NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1831108410|ref|WP_168353867|]
View 

MULTISPECIES: nitroreductase family protein [Muribaculum]

Protein Classification

nitroreductase family protein( domain architecture ID 10114890)

nitroreductase family protein may catalyze the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles, requiring NAD(P)H as an electron donor in an obligatory two-electron transfer and using FMN as cofactor

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
nitroreductase cd02150
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 43-202 3.64e-78

nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.often found to be homodimers.


:

Pssm-ID: 380325 [Multi-domain]  Cd Length: 156  Bit Score: 230.95  E-value: 3.64e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  43 IYTRTSVRQYdASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAEGLPYAKMLKHAPLAIIPCGDLDKA 122
Cdd:cd02150     1 ILTRRSIRKY-TDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREKLDKIAEAHPYGKMLKEAPLAIVVCGDPSKE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 123 legDGQAFWIQDVSAATENMLIAANALGVGAVWTAVYPDESRIDAVRKVLGMPATIMPLAVVPMGYPAGEHHPKDKWKPE 202
Cdd:cd02150    80 ---KAPGYWVQDCSAATENILLAAHALGLGAVWLGVYPFEERVKAIREILNIPENIIPFCVIALGYPAEEKEPKDRFDEE 156
 
Name Accession Description Interval E-value
nitroreductase cd02150
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 43-202 3.64e-78

nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.often found to be homodimers.


Pssm-ID: 380325 [Multi-domain]  Cd Length: 156  Bit Score: 230.95  E-value: 3.64e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  43 IYTRTSVRQYdASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAEGLPYAKMLKHAPLAIIPCGDLDKA 122
Cdd:cd02150     1 ILTRRSIRKY-TDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREKLDKIAEAHPYGKMLKEAPLAIVVCGDPSKE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 123 legDGQAFWIQDVSAATENMLIAANALGVGAVWTAVYPDESRIDAVRKVLGMPATIMPLAVVPMGYPAGEHHPKDKWKPE 202
Cdd:cd02150    80 ---KAPGYWVQDCSAATENILLAAHALGLGAVWLGVYPFEERVKAIREILNIPENIIPFCVIALGYPAEEKEPKDRFDEE 156
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 39-204 7.10e-47

Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 151.93  E-value: 7.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  39 ALDAIYTRTSVRQYDaSRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAEGLPYA--KMLKHAPLAIIPC 116
Cdd:COG0778     1 LLELLLTRRSVRKFT-DKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEAnqEWVADAPVLIVVC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 117 GDLDKAlEGDGQAFWIQDVSAATENMLIAANALGVGAVWTAVYpdesRIDAVRKVLGMPATIMPLAVVPMGYPAGEHHPK 196
Cdd:COG0778    80 ADPDRS-EKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGF----DPEKVRELLGLPEGEEPVALLALGYPAEELNPR 154


                  ....*...
gi 1831108410 197 DKWKPENI 204
Cdd:COG0778   155 PRKPLEEV 162
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 43-188 1.75e-25

Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds.


Pssm-ID: 425926 [Multi-domain]  Cd Length: 168  Bit Score: 97.08  E-value: 1.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  43 IYTRTSVRQYDASRaIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAE------------------------ 98
Cdd:pfam00881   1 IRQRRSVRKFDPEP-VPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEaalelllvepaaalllllrrdanl 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  99 GLPYAKMLKHAPLAIIPCGDLDKALEGDGQAFW---IQDVSAATENMLIAANALGVGAVWTAVYPDEsridAVRKVLGMP 175
Cdd:pfam00881  80 KLLLQDFLRGAPVLIVITASLSTYLRKAAERAYreaLLDAGAAAQNLLLAATSLGLGSCPIGGFDAA----AVRELLGLP 155

                         170
                  ....*....|...
gi 1831108410 176 ATIMPLAVVPMGY 188
Cdd:pfam00881 156 DDERLVGLIAVGY 168
PRK13294 PRK13294
F420-0--gamma-glutamyl ligase; Provisional
 30-203 2.64e-12

F420-0--gamma-glutamyl ligase; Provisional


Pssm-ID: 183957 [Multi-domain]  Cd Length: 448  Bit Score: 64.65  E-value: 2.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  30 SAPAVESNQAlDAIYTRTSVRQYdASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREI----LDSLAE------- 98
Cdd:PRK13294  245 TAEALELGRR-EAVLLRRSVREF-SDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVrtrlLDAMRDawradlr 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  99 --GLPYA---------KMLKHAPLAIIPCGDLDKALE-------GDGQAFWIQDVSAATENMLIAANALGVGAVWTAvyp 160
Cdd:PRK13294  323 adGLSEEsiarrvrrgDILYDAPELVVPFLVPDGAHSypdarrtAAERTMFTVAVGAAVQNLLVALAVEGLGSCWIG--- 399

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1831108410 161 deSRI---DAVRKVLGMPATIMPLAVVPMGYPAGEHHPKDKWKPEN 203
Cdd:PRK13294  400 --STIfaaDVVRAVLDLPADWEPLGAVAIGHPAEPPGPRPPRDPGD 443
 
Name Accession Description Interval E-value
nitroreductase cd02150
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 43-202 3.64e-78

nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.often found to be homodimers.


Pssm-ID: 380325 [Multi-domain]  Cd Length: 156  Bit Score: 230.95  E-value: 3.64e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  43 IYTRTSVRQYdASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAEGLPYAKMLKHAPLAIIPCGDLDKA 122
Cdd:cd02150     1 ILTRRSIRKY-TDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREKLDKIAEAHPYGKMLKEAPLAIVVCGDPSKE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 123 legDGQAFWIQDVSAATENMLIAANALGVGAVWTAVYPDESRIDAVRKVLGMPATIMPLAVVPMGYPAGEHHPKDKWKPE 202
Cdd:cd02150    80 ---KAPGYWVQDCSAATENILLAAHALGLGAVWLGVYPFEERVKAIREILNIPENIIPFCVIALGYPAEEKEPKDRFDEE 156
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 39-204 7.10e-47

Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 151.93  E-value: 7.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  39 ALDAIYTRTSVRQYDaSRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAEGLPYA--KMLKHAPLAIIPC 116
Cdd:COG0778     1 LLELLLTRRSVRKFT-DKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEAnqEWVADAPVLIVVC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 117 GDLDKAlEGDGQAFWIQDVSAATENMLIAANALGVGAVWTAVYpdesRIDAVRKVLGMPATIMPLAVVPMGYPAGEHHPK 196
Cdd:COG0778    80 ADPDRS-EKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGF----DPEKVRELLGLPEGEEPVALLALGYPAEELNPR 154


                  ....*...
gi 1831108410 197 DKWKPENI 204
Cdd:COG0778   155 PRKPLEEV 162
nitroreductase cd02139
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 40-207 8.28e-41

nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.


Pssm-ID: 380316 [Multi-domain]  Cd Length: 165  Bit Score: 136.45  E-value: 8.28e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  40 LDAIYTRTSVRQYDaSRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAEGLPYAKMLKHAPLAIIPCGDL 119
Cdd:cd02139     2 YEAIKKRRSIRKYK-PTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELKEKLAEAANGQKFIAEAPVVIVACADP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 120 DKALEGDGQAFWIQDVSAATENMLIAANALGVGAVWTAVYpDEsriDAVRKVLGMPATIMPLAVVPMGYPAGE--HHPKd 197
Cdd:cd02139    81 SESGMGCGKPYYLVDVAIAMEHLVLAATEEGLGTCWIGAF-DE---DKVKEILGIPEEYRVVALTPLGYPAEEppPRPR- 155

                         170
                  ....*....|..
gi 1831108410 198 kwKP--ENIHYN 207
Cdd:cd02139   156 --KPleEIVFYE 165
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 43-188 5.93e-38

nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Enzymes of this family are described as NAD(P)H:FMN oxidoreductases, oxygen-insensitive nitroreductase, flavin reductase P, dihydropteridine reductase, NADH oxidase or NADH dehydrogenase.


Pssm-ID: 380311 [Multi-domain]  Cd Length: 139  Bit Score: 128.18  E-value: 5.93e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  43 IYTRTSVRQYDaSRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLA-EGLPYAKMLKHAPLAIIPCGDLDK 121
Cdd:cd02062     1 IKTRRSIRKFT-DKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLAkLAAPNQKFIAGAPVVIVVVADPDK 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831108410 122 AlegdgQAFWIQDVSAATENMLIAANALGVGAVWTAVYPDESriDAVRKVLGMPATIMPLAVVPMGY 188
Cdd:cd02062    80 S-----RPWALEDAGAAAQNLLLAAAALGLGSCWIGGFDFRE--DKVRELLGIPENLRPVALIAIGY 139
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 40-188 2.65e-37

nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.often found to be homodimers.


Pssm-ID: 380330 [Multi-domain]  Cd Length: 145  Bit Score: 126.73  E-value: 2.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  40 LDAIYTRTSVRQYDaSRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAEGlpyAKMLKHAPLAIIPCGDL 119
Cdd:cd20609     3 LELAKKRYSVRKFS-DKPVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKLAKA---TPRFFGAPLVIVVCYDK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831108410 120 DKAL--EGDGQAFWIQDVSAATENMLIAANALGVGAVWTAVYpDEsriDAVRKVLGMPATIMPLAVVPMGY 188
Cdd:cd20609    79 DESWkrPYDGKDSGDIDAAIVATHMMLAATELGLGTCWVGNF-DP---EKVREAFNLPENLEPVAILPLGY 145
nitroreductase cd02151
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 41-198 4.43e-37

nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.often found to be homodimers..


Pssm-ID: 380326 [Multi-domain]  Cd Length: 157  Bit Score: 126.49  E-value: 4.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  41 DAIYTRTSVRQYDAsRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAEGLPY-AKMLKHAPLAIIPCGDL 119
Cdd:cd02151     1 ELLKKRRSIRKYTD-EPIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDKETLKKLSECKPHgSAFLKGAPAAIVVLADT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 120 DKAlegdgqAFWIQDVSAATENMLIAANALGVGAVWTAVY-----PDESRIDAVRKVLGMPATIMPLAVVPMGYPAGEHH 194
Cdd:cd02151    80 EKS------DTWIEDASIAATYIQLAAESLGLGSCWIQIRnretqDGKTAEEYVRELLGIPENYRVLCIIALGYPDEEKP 153


                  ....
gi 1831108410 195 PKDK 198
Cdd:cd02151   154 PHED 157
nitroreductase cd20608
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 40-188 4.07e-35

nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Enzymes of this family are described as NAD(P)H:FMN oxidoreductases, oxygen-insensitive nitroreductase, flavin reductase P, dihydropteridine reductase, NADH oxidase or NADH dehydrogenase.


Pssm-ID: 380329 [Multi-domain]  Cd Length: 145  Bit Score: 121.29  E-value: 4.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  40 LDAIYTRTSVRQYdASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAE-GLPYAKMLKHAPLAIIPCGD 118
Cdd:cd20608     1 FEAIKTRRSVRRF-SDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTDKETLSELAKkESPSNGWLKDAPVIIVVCAD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 119 LDKALEGDGQAFWIQDVSAATENMLIAANALGVGAVWTAVYpDESRidaVRKVLGMPATIMPLAVVPMGY 188
Cdd:cd20608    80 PKDSGWLNGQNYYLVDAAIAMQNLMLAATDLGLGTCWIGAF-DEKK---VKEILGIPENIRVVALTPLGY 145
PnbA_NfnB-like cd02136
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ...
 42-193 3.68e-32

nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as a cofactor and catalyze reduction of a variety of nitroaromatic compounds, including nitrofurans, nitrobenzens, nitrophenol, nitrobenzoate and quinones by using either NADH or NADPH as a source of reducing equivalents in an obligatory two-election transfer mechanism. The enzyme is typically a homodimer. Mycobacterium smegmatis nitroreductase NfnB plays a role in resistance to benzothiazinone.


Pssm-ID: 380313 [Multi-domain]  Cd Length: 152  Bit Score: 113.84  E-value: 3.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  42 AIYTRTSVRQYDaSRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVI--DKREILdslaeglpyAKMLKHAPLAIIPCgdL 119
Cdd:cd02136     1 AIKSRRSVRAFK-DKPVPKETIEKILEAARRAPSGKNTQPWRVYVVtgKARERL---------KKAFFGAPVALFLT--M 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831108410 120 DKALEgdgqAFWIQDVSAATENMLIAANALGVGAVWTAVYPDESriDAVRKVLGMPATIMPLAVVPMGYPAGEH 193
Cdd:cd02136    69 DKVLG----PWSWFDLGAFLQNLMLAAHALGLGTCPQGALAGYP--DVVRKELGIPDDEELVCGIALGYPDPDA 136
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 43-188 1.75e-25

Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds.


Pssm-ID: 425926 [Multi-domain]  Cd Length: 168  Bit Score: 97.08  E-value: 1.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  43 IYTRTSVRQYDASRaIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAE------------------------ 98
Cdd:pfam00881   1 IRQRRSVRKFDPEP-VPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEaalelllvepaaalllllrrdanl 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  99 GLPYAKMLKHAPLAIIPCGDLDKALEGDGQAFW---IQDVSAATENMLIAANALGVGAVWTAVYPDEsridAVRKVLGMP 175
Cdd:pfam00881  80 KLLLQDFLRGAPVLIVITASLSTYLRKAAERAYreaLLDAGAAAQNLLLAATSLGLGSCPIGGFDAA----AVRELLGLP 155

                         170
                  ....*....|...
gi 1831108410 176 ATIMPLAVVPMGY 188
Cdd:pfam00881 156 DDERLVGLIAVGY 168
nitroreductase cd20610
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 43-188 2.81e-20

nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Enzymes of this family are described as NAD(P)H:FMN oxidoreductases, oxygen-insensitive nitroreductase, flavin reductase P, dihydropteridine reductase, NADH oxidase or NADH dehydrogenase.


Pssm-ID: 380331 [Multi-domain]  Cd Length: 167  Bit Score: 83.48  E-value: 2.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  43 IYTRTSVRQYdASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLA-------EGLP-------------- 101
Cdd:cd20610     1 IKKRRSIRKF-KPDPVPKEDIEKILEAANWAPSGMNRQNWEFVVVKGGEKIEKIGisikkknEEIArllekvfaekpirf 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 102 -----YAKMLKHAPLAIIPCGDLDKALEGDGQAfwIQDVSAATENMLIAANALGVGAVW-TAVYPDESRIdavRKVLGMP 175
Cdd:cd20610    80 rkfrrFFTLFGGAPVLVVVYTEPYKPPEERKPD--LQSVSAAIQNLLLAAHALGLGTCWmTGPLYAEDEI---EEILEIP 154

                         170
                  ....*....|...
gi 1831108410 176 ATIMPLAVVPMGY 188
Cdd:cd20610   155 DDKELVAVTPLGY 167
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
 40-196 1.50e-19

nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily of the nitroreductase family containing uncharacterized proteins; includes nitroreductases MhqN, YodC, YdgI, DrgA. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.


Pssm-ID: 380314 [Multi-domain]  Cd Length: 147  Bit Score: 81.13  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  40 LDAIYTRTSVRQYDASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAEGLPYAKMLKHAPLAIIPCGDL 119
Cdd:cd02137     1 LEVIKSRRSVRNFDPDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAAYNQPQVTTASAVILVLGDL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831108410 120 DKALegdgqafwiqdvsaATENMLIAANALGVGAVwtavyP-DESRIDAVRKVLGMPATIMPLAVVPMGYPAGEHHPK 196
Cdd:cd02137    81 NAGL--------------AAMNLMLAAKAKGYDTC-----PmGGFDKEKVAELLNLPDRYVPVLLIAIGKAADKAPRS 139
YdjA-like cd02135
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ...
 40-188 9.10e-18

nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to nitroreductase YdjA from Escherichia coli. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer. Members of this family are also called NADH dehydrogenase, oxygen-insensitive NAD(P)H nitrogenase or dihydropteridine reductase.


Pssm-ID: 380312 [Multi-domain]  Cd Length: 162  Bit Score: 76.87  E-value: 9.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  40 LDAIYTRTSVRQYDASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDK----------REILDSLAEGLPYAKMLKH- 108
Cdd:cd02135     1 LELIKTRRSIRKFKLTGAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGegrerlaellAAAAAARAPGADPEKLEKAr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 109 -----APLAIIPCGDLDKALEGDgqafWIQD---VSAATENMLIAANALGVGAVWTAvyPDESRIDAVRKVLGMPATIMP 180
Cdd:cd02135    81 ekalrAPVVIAVVAKPDEDPKVP----EWEQyaaVGAAVQNLLLAAHALGLGAVWRT--GPVTYDPAVREALGLPEDERI 154


                  ....*...
gi 1831108410 181 LAVVPMGY 188
Cdd:cd02135   155 VGFLYLGT 162
NfsA-like cd02146
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ...
 40-207 4.39e-17

nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin reductase and oxygen-insensitive nitroreductase. These enzymes are homodimeric flavoproteins that contain one FMN per monomer as a cofactor. Flavin reductase catalyzes the reduction of flavin by using NADPH as an electron donor. Oxygen-insensitive nitroreductase, such as NfsA protein in Escherichia coli, catalyzes reduction of nitrocompounds using NADPH as electron donor.


Pssm-ID: 380322 [Multi-domain]  Cd Length: 229  Bit Score: 76.51  E-value: 4.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  40 LDAIYTRTSVRQYDAsRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAEGLPYAKMLKHAPLAIIPCGDL 119
Cdd:cd02146     2 IETILNHRSVRKFTD-EPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKLAELAGNQPYVAQAPVFLVFCADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 120 D---KALEGDGQA-----------FWIQDVSAATENMLIAANALGVGAVWT-AVYPDesrIDAVRKVLGMPATIMPLAVV 184
Cdd:cd02146    81 YrhqKIAEEAGGKdvgldylesflVGVVDAALAAQNALVAAESLGLGIVYIgGIRNN---PEEVIELLGLPEYVFPLFGL 157

                         170       180
                  ....*....|....*....|....
gi 1831108410 185 PMGYPAGEHHPKDKWKPENI-HYN 207
Cdd:cd02146   158 TVGHPDPTPEVKPRLPLEAVvHEE 181
TdsD-like cd02138
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ...
 42-190 1.50e-15

nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to Burkholderia pseudomallei TdsD, may be involved in the processing of organosulfur compounds. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.


Pssm-ID: 380315 [Multi-domain]  Cd Length: 174  Bit Score: 71.04  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  42 AIYTRTSVRQYDaSRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKRE-----ILDSLAEG-LPYAkmlKHAPLAIIP 115
Cdd:cd02138     1 LIAERWSPRAFS-PEPISEEDLLSLFEAARWAPSCFNEQPWRFVVARRDTeafekLLDLLAEGnQSWA---KNAPVLIVV 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831108410 116 CGDLDKALEGDGQAFWIQDVSAATENMLIAANALGVgavwtAVYP----DEsriDAVRKVLGMPATIMPLAVVPMGYPA 190
Cdd:cd02138    77 LAKTEFDHNGKPNRYALFDTGAAVANLALQATALGL-----VVHQmagfDP---EKAKEALGIPDEYEPITMIAIGYPG 147
nitroreductase_FeS-like cd02143
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ...
 45-190 2.40e-14

nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family utilize FMN as a cofactor. This family may be involved in the reduction of flavin or nitroaromatic compounds via an obligatory two-electron transfer. Nitroreductase is homodimer. Each subunit contains one FMN molecule.


Pssm-ID: 380319 [Multi-domain]  Cd Length: 187  Bit Score: 68.27  E-value: 2.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  45 TRTSVRQYdASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAE------------GLPYAKM------- 105
Cdd:cd02143     4 SRRSIRRY-KDKPVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDPEKVRRLAElvidwmrelikeDPELAGKlfldgiv 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 106 ----------LKHAPLAIIPCGDLDKALegdGQAfwiqDVSAATENMLIAANALGVGAVW-----TAV--YPDesridaV 168
Cdd:cd02143    83 aawekgidviLRGAPHLVVAHAPKDAPT---PPV----DCAIALTYLELAAPSLGLGTCWagfftAAAnnYPP------L 149

                         170       180
                  ....*....|....*....|..
gi 1831108410 169 RKVLGMPATIMPLAVVPMGYPA 190
Cdd:cd02143   150 REALGLPEGHKVGGAMMLGYPK 171
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
 40-204 1.63e-13

nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This domain catalyzes the reduction of flavin, nitrocompound, quinones and azo compounds using NADH or NADPH as an electron donor. The enzyme is a homodimer, and each monomer binds a FMN as co-factor. This family includes FRase I in Vibrio fischeri, wihich reduces FMN into FMNH2 as part of the bioluminescent reaction. The family also includes oxygen-insensitive nitroreductases that use NADH or NADPH as an electron donor in the ping pong bi bi mechanism. This type of nitroreductase can be used in cancer chemotherapy to activate a range of prodrugs.


Pssm-ID: 380324 [Multi-domain]  Cd Length: 156  Bit Score: 65.35  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  40 LDAIYTRTSVRQYDASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAEGLPYA-KMLKHAPLAIIPCGD 118
Cdd:cd02149     3 LELLNFRYATKKFDPNKKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLAPAAWFNqPQIKDASHVVVFLAK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 119 LDkalegdgqafWIQ-DVSAATENMLIAANALGVGAVwtavyPDESrIDA--VRKVLGMPATIMPLAV-VPMGYPAGEHH 194
Cdd:cd02149    83 KD----------WSAkQTYIALGNMLLAAAMLGIDSC-----PIEG-FDPakLDEILGLDEKGYKISVmVAFGYRSEEKL 146

                         170
                  ....*....|
gi 1831108410 195 PKDKWKPENI 204
Cdd:cd02149   147 PKSRKPLEDV 156
nitroreductase cd03370
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ...
 41-194 1.17e-12

uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus thermophilus NADH oxidase and other, uncharacterized proteins. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer.


Pssm-ID: 380327 [Multi-domain]  Cd Length: 191  Bit Score: 63.88  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  41 DAIYTRTSVRQYdASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSLAEGLPYAKMLKHAPLAIIPCGDLD 120
Cdd:cd03370     3 EAIESRRSIRKY-TQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQLQAAAYGQAQVTSAPAVIVIYSDME 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 121 KALE-----------GDGQAFWIQDVSAATENM--------------------LIAANALGVGAVwtavyP----DEsri 165
Cdd:cd03370    82 DALAnleetihpglsEERRQREAAGLRGAFGKMsveqrgqwglaqanialgflLLAAQSLGYDTS-----PmlgfDP--- 153

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1831108410 166 DAVRKVLGMPATIMPLAVVPMGYPAGE---HH 194
Cdd:cd03370   154 EKVKALLGLPEHVTIAALVALGKPAEEgypHH 185
PRK13294 PRK13294
F420-0--gamma-glutamyl ligase; Provisional
 30-203 2.64e-12

F420-0--gamma-glutamyl ligase; Provisional


Pssm-ID: 183957 [Multi-domain]  Cd Length: 448  Bit Score: 64.65  E-value: 2.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  30 SAPAVESNQAlDAIYTRTSVRQYdASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREI----LDSLAE------- 98
Cdd:PRK13294  245 TAEALELGRR-EAVLLRRSVREF-SDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVrtrlLDAMRDawradlr 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  99 --GLPYA---------KMLKHAPLAIIPCGDLDKALE-------GDGQAFWIQDVSAATENMLIAANALGVGAVWTAvyp 160
Cdd:PRK13294  323 adGLSEEsiarrvrrgDILYDAPELVVPFLVPDGAHSypdarrtAAERTMFTVAVGAAVQNLLVALAVEGLGSCWIG--- 399

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1831108410 161 deSRI---DAVRKVLGMPATIMPLAVVPMGYPAGEHHPKDKWKPEN 203
Cdd:PRK13294  400 --STIfaaDVVRAVLDLPADWEPLGAVAIGHPAEPPGPRPPRDPGD 443
iodotyrosine_dehalogenase cd02144
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ...
 46-204 4.77e-10

iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the 3, 5 positions of L-tyosine in thyroid, liver and kidney, using NADPH as electron donor. This enzyme is a homolog of the nitroreductase family. These enzymes are usually homodimers.


Pssm-ID: 380320  Cd Length: 192  Bit Score: 56.39  E-value: 4.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  46 RTSVRQYdASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDSL------AEGLPYAKMLKH----------- 108
Cdd:cd02144     8 RRSVRDF-SSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRKIreaaeeEEKEFYEKRMGEewvwdlkplgt 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 109 ---------APLAIIPCGDLDKALEgDGQA----FWIQDVSAATeNMLIAA--NAlGVGAVWTAvyPDESRidAVRKVLG 173
Cdd:cd02144    87 nwekpylteAPYLIVVFKQKYGVLP-DGKKkkhyYNEESVGIAV-GILLAAlhNA-GLVTLTHT--PSPMP--FLRDLLG 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1831108410 174 MPATIMPLAVVPMGYPA-GEHHPKDKWKP-ENI 204
Cdd:cd02144   160 RPKNEKPLLLLPVGYPAeDATVPDLKRKPlEEI 192
BluB cd02145
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ...
 42-209 5.33e-09

5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5,6-dimethylbenzimidazole (DMB), a component of vitamin B12; is is a subfamily of the nitroreductase family; nitroreductases typically reduce their substrates by using NAD(P)H as electron donor and often use FMN as a cofactor.


Pssm-ID: 380321  Cd Length: 196  Bit Score: 53.90  E-value: 5.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  42 AIYTRTSVRQYDASrAIAKDTVDMILRAAMSAPTAVNRQPWAFVVID----KREILDSL-------AEGLP------YAK 104
Cdd:cd02145     3 VIRWRRDVRHFRPD-PVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRsaatRKAVHELFqranaeaAEMYTgeraaqYRT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 105 M----LKHAPLAIIPCGDLDKA----LEGDGQAFWI-QDVSAATENMLIAANALGVGAVWTAVYPDesriDAVRKVLGMP 175
Cdd:cd02145    82 LklegIEEAPLQLAVFCDRARAgghgLGRTTMPEMDlYSSVCAVQNLWLAARAEGLGVGWVSILDP----DEVKRLLGIP 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1831108410 176 ATIMPLAVVPMGYPAGEHHpkdkwKPEnIHYNGW 209
Cdd:cd02145   158 EHWEPVAYLCIGYPEFFYD-----EPE-LEQAGW 185
PRK11053 PRK11053
oxygen-insensitive NAD(P)H nitroreductase;
40-204 3.23e-08

oxygen-insensitive NAD(P)H nitroreductase;


Pssm-ID: 182929 [Multi-domain]  Cd Length: 217  Bit Score: 51.90  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  40 LDAIYTRTSVRQYDASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVID----KREILDSLAEGLPY--AKMLkHAPLAI 113
Cdd:PRK11053    4 VSVAKKRYTTKAFDPSKKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASteegKARIAKAAAGNYAFneRKIL-DASHVV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 114 IPCG--DLD----------------------KALEGDGQAF--------------WIQD-VSAATENMLIAANALGVGAV 154
Cdd:PRK11053   83 VFCAktDMDdaylelvleqedadgrfateeaKAAQDKGRRFfadmhrkelkdlqhWMEKqVYLALGNLLLGAAALGIDAT 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831108410 155 wtavyP----DESRIDAvrkVLGMPAT-IMPLAVVPMGYPAGEHH----PKDKWKPENI 204
Cdd:PRK11053  163 -----PiegfDAAILDA---EFGLREKgLTSSVVVPLGYHSEEDFnaklPKSRLPQETI 213
PRK10765 PRK10765
oxygen-insensitive NADPH nitroreductase;
36-190 4.45e-08

oxygen-insensitive NADPH nitroreductase;


Pssm-ID: 182710  Cd Length: 240  Bit Score: 51.51  E-value: 4.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  36 SNQALDAIYTRTSVRQYdASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVI---DKREILDSLAEGLPYakmLKHAPLA 112
Cdd:PRK10765    1 MTPTIELILSHRSIRHF-TDEPISEAQREAIINAARAASSSSFLQCSSIIRItdkALREALVELTGGQKY---VAQAAEF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 113 IIPCGDLDKALE--GDGQAFW-----IQDVSAA--TENMLIAANALGVGAVWTAVYpdESRIDAVRKVLGMPATIMPLAV 183
Cdd:PRK10765   77 WVFCADFNRHLQicPDAQLGLaeqllIGAVDTAimAQNALLAAESLGLGGVYIGGL--RNNIEAVTELLKLPQHVLPLFG 154


                  ....*..
gi 1831108410 184 VPMGYPA 190
Cdd:PRK10765  155 LCLGWPA 161
FbiB_C-like cd20607
nitroreductase family domain similar to the C-terminal domain of F420:gamma-glutamyl ligase ...
 135-197 6.14e-07

nitroreductase family domain similar to the C-terminal domain of F420:gamma-glutamyl ligase FbiB; Proteins of this family catalyze the reduction of flavin or nitrocompounds using NAD(P)H as electron donor in a obligatory two-electron transfer, utilizing FMN or FAD as cofactor. They are often found to be homodimers. Mycobacterium tuberculosis FbiB, is a two-domain protein and produces F420 with predominantly 5 to 7 L-glutamate residues in the poly-gamma-glutamate tail, its C-terminal domain is homologous to FMN-dependent nitroreductases.


Pssm-ID: 380328 [Multi-domain]  Cd Length: 155  Bit Score: 47.46  E-value: 6.14e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831108410 135 VSAATENMLIAANALGVGAVWTAvypdeSRI---DAVRKVLGMPATIMPLAVVPMGYPAGEHHPKD 197
Cdd:cd20607    89 VGAAVQALLVALAVRGLGSCWIG-----STIfapDVVRDELDLPDDWEPLGAIAIGYPLEPPPPRP 149
TM1586_NiRdase pfam14512
Putative TM nitroreductase; Compared with the more traditional NADH oxidase/flavin reductase ...
 66-92 5.91e-05

Putative TM nitroreductase; Compared with the more traditional NADH oxidase/flavin reductase family, this family is a duplication, consisting of two similar domains arranged as the subunits of the dimeric NADH oxidase/flavin reductase with one conserved active site.


Pssm-ID: 405236 [Multi-domain]  Cd Length: 214  Bit Score: 42.28  E-value: 5.91e-05
                          10        20
                  ....*....|....*....|....*..
gi 1831108410  66 ILRAAMSAPTAVNRQPWAFVVIDKREI 92
Cdd:pfam14512 162 GMEAARLAPSAMNQQPWRFVLVDDNRI 188
PRK10828 PRK10828
putative oxidoreductase; Provisional
 39-155 2.00e-04

putative oxidoreductase; Provisional


Pssm-ID: 182761  Cd Length: 183  Bit Score: 40.44  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  39 ALDAIYTRTSvrqydASR----AIAKDTVDMILRAAMSAPTAVNRQPWAFVVI--DKREILDSL------AEGLPYAKML 106
Cdd:PRK10828    3 ALELLLNRRS-----ASRlaepAPTGEQLQNILRAGMRAPDHGSLQPWRFFVIegEGRERFSALleqgaiAAGSDEKAIE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410 107 K------HAPLAII---PCGDLDKALEgdgqafWIQDVSA--ATENMLIAANALGVGAVW 155
Cdd:PRK10828   78 KarnapfRAPLIITvvaKCEENHKVPR------WEQEVSAgcAVMAMQMAAVAQGFNGIW 131
PRK14851 PRK14851
hypothetical protein; Provisional
 38-171 2.24e-04

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 41.38  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  38 QALDAIYTRTSVRQYDASRA--IAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKReILDSLAEGLPYAKMLKHAPLAIIP 115
Cdd:PRK14851  301 RNTDQARVREPEPPVSVAHFdsLPQGVGDYILQAGIQAPSGDNVQPWQFALAGND-IHLYLDPEADVSFFNVRQTASIIS 379

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831108410 116 CGdldkalegdgqafwiqdvsAATENMLIAANALGVGAVwTAVYPDESRIDAVRKV 171
Cdd:PRK14851  380 CG-------------------AVMENMRIAATTFGLDAT-TQYRPDAAQEDLMATV 415
PRK14852 PRK14852
hypothetical protein; Provisional
 58-200 1.86e-03

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 38.91  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  58 IAKDTVDMILRAAMSAPTAVNRQPWAFVvidkreildslaeglPYAKMLKHaplaiipcgDLDKalEGDGQAFWIQDVS- 136
Cdd:PRK14852  611 IPLETLHYVARAAMQAPSGDNVQPWRFV---------------PHATGLHI---------HLDR--QADGSFFDYRHVAs 664

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831108410 137 -----AATENMLIAANALGVGAVwTAVYPDESRidavrkvlgmPATIMPLAVVPMGYPAGEHHPKDKWK 200
Cdd:PRK14852  665 llacgAAVQNAVYASGSAGLDAT-LSLFPDATK----------PDRVASLHCTPLGVPSHEIMTAALWR 722
PRK07877 PRK07877
Rv1355c family protein;
54-168 5.62e-03

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 37.28  E-value: 5.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831108410  54 ASRAIAKDTVDMILRAAMSAPTAVNRQPWAFVVIDKREILDslaeglpyakmlkHAPlaiipcgDLDKALEGDGQAFWIQ 133
Cdd:PRK07877  368 AAEALPQDALEIVAAAAIRAPSGGNVQPWHIEADQDRLTIR-------------LAP-------EHTSAMDVGYRGSAVA 427

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1831108410 134 dVSAATENMLIAANALGV-GAVWTAVYPDESRIDAV 168
Cdd:PRK07877  428 -VGAALFNARVAAAAHGLlGPVEFFPGDEGSPLRAT 462
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH