 328 SEADRAKGQFdsEGLMDLSKLEGAFSDP----TMQFYLCGPVGFMQFTAKQLVDLGV------KQENIHYE 388
Cdd:cd06195 171 KENGALTGRI--PDLIESGELEEHAGLPldpeTSHVMLCGNPQMIDDTQELLKEKGFsknhrrKPGNITVE 239
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
175-368 1.15e-07

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: 52.72  E-value: 1.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 175 VDGGAVAEYRPGQYLGVWlkpEGFPHQeIRQYSLTRKPDGKGYR--IAVKREEG---------GQVSNWLHNhANVGDVV 243
Cdd:cd06182  24 LSGNSVLKYQPGDHLGVI---PPNPLQ-PRYYSIASSPDVDPGEvhLCVRVVSYeapagrirkGVCSNFLAG-LQLGAKV 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 244 KL-VAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQvnwfhaaENGDVHAF------ADEV---KELGQ 313
Cdd:cd06182  99 TVfIRPAPSFRLPKDPTTPIIMVGPGTGIAPFRGFLQERAALRANGK-------ARGPAWLFfgcrnfASDYlyrEELQE 171
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130477 314 SLPR---FTAHT-WYRQPSEADR---AKGQFDSEGLMDLSKlEGAfsdptmQFYLCGPVGFM 368
Cdd:cd06182 172 ALKDgalTRLDVaFSREQAEPKVyvqDKLKEHAEELRRLLN-EGA------HIYVCGDAKSM 226
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
182-290 7.29e-07

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


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 50.64  E-value: 7.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  182 EYRPGQYLGVWLKpEGfphqEIRQYSLTRKP-DGKGYRIAVKREEGGQVSNWLHNHANVGDVVKLVAPAGDFFMAVADDT 260
Cdd:PRK07609 131 QYLAGQYIEFILK-DG----KRRSYSIANAPhSGGPLELHIRHMPGGVFTDHVFGALKERDILRIEGPLGTFFLREDSDK 205
                         90       100       110
                 ....*....|....*....|....*....|
gi 16130477  261 PVTLISAGVGQTPMLAMLDTLAKAGHTAQV 290
Cdd:PRK07609 206 PIVLLASGTGFAPIKSIVEHLRAKGIQRPV 235
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
167-324 1.12e-06

FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and have a variety of physiological functions in a variety of organisms including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99794  Cd Length: 220  Bit Score: 48.93  E-value: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 167 ITSFELEPVDGGAVAEYRPGQYLGVWLKPE---GFPHQE-----------IRQYSLTRKPDGKG----YRIAVKREegGQ 228
Cdd:cd06197  10 LTRFTFELSPPDVVGKWTPGQYITLDFSSEldsGYSHMAdddpqslnddfVRTFTVSSAPPHDPatdeFEITVRKK--GP 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 229 VSNWLHNHA----NVGDVVKLVAPAGDFFM---AVADDTPVTLISAGVGQTPMLAMLDTLAkagHTAQVNW-FH------ 294
Cdd:cd06197  88 VTGFLFQVArrlrEQGLEVPVLGVGGEFTLslpGEGAERKMVWIAGGVGITPFLAMLRAIL---SSRNTTWdITllwslr 164
                       170       180       190
                ....*....|....*....|....*....|
gi 16130477 295 AAENGDVHAFADEVKELGQSLPRFTAHTWY 324
Cdd:cd06197 165 EDDLPLVMDTLVRFPGLPVSTTLFITSEVY 194
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
161-386 1.48e-06

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 49.42  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  161 TPRSALITsFELEPVDGGAVAEYRPGQYlgVWLKPEGFPHQEIrqySLTRKPDGKGY-RIAVKReeGGQVSNWLHNhANV 239
Cdd:PRK08345  17 TEREKLFL-LRFEDPELAESFTFKPGQF--VQVTIPGVGEVPI---SICSSPTRKGFfELCIRR--AGRVTTVIHR-LKE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  240 GDVVKLVAPAGDFF-MAVADDTPVTLISAGVGQTPM----LAMLDTLAKAGHtaqVNWFHAAENGDVHAFADEVKELGQS 314
Cdd:PRK08345  88 GDIVGVRGPYGNGFpVDEMEGMDLLLIAGGLGMAPLrsvlLYAMDNRWKYGN---ITLIYGAKYYEDLLFYDELIKDLAE 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130477  315 LPRFTAHTWYRQ----PSEADRAKG--QFDSEGLMdLSKLEGAFSDPTMQFYL-CGPVGFMQFTAKQLVDLGVKQENIH 386
Cdd:PRK08345 165 AENVKIIQSVTRdpewPGCHGLPQGfiERVCKGVV-TDLFREANTDPKNTYAAiCGPPVMYKFVFKELINRGYRPERIY 242
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ...
29-127 2.63e-06

Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly expressed in neurons of the brain and retina. In the human brain, it is highly expressed in the hypothalamus, amygdala, and in the pontine tegmental nuclei. It affords protection of brain neurons from ischemia and hypoxia. In rats, it plays a role in the neuroprotection of limb ischemic preconditioning (LIP). It plays roles as: a sensor of oxygen levels; a store or reservoir for oxygen; a facilitator for oxygen transport; a regulator of ROS; and a scavenger of nitric oxide. It also functions in the protection against apoptosis and in sleep regulation. This subgroup contains Ngb from mammalian and non-mammalian vertebrates, including fish, amphibians and reptiles; the functionally pentacoordinated acoelomorph Symsagittifera roscoffensis Ngb does not belong to this subgroup.


Pssm-ID: 271272  Cd Length: 148  Bit Score: 46.75  E-value: 2.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  29 YDRMFTHNPELKEIFNMSNQRNGDQREALFNA------------IAAYASNIENLPALLPAVEKIAQKHTSFQIKPEQYN 96
Cdd:cd08920  28 FSRLFELEPDLLPLFQYNGRQFSSPQDCLSSPefldhirkvmlvIDAAVSHLEDLSSLEEYLTSLGRKHRAVGVKLESFS 107
                        90       100       110
                ....*....|....*....|....*....|...
gi 16130477  97 IVGEHLLATLDEMFSPG--QEVLDAWGKAYGVL 127
Cdd:cd08920 108 TVGESLLYMLESSLGPAftPDTREAWSTLYGAV 140
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
154-253 5.43e-06

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 44.49  E-value: 5.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   154 DFRIVAKT--PRSALITSFELEPVDggAVAEYRPGQYLGVWLKPEGfpHQEIRQYSLTRKPDGKGY-RIAVKREEGGQVS 230
Cdd:pfam00970   1 PLTLVEKElvSHDTRIFRFALPHPD--QVLGLPVGQHLFLRLPIDG--ELVIRSYTPISSDDDKGYlELLVKVYPGGKMS 76
                          90       100
                  ....*....|....*....|...
gi 16130477   231 NWLhNHANVGDVVKLVAPAGDFF 253
Cdd:pfam00970  77 QYL-DELKIGDTIDFKGPLGRFE 98
YjbI COG2346
Truncated hemoglobin YjbI [Inorganic ion transport and metabolism];
23-134 1.60e-05

Truncated hemoglobin YjbI [Inorganic ion transport and metabolism];


Pssm-ID: 441915  Cd Length: 120  Bit Score: 43.70  E-value: 1.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  23 KLTAHFYDRMFTHnPELKEIFNmsNQRNGDQREALFNAIAAYAsnienlpaLLPAV---EKIAQKHTSFQIKPEQYNIVG 99
Cdd:COG2346  18 ALVDRFYDRVRAD-PLLGPIFP--EADLEEHREKLADFLSQVL--------GGPGLysgRRMRARHAPLPITEEHFDRWL 86
                        90       100       110
                ....*....|....*....|....*....|....*
gi 16130477 100 EHLLATLDEMFSPGQEVLDAWGKAYGvLANVFINR 134
Cdd:COG2346  87 ELMREALDELGVPPELAEELLARLER-IADDMVNR 120
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
175-312 2.25e-05

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 45.63  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477  175 VDGGAVAEYRPGQYLGVWLkPEGFPHQEiRQYSLTRKpDGKGYRIAVKREegGQVSNWLHNHAnVGDVVKLVAPAGDFFM 254
Cdd:PRK00054  24 LDGEKVFDMKPGQFVMVWV-PGVEPLLE-RPISISDI-DKNEITILYRKV--GEGTKKLSKLK-EGDELDIRGPLGNGFD 97
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16130477  255 AVADDTPVTLISAGVGQTPMLAMLDTLAKAGhtAQVNWFHAAENGDVHAFADEVKELG 312
Cdd:PRK00054  98 LEEIGGKVLLVGGGIGVAPLYELAKELKKKG--VEVTTVLGARTKDEVIFEEEFAKVG 153
globin_sensor cd01068
Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor ...
2-123 1.27e-04

Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor single-domain globins (SSDgbs); S family; This family includes sensor domains which binds porphyrins, and other non-heme cofactors. GCSs have an N-terminal sensor domain coupled to a functional domain. For heme-bound oxygen sensing/binding globin domains, O2 binds to/dissociates from the heme iron complex inducing a structural change in the sensor domain, which is then transduced to the functional domain, switching on (or off) the function of the latter. Functional domains include DGC/GGDEF, EAL, histidine kinase, MCP, PAS, and GAF domains. Characterized members include Bacillus subtilis heme-based aerotaxis transducer (HemAT-Bs) which has a sensor domain coupled to an MCP domain. HemAT-Bs mediates an aerophilic response, and may control the movement direction of bacteria and archaea. Its MCP domain interacts with the CheA histidine kinase, a component of the CheA/CheY signal transduction system that regulates the rotational direction of flagellar motors. Another GCS having the sensor domain coupled to an MCP domain is Caulobacter crescentus McpB. McpB is encoded by a gene which lies adjacent to the major chemotaxis operon. Like McpA (encoded on this operon), McpB has three potential methylation sites, a C-terminal CheBR docking motif, and a motif needed for proteolysis via a ClpX-dependent pathway during the swarmer-to-stalked cell transition. Also included is Geobacter sulfurreducens GCS, a GCS of unknown function, in which the sensor domain is coupled to a transmembrane signal-transduction domain. Pgbs are single-domain globins of unknown function. Methanosarcina acetivorans Pgbs is dimeric and has an N-terminal extension, which together with other Pgb-specific loops, buries the heme within the protein; small ligand molecules gain access to the heme via two orthogonal apolar tunnels. Pgbs and other single-domain globins can function as sensors, when coupled to an appropriate regulator domain.


Pssm-ID: 381256 [Multi-domain]  Cd Length: 146  Bit Score: 41.80  E-value: 1.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477   2 LDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHnPELKEIFNMSNQRN---GDQR---EALFNAI--AAYASNienlpa 73
Cdd:cd01068   8 LTEEDLALLRELRPLIEPHLDEILDAFYDHLLSF-PELAAIFDDHSTIErlkQTQRahwLELFSGDfdEAYVER------ 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16130477  74 llpaVEKIAQKHTSFQIKPEQY----NIVGEHLLATLDEMFSPGQE----VLDAWGKA 123
Cdd:cd01068  81 ----RRRIGRVHVRIGLEPRWYigayALLLEELIEIIAEELRKDPEelaeLLLALVKA 134
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
183-278 3.08e-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: 42.31  E-value: 3.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 183 YRPGQYLGVWlkPEGF------PHQeIRQYSL--TRKPDGKGYR---IAVKREEG----------GQVSNWLHNhANVGD 241
Cdd:cd06208  41 YLEGQSIGII--PPGTdakngkPHK-LRLYSIasSRYGDDGDGKtlsLCVKRLVYtdpetdetkkGVCSNYLCD-LKPGD 116
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 16130477 242 VVKLVAPAGDFF-MAVADDTPVTLISAGVGQTPMLAML 278
Cdd:cd06208 117 DVQITGPVGKTMlLPEDPNATLIMIATGTGIAPFRSFL 154
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
120-280 3.39e-04

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: 41.93  E-value: 3.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 120 WGKAYGVLanvfINREAEI-YNENASKAGGWE--GTRDFRIVAKTPRSalITSFEL--EPVDGGAVAEYRPGQYLGVWLK 194
Cdd:cd06201  22 WGRDLGEA----LGLDLPLdHKKRLPRTKALElvERKDYGAAVQAPTA--ILRFKPakRKLSGKGLPSFEAGDLLGILPP 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 195 PEGFPhqeiRQYSLTRKPDGKGYRIAVKREEGGQVSNWLHNhANVGDVVK-LVAPAGDFFMAvADDTPVTLISAGVGQTP 273
Cdd:cd06201  96 GSDVP----RFYSLASSSSDGFLEICVRKHPGGLCSGYLHG-LKPGDTIKaFIRPNPSFRPA-KGAAPVILIGAGTGIAP 169

                ....*..
gi 16130477 274 MLAMLDT 280
Cdd:cd06201 170 LAGFIRA 176
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
183-287 8.68e-04

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: 40.69  E-value: 8.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477 183 YRPGQYLGVWL-----KPEGFphqeirqySLTRKPDGkgyrIAVKREegGQVSNWLHNhANVGDVVKLVAPAGDFFMAVA 257
Cdd:cd06220  24 FKPGQFVMVWVpgvdeIPMSL--------SYIDGPNS----ITVKKV--GEATSALHD-LKEGDKLGIRGPYGNGFELVG 88
                        90       100       110
                ....*....|....*....|....*....|
gi 16130477 258 DDtpVTLISAGVGQTPMLAMLDTLAKAGHT 287
Cdd:cd06220  89 GK--VLLIGGGIGIAPLAPLAERLKKAADV 116
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
239-312 1.41e-03

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


Pssm-ID: 99814 [Multi-domain]  Cd Length: 246  Bit Score: 39.84  E-value: 1.41e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130477 239 VGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGhtAQVNWFHAAENGDVHAFADEVKELG 312
Cdd:cd06218  78 AGDELDVLGPLGNGFDLPDDDGKVLLVGGGIGIAPLLFLAKQLAERG--IKVTVLLGFRSADDLFLVEEFEALG 149
Protoglobin pfam11563
Protoglobin; This family includes protoglobin from Methanosarcina acetivorans C2A. It is also ...
1-123 4.08e-03

Protoglobin; This family includes protoglobin from Methanosarcina acetivorans C2A. It is also found near the N-terminus of the Haem-based aerotactic transducer HemAT in Bacillus subtilis. It is part of the haemoglobin superfamily. Protoglobin has specific loops and an amino-terminal extension which leads to the burying of the haem within the matrix of the protein. Protoglobin-specific apolar tunnels allow the access of O2, CO and NO to the haem distal site. In HemAT it acts as an oxygen sensor domain. It can also recognize cyanide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 431935 [Multi-domain]  Cd Length: 149  Bit Score: 37.57  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130477     1 MLDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHnPELKEIFNmsnqrNGDQREALFNAIAAYasnIENL------PAL 74
Cdd:pfam11563  12 GFTEEDLAALRALRPLIEPHIPAIVDAFYDKLLSF-PETARIFT-----TSSQIERLKDTLKAY---LLRLfsgpydEAY 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 16130477    75 LPAVEKIAQKHTSFQIKPEQYN----IVGEHLLATL-DEMFSPGQEVLD---AWGKA 123
Cdd:pfam11563  83 VEYRLKIGKMHVRLGLEPRWYIaayaLILEGLLEALlEKIKLSAAEKSAlvrALSKL 139
 
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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