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Conserved domains on  [gi|1469296420|ref|WP_117638263|]
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MULTISPECIES: UDP-N-acetylmuramate dehydrogenase [unclassified Collinsella]

Protein Classification

UDP-N-acetylmuramate dehydrogenase( domain architecture ID 11486939)

UDP-N-acetylmuramate dehydrogenase is responsible for the synthesis of UDP-N-acetylmuramic acid in bacterial cell wall biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
23-319 1.95e-160

UDP-N-acetylmuramate dehydrogenase;


:

Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 449.18  E-value: 1.95e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  23 NVLMSEPMRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDLLVGDKGIRGVVVALGEGLSDITVNG 102
Cdd:PRK13905   12 RLLENEPLARYTSFRVGGPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVRDGGIRGVVIRLGKGLNEIEVEG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 103 THVTAAAGALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRVykparmLDDgtrgSGNIIEF 182
Cdd:PRK13905   92 NRITAGAGAPLIKLARFAAEAGLSGLEFAAGIPGTVGGAVFMNAGAYGGETADVLESVEV------LDR----DGEIKTL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 183 DVDELNLGYRKSRIADDGFVVLSATFNLAPGNAAMIKADMDDYHQRREDKQPLDMPSAGSTFKRPEGYFAGKLIMDAGLR 262
Cdd:PRK13905  162 SNEELGFGYRHSALQEEGLIVLSATFQLEPGDKEEIKARMDELLARREATQPLEYPSAGSVFKNPPGHFAGKLIEEAGLK 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1469296420 263 GHAIGGAQVSEKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEPEVHRVGEF 319
Cdd:PRK13905  242 GYRIGGAQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRIIGEF 298
 
Name Accession Description Interval E-value
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
23-319 1.95e-160

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 449.18  E-value: 1.95e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  23 NVLMSEPMRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDLLVGDKGIRGVVVALGEGLSDITVNG 102
Cdd:PRK13905   12 RLLENEPLARYTSFRVGGPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVRDGGIRGVVIRLGKGLNEIEVEG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 103 THVTAAAGALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRVykparmLDDgtrgSGNIIEF 182
Cdd:PRK13905   92 NRITAGAGAPLIKLARFAAEAGLSGLEFAAGIPGTVGGAVFMNAGAYGGETADVLESVEV------LDR----DGEIKTL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 183 DVDELNLGYRKSRIADDGFVVLSATFNLAPGNAAMIKADMDDYHQRREDKQPLDMPSAGSTFKRPEGYFAGKLIMDAGLR 262
Cdd:PRK13905  162 SNEELGFGYRHSALQEEGLIVLSATFQLEPGDKEEIKARMDELLARREATQPLEYPSAGSVFKNPPGHFAGKLIEEAGLK 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1469296420 263 GHAIGGAQVSEKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEPEVHRVGEF 319
Cdd:PRK13905  242 GYRIGGAQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRIIGEF 298
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
 28-316 5.69e-146

UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylenolpyruvoylglucosamine reductase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440574 [Multi-domain]  Cd Length: 279  Bit Score: 412.10  E-value: 5.69e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  28 EPMRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDLLVGDKGIRGVVVALGeGLSDITV-NGTHVT 106
Cdd:COG0812     1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLG-RLKGIEVdDGVLVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 107 AAAGALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRVYKParmlddgtrgSGNIIEFDVDE 186
Cdd:COG0812    80 AGAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDR----------TGEVRTLSAEE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 187 LNLGYRKSRIADDGFVVLSATFNLAPGNAAMIKADMDDYHQRREDKQPLDMPSAGSTFKRPEGYFAGKLIMDAGLRGHAI 266
Cdd:COG0812   150 CGFGYRDSIFKRERYIILSVTFRLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRI 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1469296420 267 GGAQVSEKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEPEVHRV 316
Cdd:COG0812   230 GGAQVSEKHANFLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
 30-317 1.25e-76

UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, UDP-N-acetylenolpyruvoylglucosamine reductase, which is also called UDP-N-acetylmuramate dehydrogenase. It is part of the pathway for the biosynthesis of the UDP-N-acetylmuramoyl-pentapeptide that is a precursor of bacterial peptidoglycan. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 272945 [Multi-domain]  Cd Length: 284  Bit Score: 236.19  E-value: 1.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  30 MRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDLLVGDKGIRGVVVALGEGLSDITVNGTHVTAAA 109
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGIDIEDDEGEYVHVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 110 GALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRVykparMLDDGTrgsgnIIEFDVDELNL 189
Cdd:TIGR00179  81 GENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATI-----LLATGK-----TEWLTNEQLGF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 190 GYRKSRIADD-GFVVLSATFNLAPG-----NAAMIKADMDDYHQRREDKQPLDMPSAGSTFKRPEGYFAGKLIMDAGLRG 263
Cdd:TIGR00179 151 GYRTSIFQHKyVGLVLKAEFQLTLGfgtrlDPETITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKG 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1469296420 264 HAIGGAQVSEKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEPEVHRVG 317
Cdd:TIGR00179 231 YQIGGAAVSKQHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKIIG 284
MurB_C pfam02873
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ...
 218-316 4.99e-57

UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are UDP-N-acetylenolpyruvoylglucosamine reductase enzymes EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 460730 [Multi-domain]  Cd Length: 99  Bit Score: 179.47  E-value: 4.99e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 218 IKADMDDYHQRREDKQPLDMPSAGSTFKRPEGYFAGKLIMDAGLRGHAIGGAQVSEKHCGFIVNADHATAADVDELIRHI 297
Cdd:pfam02873   1 IRAAMLELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEV 80

                          90
                  ....*....|....*....
gi 1469296420 298 QTTVKDQFDVDLEPEVHRV 316
Cdd:pfam02873  81 RERVKEKFGVELEPEVRII 99
 
Name Accession Description Interval E-value
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
23-319 1.95e-160

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 449.18  E-value: 1.95e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  23 NVLMSEPMRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDLLVGDKGIRGVVVALGEGLSDITVNG 102
Cdd:PRK13905   12 RLLENEPLARYTSFRVGGPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVRDGGIRGVVIRLGKGLNEIEVEG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 103 THVTAAAGALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRVykparmLDDgtrgSGNIIEF 182
Cdd:PRK13905   92 NRITAGAGAPLIKLARFAAEAGLSGLEFAAGIPGTVGGAVFMNAGAYGGETADVLESVEV------LDR----DGEIKTL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 183 DVDELNLGYRKSRIADDGFVVLSATFNLAPGNAAMIKADMDDYHQRREDKQPLDMPSAGSTFKRPEGYFAGKLIMDAGLR 262
Cdd:PRK13905  162 SNEELGFGYRHSALQEEGLIVLSATFQLEPGDKEEIKARMDELLARREATQPLEYPSAGSVFKNPPGHFAGKLIEEAGLK 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1469296420 263 GHAIGGAQVSEKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEPEVHRVGEF 319
Cdd:PRK13905  242 GYRIGGAQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRIIGEF 298
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
 28-316 5.69e-146

UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylenolpyruvoylglucosamine reductase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440574 [Multi-domain]  Cd Length: 279  Bit Score: 412.10  E-value: 5.69e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  28 EPMRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDLLVGDKGIRGVVVALGeGLSDITV-NGTHVT 106
Cdd:COG0812     1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLG-RLKGIEVdDGVLVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 107 AAAGALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRVYKParmlddgtrgSGNIIEFDVDE 186
Cdd:COG0812    80 AGAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDR----------TGEVRTLSAEE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 187 LNLGYRKSRIADDGFVVLSATFNLAPGNAAMIKADMDDYHQRREDKQPLDMPSAGSTFKRPEGYFAGKLIMDAGLRGHAI 266
Cdd:COG0812   150 CGFGYRDSIFKRERYIILSVTFRLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRI 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1469296420 267 GGAQVSEKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEPEVHRV 316
Cdd:COG0812   230 GGAQVSEKHANFLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
murB PRK13906
UDP-N-acetylmuramate dehydrogenase;
8-318 5.10e-95

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184386 [Multi-domain]  Cd Length: 307  Bit Score: 283.63  E-value: 5.10e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420   8 NEDLLCALAGVAGEDNVLMSEPMRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDLLVGDKGIRGV 87
Cdd:PRK13906    3 NKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  88 VVALgEGLSDITVNGTHVTAAAGALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRVykpar 167
Cdd:PRK13906   83 VISL-LSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALC----- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 168 mlddgTRGSGNIIEFDVDELNLGYRKSRIADDGFVVLSATFNLAPGNAAMIKADMDDYHQRREDKQPLDMPSAGSTFKRP 247
Cdd:PRK13906  157 -----VNEQGSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRP 231

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469296420 248 EGYFAGKLIMDAGLRGHAIGGAQVSEKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEPEVHRVGE 318
Cdd:PRK13906  232 PGHFAGKLIQDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGE 302
PRK12436 PRK12436
UDP-N-acetylmuramate dehydrogenase;
15-318 1.05e-89

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 171497 [Multi-domain]  Cd Length: 305  Bit Score: 270.34  E-value: 1.05e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  15 LAGVAGEDNVLMSEPMRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDLLVGDKGIRGVVVALGEg 94
Cdd:PRK12436   10 LSTVLPEGHVKQDEMLKNHTHIKVGGKADVFVAPTNYDEIQEVIKYANKYNIPVTFLGNGSNVIIKDGGIRGITVSLIH- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  95 LSDITVNGTHVTAAAGALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRVYKparmlddgtr 174
Cdd:PRK12436   89 ITGVTVTGTTIVAQCGAAIIDVSRIALDHNLTGLEFACGIPGSVGGALYMNAGAYGGEISFVLTEAVVMT---------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 175 GSGNIIEFDVDELNLGYRKSRIADDGFVVLSATFNLAPGNAAMIKADMDDYHQRREDKQPLDMPSAGSTFKRPEGYFAGK 254
Cdd:PRK12436  159 GDGELRTLTKEAFEFGYRKSVFANNHYIILEARFELEEGVYEEIKAKMDDLTFKRESKQPLEYPSCGSVFKRPPNNFAGK 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469296420 255 LIMDAGLRGHAIGGAQVSEKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEPEVHRVGE 318
Cdd:PRK12436  239 LIQESGLQGKRIGGVEVSLKHAGFMVNVDNGTAQDYIDLIHFVQKTVEEKFGVKLEREVRIIGE 302
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
 30-317 1.25e-76

UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, UDP-N-acetylenolpyruvoylglucosamine reductase, which is also called UDP-N-acetylmuramate dehydrogenase. It is part of the pathway for the biosynthesis of the UDP-N-acetylmuramoyl-pentapeptide that is a precursor of bacterial peptidoglycan. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 272945 [Multi-domain]  Cd Length: 284  Bit Score: 236.19  E-value: 1.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  30 MRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDLLVGDKGIRGVVVALGEGLSDITVNGTHVTAAA 109
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGIDIEDDEGEYVHVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 110 GALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRVykparMLDDGTrgsgnIIEFDVDELNL 189
Cdd:TIGR00179  81 GENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATI-----LLATGK-----TEWLTNEQLGF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 190 GYRKSRIADD-GFVVLSATFNLAPG-----NAAMIKADMDDYHQRREDKQPLDMPSAGSTFKRPEGYFAGKLIMDAGLRG 263
Cdd:TIGR00179 151 GYRTSIFQHKyVGLVLKAEFQLTLGfgtrlDPETITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKG 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1469296420 264 HAIGGAQVSEKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEPEVHRVG 317
Cdd:TIGR00179 231 YQIGGAAVSKQHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKIIG 284
PRK14653 PRK14653
UDP-N-acetylmuramate dehydrogenase;
23-313 4.72e-70

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237778 [Multi-domain]  Cd Length: 297  Bit Score: 219.71  E-value: 4.72e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  23 NVLMSEPMRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDlPLTIVGNGSDLLVGDKGIRGVVVALgEGLSDITVNG 102
Cdd:PRK14653   15 DVFINEEMKCHVSFKIGGPVPLFAIPNSTNGFIETINLLKEGI-EVKILGNGTNVLPKDEPMDFVVVST-ERLDDIFVDN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 103 THVTAAAGALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRVYkparmldDGTRgsgnIIEF 182
Cdd:PRK14653   93 DKIICESGLSLKKLCLVAAKNGLSGFENAYGIPGSVGGAVYMNAGAYGWETAENIVEVVAY-------DGKK----IIRL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 183 DVDELNLGYRKSRI-ADDGFVVLSATFNLAPGNAAMIKADMDDYHQRREDKQPLDMPSAGSTFKRP-EGYFAGKLIMDAG 260
Cdd:PRK14653  162 GKNEIKFSYRNSIFkEEKDLIILRVTFKLKKGNKNEIYNLMLETMKKRVEKQPLEFPSAGSVFKRPrKDFYVGSAIEKLG 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1469296420 261 LRGHAIGGAQVSEKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEPEV 313
Cdd:PRK14653  242 LKGFSIGGAQISEKHAGFIINYNNAKAEDVLKLIEYVKDKIYENYNVELETEI 294
PRK14652 PRK14652
UDP-N-acetylmuramate dehydrogenase;
21-320 8.05e-65

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237777 [Multi-domain]  Cd Length: 302  Bit Score: 206.65  E-value: 8.05e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  21 EDNVLMSEPMRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDLLVGDKGIRGVVVALGEGLSDITV 100
Cdd:PRK14652   15 RGEVLRDAPLAPRTAVRVGGPADLLVRPADPDALSALLRAVRELGVPLSILGGGANTLVADAGVRGVVLRLPQDFPGEST 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 101 NGTHVTAAAGALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRVYKParmlddgtRGSGNII 180
Cdd:PRK14652   95 DGGRLVLGAGAPISRLPARAHAHGLVGMEFLAGIPGTLGGAVAMNAGTKLGEMKDVVTAVELATA--------DGAGFVP 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 181 EfdvDELNLGYRKSRIADdGFVVLSATFNLAPGNAAMIKADMDDYHQRREDKQPLDMPSAGSTFKRPEGYFAGKLIMDAG 260
Cdd:PRK14652  167 A---AALGYAYRTCRLPP-GAVITRVEVRLRPGDVAASEALMRADRERRRRTQPLDRPTFGSTFTNPPGDYAGRLVEAVG 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 261 LRGHAIGGAQVSEKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEPEVHRVGEFL 320
Cdd:PRK14652  243 LKGHRVGGAIWSPVHANFVTNLGGATARDVLALVRLARARVKERFGIALETEVRLLGEFL 302
PRK14649 PRK14649
UDP-N-acetylmuramate dehydrogenase;
28-317 1.63e-58

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173112 [Multi-domain]  Cd Length: 295  Bit Score: 190.05  E-value: 1.63e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  28 EPMRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDLLVGDKGIRGVVVALGEGLSDITVNGTHVTA 107
Cdd:PRK14649    7 EPLAPYTSWRIGGPARYFVEPTTPDEAIAAAAWAEQRQLPLFWLGGGSNLLVRDEGFDGLVARYRGQRWELHEHGDTAEV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 108 --AAGALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESvrvykpARMLDDGTRgsgnIIEFDVD 185
Cdd:PRK14649   87 wvEAGAPMAGTARRLAAQGWAGLEWAEGLPGTIGGAIYGNAGCYGGDTATVLIR------AWLLLNGSE----CVEWSVH 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 186 ELNLGYRKS---RIADDGF-----VVLSATFNLAPGNAAMIKADMDDYHQRREDKQPLDmPSAGSTFKRPEGYFAGKLIM 257
Cdd:PRK14649  157 DFAYGYRTSvlkQLRADGItwrppLVLAARFRLHRDDPTALAARMEAIAAERKQKTPAG-SSCGSVFKNPPGDSAGRLIE 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 258 DAGLRGHAIGGAQVSEKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEPEVHRVG 317
Cdd:PRK14649  236 AAGLKGTRIGDAEIATRHANYIINLGGARAADILRLIDLARTRVLAQFGIELELEVRIIG 295
MurB_C pfam02873
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ...
 218-316 4.99e-57

UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are UDP-N-acetylenolpyruvoylglucosamine reductase enzymes EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 460730 [Multi-domain]  Cd Length: 99  Bit Score: 179.47  E-value: 4.99e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 218 IKADMDDYHQRREDKQPLDMPSAGSTFKRPEGYFAGKLIMDAGLRGHAIGGAQVSEKHCGFIVNADHATAADVDELIRHI 297
Cdd:pfam02873   1 IRAAMLELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEV 80

                          90
                  ....*....|....*....
gi 1469296420 298 QTTVKDQFDVDLEPEVHRV 316
Cdd:pfam02873  81 RERVKEKFGVELEPEVRII 99
PRK14651 PRK14651
UDP-N-acetylmuramate dehydrogenase;
29-310 9.18e-53

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237776 [Multi-domain]  Cd Length: 273  Bit Score: 174.62  E-value: 9.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  29 PMRDHTTFKIGGPADVFVTPDTEQgLVATLDTCYRcdlpltIVGNGSDLLVGDKGIRGVVVALGEGLSDITVNGThvtAA 108
Cdd:PRK14651    8 PLARYTTLGVGGPAELWTVETHEQ-LAEATEAPYR------VLGGGSNLLVSDAGVPERVIRLGGEFAEWDLDGW---VG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 109 AGALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRVYKPARMLddgtrgsgniiEFDVDELN 188
Cdd:PRK14651   78 GGVPLPGLVRRAARLGLSGLEGLVGIPAQVGGAVKMNAGTRFGEMADALHTVEIVHDGGFH-----------QYSPDELG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 189 LGYRKSRIADdGFVVLSATFNLAPGNAAMIKADMDDYHQRREDkQPlDMPSAGSTFKRPEGYFAGKLIMDAGLRGHAIGG 268
Cdd:PRK14651  147 FGYRHSGLPP-GHVVTRVRLKLRPSTPEAVLAKMALVDAARKG-QP-KKKSAGCAFKNPPGDSAGRLIDEAGLKGTRVGD 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1469296420 269 AQVSEKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLE 310
Cdd:PRK14651  224 AMISPEHGNFIVNLGGATAADVHALLRRVRARVGLPLELEWE 265
murB PRK13903
UDP-N-acetylmuramate dehydrogenase;
14-312 1.66e-48

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237552 [Multi-domain]  Cd Length: 363  Bit Score: 165.90  E-value: 1.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  14 ALAGVAGEDNVlmsePMRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDLLVGDKGIRGVVVALGE 93
Cdd:PRK13903    9 AFAGAEVAEDV----PLAPLTTLRVGGPARRLVTCTSTEELVAAVRELDAAGEPLLVLGGGSNLVIADDGFDGTVVRVAT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  94 GLSDITVNGTHVTAAAGALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRVYKparmlddgt 173
Cdd:PRK13903   85 RGVTVDCGGGLVRAEAGAVWDDVVARTVEAGLGGLECLSGIPGSAGATPVQNVGAYGQEVSDTITRVRLLD--------- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 174 RGSGNIIEFDVDELNLGYRKSRI-ADDGFVVLSATFNLAPGN----------AAMIKADMDDY---HQRRE--------- 230
Cdd:PRK13903  156 RRTGEVRWVPAADLGFGYRTSVLkHSDRAVVLEVEFQLDPSGlsaplrygelARALGVEPGERvppAAVREavlalragk 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 231 ----DKQPLDMPSAGSTFKRP----------------------------EGYF---AGKLIMDAGL-RGH--AIGGAQVS 272
Cdd:PRK13903  236 gmvlDPADHDTWSAGSFFTNPvvspavaerlaarvaerlgdpvprypagDGGVklsAAWLIERAGFgKGYpgGGAPARLS 315

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1469296420 273 EKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEPE 312
Cdd:PRK13903  316 TKHTLALTNRGGATTADLVALAREVRDGVRDAFGVTLVPE 355
PRK14650 PRK14650
UDP-N-acetylmuramate dehydrogenase;
27-317 2.61e-44

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173113 [Multi-domain]  Cd Length: 302  Bit Score: 153.46  E-value: 2.61e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  27 SEPMRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDLLVGDKGIRGVVVALGEGLSDITVNGTHVT 106
Cdd:PRK14650   18 TKNLANYTTYKIGGISKLFLTPKTIKDAEHIFKAAIEEKIKIFILGGGSNILINDEEEIDFPIIYTGHLNKIEIHDNQIV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 107 AAAGALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRvykparMLDDgtrgSGNII--EFDV 184
Cdd:PRK14650   98 AECGTNFEDLCKFALQNELSGLEFIYGLPGTLGGAIWMNARCFGNEISEILDKIT------FIDE----KGKTIckKFKK 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 185 DELNlgYRKSRIADDGFVVLSATFNLAPGNAAMIKADMDDYHQRREDKQPLDMPSAGSTFKRPEGYF--AGKLIMDAGLR 262
Cdd:PRK14650  168 EEFK--YKISPFQNKNTFILKATLNLKKGNKKHIEEIMKQNKQIRINKGHYLFPSSGSTFKNNKAFLkpTGQIIEECKLK 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1469296420 263 GHAIGGAQVSEKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEPEVHRVG 317
Cdd:PRK14650  246 GLSIGGATVSHYHGNFIININNATSKDIKTLIEKVKTEVQIKTGFLLEEEVLYIG 300
murB PRK13904
UDP-N-acetylmuramate dehydrogenase;
37-313 1.84e-41

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184384 [Multi-domain]  Cd Length: 257  Bit Score: 144.68  E-value: 1.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  37 KIGGPADVFVtpdteqglvatLDTCYRCDLPLTIVGNGSDLLVGDK----GIrgvvvaLGEGLSDITVNGTHVTAAAGAL 112
Cdd:PRK13904   14 KIGPPLEVLV-----------LEEIDDFSQDGQIIGGANNLLISPNpknlAI------LGKNFDYIKIDGECLEIGGATK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 113 LSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRVykparmlDDGtrgsgniiEFDVDELNLGYR 192
Cdd:PRK13904   77 SGKIFNYAKKNNLGGFEFLGKLPGTLGGLVKMNAGLKEYEISNNLESICT-------NGG--------WIEKEDIGFGYR 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 193 KSRIadDGfVVLSATFNLAPGnaamIKADMDDYHQRREDKQPlDMPSAGSTFKRPEGYFAGKLIMDAGLRGHAIGGAQVS 272
Cdd:PRK13904  142 SSGI--NG-VILEARFKKTHG----FDEELLEAFKSMRKNQP-KGPSFGSCFKNPKGDYAGRLIEAVGLKGYCKGGAGFS 213

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1469296420 273 EKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEPEV 313
Cdd:PRK13904  214 EEHANFLVNLGGATFEDALDLIELAKKRVLEEFGINLEEEV 254
PRK14648 PRK14648
UDP-N-acetylmuramate dehydrogenase;
29-318 3.40e-38

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173111 [Multi-domain]  Cd Length: 354  Bit Score: 138.70  E-value: 3.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  29 PMRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDLLVGDKGIRGVVVALGEGLSDITVN----GTH 104
Cdd:PRK14648   17 PLAERCSFRIGGAAQFWAEPRSCTQLRALIEEAQRARIPLSLIGGGSNVLIADEGVPGLMLSLRRFRSLHTQTqrdgSVL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 105 VTAAAGALLSDVAATAAEAGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVR--VYKPARM-------------- 168
Cdd:PRK14648   97 VHAGAGLPVAALLAFCAHHALRGLETFAGLPGSVGGAAYMNARCYGRAIADCFHSARtlVLHPVRSrakelpevrknaqd 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 169 -------LDDGTRGSGNIIEFDVDELNLGYRKSRIADDGFV--------VLSATFNLAPGNAAMIKADMDDYHQRREDKQ 233
Cdd:PRK14648  177 krgeclgLDGGPFTCSSFQTVFARAGDWGYKRSPFQSPHGVelhagrrlILSLCVRLTPGNPAQIRKHMQEKIADRISKG 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 234 PLDMPSAGSTFKRPE--GYFAGKLIMDAGLRGHAIGGAQVSEKHCGFIVNADHATAADVDELIRHIQTTVKDQFDVDLEP 311
Cdd:PRK14648  257 QFRFPSAGSAFKNNPafGKPSGILIEEAGLRGTSCGAAQVAPWHGNLIINTGNATAHQVRTLLRVVRQRVFETHGVWLER 336


                  ....*..
gi 1469296420 312 EVHRVGE 318
Cdd:PRK14648  337 EIIFSGE 343
murB PRK00046
UDP-N-acetylmuramate dehydrogenase;
24-313 1.41e-37

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 234593 [Multi-domain]  Cd Length: 334  Bit Score: 136.43  E-value: 1.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  24 VLMSEPMRDHTTFKIGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSD-LLVGDkgIRGVVVALGegLSDITV-- 100
Cdd:PRK00046    3 LQMNHSLKPLNTFGIDARARHLVEAESEEQLLEALADARAAGLPVLVLGGGSNvLFTED--FDGTVLLNR--IKGIEVls 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 101 -NGTH--VTAAAG----ALlsdVAATAAEaGLTGMEPISGIPGSVGGACYMNAGAYGACMADVLESVRVYKparmlddgt 173
Cdd:PRK00046   79 eDDDAwyLHVGAGenwhDL---VLWTLQQ-GMPGLENLALIPGTVGAAPIQNIGAYGVELKDVCDYVEALD--------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 174 RGSGNIIEFDVDELNLGYRKS---RIADDGFVVLSATFNLA----P----GNAAMIKAD----MDDYHQ----RRE---D 231
Cdd:PRK00046  146 LATGEFVRLSAAECRFGYRDSifkHEYPDRYAITAVGFRLPkqwqPvldyGDLARLDPDtvtaQDVFDAvcaiRRSklpD 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 232 kqPLDMPSAGSTFKRP-----------------EGYF---------AGKLIMDAGLRGHAIGGAQVSEKHCGFIVNADHA 285
Cdd:PRK00046  226 --PKVLGNAGSFFKNPvvsaeqfeallaqypdiPHYPqadgsvklaAGWLIDQCGLKGFQIGGAAVHEKQALVLVNYGNA 303

                         330       340
                  ....*....|....*....|....*...
gi 1469296420 286 TAADVDELIRHIQTTVKDQFDVDLEPEV 313
Cdd:PRK00046  304 TGADVLALARHIQQDVREKFGVELEPEP 331
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 42-173 5.29e-19

FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 426326 [Multi-domain]  Cd Length: 139  Bit Score: 81.86  E-value: 5.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  42 ADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDLLVGDKGIRGVVVALGE--GLSDITVNGTHVTAAAGALLSDVAAT 119
Cdd:pfam01565   1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQTGGIVLDLSRlnGILEIDPEDGTATVEAGVTLGDLVRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1469296420 120 AAEAGLT-GMEPISGIPGSVGGACYMNAGAYGAC----MADVLESVRVykparMLDDGT 173
Cdd:pfam01565  81 LAAKGLLlGLDPGSGIPGTVGGAIATNAGGYGSEkyglTRDNVLGLEV-----VLADGE 134
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
38-212 1.47e-08

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 55.67  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420  38 IGGPADVFVTPDTEQGLVATLDTCYRCDLPLTIVGNGSDL---LVGDKGirGVVVALgEGLSDI----TVNGThVTAAAG 110
Cdd:COG0277    36 YRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLaggAVPLDG--GVVLDL-SRMNRIlevdPEDRT-ATVEAG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469296420 111 ALLSDVAATAAEAGLT-GMEPISGIPGSVGG-----ACYMNAGAYGAcMADVLESVRVykparMLDDGT--RGSGNII-- 180
Cdd:COG0277   112 VTLADLNAALAPHGLFfPPDPSSQGTATIGGniatnAGGPRSLKYGL-TRDNVLGLEV-----VLADGEvvRTGGRVPkn 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1469296420 181 --EFDVDEL------NLGyrksriaddgfVVLSATFNLAP 212
Cdd:COG0277   186 vtGYDLFWLlvgsegTLG-----------VITEATLRLHP 214
 
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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