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Conserved domains on  [gi|492444240|ref|WP_005845890|]
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MULTISPECIES: nitroreductase family protein [Bacteroidaceae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 2-148 2.63e-83

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: 241.52  E-value: 2.63e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   2 NFLELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYSCYKRewLATAPCIIVACVDH 81
Cdd:cd20609    1 DFLELAKKRYSVRKFSDKPVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKLAKATPR--FFGAPLVIVVCYDK 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492444240  82 NESWHRRADNKDHADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGLPENLEPAVLIPVGY 148
Cdd:cd20609   79 DESWKRPYDGKDSGDIDAAIVATHMMLAATELGLGTCWVGNFDPEKVREAFNLPENLEPVAILPLGY 145
 
Name Accession Description Interval E-value
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 2-148 2.63e-83

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: 241.52  E-value: 2.63e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   2 NFLELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYSCYKRewLATAPCIIVACVDH 81
Cdd:cd20609    1 DFLELAKKRYSVRKFSDKPVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKLAKATPR--FFGAPLVIVVCYDK 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492444240  82 NESWHRRADNKDHADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGLPENLEPAVLIPVGY 148
Cdd:cd20609   79 DESWKRPYDGKDSGDIDAAIVATHMMLAATELGLGTCWVGNFDPEKVREAFNLPENLEPVAILPLGY 145
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 3-165 3.82e-60

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 183.90  E-value: 3.82e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   3 FLELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYSCYK---REWLATAPCIIVACV 79
Cdd:COG0778    1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAeanQEWVADAPVLIVVCA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  80 DHNESWHRRadnKDHADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGLPENLEPAVLIPVGYAEDEPTEKKRK 159
Cdd:COG0778   81 DPDRSEKVP---ERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEGEEPVALLALGYPAEELNPRPRK 157


                 ....*.
gi 492444240 160 PLNEIL 165
Cdd:COG0778  158 PLEEVV 163
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 7-148 1.90e-36

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: 123.66  E-value: 1.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240    7 VKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKAL-------------------------YS 61
Cdd:pfam00881   1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLaeaalelllvepaaalllllrrdanLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   62 CYKREWLATAPCIIVACVDHNESWHRRADNKDH-ADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGLPENLEP 140
Cdd:pfam00881  81 LLLQDFLRGAPVLIVITASLSTYLRKAAERAYReALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDDERL 160


                  ....*...
gi 492444240  141 AVLIPVGY 148
Cdd:pfam00881 161 VGLIAVGY 168
BluB TIGR02476
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ...
 3-165 1.28e-13

5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in cobalamin biosynthesis, is EC 1.16.8.1 (cob(II)yrinic acid a,c-diamide reductase) is now contradicted by newer work ascribing a role in 5,6-dimethylbenzimidazole (DMB) biosynthesis. The BluB protein is related to the nitroreductase family (pfam0881). [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 162875  Cd Length: 205  Bit Score: 65.54  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240    3 FLELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKA----------------------LY 60
Cdd:TIGR02476   9 VYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAvhalftranqaaaaiydgerasQY 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   61 SCYKREWLATAPC-IIVACVDHNESWHR--RADNKDHADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGLPEN 137
Cdd:TIGR02476  89 HRLKLEGIREAPVqLAVFCDDARGEGHGlgRHTMPEMLRYSVACAIQNLWLAARAEGLGVGWVSILDPDAVRRLLGVPEG 168

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 492444240  138 LEPAVLIPVGYAEDEPTE--------KKRKPLNEIL 165
Cdd:TIGR02476 169 WRLVAYLCLGWPDAFYDEpeleragwQERRPLEWRR 204
PRK11053 PRK11053
oxygen-insensitive NAD(P)H nitroreductase;
1-165 2.13e-13

oxygen-insensitive NAD(P)H nitroreductase;


Pssm-ID: 182929 [Multi-domain]  Cd Length: 217  Bit Score: 64.99  E-value: 2.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   1 MNFLELVKARYSARKY-ANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIV-TDEA---VLKAL---YScYKREWLATAP 72
Cdd:PRK11053   1 MDIVSVAKKRYTTKAFdPSKKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVAsTEEGkarIAKAAagnYA-FNERKILDAS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  73 CIIVAC--VDHNESW---------------------------------HRRaDNKDhADIDIA----IAVEHLCLAAAEQ 113
Cdd:PRK11053  80 HVVVFCakTDMDDAYlelvleqedadgrfateeakaaqdkgrrffadmHRK-ELKD-LQHWMEkqvyLALGNLLLGAAAL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492444240 114 GLGTCWVCNFDAPQCSEVLGLPEN-LEPAVLIPVGYAEDE------PteKKRKPLNEIL 165
Cdd:PRK11053 158 GIDATPIEGFDAAILDAEFGLREKgLTSSVVVPLGYHSEEdfnaklP--KSRLPQETIF 214
 
Name Accession Description Interval E-value
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 2-148 2.63e-83

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: 241.52  E-value: 2.63e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   2 NFLELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYSCYKRewLATAPCIIVACVDH 81
Cdd:cd20609    1 DFLELAKKRYSVRKFSDKPVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKLAKATPR--FFGAPLVIVVCYDK 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492444240  82 NESWHRRADNKDHADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGLPENLEPAVLIPVGY 148
Cdd:cd20609   79 DESWKRPYDGKDSGDIDAAIVATHMMLAATELGLGTCWVGNFDPEKVREAFNLPENLEPVAILPLGY 145
nitroreductase cd02139
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 3-164 1.80e-63

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: 192.30  E-value: 1.80e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   3 FLELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYS-CYKREWLATAPCIIVACVDH 81
Cdd:cd02139    1 VYEAIKKRRSIRKYKPTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELKEKLAEaANGQKFIAEAPVVIVACADP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  82 NESWHRraDNKDHADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGLPENLEPAVLIPVGYAEDEPTEKKRKPL 161
Cdd:cd02139   81 SESGMG--CGKPYYLVDVAIAMEHLVLAATEEGLGTCWIGAFDEDKVKEILGIPEEYRVVALTPLGYPAEEPPPRPRKPL 158


                 ...
gi 492444240 162 NEI 164
Cdd:cd02139  159 EEI 161
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 3-165 3.82e-60

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 183.90  E-value: 3.82e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   3 FLELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYSCYK---REWLATAPCIIVACV 79
Cdd:COG0778    1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAeanQEWVADAPVLIVVCA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  80 DHNESWHRRadnKDHADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGLPENLEPAVLIPVGYAEDEPTEKKRK 159
Cdd:COG0778   81 DPDRSEKVP---ERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEGEEPVALLALGYPAEELNPRPRK 157


                 ....*.
gi 492444240 160 PLNEIL 165
Cdd:COG0778  158 PLEEVV 163
nitroreductase cd20608
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 4-148 1.36e-47

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: 151.33  E-value: 1.36e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   4 LELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYSC--YKREWLATAPCIIVACVDH 81
Cdd:cd20608    1 FEAIKTRRSVRRFSDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTDKETLSELAKKesPSNGWLKDAPVIIVVCADP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492444240  82 NESWHRraDNKDHADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGLPENLEPAVLIPVGY 148
Cdd:cd20608   81 KDSGWL--NGQNYYLVDAAIAMQNLMLAATDLGLGTCWIGAFDEKKVKEILGIPENIRVVALTPLGY 145
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 7-148 6.59e-45

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: 144.36  E-value: 6.59e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   7 VKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYS--CYKREWLATAPCIIVACVDHNES 84
Cdd:cd02062    1 IKTRRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLAKlaAPNQKFIAGAPVVIVVVADPDKS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492444240  85 WHrradnkdHADIDIAIAVEHLCLAAAEQGLGTCWV--CNFDAPQCSEVLGLPENLEPAVLIPVGY 148
Cdd:cd02062   81 RP-------WALEDAGAAAQNLLLAAAALGLGSCWIggFDFREDKVRELLGIPENLRPVALIAIGY 139
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 7-148 1.90e-36

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: 123.66  E-value: 1.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240    7 VKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKAL-------------------------YS 61
Cdd:pfam00881   1 IRQRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLaeaalelllvepaaalllllrrdanLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   62 CYKREWLATAPCIIVACVDHNESWHRRADNKDH-ADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGLPENLEP 140
Cdd:pfam00881  81 LLLQDFLRGAPVLIVITASLSTYLRKAAERAYReALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDDERL 160


                  ....*...
gi 492444240  141 AVLIPVGY 148
Cdd:pfam00881 161 VGLIAVGY 168
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
 4-164 4.29e-35

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: 119.65  E-value: 4.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   4 LELVKARYSARKY-ANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYS-CYKREWLATAPCIIVACvdh 81
Cdd:cd02137    1 LEVIKSRRSVRNFdPDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEaAYNQPQVTTASAVILVL--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  82 neswhrradnkdhADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGLPENLEPAVLIPVGYAEDEPTEKKRKPL 161
Cdd:cd02137   78 -------------GDLNAGLAAMNLMLAAKAKGYDTCPMGGFDKEKVAELLNLPDRYVPVLLIAIGKAADKAPRSGRLPV 144


                 ...
gi 492444240 162 NEI 164
Cdd:cd02137  145 DEV 147
nitroreductase cd02151
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 5-157 3.91e-34

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: 117.25  E-value: 3.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   5 ELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYSCYKR--EWLATAPCIIVACVDHN 82
Cdd:cd02151    1 ELLKKRRSIRKYTDEPIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDKETLKKLSECKPHgsAFLKGAPAAIVVLADTE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  83 ES--WHrradnkdhadIDIAIAVEHLCLAAAEQGLGTCW--VCNFDAPQCS-------EVLGLPENLEPAVLIPVGYAED 151
Cdd:cd02151   81 KSdtWI----------EDASIAATYIQLAAESLGLGSCWiqIRNRETQDGKtaeeyvrELLGIPENYRVLCIIALGYPDE 150


                 ....*.
gi 492444240 152 EPTEKK 157
Cdd:cd02151  151 EKPPHE 156
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
 2-164 5.13e-32

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: 111.96  E-value: 5.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   2 NFLELVKARYSARKY-ANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKAL--YSCYKREWLATAPCIIVAC 78
Cdd:cd02149    1 NILELLNFRYATKKFdPNKKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLapAAWFNQPQIKDASHVVVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  79 VDhneswhrradnKDHADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGLPEN-LEPAVLIPVGYAEDEPTEKK 157
Cdd:cd02149   81 AK-----------KDWSAKQTYIALGNMLLAAAMLGIDSCPIEGFDPAKLDEILGLDEKgYKISVMVAFGYRSEEKLPKS 149


                 ....*..
gi 492444240 158 RKPLNEI 164
Cdd:cd02149  150 RKPLEDV 156
nitroreductase cd02150
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 7-158 5.53e-31

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: 109.23  E-value: 5.53e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   7 VKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKAL--YSCYkREWLATAPCIIVACVDHNES 84
Cdd:cd02150    1 ILTRRSIRKYTDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTDREKLDKIaeAHPY-GKMLKEAPLAIVVCGDPSKE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  85 WHrradnKDHADIDIAIAVEHLCLAAAEQGLGTCW---------VCNFdapqcSEVLGLPENLEPAVLIPVGYAEDEPTE 155
Cdd:cd02150   80 KA-----PGYWVQDCSAATENILLAAHALGLGAVWlgvypfeerVKAI-----REILNIPENIIPFCVIALGYPAEEKEP 149


                 ...
gi 492444240 156 KKR 158
Cdd:cd02150  150 KDR 152
PnbA_NfnB-like cd02136
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ...
 6-164 8.80e-30

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: 106.13  E-value: 8.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   6 LVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAvlkalyscykREWLAT----APCIIVACVDH 81
Cdd:cd02136    1 AIKSRRSVRAFKDKPVPKETIEKILEAARRAPSGKNTQPWRVYVVTGKA----------RERLKKaffgAPVALFLTMDK 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  82 NESWhrradnkdHADIDIAIAVEHLCLAAAEQGLGTCWVCNF--DAPQCSEVLGLPENLEPAVLIPVGYA-EDEPTEK-- 156
Cdd:cd02136   71 VLGP--------WSWFDLGAFLQNLMLAAHALGLGTCPQGALagYPDVVRKELGIPDDEELVCGIALGYPdPDAPVNQfr 142


                 ....*....
gi 492444240 157 -KRKPLNEI 164
Cdd:cd02136  143 tPREPLEEF 151
TdsD-like cd02138
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ...
 6-166 7.87e-29

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: 104.55  E-value: 7.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   6 LVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVT-DEAVLKALYSC---YKREWLATAPCIIVACVDH 81
Cdd:cd02138    1 LIAERWSPRAFSPEPISEEDLLSLFEAARWAPSCFNEQPWRFVVARrDTEAFEKLLDLlaeGNQSWAKNAPVLIVVLAKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  82 NESwhRRADNKDHADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGLPENLEPAVLIPVGYAEDEPT------- 154
Cdd:cd02138   81 EFD--HNGKPNRYALFDTGAAVANLALQATALGLVVHQMAGFDPEKAKEALGIPDEYEPITMIAIGYPGDPESlpeklle 158

                        170
                 ....*....|....*.
gi 492444240 155 -EKK---RKPLNEILL 166
Cdd:cd02138  159 rEEAprtRKPLSEIVF 174
iodotyrosine_dehalogenase cd02144
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ...
 3-164 1.73e-25

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: 96.45  E-value: 1.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   3 FLELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAV--------------------------- 55
Cdd:cd02144    1 FYELMKKRRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIkrkireaaeeeekefyekrmgeewvwd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  56 LKALYSCYKREWLATAPCIIVACVdhnESWHRRADNKD----HADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEV 131
Cdd:cd02144   81 LKPLGTNWEKPYLTEAPYLIVVFK---QKYGVLPDGKKkkhyYNEESVGIAVGILLAALHNAGLVTLTHTPSPMPFLRDL 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 492444240 132 LGLPENLEPAVLIPVGYAEDEPT--EKKRKPLNEI 164
Cdd:cd02144  158 LGRPKNEKPLLLLPVGYPAEDATvpDLKRKPLEEI 192
nitroreductase cd20610
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 7-148 8.92e-25

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: 93.88  E-value: 8.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   7 VKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYSCYK-------REW------------ 67
Cdd:cd20610    1 IKKRRSIRKFKPDPVPKEDIEKILEAANWAPSGMNRQNWEFVVVKGGEKIEKIGISIKkkneeiaRLLekvfaekpirfr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  68 --------LATAPCIIVACVDHNESWHRRadnkdHADID-IAIAVEHLCLAAAEQGLGTCWVC--NFDAPQCSEVLGLPE 136
Cdd:cd20610   81 kfrrfftlFGGAPVLVVVYTEPYKPPEER-----KPDLQsVSAAIQNLLLAAHALGLGTCWMTgpLYAEDEIEEILEIPD 155

                        170
                 ....*....|..
gi 492444240 137 NLEPAVLIPVGY 148
Cdd:cd20610  156 DKELVAVTPLGY 167
nitroreductase_FeS-like cd02143
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ...
 6-137 5.01e-24

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: 92.15  E-value: 5.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   6 LVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKAL-----------------------YSC 62
Cdd:cd02143    1 LLRSRRSIRRYKDKPVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDPEKVRRLaelvidwmrelikedpelagklfLDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  63 YKREW-------LATAPCIIVACVDHNESWhrradnkdhADIDIAIAVEHLCLAAAEQGLGTCW-----VCNFDAPQCSE 130
Cdd:cd02143   81 IVAAWekgidviLRGAPHLVVAHAPKDAPT---------PPVDCAIALTYLELAAPSLGLGTCWagfftAAANNYPPLRE 151


                 ....*..
gi 492444240 131 VLGLPEN 137
Cdd:cd02143  152 ALGLPEG 158
NfsA-like cd02146
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ...
 4-165 3.06e-23

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: 91.53  E-value: 3.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   4 LELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYS-CYKREWLATAPCIIVACVDHN 82
Cdd:cd02146    2 IETILNHRSVRKFTDEPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKLAElAGNQPYVAQAPVFLVFCADLY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  83 EswHRRADNKDHAD--------------IDIAIAVEHLCLAAAEQGLGTCWV--CNFDAPQCSEVLGLPENLEPAVLIPV 146
Cdd:cd02146   82 R--HQKIAEEAGGKdvgldylesflvgvVDAALAAQNALVAAESLGLGIVYIggIRNNPEEVIELLGLPEYVFPLFGLTV 159

                        170
                 ....*....|....*....
gi 492444240 147 GYAEDEPTEKKRKPLNEIL 165
Cdd:cd02146  160 GHPDPTPEVKPRLPLEAVV 178
nitroreductase cd03370
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ...
 5-162 7.71e-23

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: 89.30  E-value: 7.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   5 ELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYS-CYKREWLATAPCIIVACVDHNE 83
Cdd:cd03370    3 EAIESRRSIRKYTQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQLQAaAYGQAQVTSAPAVIVIYSDMED 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  84 SWHRRAD------NKDHADIDIA-----------------------IAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGL 134
Cdd:cd03370   83 ALANLEEtihpglSEERRQREAAglrgafgkmsveqrgqwglaqanIALGFLLLAAQSLGYDTSPMLGFDPEKVKALLGL 162

                        170       180
                 ....*....|....*....|....*...
gi 492444240 135 PENLEPAVLIPVGYAEDEPTEKKRKPLN 162
Cdd:cd03370  163 PEHVTIAALVALGKPAEEGYPHHRHSLE 190
TM1586_NiRdase pfam14512
Putative TM nitroreductase; Compared with the more traditional NADH oxidase/flavin reductase ...
 2-164 5.58e-14

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: 66.55  E-value: 5.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240    2 NFLELVKARYSARKYANRPVEAEKL----DYIMECVRFAPSavnfqpwRFRIVTDEavLKALYSCYKREWLATAPCIIVA 77
Cdd:pfam14512   1 NLYEAIFKRHSVRKYTDEPIPEELLeelkNAIDEINKLSGL-------NIQLVIDD--PDAFKGKAKYGKFKGVPNYIAA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   78 CvdhneswhrrADNKDHADIDIAIAVEHLCLAAAEQGLGTCWVCN-FDAPQCSEVLGLPENLepAVLIPVGYAEDEPTEK 156
Cdd:pfam14512  72 Y----------GEKDDDLLENAGYYGEQIVLYATALGLGTCWVGGtYSKSKVKAKIKKGEKL--VIVIAFGYGATKGVRA 139


                  ....*...
gi 492444240  157 KRKPLNEI 164
Cdd:pfam14512 140 KRKPLDEL 147
BluB TIGR02476
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ...
 3-165 1.28e-13

5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in cobalamin biosynthesis, is EC 1.16.8.1 (cob(II)yrinic acid a,c-diamide reductase) is now contradicted by newer work ascribing a role in 5,6-dimethylbenzimidazole (DMB) biosynthesis. The BluB protein is related to the nitroreductase family (pfam0881). [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 162875  Cd Length: 205  Bit Score: 65.54  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240    3 FLELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKA----------------------LY 60
Cdd:TIGR02476   9 VYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAvhalftranqaaaaiydgerasQY 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   61 SCYKREWLATAPC-IIVACVDHNESWHR--RADNKDHADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGLPEN 137
Cdd:TIGR02476  89 HRLKLEGIREAPVqLAVFCDDARGEGHGlgRHTMPEMLRYSVACAIQNLWLAARAEGLGVGWVSILDPDAVRRLLGVPEG 168

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 492444240  138 LEPAVLIPVGYAEDEPTE--------KKRKPLNEIL 165
Cdd:TIGR02476 169 WRLVAYLCLGWPDAFYDEpeleragwQERRPLEWRR 204
PRK11053 PRK11053
oxygen-insensitive NAD(P)H nitroreductase;
1-165 2.13e-13

oxygen-insensitive NAD(P)H nitroreductase;


Pssm-ID: 182929 [Multi-domain]  Cd Length: 217  Bit Score: 64.99  E-value: 2.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   1 MNFLELVKARYSARKY-ANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIV-TDEA---VLKAL---YScYKREWLATAP 72
Cdd:PRK11053   1 MDIVSVAKKRYTTKAFdPSKKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVAsTEEGkarIAKAAagnYA-FNERKILDAS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  73 CIIVAC--VDHNESW---------------------------------HRRaDNKDhADIDIA----IAVEHLCLAAAEQ 113
Cdd:PRK11053  80 HVVVFCakTDMDDAYlelvleqedadgrfateeakaaqdkgrrffadmHRK-ELKD-LQHWMEkqvyLALGNLLLGAAAL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492444240 114 GLGTCWVCNFDAPQCSEVLGLPEN-LEPAVLIPVGYAEDE------PteKKRKPLNEIL 165
Cdd:PRK11053 158 GIDATPIEGFDAAILDAEFGLREKgLTSSVVVPLGYHSEEdfnaklP--KSRLPQETIF 214
BluB cd02145
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ...
 5-163 6.16e-13

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: 63.53  E-value: 6.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   5 ELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKAL----------------------YSC 62
Cdd:cd02145    2 RVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVhelfqranaeaaemytgeraaqYRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  63 YKREWLATAPCIIVACVDHNESWHR---RADNKDHADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAPQCSEVLGLPENLE 139
Cdd:cd02145   82 LKLEGIEEAPLQLAVFCDRARAGGHglgRTTMPEMDLYSSVCAVQNLWLAARAEGLGVGWVSILDPDEVKRLLGIPEHWE 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 492444240 140 PAVLIPVGYAEDEPTE--------KKRKPLNE 163
Cdd:cd02145  162 PVAYLCIGYPEFFYDEpeleqagwEQRRPLEW 193
PRK13294 PRK13294
F420-0--gamma-glutamyl ligase; Provisional
 5-166 1.16e-12

F420-0--gamma-glutamyl ligase; Provisional


Pssm-ID: 183957 [Multi-domain]  Cd Length: 448  Bit Score: 64.65  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   5 ELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYSCYKREWLA--------------- 69
Cdd:PRK13294 255 EAVLLRRSVREFSDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVRTRLLDAMRDAWRAdlradglseesiarr 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  70 --------TAPCIIVACV----DHNESWHRRADnKDHADIDIAI--AVEHLCLAAAEQGLGTCWVCN--FDAPQCSEVLG 133
Cdd:PRK13294 335 vrrgdilyDAPELVVPFLvpdgAHSYPDARRTA-AERTMFTVAVgaAVQNLLVALAVEGLGSCWIGStiFAADVVRAVLD 413

                        170       180       190
                 ....*....|....*....|....*....|...
gi 492444240 134 LPENLEPAVLIPVGYAEDEPTEKKRKPLNEILL 166
Cdd:PRK13294 414 LPADWEPLGAVAIGHPAEPPGPRPPRDPGDFLV 446
YdjA-like cd02135
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ...
 4-148 1.79e-12

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: 61.47  E-value: 1.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   4 LELVKARYSARKY-ANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAvLKALYSCYK------------------ 64
Cdd:cd02135    1 LELIKTRRSIRKFkLTGAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGEG-RERLAELLAaaaaarapgadpekleka 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  65 REWLATAPCIIVACVDHNESWHRRADNKDHAdidIAIAVEHLCLAAAEQGLGTCWVCN--FDAPQCSEVLGLPENLEPAV 142
Cdd:cd02135   80 REKALRAPVVIAVVAKPDEDPKVPEWEQYAA---VGAAVQNLLLAAHALGLGAVWRTGpvTYDPAVREALGLPEDERIVG 156


                 ....*.
gi 492444240 143 LIPVGY 148
Cdd:cd02135  157 FLYLGT 162
PRK10765 PRK10765
oxygen-insensitive NADPH nitroreductase;
1-165 1.71e-11

oxygen-insensitive NADPH nitroreductase;


Pssm-ID: 182710  Cd Length: 240  Bit Score: 60.37  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   1 MN-FLELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYSCY-KREWLATAPCIIVAC 78
Cdd:PRK10765   1 MTpTIELILSHRSIRHFTDEPISEAQREAIINAARAASSSSFLQCSSIIRITDKALREALVELTgGQKYVAQAAEFWVFC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  79 VDHNEswHRRADNKDHAD---------IDIAIAVEHlCLAAAEQ-GLGTCWV---CNfDAPQCSEVLGLPENLEPAVLIP 145
Cdd:PRK10765  81 ADFNR--HLQICPDAQLGlaeqlligaVDTAIMAQN-ALLAAESlGLGGVYIgglRN-NIEAVTELLKLPQHVLPLFGLC 156

                        170       180
                 ....*....|....*....|
gi 492444240 146 VGYAEDEPTEKKRKPLNEIL 165
Cdd:PRK10765 157 LGWPAQNPDLKPRLPASLLV 176
FbiB_C-like cd20607
nitroreductase family domain similar to the C-terminal domain of F420:gamma-glutamyl ligase ...
 43-160 1.92e-09

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: 53.24  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  43 QPWRFRIVTDEAVLKALYSCYKREW-----------------------LATAPCIIVACV--DHNESW---HRRADNKDH 94
Cdd:cd20607    5 RPWRFVWLQDPAIRKELLDRMADRWeadltgdgltpeaiarrvsrgqiLYDAPEVVIPFLvpDGAHTYpdaRRTDAEHTM 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492444240  95 ADIDIAIAVEHLCLAAAEQGLGTCWVCN--FDAPQCSEVLGLPENLEPAVLIPVGYAEDEPTEKKRKP 160
Cdd:cd20607   85 FTVAVGAAVQALLVALAVRGLGSCWIGStiFAPDVVRDELDLPDDWEPLGAIAIGYPLEPPPPRPPAP 152
TM1586_NiRdase pfam14512
Putative TM nitroreductase; Compared with the more traditional NADH oxidase/flavin reductase ...
 24-52 3.09e-07

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: 48.06  E-value: 3.09e-07
                          10        20
                  ....*....|....*....|....*....
gi 492444240   24 EKLDYIMECVRFAPSAVNFQPWRFRIVTD 52
Cdd:pfam14512 157 EWFKEGMEAARLAPSAMNQQPWRFVLVDD 185
PRK05365 PRK05365
malonic semialdehyde reductase; Provisional
 9-88 1.30e-05

malonic semialdehyde reductase; Provisional


Pssm-ID: 180040 [Multi-domain]  Cd Length: 195  Bit Score: 43.26  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   9 ARySARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIV-TDEAV--LKALYSCYKREWLATAPCIIVACVDHNesW 85
Cdd:PRK05365  16 AR-THNGWLDEPVSDEQLRELYDLVKWGPTSANCSPARFVFVrSAEAKerLRPALSEGNLAKTLAAPVTAIVAYDTE--F 92


                 ...
gi 492444240  86 HRR 88
Cdd:PRK05365  93 HEH 95
RutE-like cd02148
nitroreductase similar to Escherichia coli RutE; A subfamily of the nitroreductase family ...
 9-126 1.39e-05

nitroreductase similar to Escherichia coli RutE; A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to nitroreductase. 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. RutE is involved in the utilization of uracil as the sole nitrogen source; it appears to have the same function as YdfG, which reduces malonic semialdehyde to 3-hydroxypropionic acid.


Pssm-ID: 380323 [Multi-domain]  Cd Length: 186  Bit Score: 43.01  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   9 ARySARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDEAVLKALYSCY---KREWLATAPCIIVACVDHN--E 83
Cdd:cd02148    9 AR-THNAWEDKPVSDEELRAIYDLAKWGPTAANCSPARIVFVRSAEAKERLVPHLsegNREKTMAAPVTAILAYDTEfyE 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492444240  84 SWHR----RADNKDHADIDIAIAVE-----------HLCLAAAEQGLGTCWVCNFDAP 126
Cdd:cd02148   88 HLPRlfphGDARSWFFGSGPARAEEtafrnaslqaaYFILAARALGLDCGPMSGFDAA 145
McbC_SagB-like_oxidoreductase cd02142
oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain ...
 1-147 1.52e-05

oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain of NRPS (non-ribosomal peptide synthetase) and other systems that modify polypeptides by cyclizing a thioester to form a ring. These include EpoB, part of the epothilone biosynthesis pathway; TubD, part of the tubulysin biosynthesis pathway, MtsD, part of the myxothiozol biosynthesis pathway; IndC, part of the indigoidine biosynthesis pathway and TfxB, part of the trifitoxin processing pathway. All are FMN-dependent and oxidize the product of the cyclization of thioesters in short polypeptides.


Pssm-ID: 380318  Cd Length: 200  Bit Score: 43.18  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   1 MNFLELVKARYSARKYANRPVEAEKLDYIMEC--------VRFAPSAVN----------------------FQPWRFRIV 50
Cdd:cd02142   18 LDLSEALLNRRSRRTFSSEPLTLRELSRLAARgipgsgygLRPYPSAGAlypievyvivknveglpagiyhYDPKRHRLV 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240  51 ---TDEAVLKALYSCYKREWLATAPCIIVACVDHN-ESWHRRADNKDHADIDIAIAVEHLCLAAAEQGLGTCWVCNFDAP 126
Cdd:cd02142   98 lirEGDFRLDLAHAAGNQAAFGSAAFSLIIVARFErIAWKYGERAYRYILLEAGHLAQNLYLAATALGLGLCAIGAFDDD 177

                        170       180
                 ....*....|....*....|..
gi 492444240 127 QCSEVLGLPENLEPAV-LIPVG 147
Cdd:cd02142  178 ALRELLGLDEVEEVVLyAFVVG 199
PRK10828 PRK10828
putative oxidoreductase; Provisional
 1-119 1.76e-03

putative oxidoreductase; Provisional


Pssm-ID: 182761  Cd Length: 183  Bit Score: 37.36  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492444240   1 MNFLELVKARYSARKYANRPVEAEKLDYIMECVRFAPSAVNFQPWRFRIVTDE---------------------AVLKAL 59
Cdd:PRK10828   1 MDALELLLNRRSASRLAEPAPTGEQLQNILRAGMRAPDHGSLQPWRFFVIEGEgrerfsalleqgaiaagsdekAIEKAR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492444240  60 YSCYKrewlatAPCII--VA-CVDHNE--SWHRradnkdhaDIDIAIAVEHLCLAAAEQGLGTCW 119
Cdd:PRK10828  81 NAPFR------APLIItvVAkCEENHKvpRWEQ--------EVSAGCAVMAMQMAAVAQGFNGIW 131
Frm2-like cd02140
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 3-54 4.70e-03

nitroreductase family protein; A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to nitroreductase. 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: 380317  Cd Length: 192  Bit Score: 36.13  E-value: 4.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492444240   3 FLELVKARYSARKYA-NRPVEAEKLDYIM-ECVRFAPSAVNFQPWRFRIVTDEA 54
Cdd:cd02140    1 FLEAAKARRTIYALGkNSPVSDEEIEEIVkEAVKHVPSSFNSQSSRAVILLGDE 54
 
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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