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Conserved domains on  [gi|15600383|ref|NP_253877|]
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nitroreductase [Pseudomonas aeruginosa PAO1]

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 ...
 4-194 2.98e-61

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: 187.45  E-value: 2.98e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   4 EDAVRSRRAIKGYDSSFSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREVAWDQAQVTDAAMLVVVCAQL 83
Cdd:cd02137   1 LEVIKSRRSVRNFDPDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAAYNQPQVTTASAVILVLGDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  84 DswernaqrvwdgapeavqafmagaidtyyrgkpqvqrdeamrsCGLLAQTLMLVARGQGLDSCPMDGFDFDAVARLINL 163
Cdd:cd02137  81 N-------------------------------------------AGLAAMNLMLAAKAKGYDTCPMGGFDKEKVAELLNL 117

                       170       180       190
                ....*....|....*....|....*....|.
gi 15600383 164 PDNHVIGLMVAVGKKAvEPWPRSGKLPREEL 194
Cdd:cd02137 118 PDRYVPVLLIAIGKAA-DKAPRSGRLPVDEV 147
 
Name Accession Description Interval E-value
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
 4-194 2.98e-61

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: 187.45  E-value: 2.98e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   4 EDAVRSRRAIKGYDSSFSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREVAWDQAQVTDAAMLVVVCAQL 83
Cdd:cd02137   1 LEVIKSRRSVRNFDPDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAAYNQPQVTTASAVILVLGDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  84 DswernaqrvwdgapeavqafmagaidtyyrgkpqvqrdeamrsCGLLAQTLMLVARGQGLDSCPMDGFDFDAVARLINL 163
Cdd:cd02137  81 N-------------------------------------------AGLAAMNLMLAAKAKGYDTCPMGGFDKEKVAELLNL 117

                       170       180       190
                ....*....|....*....|....*....|.
gi 15600383 164 PDNHVIGLMVAVGKKAvEPWPRSGKLPREEL 194
Cdd:cd02137 118 PDRYVPVLLIAIGKAA-DKAPRSGRLPVDEV 147
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 7-177 1.98e-44

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: 145.23  E-value: 1.98e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383     7 VRSRRAIKGYDSSfSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREVAWDQAQVTDAAMLVVVCAQLDSW 86
Cdd:pfam00881   1 IRQRRSVRKFDPE-PVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAALLLLLRRDANL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383    87 ERNAQRVWDGAPeaVQAFMAGAIDTYYRGKPQVQRDEAMRSCGLLAQTLMLVARGQGLDSCPMDGFDFDAVARLINLPDN 166
Cdd:pfam00881  80 KLLLQDFLRGAP--VLIVITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDD 157

                         170
                  ....*....|.
gi 15600383   167 HVIGLMVAVGK 177
Cdd:pfam00881 158 ERLVGLIAVGY 168
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 3-195 6.62e-41

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 136.14  E-value: 6.62e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   3 IEDAVRSRRAIKGYDSsFSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLRE--VAWDQAQVTDAAMLVVVC 80
Cdd:COG0778   1 LLELLLTRRSVRKFTD-KPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEalAEANQEWVADAPVLIVVC 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  81 AQLDSWERnaqrvwdgapeavqafmagaidtyyrgkpqVQRDEAMRSCGLLAQTLMLVARGQGLDSCPMDGFDFDAVARL 160
Cdd:COG0778  80 ADPDRSEK------------------------------VPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVREL 129

                       170       180       190
                ....*....|....*....|....*....|....*
gi 15600383 161 INLPDNHVIGLMVAVGKKAVEPWPRSgKLPREELV 195
Cdd:COG0778 130 LGLPEGEEPVALLALGYPAEELNPRP-RKPLEEVV 163
PRK10765 PRK10765
oxygen-insensitive NADPH nitroreductase;
5-200 3.44e-13

oxygen-insensitive NADPH nitroreductase;


Pssm-ID: 182710  Cd Length: 240  Bit Score: 65.77  E-value: 3.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383    5 DAVRSRRAIKGYdSSFSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREVAWDQAQVTDAAMLVVVCAqld 84
Cdd:PRK10765   6 ELILSHRSIRHF-TDEPISEAQREAIINAARAASSSSFLQCSSIIRITDKALREALVELTGGQKYVAQAAEFWVFCA--- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   85 SWERNAQRVWDGAPEAVQAFMAGAIDTyyrgkpqvqrdeamrscGLLAQTLMLVARGQGLDSCPMDGF--DFDAVARLIN 162
Cdd:PRK10765  82 DFNRHLQICPDAQLGLAEQLLIGAVDT-----------------AIMAQNALLAAESLGLGGVYIGGLrnNIEAVTELLK 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15600383  163 LPDnHVIGLM-VAVGKKAVEPW--PRsgkLPREELVIRDRF 200
Cdd:PRK10765 145 LPQ-HVLPLFgLCLGWPAQNPDlkPR---LPASLLVHENQY 181
antibiot_sagB TIGR03605
SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation ...
 129-177 3.31e-05

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: 42.68  E-value: 3.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15600383   129 GLLAQTLMLVARGQGLDSCPMDGFDFDAVARLINLPD--NHVIGlMVAVGK 177
Cdd:TIGR03605 124 GIIIQNFYLVATALGLGSCAIGGFDDDYIAELLGLDGieEHVVG-VFPVGR 173
 
Name Accession Description Interval E-value
MhqN-like cd02137
nitroreductase family protein similar to the NAD(P)H nitroreductase MhqN; A diverse subfamily ...
 4-194 2.98e-61

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: 187.45  E-value: 2.98e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   4 EDAVRSRRAIKGYDSSFSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREVAWDQAQVTDAAMLVVVCAQL 83
Cdd:cd02137   1 LEVIKSRRSVRNFDPDHKIPKEELKEILELATLAPSSFNLQPWRFVVVRDPELKAKLAEAAYNQPQVTTASAVILVLGDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  84 DswernaqrvwdgapeavqafmagaidtyyrgkpqvqrdeamrsCGLLAQTLMLVARGQGLDSCPMDGFDFDAVARLINL 163
Cdd:cd02137  81 N-------------------------------------------AGLAAMNLMLAAKAKGYDTCPMGGFDKEKVAELLNL 117

                       170       180       190
                ....*....|....*....|....*....|.
gi 15600383 164 PDNHVIGLMVAVGKKAvEPWPRSGKLPREEL 194
Cdd:cd02137 118 PDRYVPVLLIAIGKAA-DKAPRSGRLPVDEV 147
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 7-177 1.98e-44

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: 145.23  E-value: 1.98e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383     7 VRSRRAIKGYDSSfSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREVAWDQAQVTDAAMLVVVCAQLDSW 86
Cdd:pfam00881   1 IRQRRSVRKFDPE-PVPKEVLEEILEAARRAPSAGNLQPWRFYVVTDGELRYRLAEAALELLLVEPAAALLLLLRRDANL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383    87 ERNAQRVWDGAPeaVQAFMAGAIDTYYRGKPQVQRDEAMRSCGLLAQTLMLVARGQGLDSCPMDGFDFDAVARLINLPDN 166
Cdd:pfam00881  80 KLLLQDFLRGAP--VLIVITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLPDD 157

                         170
                  ....*....|.
gi 15600383   167 HVIGLMVAVGK 177
Cdd:pfam00881 158 ERLVGLIAVGY 168
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 3-195 6.62e-41

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


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 136.14  E-value: 6.62e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   3 IEDAVRSRRAIKGYDSsFSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLRE--VAWDQAQVTDAAMLVVVC 80
Cdd:COG0778   1 LLELLLTRRSVRKFTD-KPVSDEELEELLEAARLAPSAGNLQPWRFVVVRDPELRERLAEalAEANQEWVADAPVLIVVC 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  81 AQLDSWERnaqrvwdgapeavqafmagaidtyyrgkpqVQRDEAMRSCGLLAQTLMLVARGQGLDSCPMDGFDFDAVARL 160
Cdd:COG0778  80 ADPDRSEK------------------------------VPERYALLDAGIAAQNLLLAARALGLGTCWIGGFDPEKVREL 129

                       170       180       190
                ....*....|....*....|....*....|....*
gi 15600383 161 INLPDNHVIGLMVAVGKKAVEPWPRSgKLPREELV 195
Cdd:COG0778 130 LGLPEGEEPVALLALGYPAEELNPRP-RKPLEEVV 163
nitroreductase cd03370
uncharacterized nitroreductase family proteins; Nitroreductase family containing Thermus ...
 5-184 1.58e-30

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: 110.49  E-value: 1.58e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   5 DAVRSRRAIKGYDSSfSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREVAWDQAQVTDAAMLVVVCAQL- 83
Cdd:cd03370   3 EAIESRRSIRKYTQE-PVPDEDLREILRLAGLAPSAWNIQPWRFVVVRDAELKEQLQAAAYGQAQVTSAPAVIVIYSDMe 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  84 DSWERNAQRVWDGAPEAVQAFMAGAIDTYYRGKPQVQRDEAMrscglLAQT------LMLVARGQGLDSCPMDGFDFDAV 157
Cdd:cd03370  82 DALANLEETIHPGLSEERRQREAAGLRGAFGKMSVEQRGQWG-----LAQAnialgfLLLAAQSLGYDTSPMLGFDPEKV 156

                       170       180
                ....*....|....*....|....*..
gi 15600383 158 ARLINLPDNHVIGLMVAVGKKAVEPWP 184
Cdd:cd03370 157 KALLGLPEHVTIAALVALGKPAEEGYP 183
NfsB-like cd02149
nitroreductase similar to Escherichia coli NfsB; NAD(P)H:FMN oxidoreductase family. This ...
 3-194 6.28e-24

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: 92.31  E-value: 6.28e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   3 IEDAVRSRRAIKGYDSSFSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREVAW-DQAQVTDAAMLVVVCA 81
Cdd:cd02149   2 ILELLNFRYATKKFDPNKKISDEDLETILEALRLSPSSFGLEPWKFLVVENPELKAKLAPAAWfNQPQIKDASHVVVFLA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  82 QLDsWernAQRvwdgapeavQAFMAGAIdtyyrgkpqvqrdeamrscgllaqtLMLVARGQGLDSCPMDGFDFDAVARLI 161
Cdd:cd02149  82 KKD-W---SAK---------QTYIALGN-------------------------MLLAAAMLGIDSCPIEGFDPAKLDEIL 123

                       170       180       190
                ....*....|....*....|....*....|....
gi 15600383 162 NL-PDNHVIGLMVAVGKKAVEPWPRSgKLPREEL 194
Cdd:cd02149 124 GLdEKGYKISVMVAFGYRSEEKLPKS-RKPLEDV 156
Nitro_FMN_reductase cd02062
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 7-176 5.48e-22

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: 86.97  E-value: 5.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   7 VRSRRAIKGYDSSfSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLR-EVAWDQAQVTDAAMLVVVCAqlds 85
Cdd:cd02062   1 IKTRRSIRKFTDK-PVPEEKLRKILEAARLAPSAGNLQPWRFIVVRDREKKEKLAkLAAPNQKFIAGAPVVIVVVA---- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  86 wernaqrvwdgapeavqafmagaidtyyrgKPQVQRDEAMRSCGLLAQTLMLVARGQGLDSCPMDGFDF--DAVARLINL 163
Cdd:cd02062  76 ------------------------------DPDKSRPWALEDAGAAAQNLLLAAAALGLGSCWIGGFDFreDKVRELLGI 125

                       170
                ....*....|...
gi 15600383 164 PDNHVIGLMVAVG 176
Cdd:cd02062 126 PENLRPVALIAIG 138
nitroreductase cd02139
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 5-195 2.57e-18

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: 77.90  E-value: 2.57e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   5 DAVRSRRAIKGYDSsfslTREEKDHL---LDLALHAPSAFNLQHVRLVEVSDPQLRVQLREVAWDQAQVTDAAMLVVVCA 81
Cdd:cd02139   3 EAIKKRRSIRKYKP----TPVEEEKLlriLEAARLAPSAKNRQPWRFIVVKDKELKEKLAEAANGQKFIAEAPVVIVACA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  82 -QLDSWERNAQRvwdgapeavqafmAGAIDtyyrgkpqvqrdeamrsCGLLAQTLMLVARGQGLDSCPMDGFDFDAVARL 160
Cdd:cd02139  79 dPSESGMGCGKP-------------YYLVD-----------------VAIAMEHLVLAATEEGLGTCWIGAFDEDKVKEI 128

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15600383 161 INLPDN-HVIGLMvAVGKKAVEPWPRSGKlPREELV 195
Cdd:cd02139 129 LGIPEEyRVVALT-PLGYPAEEPPPRPRK-PLEEIV 162
NfsA-like cd02146
nitroreductase similar to Escherichia coli NfsA; This family contains NADPH-dependent flavin ...
 5-200 3.40e-17

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


Pssm-ID: 380322 [Multi-domain]  Cd Length: 229  Bit Score: 76.51  E-value: 3.40e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   5 DAVRSRRAIKGYDSSfSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREVAWDQAQVTDAAMLVVVCAqld 84
Cdd:cd02146   3 ETILNHRSVRKFTDE-PLTDETLETLIAAAQSASTSSNLQAYSVIVVTDPELREKLAELAGNQPYVAQAPVFLVFCA--- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  85 SWERNAQ-----RVWDGAPEAVQAFMAGAIDTyyrgkpqvqrdeamrscGLLAQTLMLVARGQGLDSCPMDGF--DFDAV 157
Cdd:cd02146  79 DLYRHQKiaeeaGGKDVGLDYLESFLVGVVDA-----------------ALAAQNALVAAESLGLGIVYIGGIrnNPEEV 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15600383 158 ARLINLPDnHVIGLM-VAVGKKAVEPW--PRsgkLPREELVIRDRF 200
Cdd:cd02146 142 IELLGLPE-YVFPLFgLTVGHPDPTPEvkPR---LPLEAVVHEETY 183
nitroreductase cd20608
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 5-176 5.01e-16

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: 71.60  E-value: 5.01e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   5 DAVRSRRAIKGYdSSFSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREVA-WDQAQVTDAAMLVVVCAQ- 82
Cdd:cd20608   2 EAIKTRRSVRRF-SDKPVEEEKLEKILEAARLAPSWANKQCWRFIVVTDKETLSELAKKEsPSNGWLKDAPVIIVVCADp 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  83 LDSWERNAQRVWdgapeavqaFMAGAIdtyyrgkpqvqrdeAMrscgllaQTLMLVARGQGLDSCPMDGFDFDAVARLIN 162
Cdd:cd20608  81 KDSGWLNGQNYY---------LVDAAI--------------AM-------QNLMLAATDLGLGTCWIGAFDEKKVKEILG 130

                       170
                ....*....|....
gi 15600383 163 LPDNHVIGLMVAVG 176
Cdd:cd20608 131 IPENIRVVALTPLG 144
PnbA_NfnB-like cd02136
nitroreductase similar to Mycobacterium smegmatis NfnB; Members of this family utilize FMN as ...
 6-195 5.38e-14

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: 66.07  E-value: 5.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   6 AVRSRRAIKGYDSSfSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRvQLREVAWDqaqvtdAAMLVVVCAQLDS 85
Cdd:cd02136   1 AIKSRRSVRAFKDK-PVPKETIEKILEAARRAPSGKNTQPWRVYVVTGKARE-RLKKAFFG------APVALFLTMDKVL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  86 WERNAQrvwdgapeavqafmagaidtyyrgkpqvqrdeamrSCGLLAQTLMLVARGQGLDSCPM-DGFDFDAVARLI-NL 163
Cdd:cd02136  73 GPWSWF-----------------------------------DLGAFLQNLMLAAHALGLGTCPQgALAGYPDVVRKElGI 117

                       170       180       190
                ....*....|....*....|....*....|....*
gi 15600383 164 PDNHVIGLMVAVG---KKAVEPWPRSGKLPREELV 195
Cdd:cd02136 118 PDDEELVCGIALGypdPDAPVNQFRTPREPLEEFV 152
PRK10765 PRK10765
oxygen-insensitive NADPH nitroreductase;
5-200 3.44e-13

oxygen-insensitive NADPH nitroreductase;


Pssm-ID: 182710  Cd Length: 240  Bit Score: 65.77  E-value: 3.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383    5 DAVRSRRAIKGYdSSFSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREVAWDQAQVTDAAMLVVVCAqld 84
Cdd:PRK10765   6 ELILSHRSIRHF-TDEPISEAQREAIINAARAASSSSFLQCSSIIRITDKALREALVELTGGQKYVAQAAEFWVFCA--- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   85 SWERNAQRVWDGAPEAVQAFMAGAIDTyyrgkpqvqrdeamrscGLLAQTLMLVARGQGLDSCPMDGF--DFDAVARLIN 162
Cdd:PRK10765  82 DFNRHLQICPDAQLGLAEQLLIGAVDT-----------------AIMAQNALLAAESLGLGGVYIGGLrnNIEAVTELLK 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15600383  163 LPDnHVIGLM-VAVGKKAVEPW--PRsgkLPREELVIRDRF 200
Cdd:PRK10765 145 LPQ-HVLPLFgLCLGWPAQNPDlkPR---LPASLLVHENQY 181
TdsD-like cd02138
nitroreductase similar to Burkholderia pseudomallei TdsD; A subfamily of the nitroreductase ...
 8-199 1.41e-11

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: 60.25  E-value: 1.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   8 RSRRAIkgydSSFSLTREEKDHLLDLALHAPSAFNLQHVR-LVEVSDPQLRVQLRE--VAWDQAQVTDAAMLVVVCAQLD 84
Cdd:cd02138   6 WSPRAF----SPEPISEEDLLSLFEAARWAPSCFNEQPWRfVVARRDTEAFEKLLDllAEGNQSWAKNAPVLIVVLAKTE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  85 SwERNaqrvwdgapeavqafmagaidtyyrGKPqvqRDEAMRSCGLLAQTLMLVARGQGLDSCPMDGFDFDAVARLINLP 164
Cdd:cd02138  82 F-DHN-------------------------GKP---NRYALFDTGAAVANLALQATALGLVVHQMAGFDPEKAKEALGIP 132

                       170       180       190
                ....*....|....*....|....*....|....*
gi 15600383 165 DNHVIGLMVAVGKKAvEPWPRSGKLPREELVIRDR 199
Cdd:cd02138 133 DEYEPITMIAIGYPG-DPESLPEKLLEREEAPRTR 166
PRK11053 PRK11053
oxygen-insensitive NAD(P)H nitroreductase;
1-194 4.98e-11

oxygen-insensitive NAD(P)H nitroreductase;


Pssm-ID: 182929 [Multi-domain]  Cd Length: 217  Bit Score: 59.60  E-value: 4.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383    1 MHIEDAVRSRRAIKGYDSSFSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREV-----AWDQAQVTDAAM 75
Cdd:PRK11053   1 MDIVSVAKKRYTTKAFDPSKKLPAEQIEQIKTLLRFSPSSVNSQPWHFIVASTEEGKARIAKAaagnyAFNERKILDASH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   76 LVVVCAQLDSWERNAQRVW-----DG---APEAVQA------FMAGaidtYYRGKPQvQRDEAMRSCGLLA-QTLMLVAR 140
Cdd:PRK11053  81 VVVFCAKTDMDDAYLELVLeqedaDGrfaTEEAKAAqdkgrrFFAD----MHRKELK-DLQHWMEKQVYLAlGNLLLGAA 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600383  141 GQGLDSCPMDGFDFDAVARLINLPDNhviGL----MVAVGKKAVEPW----PRSgKLPREEL 194
Cdd:PRK11053 156 ALGIDATPIEGFDAAILDAEFGLREK---GLtssvVVPLGYHSEEDFnaklPKS-RLPQETI 213
McbC_SagB-like_oxidoreductase cd02142
oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain ...
 43-177 6.82e-09

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: 53.19  E-value: 6.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  43 LQHvRLVEVSDPQLRVQLREVAWDQAQVTDAAMLVVVCAQLdswERNAQRvwdgapeavqafmagaidtyyrgkpqvQRD 122
Cdd:cd02142  92 KRH-RLVLIREGDFRLDLAHAAGNQAAFGSAAFSLIIVARF---ERIAWK---------------------------YGE 140

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600383 123 EAMRSC----GLLAQTLMLVARGQGLDSCPMDGFDFDAVARLINLPDN--HVIGLMVaVGK 177
Cdd:cd02142 141 RAYRYIlleaGHLAQNLYLAATALGLGLCAIGAFDDDALRELLGLDEVeeVVLYAFV-VGG 200
nitroreductase cd20609
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 5-176 1.10e-08

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: 51.62  E-value: 1.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   5 DAVRSRRAIKGYDSSfSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREVAwdqAQVTDAAMLVVVCAQLD 84
Cdd:cd20609   4 ELAKKRYSVRKFSDK-PVEKEKLDKILEAGRLAPTAVNYQPQRILVVRSEEALEKLAKAT---PRFFGAPLVIVVCYDKD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  85 -SWERnaqrvwdgapeavqafmagaidtYYRGKPQVQRDEAmrscgLLAQTLMLVARGQGLDSCPMDGFDFDAVARLINL 163
Cdd:cd20609  80 eSWKR-----------------------PYDGKDSGDIDAA-----IVATHMMLAATELGLGTCWVGNFDPEKVREAFNL 131

                       170
                ....*....|...
gi 15600383 164 PDNHVIGLMVAVG 176
Cdd:cd20609 132 PENLEPVAILPLG 144
PRK05365 PRK05365
malonic semialdehyde reductase; Provisional
 23-193 1.86e-08

malonic semialdehyde reductase; Provisional


Pssm-ID: 180040 [Multi-domain]  Cd Length: 195  Bit Score: 52.12  E-value: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   23 TREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREV--AWDQAQVTDAAMLVVVCAQLDSWERnaqrvwdgAPea 100
Cdd:PRK05365  28 SDEQLRELYDLVKWGPTSANCSPARFVFVRSAEAKERLRPAlsEGNLAKTLAAPVTAIVAYDTEFHEH--------LP-- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  101 vQAFMAGAIDTYYRGKPQVQRDEAMRSCGLLAQTLMLVARGQGLDSCPMDGFDFDAVARLInLPDNHVIGLM-VAVGKKA 179
Cdd:PRK05365  98 -KLFPHADARSWFAGNPALAEETAFRNSSLQGAYLILAARALGLDAGPMSGFDAAAVDAEF-FAGTTWKSNFlVNIGYGD 175

                        170
                 ....*....|....*
gi 15600383  180 VEPW-PRSGKLPREE 193
Cdd:PRK05365 176 PAKLfPRLPRLSFDE 190
nitroreductase cd02151
nitroreductase family protein; A subfamily of the nitroreductase family containing ...
 5-185 1.71e-07

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: 48.68  E-value: 1.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   5 DAVRSRRAIKGYDSSfSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREV-AWDQAQVTDAAMLVVVCAql 83
Cdd:cd02151   1 ELLKKRRSIRKYTDE-PIEEEKLEEILEAALLAPSSRNSRPVEFIVVDDKETLKKLSECkPHGSAFLKGAPAAIVVLA-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  84 dswERNAQRVWdgapeavqafmagaidtyyrgkpqvqrdeaMRSCGLLAQTLMLVARGQGLDSC------PMDGFDFDA- 156
Cdd:cd02151  78 ---DTEKSDTW------------------------------IEDASIAATYIQLAAESLGLGSCwiqirnRETQDGKTAe 124

                       170       180       190
                ....*....|....*....|....*....|.
gi 15600383 157 --VARLINLPDNHVIGLMVAVGKKAVEPWPR 185
Cdd:cd02151 125 eyVRELLGIPENYRVLCIIALGYPDEEKPPH 155
RutE-like cd02148
nitroreductase similar to Escherichia coli RutE; A subfamily of the nitroreductase family ...
 21-157 3.24e-07

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: 48.40  E-value: 3.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  21 SLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLREVAWD--QAQVTDAAMLVVVCAQLDSWERnaqrvwdgAP 98
Cdd:cd02148  19 PVSDEELRAIYDLAKWGPTAANCSPARIVFVRSAEAKERLVPHLSEgnREKTMAAPVTAILAYDTEFYEH--------LP 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  99 eavQAFMAGAIDTYYRGKPQVQRDE-AMRSCGLLAQTLMLVARGQGLDSCPMDGFDFDAV 157
Cdd:cd02148  91 ---RLFPHGDARSWFFGSGPARAEEtAFRNASLQAAYFILAARALGLDCGPMSGFDAAGV 147
nitroreductase cd20610
nitroreductase family protein; Proteins of this family catalyze the reduction of flavin or ...
 7-176 9.71e-07

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: 46.89  E-value: 9.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   7 VRSRRAIKGYDSSfSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQL--------RVQLREVAWDQAQVTDAAMLVV 78
Cdd:cd20610   1 IKKRRSIRKFKPD-PVPKEDIEKILEAANWAPSGMNRQNWEFVVVKGGEKiekigisiKKKNEEIARLLEKVFAEKPIRF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  79 VcaqldSWERNAQRVwDGAPEAVQAFmagaidtYYRGKPQVQRDEAMRSCGLLAQTLMLVARGQGLDSCPMDG--FDFDA 156
Cdd:cd20610  80 R-----KFRRFFTLF-GGAPVLVVVY-------TEPYKPPEERKPDLQSVSAAIQNLLLAAHALGLGTCWMTGplYAEDE 146

                       170       180
                ....*....|....*....|
gi 15600383 157 VARLINLPDNHVIGLMVAVG 176
Cdd:cd20610 147 IEEILEIPDDKELVAVTPLG 166
nitroreductase_FeS-like cd02143
nitroreductases with an N-terminal iron-sulfur cluster-binding domain; Members of this family ...
 7-180 1.01e-05

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: 44.00  E-value: 1.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   7 VRSRRAIKGYDSSfSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRVQLRE--VAW---DQAQVTDAAMLVVVCA 81
Cdd:cd02143   2 LRSRRSIRRYKDK-PVPRETLEKLLDIARYAPTGHNSQPVHWLVVDDPEKVRRLAElvIDWmreLIKEDPELAGKLFLDG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  82 QLDSWERNAQRVWDGAPEAVQAFMAGAIDTyyrgkpqvqrdeAMRSCGLLAQTLMLVARGQGLDSCpMDGF------DFD 155
Cdd:cd02143  81 IVAAWEKGIDVILRGAPHLVVAHAPKDAPT------------PPVDCAIALTYLELAAPSLGLGTC-WAGFftaaanNYP 147

                       170       180
                ....*....|....*....|....*
gi 15600383 156 AVARLINLPDNHVIGLMVAVGKKAV 180
Cdd:cd02143 148 PLREALGLPEGHKVGGAMMLGYPKY 172
antibiot_sagB TIGR03605
SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation ...
 129-177 3.31e-05

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: 42.68  E-value: 3.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15600383   129 GLLAQTLMLVARGQGLDSCPMDGFDFDAVARLINLPD--NHVIGlMVAVGK 177
Cdd:TIGR03605 124 GIIIQNFYLVATALGLGSCAIGGFDDDYIAELLGLDGieEHVVG-VFPVGR 173
YdjA-like cd02135
nitroreductase family protein similar to Escherichia coli YdjA; A subfamily of the ...
 5-176 3.63e-04

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: 39.51  E-value: 3.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383   5 DAVRSRRAIKGYDSSFSLTREEKDHLLDLALHAPSAFNLQHVRLVEVSDPQLRV---QLREVAWDQAQVTDAAMLvvvca 81
Cdd:cd02135   2 ELIKTRRSIRKFKLTGAPPEEQLEELLEAAMWAPNHGKLEPWRFIVVTGEGRERlaeLLAAAAAARAPGADPEKL----- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600383  82 qldswERNAQRVWDgAPeAVQAFMAgAIDTyyrgKPQVQRDEAMRSCGLLAQTLMLVARGQGLDSC---PMDGFDfDAVA 158
Cdd:cd02135  77 -----EKAREKALR-AP-VVIAVVA-KPDE----DPKVPEWEQYAAVGAAVQNLLLAAHALGLGAVwrtGPVTYD-PAVR 143

                       170
                ....*....|....*...
gi 15600383 159 RLINLPDNHVIGLMVAVG 176
Cdd:cd02135 144 EALGLPEDERIVGFLYLG 161
 
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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