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Conserved domains on  [gi|1750305816|gb|KAA8387490|]
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5,6-dimethylbenzimidazole synthase [Acetobacter tropicalis]

Protein Classification

5,6-dimethylbenzimidazole synthase( domain architecture ID 10114863)

5,6-dimethylbenzimidazole synthase (BluB) catalyzes the oxidative fragmentation and contraction of the isoalloxazine heterocycle and the cleavage of the ribityl tail of FMNH(2) to form 5,6-dimethylbenzimidazole (DMB) and D-erythrose 4-phosphate (E4P)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BluB cd02145
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ...
 21-211 1.26e-90

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: 264.60  E-value: 1.26e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  21 DQLFTWRRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRANFARCNTQALSGHGGEDAQRYA 100
Cdd:cd02145     1 YRVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELFQRANAEAAEMYTGERAAQYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 101 TLKLAGLDDAPHQIAVFCDTAPEQGRGLGRGTMPETTVWSAVMAIHTFWLAATAQGVGVGWVSILNPQEAASTLCVNPNW 180
Cdd:cd02145    81 TLKLEGIEEAPLQLAVFCDRARAGGHGLGRTTMPEMDLYSSVCAVQNLWLAARAEGLGVGWVSILDPDEVKRLLGIPEHW 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1750305816 181 QFLAYLCVGYPQEQADTPELERKGWEQRNPA 211
Cdd:cd02145   161 EPVAYLCIGYPEFFYDEPELEQAGWEQRRPL 191
 
Name Accession Description Interval E-value
BluB cd02145
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ...
 21-211 1.26e-90

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: 264.60  E-value: 1.26e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  21 DQLFTWRRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRANFARCNTQALSGHGGEDAQRYA 100
Cdd:cd02145     1 YRVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELFQRANAEAAEMYTGERAAQYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 101 TLKLAGLDDAPHQIAVFCDTAPEQGRGLGRGTMPETTVWSAVMAIHTFWLAATAQGVGVGWVSILNPQEAASTLCVNPNW 180
Cdd:cd02145    81 TLKLEGIEEAPLQLAVFCDRARAGGHGLGRTTMPEMDLYSSVCAVQNLWLAARAEGLGVGWVSILDPDEVKRLLGIPEHW 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1750305816 181 QFLAYLCVGYPQEQADTPELERKGWEQRNPA 211
Cdd:cd02145   161 EPVAYLCIGYPEFFYDEPELEQAGWEQRRPL 191
BluB TIGR02476
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ...
 16-210 1.44e-85

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: 251.98  E-value: 1.44e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  16 FRTQLDQLFTWRRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRANFARCNTQALSGHGGED 95
Cdd:TIGR02476   5 ERAAVYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRANQAAAAIYDGER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  96 AQRYATLKLAGLDDAPHQIAVFCDTAPEQGRGLGRGTMPETTVWSAVMAIHTFWLAATAQGVGVGWVSILNPQEAASTLC 175
Cdd:TIGR02476  85 ASQYHRLKLEGIREAPVQLAVFCDDARGEGHGLGRHTMPEMLRYSVACAIQNLWLAARAEGLGVGWVSILDPDAVRRLLG 164

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1750305816 176 VNPNWQFLAYLCVGYPQEQADTPELERKGWEQRNP 210
Cdd:TIGR02476 165 VPEGWRLVAYLCLGWPDAFYDEPELERAGWQERRP 199
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 20-207 3.63e-40

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 134.98  E-value: 3.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  20 LDQLFTWRRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRANFARCNTQalsghggedaqry 99
Cdd:COG0778     1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEANQE------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 100 atlklaGLDDAPHQIAVFCDtapeqgRGLGRGTMPETTVWSAVMAIHTFWLAATAQGVGVGWVSILNPQEAASTLCVNPN 179
Cdd:COG0778    68 ------WVADAPVLIVVCAD------PDRSEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEG 135

                         170       180
                  ....*....|....*....|....*...
gi 1750305816 180 WQFLAYLCVGYPQEqaDTPELERKGWEQ 207
Cdd:COG0778   136 EEPVALLALGYPAE--ELNPRPRKPLEE 161
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 26-190 6.81e-29

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: 106.32  E-value: 6.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  26 WRRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRANFARCNT---QALSGHGGEDAQRYATL 102
Cdd:pfam00881   3 QRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLvepAAALLLLLRRDANLKLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 103 KLAGLDDAPHQIavFCDTAPEQGRGLGRGTMPETTVWSAVMAIHTFWLAATAQGVGVGWVSILNPQEAASTLCVNPNWQF 182
Cdd:pfam00881  83 LQDFLRGAPVLI--VITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDDERL 160


                  ....*...
gi 1750305816 183 LAYLCVGY 190
Cdd:pfam00881 161 VGLIAVGY 168
PRK13294 PRK13294
F420-0--gamma-glutamyl ligase; Provisional
 27-196 3.27e-08

F420-0--gamma-glutamyl ligase; Provisional


Pssm-ID: 183957 [Multi-domain]  Cd Length: 448  Bit Score: 53.09  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  27 RRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRANFARCNTQALSGHG-GEDAQRYATLKLA 105
Cdd:PRK13294  260 RRSVREFSDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVRTRLLDAMRDAWRADLRADGlSEESIARRVRRGD 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 106 GLDDAPHQIAVFCDTAPEQGRGLGRGTMPETTVWSAVM--AIHTFWLAATAQGVGVGWVS--ILNPQEAASTLCVNPNWQ 181
Cdd:PRK13294  340 ILYDAPELVVPFLVPDGAHSYPDARRTAAERTMFTVAVgaAVQNLLVALAVEGLGSCWIGstIFAADVVRAVLDLPADWE 419

                         170
                  ....*....|....*
gi 1750305816 182 FLAYLCVGYPQEQAD 196
Cdd:PRK13294  420 PLGAVAIGHPAEPPG 434
 
Name Accession Description Interval E-value
BluB cd02145
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ...
 21-211 1.26e-90

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: 264.60  E-value: 1.26e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  21 DQLFTWRRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRANFARCNTQALSGHGGEDAQRYA 100
Cdd:cd02145     1 YRVIRWRRDVRHFRPDPVPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELFQRANAEAAEMYTGERAAQYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 101 TLKLAGLDDAPHQIAVFCDTAPEQGRGLGRGTMPETTVWSAVMAIHTFWLAATAQGVGVGWVSILNPQEAASTLCVNPNW 180
Cdd:cd02145    81 TLKLEGIEEAPLQLAVFCDRARAGGHGLGRTTMPEMDLYSSVCAVQNLWLAARAEGLGVGWVSILDPDEVKRLLGIPEHW 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1750305816 181 QFLAYLCVGYPQEQADTPELERKGWEQRNPA 211
Cdd:cd02145   161 EPVAYLCIGYPEFFYDEPELEQAGWEQRRPL 191
BluB TIGR02476
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ...
 16-210 1.44e-85

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: 251.98  E-value: 1.44e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  16 FRTQLDQLFTWRRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRANFARCNTQALSGHGGED 95
Cdd:TIGR02476   5 ERAAVYRLIRERRDVRHFRSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALFTRANQAAAAIYDGER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  96 AQRYATLKLAGLDDAPHQIAVFCDTAPEQGRGLGRGTMPETTVWSAVMAIHTFWLAATAQGVGVGWVSILNPQEAASTLC 175
Cdd:TIGR02476  85 ASQYHRLKLEGIREAPVQLAVFCDDARGEGHGLGRHTMPEMLRYSVACAIQNLWLAARAEGLGVGWVSILDPDAVRRLLG 164

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1750305816 176 VNPNWQFLAYLCVGYPQEQADTPELERKGWEQRNP 210
Cdd:TIGR02476 165 VPEGWRLVAYLCLGWPDAFYDEPELERAGWQERRP 199
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 20-207 3.63e-40

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 134.98  E-value: 3.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  20 LDQLFTWRRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRANFARCNTQalsghggedaqry 99
Cdd:COG0778     1 LLELLLTRRSVRKFTDKPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAEANQE------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 100 atlklaGLDDAPHQIAVFCDtapeqgRGLGRGTMPETTVWSAVMAIHTFWLAATAQGVGVGWVSILNPQEAASTLCVNPN 179
Cdd:COG0778    68 ------WVADAPVLIVVCAD------PDRSEKVPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGLPEG 135

                         170       180
                  ....*....|....*....|....*...
gi 1750305816 180 WQFLAYLCVGYPQEqaDTPELERKGWEQ 207
Cdd:COG0778   136 EEPVALLALGYPAE--ELNPRPRKPLEE 161
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 26-190 6.81e-29

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: 106.32  E-value: 6.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  26 WRRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRANFARCNT---QALSGHGGEDAQRYATL 102
Cdd:pfam00881   3 QRRSVRKFDPEPVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLvepAAALLLLLRRDANLKLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 103 KLAGLDDAPHQIavFCDTAPEQGRGLGRGTMPETTVWSAVMAIHTFWLAATAQGVGVGWVSILNPQEAASTLCVNPNWQF 182
Cdd:pfam00881  83 LQDFLRGAPVLI--VITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDDERL 160


                  ....*...
gi 1750305816 183 LAYLCVGY 190
Cdd:pfam00881 161 VGLIAVGY 168
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 27-190 7.42e-23

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: 89.66  E-value: 7.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  27 RRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIrANFARCNTQALSGhggedaqryatlklag 106
Cdd:cd02062     4 RRSIRKFTDKPVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKL-AKLAAPNQKFIAG---------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 107 lddAPHQIAVFCDTAPEQGRGLgrgtmpettvWSAVMAIHTFWLAATAQGVGVGWVSILNPQEAA--STLCVNPNWQFLA 184
Cdd:cd02062    67 ---APVVIVVVADPDKSRPWAL----------EDAGAAAQNLLLAAAALGLGSCWIGGFDFREDKvrELLGIPENLRPVA 133


                  ....*.
gi 1750305816 185 YLCVGY 190
Cdd:cd02062   134 LIAIGY 139
YdjA-like cd02135
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ...
 27-190 7.74e-19

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: 79.95  E-value: 7.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  27 RRDVRHFR-TDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEH--ADRRAAIRANFARCNTQALSGHGGEDAQRYATlk 103
Cdd:cd02135     7 RRSIRKFKlTGAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGegRERLAELLAAAAAARAPGADPEKLEKAREKAL-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 104 lagldDAPHQIAVFCDTAPeqgrglgRGTMPETTVWSAV-MAIHTFWLAATAQGVGVGWVS--ILNPQEAASTLCVNPNW 180
Cdd:cd02135    85 -----RAPVVIAVVAKPDE-------DPKVPEWEQYAAVgAAVQNLLLAAHALGLGAVWRTgpVTYDPAVREALGLPEDE 152

                         170
                  ....*....|
gi 1750305816 181 QFLAYLCVGY 190
Cdd:cd02135   153 RIVGFLYLGT 162
iodotyrosine_dehalogenase cd02144
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ...
 27-207 2.46e-17

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: 76.42  E-value: 2.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  27 RRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRA--------NFARCNTQalsghggedaQR 98
Cdd:cd02144     8 RRSVRDFSSEPVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRKIREaaeeeekeFYEKRMGE----------EW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  99 YATLKLAG-------LDDAPHQIAVFCDTAPEQGRGLGRGTM-PETTVWSAV----MAIHTfwlaataqgvgVGWVSI-- 164
Cdd:cd02144    78 VWDLKPLGtnwekpyLTEAPYLIVVFKQKYGVLPDGKKKKHYyNEESVGIAVgillAALHN-----------AGLVTLth 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1750305816 165 --LNPQEAASTLCVNPNWQFLAYLCVGYPQEQADTPELERKGWEQ 207
Cdd:cd02144   147 tpSPMPFLRDLLGRPKNEKPLLLLPVGYPAEDATVPDLKRKPLEE 191
nitroreductase cd20608
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 27-190 5.36e-15

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: 69.29  E-value: 5.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  27 RRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRANFARCNTqalsghggedaqryatlklaG 106
Cdd:cd20608     7 RRSVRRFSDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTDKETLSELAKKESPSNG--------------------W 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 107 LDDAPHQIAVfCDTAPEQGRGLGRGTMpettVWSAVMAIHTFWLAATAQGVGVGWVSILNPQEAASTLCVNPNWQFLAYL 186
Cdd:cd20608    67 LKDAPVIIVV-CADPKDSGWLNGQNYY----LVDAAIAMQNLMLAATDLGLGTCWIGAFDEKKVKEILGIPENIRVVALT 141


                  ....
gi 1750305816 187 CVGY 190
Cdd:cd20608   142 PLGY 145
nitroreductase cd02151
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 27-194 1.18e-12

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: 63.32  E-value: 1.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  27 RRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVehaDRRAAIRanfarcntqALSghggeDAQRYATLKLAg 106
Cdd:cd02151     6 RRSIRKYTDEPIEEEKLEEILEAALLAPSSRNSRPVEFIVV---DDKETLK---------KLS-----ECKPHGSAFLK- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 107 ldDAPHQIAVFCDTApeqgrglgrgtmpETTVW---SAVMAIHtFWLAATAQGVGVGWVSILN-----PQEAA----STL 174
Cdd:cd02151    68 --GAPAAIVVLADTE-------------KSDTWiedASIAATY-IQLAAESLGLGSCWIQIRNretqdGKTAEeyvrELL 131

                         170       180
                  ....*....|....*....|
gi 1750305816 175 CVNPNWQFLAYLCVGYPQEQ 194
Cdd:cd02151   132 GIPENYRVLCIIALGYPDEE 151
nitroreductase cd02139
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 27-194 1.31e-12

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: 63.26  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  27 RRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRanfARCNTQalsghggedaqryatlklAG 106
Cdd:cd02139     8 RRSIRKYKPTPVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELKEKLA---EAANGQ------------------KF 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 107 LDDAPHqIAVFCdtAPEQGRGLGRGtMPETTVWSAvMAIHTFWLAATAQGVGVGWVSILNPQEAASTLCVNPNWQFLAYL 186
Cdd:cd02139    67 IAEAPV-VIVAC--ADPSESGMGCG-KPYYLVDVA-IAMEHLVLAATEEGLGTCWIGAFDEDKVKEILGIPEEYRVVALT 141


                  ....*...
gi 1750305816 187 CVGYPQEQ 194
Cdd:cd02139   142 PLGYPAEE 149
PnbA_NfnB-like cd02136
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ...
 27-196 4.29e-11

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: 58.75  E-value: 4.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  27 RRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVrvehadrraairanfarcntqALSGHGGEdaqryaTLKLAG 106
Cdd:cd02136     5 RRSVRAFKDKPVPKETIEKILEAARRAPSGKNTQPWRVY---------------------VVTGKARE------RLKKAF 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 107 LdDAPHQIAVFCDTAPEQgrglgrgtmpettvWSAV---MAIHTFWLAATAQGVGVGW-VSILN-PQEAASTLCVNPNWQ 181
Cdd:cd02136    58 F-GAPVALFLTMDKVLGP--------------WSWFdlgAFLQNLMLAAHALGLGTCPqGALAGyPDVVRKELGIPDDEE 122

                         170
                  ....*....|....*
gi 1750305816 182 FLAYLCVGYPQEQAD 196
Cdd:cd02136   123 LVCGIALGYPDPDAP 137
nitroreductase cd02150
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 27-194 1.64e-09

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: 54.53  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  27 RRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEhaDRRAAIRAnfarcntqalsghggEDAQRYATLklag 106
Cdd:cd02150     4 RRSIRKYTDKPVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVT--DREKLDKI---------------AEAHPYGKM---- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 107 LDDAPHQIAVFCDTAPEQGRGLgrgtmpettvW----SAvmAIHTFWLAATAQGVGVGWVSIlNPQEAA-----STLCVN 177
Cdd:cd02150    63 LKEAPLAIVVCGDPSKEKAPGY----------WvqdcSA--ATENILLAAHALGLGAVWLGV-YPFEERvkairEILNIP 129

                         170
                  ....*....|....*..
gi 1750305816 178 PNWQFLAYLCVGYPQEQ 194
Cdd:cd02150   130 ENIIPFCVIALGYPAEE 146
PRK13294 PRK13294
F420-0--gamma-glutamyl ligase; Provisional
 27-196 3.27e-08

F420-0--gamma-glutamyl ligase; Provisional


Pssm-ID: 183957 [Multi-domain]  Cd Length: 448  Bit Score: 53.09  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  27 RRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRANFARCNTQALSGHG-GEDAQRYATLKLA 105
Cdd:PRK13294  260 RRSVREFSDDPVDPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVRTRLLDAMRDAWRADLRADGlSEESIARRVRRGD 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 106 GLDDAPHQIAVFCDTAPEQGRGLGRGTMPETTVWSAVM--AIHTFWLAATAQGVGVGWVS--ILNPQEAASTLCVNPNWQ 181
Cdd:PRK13294  340 ILYDAPELVVPFLVPDGAHSYPDARRTAAERTMFTVAVgaAVQNLLVALAVEGLGSCWIGstIFAADVVRAVLDLPADWE 419

                         170
                  ....*....|....*
gi 1750305816 182 FLAYLCVGYPQEQAD 196
Cdd:PRK13294  420 PLGAVAIGHPAEPPG 434
nitroreductase_FeS-like cd02143
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ...
 27-215 9.38e-08

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: 50.16  E-value: 9.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  27 RRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHAD---RRAAIRANFARcnTQALSGHGGEDAQRYATLK 103
Cdd:cd02143     5 RRSIRRYKDKPVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDPEkvrRLAELVIDWMR--ELIKEDPELAGKLFLDGIV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 104 LA---GLD----DAPHQIAVfcdTAPEQGRglgrgtMPETtvwSAVMAIHTFWLAATAQGVGVGWVSILnpQEAAST--- 173
Cdd:cd02143    83 AAwekGIDvilrGAPHLVVA---HAPKDAP------TPPV---DCAIALTYLELAAPSLGLGTCWAGFF--TAAANNypp 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1750305816 174 ----LCVNPNWQFLAYLCVGYPQEQ-ADTPelerkgweQRNPARRQW 215
Cdd:cd02143   149 lreaLGLPEGHKVGGAMMLGYPKYKyHRIP--------PRKPARVTW 187
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
 27-195 2.38e-07

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: 48.39  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  27 RRDVRHFRTD-PVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRANfarCNTQalsghggedaqryatlklA 105
Cdd:cd02137     7 RRSVRNFDPDhKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEA---AYNQ------------------P 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 106 GLDDAPHQIAVFCDTapeqgrglgrgtmpettvwSAVMAIHTFWLAATAQGVGVGWVSILNPQEAASTLCVNPNWQFLAY 185
Cdd:cd02137    66 QVTTASAVILVLGDL-------------------NAGLAAMNLMLAAKAKGYDTCPMGGFDKEKVAELLNLPDRYVPVLL 126

                         170
                  ....*....|
gi 1750305816 186 LCVGYPQEQA 195
Cdd:cd02137   127 IAIGKAADKA 136
nitroreductase cd03370
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ...
 27-78 4.00e-07

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: 48.47  E-value: 4.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1750305816  27 RRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRA 78
Cdd:cd03370     8 RRSIRKYTQEPVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQLQA 59
nitroreductase cd20610
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 27-161 1.42e-06

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: 46.50  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  27 RRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRR----AAIRA---NFARCNTQALSGHGGEDAQ-- 97
Cdd:cd20610     4 RRSIRKFKPDPVPKEDIEKILEAANWAPSGMNRQNWEFVVVKGGEKIekigISIKKkneEIARLLEKVFAEKPIRFRKfr 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1750305816  98 RYATLklagLDDAPHQIAVFCDTAPEQGRglgrgtmPETTVWSAVMAIHTFWLAATAQGVGVGW 161
Cdd:cd20610    84 RFFTL----FGGAPVLVVVYTEPYKPPEE-------RKPDLQSVSAAIQNLLLAAHALGLGTCW 136
NfsA-like cd02146
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ...
 27-196 4.12e-06

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: 46.08  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  27 RRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIrANFARCntqalsghggedaQRYatlklag 106
Cdd:cd02146     8 HRSVRKFTDEPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKL-AELAGN-------------QPY------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 107 LDDAPHqIAVFC-DT------APEQGRGLGR-GTMPETTVWS--AVMAIHTFWLAATAQGVGVGWV-SILNPQEAASTLC 175
Cdd:cd02146    67 VAQAPV-FLVFCaDLyrhqkiAEEAGGKDVGlDYLESFLVGVvdAALAAQNALVAAESLGLGIVYIgGIRNNPEEVIELL 145

                         170       180
                  ....*....|....*....|..
gi 1750305816 176 VNPNWQF-LAYLCVGYPQEQAD 196
Cdd:cd02146   146 GLPEYVFpLFGLTVGHPDPTPE 167
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
 19-78 4.59e-06

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: 44.93  E-value: 4.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1750305816  19 QLDQLFTWRRDVRHFrtDP---VPDAVLDHLLHTACLSPS-VGLsEPWRFVRVEHADRRAAIRA 78
Cdd:cd02149     1 NILELLNFRYATKKF--DPnkkISDEDLETILEALRLSPSsFGL-EPWKFLVVENPELKAKLAP 61
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 27-190 1.82e-05

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: 43.15  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  27 RRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRAAIRAnfarcntqalsghggedaqryATLKLAG 106
Cdd:cd20609     9 RYSVRKFSDKPVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKLAK---------------------ATPRFFG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 107 lddAPHQIAVFCDTAPEQGRGLGRGTMPETTVwSAVMAiHtFWLAATAQGVGVGWVSILNPQEAASTLCVNPNWQFLAYL 186
Cdd:cd20609    68 ---APLVIVVCYDKDESWKRPYDGKDSGDIDA-AIVAT-H-MMLAATELGLGTCWVGNFDPEKVREAFNLPENLEPVAIL 141


                  ....
gi 1750305816 187 CVGY 190
Cdd:cd20609   142 PLGY 145
TdsD-like cd02138
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ...
 23-210 5.44e-04

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: 39.45  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  23 LFTWRRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVrveHADRRAAIRANFArcntQALSGHGgedaQRYAtl 102
Cdd:cd02138     1 LIAERWSPRAFSPEPISEEDLLSLFEAARWAPSCFNEQPWRFV---VARRDTEAFEKLL----DLLAEGN----QSWA-- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816 103 klaglDDAPHQIAVFCDTA-PEQGRG-------LGrgtmpettvwSAVMAihtFWLAATAQGVGV----GWvsilNPQEA 170
Cdd:cd02138    68 -----KNAPVLIVVLAKTEfDHNGKPnryalfdTG----------AAVAN---LALQATALGLVVhqmaGF----DPEKA 125

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1750305816 171 ASTLCVNPNWQFLAYLCVGYPQEQADTPELERKGWEQRNP 210
Cdd:cd02138   126 KEALGIPDEYEPITMIAIGYPGDPESLPEKLLEREEAPRT 165
FbiB_C-like cd20607
nitroreductase family domain similar to the C-terminal domain of F420:gamma-glutamyl ligase ...
 59-196 8.10e-04

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: 38.61  E-value: 8.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750305816  59 SEPWRFVRVEHADRRAAIRANFARCNTQALSGHG--GEDAQRYATlKLAGLDDAPHQIAVF-----CDTAPEQGRGLGRG 131
Cdd:cd20607     4 TRPWRFVWLQDPAIRKELLDRMADRWEADLTGDGltPEAIARRVS-RGQILYDAPEVVIPFlvpdgAHTYPDARRTDAEH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1750305816 132 TMPETTVWSAVMAihtFWLAATAQGVGVGWVS--ILNPQEAASTLCVNPNWQFLAYLCVGYPQEQAD 196
Cdd:cd20607    83 TMFTVAVGAAVQA---LLVALAVRGLGSCWIGstIFAPDVVRDELDLPDDWEPLGAIAIGYPLEPPP 146
PRK05365 PRK05365
malonic semialdehyde reductase; Provisional
 20-74 2.33e-03

malonic semialdehyde reductase; Provisional


Pssm-ID: 180040 [Multi-domain]  Cd Length: 195  Bit Score: 37.49  E-value: 2.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1750305816  20 LDQLFTWRRDVRHFRTDPVPDAVLDHLLHTACLSPSVGLSEPWRFVRVEHADRRA 74
Cdd:PRK05365    9 LDQLFTEARTHNGWLDEPVSDEQLRELYDLVKWGPTSANCSPARFVFVRSAEAKE 63
 
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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