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Conserved domains on  [gi|523838760|gb|AGR02626|]
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NAD(P)H nitroreductase [Listeria monocytogenes]

Protein Classification

nitroreductase family protein( domain architecture ID 10114825)

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

CATH:  3.40.109.10
EC:  1.7.1.-
Gene Ontology:  GO:0016491
PubMed:  25702712|7601851|29078300
SCOP:  3001947

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
 9-206 1.23e-58

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: 181.28  E-value: 1.23e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   9 EDLMKNRRSIREYDETVKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVrFNTRQNESSSAMILVFGD 88
Cdd:cd02137    1 LEVIKSRRSVRNFDPDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAA-YNQPQVTTASAVILVLGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  89 LqnfengekiygesverglmpaevkeqqmaklsqyfasiprseaervvliDGGIVAMQLMLVARAHGYDTNPIGGFERTE 168
Cdd:cd02137   80 L-------------------------------------------------NAGLAAMNLMLAAKAKGYDTCPMGGFDKEK 110

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 523838760 169 VAEAFNMdPERYVPVMIVSIGKAKNSGYQSYRLPITDV 206
Cdd:cd02137  111 VAELLNL-PDRYVPVLLIAIGKAADKAPRSGRLPVDEV 147
 
Name Accession Description Interval E-value
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
 9-206 1.23e-58

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: 181.28  E-value: 1.23e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   9 EDLMKNRRSIREYDETVKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVrFNTRQNESSSAMILVFGD 88
Cdd:cd02137    1 LEVIKSRRSVRNFDPDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAA-YNQPQVTTASAVILVLGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  89 LqnfengekiygesverglmpaevkeqqmaklsqyfasiprseaervvliDGGIVAMQLMLVARAHGYDTNPIGGFERTE 168
Cdd:cd02137   80 L-------------------------------------------------NAGLAAMNLMLAAKAKGYDTCPMGGFDKEK 110

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 523838760 169 VAEAFNMdPERYVPVMIVSIGKAKNSGYQSYRLPITDV 206
Cdd:cd02137  111 VAELLNL-PDRYVPVLLIAIGKAADKAPRSGRLPVDEV 147
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 8-207 3.57e-48

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 155.01  E-value: 3.57e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   8 FEDLMKNRRSIREYDETvKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVR-FNTRQNESSSAMILVF 86
Cdd:COG0778    1 LLELLLTRRSVRKFTDK-PVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAeANQEWVADAPVLIVVC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  87 GDLQNFENgekiygesverglmpaevkeqqmaklsqyfasiprsEAERVVLIDGGIVAMQLMLVARAHGYDTNPIGGFER 166
Cdd:COG0778   80 ADPDRSEK------------------------------------VPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDP 123

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 523838760 167 TEVAEAFNMdPERYVPVMIVSIGKAKNSGYQSYRLPITDVT 207
Cdd:COG0778  124 EKVRELLGL-PEGEEPVALLALGYPAEELNPRPRKPLEEVV 163
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 12-190 4.73e-32

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: 114.03  E-value: 4.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   12 MKNRRSIREYDETvKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVRFNTRQNESSSAMILVFGDLQN 91
Cdd:pfam00881   1 IRQRRSVRKFDPE-PVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAALLLLLRRDANL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   92 FENGEKIYGESverglmPAEVkeqQMAKLSQYFASIPRSEAERVVLIDGGIVAMQLMLVARAHGYDTNPIGGFERTEVAE 171
Cdd:pfam00881  80 KLLLQDFLRGA------PVLI---VITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRE 150

                         170
                  ....*....|....*....
gi 523838760  172 AFNMdPERYVPVMIVSIGK 190
Cdd:pfam00881 151 LLGL-PDDERLVGLIAVGY 168
PRK11053 PRK11053
oxygen-insensitive NAD(P)H nitroreductase;
7-209 2.92e-18

oxygen-insensitive NAD(P)H nitroreductase;


Pssm-ID: 182929 [Multi-domain]  Cd Length: 217  Bit Score: 79.24  E-value: 2.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   7 DFEDLMKNRRSIREYDETVKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVR----FNTRQNESSSaM 82
Cdd:PRK11053   2 DIVSVAKKRYTTKAFDPSKKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASTEEGKARIAKAAAgnyaFNERKILDAS-H 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  83 ILVF---GDLQNfENGEKIYGESVERGLMPAEVKEQQMAKLSQYFASIPRSE-------AERVVLIDGGivamQLMLVAR 152
Cdd:PRK11053  81 VVVFcakTDMDD-AYLELVLEQEDADGRFATEEAKAAQDKGRRFFADMHRKElkdlqhwMEKQVYLALG----NLLLGAA 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523838760 153 AHGYDTNPIGGFERTEVAEAFNMDPERYVPVMIVSIGKAK----NSGYQSYRLPITDVTTF 209
Cdd:PRK11053 156 ALGIDATPIEGFDAAILDAEFGLREKGLTSSVVVPLGYHSeedfNAKLPKSRLPQETIFTE 216
BluB TIGR02476
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ...
 8-189 6.29e-10

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: 56.68  E-value: 6.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760    8 FEDLMKNRRSIREYdETVKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVrfnTRQNESSSAMilvFG 87
Cdd:TIGR02476   9 VYRLIRERRDVRHF-RSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALF---TRANQAAAAI---YD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   88 DLQnfengEKIYGESVERGLMPAEVK------EQQMAKLSQYFASIPRSEAERVVLidggivAMQLM-LVARAHGYDTNP 160
Cdd:TIGR02476  82 GER-----ASQYHRLKLEGIREAPVQlavfcdDARGEGHGLGRHTMPEMLRYSVAC------AIQNLwLAARAEGLGVGW 150

                         170       180
                  ....*....|....*....|....*....
gi 523838760  161 IGGFERTEVAEAFNMdPERYVPVMIVSIG 189
Cdd:TIGR02476 151 VSILDPDAVRRLLGV-PEGWRLVAYLCLG 178
 
Name Accession Description Interval E-value
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
 9-206 1.23e-58

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: 181.28  E-value: 1.23e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   9 EDLMKNRRSIREYDETVKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVrFNTRQNESSSAMILVFGD 88
Cdd:cd02137    1 LEVIKSRRSVRNFDPDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAA-YNQPQVTTASAVILVLGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  89 LqnfengekiygesverglmpaevkeqqmaklsqyfasiprseaervvliDGGIVAMQLMLVARAHGYDTNPIGGFERTE 168
Cdd:cd02137   80 L-------------------------------------------------NAGLAAMNLMLAAKAKGYDTCPMGGFDKEK 110

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 523838760 169 VAEAFNMdPERYVPVMIVSIGKAKNSGYQSYRLPITDV 206
Cdd:cd02137  111 VAELLNL-PDRYVPVLLIAIGKAADKAPRSGRLPVDEV 147
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 8-207 3.57e-48

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 155.01  E-value: 3.57e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   8 FEDLMKNRRSIREYDETvKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVR-FNTRQNESSSAMILVF 86
Cdd:COG0778    1 LLELLLTRRSVRKFTDK-PVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEALAeANQEWVADAPVLIVVC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  87 GDLQNFENgekiygesverglmpaevkeqqmaklsqyfasiprsEAERVVLIDGGIVAMQLMLVARAHGYDTNPIGGFER 166
Cdd:COG0778   80 ADPDRSEK------------------------------------VPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDP 123

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 523838760 167 TEVAEAFNMdPERYVPVMIVSIGKAKNSGYQSYRLPITDVT 207
Cdd:COG0778  124 EKVRELLGL-PEGEEPVALLALGYPAEELNPRPRKPLEEVV 163
nitroreductase cd03370
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ...
 12-203 5.13e-35

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: 122.43  E-value: 5.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  12 MKNRRSIREY-DETvkISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSlVRFNTRQNESSSAMILVFGD-- 88
Cdd:cd03370    5 IESRRSIRKYtQEP--VPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQLQA-AAYGQAQVTSAPAVIVIYSDme 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  89 --LQNFEngekiygESVERGlMPAEVKEQQMAKLSQYFASIPRSEAERVVLIDGGIVAMQLMLVARAHGYDTNPIGGFER 166
Cdd:cd03370   82 daLANLE-------ETIHPG-LSEERRQREAAGLRGAFGKMSVEQRGQWGLAQANIALGFLLLAAQSLGYDTSPMLGFDP 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 523838760 167 TEVAEAFNMdPERYVPVMIVSIGKAKNSGYQSYRLPI 203
Cdd:cd03370  154 EKVKALLGL-PEHVTIAALVALGKPAEEGYPHHRHSL 189
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
 7-206 3.67e-33

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: 116.58  E-value: 3.67e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   7 DFEDLMKNRRSIREYDETVKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVRFNTRQNESSSAMILVF 86
Cdd:cd02149    1 NILELLNFRYATKKFDPNKKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLAPAAWFNQPQIKDASHVVVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  87 GDlqnfengeKIYgesverglmpaevkeqqmAKLSQYFAsiprseaervvlidggivAMQLMLVARAHGYDTNPIGGFER 166
Cdd:cd02149   81 AK--------KDW------------------SAKQTYIA------------------LGNMLLAAAMLGIDSCPIEGFDP 116

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 523838760 167 TEVAEAFNMDPERYVPVMIVSIGKAKNSGYQSYRLPITDV 206
Cdd:cd02149  117 AKLDEILGLDEKGYKISVMVAFGYRSEEKLPKSRKPLEDV 156
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 12-190 4.73e-32

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: 114.03  E-value: 4.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   12 MKNRRSIREYDETvKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVRFNTRQNESSSAMILVFGDLQN 91
Cdd:pfam00881   1 IRQRRSVRKFDPE-PVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAALLLLLRRDANL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   92 FENGEKIYGESverglmPAEVkeqQMAKLSQYFASIPRSEAERVVLIDGGIVAMQLMLVARAHGYDTNPIGGFERTEVAE 171
Cdd:pfam00881  80 KLLLQDFLRGA------PVLI---VITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRE 150

                         170
                  ....*....|....*....
gi 523838760  172 AFNMdPERYVPVMIVSIGK 190
Cdd:pfam00881 151 LLGL-PDDERLVGLIAVGY 168
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 7-189 7.43e-30

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: 107.47  E-value: 7.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   7 DFEDLMKNRRSIREYDETvKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLvrfnTRQNESSSAMILVF 86
Cdd:cd20609    1 DFLELAKKRYSVRKFSDK-PVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKLAKA----TPRFFGAPLVIVVC 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  87 GDLQN---FENGEKIYGEsverglmpaevkeqqmaklsqyfasiprseaervvlIDGGIVAMQLMLVARAHGYDTNPIGG 163
Cdd:cd20609   76 YDKDEswkRPYDGKDSGD------------------------------------IDAAIVATHMMLAATELGLGTCWVGN 119

                        170       180
                 ....*....|....*....|....*.
gi 523838760 164 FERTEVAEAFNMdPERYVPVMIVSIG 189
Cdd:cd20609  120 FDPEKVREAFNL-PENLEPVAILPLG 144
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 12-189 1.99e-29

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: 106.23  E-value: 1.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  12 MKNRRSIREYDETvKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVRFNTRQNESSSAMILVFGDlqn 91
Cdd:cd02062    1 IKTRRSIRKFTDK-PVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLAKLAAPNQKFIAGAPVVIVVVAD--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  92 fengekiygesverglmpaevkeqqmaklsqyfasipRSEAERVVLIDGGIVAMQLMLVARAHGYDTNPIGGFERTE--V 169
Cdd:cd02062   77 -------------------------------------PDKSRPWALEDAGAAAQNLLLAAAALGLGSCWIGGFDFREdkV 119

                        170       180
                 ....*....|....*....|
gi 523838760 170 AEAFNMdPERYVPVMIVSIG 189
Cdd:cd02062  120 RELLGI-PENLRPVALIAIG 138
TdsD-like cd02138
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ...
 11-190 3.60e-26

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: 99.16  E-value: 3.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  11 LMKNRRSIREYDETvKISQEEMKAILEDAVTAPSSVNMQPWRFVVV-ESDAGKEKL-SSLVRFNTRQNESSSAMILVFGD 88
Cdd:cd02138    1 LIAERWSPRAFSPE-PISEEDLLSLFEAARWAPSCFNEQPWRFVVArRDTEAFEKLlDLLAEGNQSWAKNAPVLIVVLAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  89 lQNFENGEKiygesverglmpaevkeqqmaklsqyfasiPRseaeRVVLIDGGIVAMQLMLVARAHGYDTNPIGGFERTE 168
Cdd:cd02138   80 -TEFDHNGK------------------------------PN----RYALFDTGAAVANLALQATALGLVVHQMAGFDPEK 124

                        170       180
                 ....*....|....*....|..
gi 523838760 169 VAEAFNMdPERYVPVMIVSIGK 190
Cdd:cd02138  125 AKEALGI-PDEYEPITMIAIGY 145
PnbA_NfnB-like cd02136
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ...
 11-207 8.66e-20

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: 81.87  E-value: 8.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  11 LMKNRRSIREYDETvKISQEEMKAILEDAVTAPSSVNMQPWRFVVVeSDAGKEKLSSLVrfntrqnesssamilvfgdlq 90
Cdd:cd02136    1 AIKSRRSVRAFKDK-PVPKETIEKILEAARRAPSGKNTQPWRVYVV-TGKARERLKKAF--------------------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  91 nfengekiYGESVerglmpaevkeqqmaklsQYFASIPRSEAERVVLiDGGIVAMQLMLVARAHGYDTNPIGGF--ERTE 168
Cdd:cd02136   58 --------FGAPV------------------ALFLTMDKVLGPWSWF-DLGAFLQNLMLAAHALGLGTCPQGALagYPDV 110

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 523838760 169 VAEAFNMdPERYVPVMIVSIG----KAKNSGYQSYRLPITDVT 207
Cdd:cd02136  111 VRKELGI-PDDEELVCGIALGypdpDAPVNQFRTPREPLEEFV 152
PRK11053 PRK11053
oxygen-insensitive NAD(P)H nitroreductase;
7-209 2.92e-18

oxygen-insensitive NAD(P)H nitroreductase;


Pssm-ID: 182929 [Multi-domain]  Cd Length: 217  Bit Score: 79.24  E-value: 2.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   7 DFEDLMKNRRSIREYDETVKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVR----FNTRQNESSSaM 82
Cdd:PRK11053   2 DIVSVAKKRYTTKAFDPSKKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASTEEGKARIAKAAAgnyaFNERKILDAS-H 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  83 ILVF---GDLQNfENGEKIYGESVERGLMPAEVKEQQMAKLSQYFASIPRSE-------AERVVLIDGGivamQLMLVAR 152
Cdd:PRK11053  81 VVVFcakTDMDD-AYLELVLEQEDADGRFATEEAKAAQDKGRRFFADMHRKElkdlqhwMEKQVYLALG----NLLLGAA 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523838760 153 AHGYDTNPIGGFERTEVAEAFNMDPERYVPVMIVSIGKAK----NSGYQSYRLPITDVTTF 209
Cdd:PRK11053 156 ALGIDATPIEGFDAAILDAEFGLREKGLTSSVVVPLGYHSeedfNAKLPKSRLPQETIFTE 216
nitroreductase cd02151
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 10-190 1.37e-17

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: 76.03  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  10 DLMKNRRSIREYDETvKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVRFNTRQNESSSAMILVFGDl 89
Cdd:cd02151    1 ELLKKRRSIRKYTDE-PIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDKETLKKLSECKPHGSAFLKGAPAAIVVLAD- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  90 qnfengekiygesverglmpaevkeqqmaklsqyfasiprSEAERVVLIDGGIVAMQLMLVARAHGYDTNPIGGFERT-- 167
Cdd:cd02151   79 ----------------------------------------TEKSDTWIEDASIAATYIQLAAESLGLGSCWIQIRNREtq 118

                        170       180       190
                 ....*....|....*....|....*....|
gi 523838760 168 -------EVAEAFNMdPERYVPVMIVSIGK 190
Cdd:cd02151  119 dgktaeeYVRELLGI-PENYRVLCIIALGY 147
nitroreductase cd02139
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 8-189 8.10e-17

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: 74.43  E-value: 8.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   8 FEDLMKNRRSIREYDETvKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVRfNTRQNESSSAMILVFG 87
Cdd:cd02139    1 VYEAIKKRRSIRKYKPT-PVEEEKLLRILEAARLAPSAKNRQPWRFIVVKDKELKEKLAEAAN-GQKFIAEAPVVIVACA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  88 DLQnfengekiygESVERGLMPAevkeqqmaklsqYfasiprseaervvLIDGGIvAMQ-LMLVARAHGYDTNPIGGFER 166
Cdd:cd02139   79 DPS----------ESGMGCGKPY------------Y-------------LVDVAI-AMEhLVLAATEEGLGTCWIGAFDE 122

                        170       180
                 ....*....|....*....|...
gi 523838760 167 TEVAEAFNMdPERYVPVMIVSIG 189
Cdd:cd02139  123 DKVKEILGI-PEEYRVVALTPLG 144
nitroreductase cd20608
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 13-185 1.52e-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: 70.44  E-value: 1.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  13 KNRRSIREYDETvKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESdagKEKLSSLVRFNTRQNE---SSSAMILVFGDl 89
Cdd:cd20608    5 KTRRSVRRFSDK-PVEEEKLEKILEAARLAPSWANKQCWRFIVVTD---KETLSELAKKESPSNGwlkDAPVIIVVCAD- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  90 qnfengekiygesverglmPAEVKEqqMAKLSQYfasiprseaervvLIDGGIVAMQLMLVARAHGYDTNPIGGFERTEV 169
Cdd:cd20608   80 -------------------PKDSGW--LNGQNYY-------------LVDAAIAMQNLMLAATDLGLGTCWIGAFDEKKV 125

                        170
                 ....*....|....*.
gi 523838760 170 AEAFNMDPERYVPVMI 185
Cdd:cd20608  126 KEILGIPENIRVVALT 141
nitroreductase cd02150
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 13-189 2.55e-15

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: 69.94  E-value: 2.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  13 KNRRSIREYDETvKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESdagKEKLSSLVRFN--TRQNESSSAMILVFGDLQ 90
Cdd:cd02150    2 LTRRSIRKYTDK-PVEEEDIEKLLRAAMAAPSAGNQQPWHFIVVTD---REKLDKIAEAHpyGKMLKEAPLAIVVCGDPS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  91 nfenGEKIYGESVErglmpaevkeqqmaklsqyfasiprseaervvliDGGIVAMQLMLVARAHGYDTNPIGGF---ERT 167
Cdd:cd02150   78 ----KEKAPGYWVQ----------------------------------DCSAATENILLAAHALGLGAVWLGVYpfeERV 119

                        170       180
                 ....*....|....*....|...
gi 523838760 168 E-VAEAFNMdPERYVPVMIVSIG 189
Cdd:cd02150  120 KaIREILNI-PENIIPFCVIALG 141
YdjA-like cd02135
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ...
 10-189 3.21e-15

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: 69.94  E-value: 3.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  10 DLMKNRRSIREYDETVKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDaGKEKLSSLV-----------------RFN 72
Cdd:cd02135    2 ELIKTRRSIRKFKLTGAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGE-GRERLAELLaaaaaarapgadpekleKAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  73 TRQNEsSSAMILVFGDLQnfengekiygesvERGLMPAEvkEQQMAklsqyfasiprseaervvlidGGIVAMQLMLVAR 152
Cdd:cd02135   81 EKALR-APVVIAVVAKPD-------------EDPKVPEW--EQYAA---------------------VGAAVQNLLLAAH 123

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 523838760 153 AHGYD----TNPIggFERTEVAEAFNMdPERYVPVMIVSIG 189
Cdd:cd02135  124 ALGLGavwrTGPV--TYDPAVREALGL-PEDERIVGFLYLG 161
iodotyrosine_dehalogenase cd02144
iodotyrosine dehalogenase; Iodotyrosine dehalogenase catalyzes the removal of iodine from the ...
 8-64 3.66e-13

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: 65.25  E-value: 3.66e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 523838760   8 FEDLMKNRRSIREYDETvKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEK 64
Cdd:cd02144    1 FYELMKKRRSVRDFSSE-PVPREVIENAIRTAGTAPSGANTQPWTFVVVSDPEIKRK 56
RutE-like cd02148
nitroreductase similar to Escherichia coli RutE; A subfamily of the nitroreductase family ...
 27-189 5.52e-13

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: 64.58  E-value: 5.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  27 ISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVRFNTRQNESSSAMILVFG-DLQNFENGEKiygesver 105
Cdd:cd02148   20 VSDEELRAIYDLAKWGPTAANCSPARIVFVRSAEAKERLVPHLSEGNREKTMAAPVTAILAyDTEFYEHLPR-------- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760 106 gLMPaevkeqQMAKLSQYFASiPRSEAERVVLIDGGIVAMQLMLVARAHGYDTNPIGGFERTEVAEAFNMDpERYVPVMI 185
Cdd:cd02148   92 -LFP------HGDARSWFFGS-GPARAEETAFRNASLQAAYFILAARALGLDCGPMSGFDAAGVDAEFFAG-TRWKSNLV 162


                 ....
gi 523838760 186 VSIG 189
Cdd:cd02148  163 VNLG 166
nitroreductase_FeS-like cd02143
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ...
 11-69 1.15e-11

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: 60.95  E-value: 1.15e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  11 LMKNRRSIREY-DETVkiSQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLV 69
Cdd:cd02143    1 LLRSRRSIRRYkDKPV--PRETLEKLLDIARYAPTGHNSQPVHWLVVDDPEKVRRLAELV 58
NfsA-like cd02146
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ...
 10-202 4.34e-11

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: 59.94  E-value: 4.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  10 DLMKNRRSIREYDEtVKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVrFNTRQNESSSAMILVFGDL 89
Cdd:cd02146    3 ETILNHRSVRKFTD-EPLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKLAELA-GNQPYVAQAPVFLVFCADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  90 QNFengekiygesverglmpaevkeQQMAKLSQYFASIPRS-EAERVVLIDGGIVAMQLMLVARAHGYDTNPIGGFERT- 167
Cdd:cd02146   81 YRH----------------------QKIAEEAGGKDVGLDYlESFLVGVVDAALAAQNALVAAESLGLGIVYIGGIRNNp 138

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 523838760 168 -EVAEAFNMdPERYVPVMIVSIGKAKNSGYQSYRLP 202
Cdd:cd02146  139 eEVIELLGL-PEYVFPLFGLTVGHPDPTPEVKPRLP 173
nitroreductase cd20610
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 13-65 4.79e-11

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: 58.83  E-value: 4.79e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 523838760  13 KNRRSIREY-DETVkiSQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKL 65
Cdd:cd20610    2 KKRRSIRKFkPDPV--PKEDIEKILEAANWAPSGMNRQNWEFVVVKGGEKIEKI 53
PRK05365 PRK05365
malonic semialdehyde reductase; Provisional
 27-190 1.01e-10

malonic semialdehyde reductase; Provisional


Pssm-ID: 180040 [Multi-domain]  Cd Length: 195  Bit Score: 58.67  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  27 ISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLV-RFNTRQNESSSAMILVFGDLQNFENGEKiygesver 105
Cdd:PRK05365  27 VSDEQLRELYDLVKWGPTSANCSPARFVFVRSAEAKERLRPALsEGNLAKTLAAPVTAIVAYDTEFHEHLPK-------- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760 106 gLMPAevkeqqmAKLSQYFASIPrSEAERVVLIDGGIVAMQLMLVARAHGYDTNPIGGFERTEVAEAFNMDpERYVPVMI 185
Cdd:PRK05365  99 -LFPH-------ADARSWFAGNP-ALAEETAFRNSSLQGAYLILAARALGLDAGPMSGFDAAAVDAEFFAG-TTWKSNFL 168


                 ....*
gi 523838760 186 VSIGK 190
Cdd:PRK05365 169 VNIGY 173
BluB TIGR02476
5,6-dimethylbenzimidazole synthase; A previously published hypothesis that BluB, involved in ...
 8-189 6.29e-10

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: 56.68  E-value: 6.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760    8 FEDLMKNRRSIREYdETVKISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVrfnTRQNESSSAMilvFG 87
Cdd:TIGR02476   9 VYRLIRERRDVRHF-RSDPVPEAVLERLLDAAHHAPSVGFSQPWRFVRVESPATREAVHALF---TRANQAAAAI---YD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   88 DLQnfengEKIYGESVERGLMPAEVK------EQQMAKLSQYFASIPRSEAERVVLidggivAMQLM-LVARAHGYDTNP 160
Cdd:TIGR02476  82 GER-----ASQYHRLKLEGIREAPVQlavfcdDARGEGHGLGRHTMPEMLRYSVAC------AIQNLwLAARAEGLGVGW 150

                         170       180
                  ....*....|....*....|....*....
gi 523838760  161 IGGFERTEVAEAFNMdPERYVPVMIVSIG 189
Cdd:TIGR02476 151 VSILDPDAVRRLLGV-PEGWRLVAYLCLG 178
McbC_SagB-like_oxidoreductase cd02142
oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain ...
 4-190 3.94e-08

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: 51.27  E-value: 3.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760   4 LNNDFEDLMKNRRSIREYD----ETVKISQEEMKAILEDAV---TAPSSVNMQPW-RFVVVESDAGKE--------KLSS 67
Cdd:cd02142   16 ATLDLSEALLNRRSRRTFSseplTLRELSRLAARGIPGSGYglrPYPSAGALYPIeVYVIVKNVEGLPagiyhydpKRHR 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  68 LVRFntRQNESSSAMILVFGDLQNFENgekiygesverglmpaevkeqqmAKLSQYFASIP-------RSEAERVVLIDG 140
Cdd:cd02142   96 LVLI--REGDFRLDLAHAAGNQAAFGS-----------------------AAFSLIIVARFeriawkyGERAYRYILLEA 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 523838760 141 GIVAMQLMLVARAHGYDTNPIGGFERTEVAEAFNMDPERYVPVMIVSIGK 190
Cdd:cd02142  151 GHLAQNLYLAATALGLGLCAIGAFDDDALRELLGLDEVEEVVLYAFVVGG 200
Frm2-like cd02140
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 8-63 4.13e-08

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: 51.15  E-value: 4.13e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 523838760   8 FEDLMKNRRSIREYDETVKISQEEMKAILEDAVT-APSSVNMQPWRFVVVESDAGKE 63
Cdd:cd02140    1 FLEAAKARRTIYALGKNSPVSDEEIEEIVKEAVKhVPSSFNSQSSRAVILLGDEHKK 57
BluB cd02145
5,6-dimethylbenzimidazole synthase; BluB catalyzes the O2-dependent conversion of FMNH2 to 5, ...
 11-82 9.24e-07

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: 47.35  E-value: 9.24e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523838760  11 LMKNRRSIREY--DEtvkISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKLSSLVrfnTRQNESSSAM 82
Cdd:cd02145    3 VIRWRRDVRHFrpDP---VPEEVLERLLQAAHLAPSVGLMQPWRFVRVRSAATRKAVHELF---QRANAEAAEM 70
PRK13294 PRK13294
F420-0--gamma-glutamyl ligase; Provisional
 15-65 6.41e-06

F420-0--gamma-glutamyl ligase; Provisional


Pssm-ID: 183957 [Multi-domain]  Cd Length: 448  Bit Score: 45.78  E-value: 6.41e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 523838760  15 RRSIREY-DETVkiSQEEMKAILEDAVTAPSSVNMQPWRFVVVESDAGKEKL 65
Cdd:PRK13294 260 RRSVREFsDDPV--DPEAVRRAVAAALTAPAPHHTRPVRFVWLRSAAVRTRL 309
PRK10828 PRK10828
putative oxidoreductase; Provisional
 10-132 2.48e-05

putative oxidoreductase; Provisional


Pssm-ID: 182761  Cd Length: 183  Bit Score: 43.14  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  10 DLMKNRRSIREYDETVKiSQEEMKAILEDAVTAPSSVNMQPWRFVVVESDaGKEKLSSLVRFNTRQNESSSAMI------ 83
Cdd:PRK10828   5 ELLLNRRSASRLAEPAP-TGEQLQNILRAGMRAPDHGSLQPWRFFVIEGE-GRERFSALLEQGAIAAGSDEKAIekarna 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 523838760  84 -----LVFGDLQNFENGEKI--YGESVERGlmpAEVKEQQMAKLSQYFASIPRSEA 132
Cdd:PRK10828  83 pfrapLIITVVAKCEENHKVprWEQEVSAG---CAVMAMQMAAVAQGFNGIWRSGA 135
TM1586_NiRdase pfam14512
Putative TM nitroreductase; Compared with the more traditional NADH oxidase/flavin reductase ...
 30-59 1.60e-04

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: 41.12  E-value: 1.60e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 523838760   30 EEMKAILEDAVTAPSSVNMQPWRFVVVESD 59
Cdd:pfam14512 157 EWFKEGMEAARLAPSAMNQQPWRFVLVDDN 186
PRK14851 PRK14851
hypothetical protein; Provisional
 26-121 1.47e-03

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 39.07  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523838760  26 KISQEEMKAILEDAVTAPSSVNMQPWRFVVVESDA----GKEKLSSLvrFNTRQNESssaMILVFGDLQNFENGEKIYGE 101
Cdd:PRK14851 322 SLPQGVGDYILQAGIQAPSGDNVQPWQFALAGNDIhlylDPEADVSF--FNVRQTAS---IISCGAVMENMRIAATTFGL 396

                         90       100
                 ....*....|....*....|
gi 523838760 102 SVERGLMPAEVKEQQMAKLS 121
Cdd:PRK14851 397 DATTQYRPDAAQEDLMATVR 416
antibiot_sagB TIGR03605
SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation ...
 134-190 3.10e-03

SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation of streptolysin S from a ribosomally produced precursor polypeptide. Chemically similar systems operate on highly diverse sets of bacteriocin precursors in numerous other bacteria. This model describes a domain within SgaB and homologous regions from other proteins, many of which appear to be involved in biosynthesis of secondary metabolites. While some substrates may be intermediates in non-ribosomal peptide syntheses, others are involved in heterocycle-containing bacteriocin biosynthesis, and can be found near SgaC-like (see TIGR03603, cyclodehydratase) and SgaD-like (see TIGR03604, "docking") proteins. Members of this domain family are heterogeneous in length, as many have a partial second copy of the domain represented here. The incomplete second domain scores below the cutoffs to this model in most cases.


Pssm-ID: 188352  Cd Length: 173  Bit Score: 36.90  E-value: 3.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 523838760  134 RVVLIDGGIVAMQLMLVARAHGYDTNPIGGFERTEVAEAFNMDPERYVPVMIVSIGK 190
Cdd:TIGR03605 117 RLALLDVGIIIQNFYLVATALGLGSCAIGGFDDDYIAELLGLDGIEEHVVGVFPVGR 173
 
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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