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Conserved domains on  [gi|1403656416|emb|SQI96010|]
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UDP-N-acetylenolpyruvoylglucosamine reductase [Staphylococcus lugdunensis]

Protein Classification

UDP-N-acetylmuramate dehydrogenase( domain architecture ID 11486943)

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 PRK13906
UDP-N-acetylmuramate dehydrogenase;
1-307 0e+00

UDP-N-acetylmuramate dehydrogenase;


:

Pssm-ID: 184386 [Multi-domain]  Cd Length: 307  Bit Score: 624.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416   1 MSQEDILTDLKKLVPRDIIKINEPLKHYTYTKTGGNADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK13906    1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  81 GIVISLLSLNHIAVSDDAIIAGSGAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
Cdd:PRK13906   81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 161 GDLLKFTNQELELDYRNSIVQQQHLVVLEAAFTLAPGQLDDIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK13906  161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403656416 241 QDSNLQGHRIGGVEVSKKHAGFMVNVDNGTATDYENLIHHVQQVVKEKFDVELHREVRIIGDPPDKH 307
Cdd:PRK13906  241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKES 307
 
Name Accession Description Interval E-value
murB PRK13906
UDP-N-acetylmuramate dehydrogenase;
1-307 0e+00

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184386 [Multi-domain]  Cd Length: 307  Bit Score: 624.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416   1 MSQEDILTDLKKLVPRDIIKINEPLKHYTYTKTGGNADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK13906    1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  81 GIVISLLSLNHIAVSDDAIIAGSGAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
Cdd:PRK13906   81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 161 GDLLKFTNQELELDYRNSIVQQQHLVVLEAAFTLAPGQLDDIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK13906  161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403656416 241 QDSNLQGHRIGGVEVSKKHAGFMVNVDNGTATDYENLIHHVQQVVKEKFDVELHREVRIIGDPPDKH 307
Cdd:PRK13906  241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKES 307
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
 23-300 2.56e-148

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: 417.49  E-value: 2.56e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  23 EPLKHYTYTKTGGNADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGGIRGIVISLLSLNHIAVSDDAII-A 101
Cdd:COG0812     1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLGRLKGIEVDDGVLVtA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 102 GSGAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGDLLKFTNQELELDYRNSIVQ 181
Cdd:COG0812    81 GAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTGEVRTLSAEECGFGYRDSIFK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 182 QQHLVVLEAAFTLAPGQLDDIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSKKHAG 261
Cdd:COG0812   161 RERYIILSVTFRLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRIGGAQVSEKHAN 240

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1403656416 262 FMVNVDNGTATDYENLIHHVQQVVKEKFDVELHREVRII 300
Cdd:COG0812   241 FLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
 25-301 7.34e-80

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: 243.90  E-value: 7.34e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  25 LKHYTYTKTGGNADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGGIRGIVISLLSLN-HIAVSDDAIIAGS 103
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGIdIEDDEGEYVHVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 104 GAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGDLLKFTNQELELDYRNSIVQQQ 183
Cdd:TIGR00179  81 GENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATILLATGKTEWLTNEQLGFGYRTSIFQHK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 184 HL-VVLEAAFTLAPG---QLDD--IQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSK 257
Cdd:TIGR00179 161 YVgLVLKAEFQLTLGfgtRLDPetITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKGYQIGGAAVSK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1403656416 258 KHAGFMVNVDNGTATDYENLIHHVQQVVKEKFDVELHREVRIIG 301
Cdd:TIGR00179 241 QHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKIIG 284
MurB_C pfam02873
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ...
 202-300 2.51e-53

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: 169.45  E-value: 2.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 202 IQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSKKHAGFMVNVDNGTATDYENLIHHV 281
Cdd:pfam02873   1 IRAAMLELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEV 80

                          90
                  ....*....|....*....
gi 1403656416 282 QQVVKEKFDVELHREVRII 300
Cdd:pfam02873  81 RERVKEKFGVELEPEVRII 99
 
Name Accession Description Interval E-value
murB PRK13906
UDP-N-acetylmuramate dehydrogenase;
1-307 0e+00

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184386 [Multi-domain]  Cd Length: 307  Bit Score: 624.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416   1 MSQEDILTDLKKLVPRDIIKINEPLKHYTYTKTGGNADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK13906    1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  81 GIVISLLSLNHIAVSDDAIIAGSGAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
Cdd:PRK13906   81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 161 GDLLKFTNQELELDYRNSIVQQQHLVVLEAAFTLAPGQLDDIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK13906  161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403656416 241 QDSNLQGHRIGGVEVSKKHAGFMVNVDNGTATDYENLIHHVQQVVKEKFDVELHREVRIIGDPPDKH 307
Cdd:PRK13906  241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKES 307
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
9-303 2.14e-163

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 456.11  E-value: 2.14e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416   9 DLKKLVP--RDIIKINEPLKHYTYTKTGGNADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGGIRGIVISL 86
Cdd:PRK13905    1 LLKELLPalRGRLLENEPLARYTSFRVGGPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVRDGGIRGVVIRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  87 -LSLNHIAVSDDAIIAGSGAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGDLLK 165
Cdd:PRK13905   81 gKGLNEIEVEGNRITAGAGAPLIKLARFAAEAGLSGLEFAAGIPGTVGGAVFMNAGAYGGETADVLESVEVLDRDGEIKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 166 FTNQELELDYRNSIVQQQHLVVLEAAFTLAPGQLDDIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNL 245
Cdd:PRK13905  161 LSNEELGFGYRHSALQEEGLIVLSATFQLEPGDKEEIKARMDELLARREATQPLEYPSAGSVFKNPPGHFAGKLIEEAGL 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1403656416 246 QGHRIGGVEVSKKHAGFMVNVDNGTATDYENLIHHVQQVVKEKFDVELHREVRIIGDP 303
Cdd:PRK13905  241 KGYRIGGAQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRIIGEF 298
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
 23-300 2.56e-148

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: 417.49  E-value: 2.56e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  23 EPLKHYTYTKTGGNADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGGIRGIVISLLSLNHIAVSDDAII-A 101
Cdd:COG0812     1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLGRLKGIEVDDGVLVtA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 102 GSGAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGDLLKFTNQELELDYRNSIVQ 181
Cdd:COG0812    81 GAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTGEVRTLSAEECGFGYRDSIFK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 182 QQHLVVLEAAFTLAPGQLDDIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSKKHAG 261
Cdd:COG0812   161 RERYIILSVTFRLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRIGGAQVSEKHAN 240

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1403656416 262 FMVNVDNGTATDYENLIHHVQQVVKEKFDVELHREVRII 300
Cdd:COG0812   241 FLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
PRK12436 PRK12436
UDP-N-acetylmuramate dehydrogenase;
1-302 1.29e-140

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 171497 [Multi-domain]  Cd Length: 305  Bit Score: 399.00  E-value: 1.29e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416   1 MSQEDILTDLKKLVPRDIIKINEPLKHYTYTKTGGNADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK12436    1 MNMQEVYEYLSTVLPEGHVKQDEMLKNHTHIKVGGKADVFVAPTNYDEIQEVIKYANKYNIPVTFLGNGSNVIIKDGGIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  81 GIVISLLSLNHIAVSDDAIIAGSGAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
Cdd:PRK12436   81 GITVSLIHITGVTVTGTTIVAQCGAAIIDVSRIALDHNLTGLEFACGIPGSVGGALYMNAGAYGGEISFVLTEAVVMTGD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 161 GDLLKFTNQELELDYRNSIVQQQHLVVLEAAFTLAPGQLDDIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK12436  161 GELRTLTKEAFEFGYRKSVFANNHYIILEARFELEEGVYEEIKAKMDDLTFKRESKQPLEYPSCGSVFKRPPNNFAGKLI 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1403656416 241 QDSNLQGHRIGGVEVSKKHAGFMVNVDNGTATDYENLIHHVQQVVKEKFDVELHREVRIIGD 302
Cdd:PRK12436  241 QESGLQGKRIGGVEVSLKHAGFMVNVDNGTAQDYIDLIHFVQKTVEEKFGVKLEREVRIIGE 302
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
 25-301 7.34e-80

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: 243.90  E-value: 7.34e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  25 LKHYTYTKTGGNADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGGIRGIVISLLSLN-HIAVSDDAIIAGS 103
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGIdIEDDEGEYVHVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 104 GAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGDLLKFTNQELELDYRNSIVQQQ 183
Cdd:TIGR00179  81 GENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATILLATGKTEWLTNEQLGFGYRTSIFQHK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 184 HL-VVLEAAFTLAPG---QLDD--IQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSK 257
Cdd:TIGR00179 161 YVgLVLKAEFQLTLGfgtRLDPetITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKGYQIGGAAVSK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1403656416 258 KHAGFMVNVDNGTATDYENLIHHVQQVVKEKFDVELHREVRIIG 301
Cdd:TIGR00179 241 QHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKIIG 284
PRK14653 PRK14653
UDP-N-acetylmuramate dehydrogenase;
21-299 2.97e-63

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237778 [Multi-domain]  Cd Length: 297  Bit Score: 201.99  E-value: 2.97e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  21 INEPLKHYTYTKTGGNAD-FYLSPTKNEEVQAIVRYARQHDIPVtyLGNGSNIIIREGGIRGIVISLLSLNHIAVSDDAI 99
Cdd:PRK14653   18 INEEMKCHVSFKIGGPVPlFAIPNSTNGFIETINLLKEGIEVKI--LGNGTNVLPKDEPMDFVVVSTERLDDIFVDNDKI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 100 IAGSGAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALcVNEQGDLLKFTNQELELDYRNSI 179
Cdd:PRK14653   96 ICESGLSLKKLCLVAAKNGLSGFENAYGIPGSVGGAVYMNAGAYGWETAENIVEVV-AYDGKKIIRLGKNEIKFSYRNSI 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 180 V-QQQHLVVLEAAFTLAPGQLDDIQAKMDDLTERRESKQPLEYPSCGSVFQRP-PGHFAGKLIQDSNLQGHRIGGVEVSK 257
Cdd:PRK14653  175 FkEEKDLIILRVTFKLKKGNKNEIYNLMLETMKKRVEKQPLEFPSAGSVFKRPrKDFYVGSAIEKLGLKGFSIGGAQISE 254

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1403656416 258 KHAGFMVNVDNGTATDYENLIHHVQQVVKEKFDVELHREVRI 299
Cdd:PRK14653  255 KHAGFIINYNNAKAEDVLKLIEYVKDKIYENYNVELETEIEI 296
PRK14649 PRK14649
UDP-N-acetylmuramate dehydrogenase;
22-301 6.98e-63

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173112 [Multi-domain]  Cd Length: 295  Bit Score: 200.84  E-value: 6.98e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  22 NEPLKHYTYTKTGGNADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGGIRGIVISLLSLN---HIAVSDDA 98
Cdd:PRK14649    6 NEPLAPYTSWRIGGPARYFVEPTTPDEAIAAAAWAEQRQLPLFWLGGGSNLLVRDEGFDGLVARYRGQRwelHEHGDTAE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  99 IIAGSGAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGDLLKFTNQELELDYRNS 178
Cdd:PRK14649   86 VWVEAGAPMAGTARRLAAQGWAGLEWAEGLPGTIGGAIYGNAGCYGGDTATVLIRAWLLLNGSECVEWSVHDFAYGYRTS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 179 IVQQ--------QHLVVLEAAFTLAPGQLDDIQAKMDDLTERRESKQPLEyPSCGSVFQRPPGHFAGKLIQDSNLQGHRI 250
Cdd:PRK14649  166 VLKQlradgitwRPPLVLAARFRLHRDDPTALAARMEAIAAERKQKTPAG-SSCGSVFKNPPGDSAGRLIEAAGLKGTRI 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1403656416 251 GGVEVSKKHAGFMVNVDNGTATDYENLIHHVQQVVKEKFDVELHREVRIIG 301
Cdd:PRK14649  245 GDAEIATRHANYIINLGGARAADILRLIDLARTRVLAQFGIELELEVRIIG 295
PRK14652 PRK14652
UDP-N-acetylmuramate dehydrogenase;
16-302 2.35e-60

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237777 [Multi-domain]  Cd Length: 302  Bit Score: 194.71  E-value: 2.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  16 RDIIKINEPLKHYTYTKTGGNADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGGIRGIVISLLSLNHIAVS 95
Cdd:PRK14652   15 RGEVLRDAPLAPRTAVRVGGPADLLVRPADPDALSALLRAVRELGVPLSILGGGANTLVADAGVRGVVLRLPQDFPGEST 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  96 DDA-IIAGSGAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDyALCVNEQGDLLKFTNQELELD 174
Cdd:PRK14652   95 DGGrLVLGAGAPISRLPARAHAHGLVGMEFLAGIPGTLGGAVAMNAGTKLGEMKDVVT-AVELATADGAGFVPAAALGYA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 175 YRNSIVQQQHlVVLEAAFTLAPGQLDDIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVE 254
Cdd:PRK14652  174 YRTCRLPPGA-VITRVEVRLRPGDVAASEALMRADRERRRRTQPLDRPTFGSTFTNPPGDYAGRLVEAVGLKGHRVGGAI 252

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1403656416 255 VSKKHAGFMVNVDNGTATDYENLIHHVQQVVKEKFDVELHREVRIIGD 302
Cdd:PRK14652  253 WSPVHANFVTNLGGATARDVLALVRLARARVKERFGIALETEVRLLGE 300
MurB_C pfam02873
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ...
 202-300 2.51e-53

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: 169.45  E-value: 2.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 202 IQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSKKHAGFMVNVDNGTATDYENLIHHV 281
Cdd:pfam02873   1 IRAAMLELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEV 80

                          90
                  ....*....|....*....
gi 1403656416 282 QQVVKEKFDVELHREVRII 300
Cdd:pfam02873  81 RERVKEKFGVELEPEVRII 99
PRK14650 PRK14650
UDP-N-acetylmuramate dehydrogenase;
20-301 6.35e-45

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173113 [Multi-domain]  Cd Length: 302  Bit Score: 154.62  E-value: 6.35e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  20 KIN-----EPLKHYTYTKTGGNADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGG-IRGIVISLLSLNHIA 93
Cdd:PRK14650   11 KINikpqtKNLANYTTYKIGGISKLFLTPKTIKDAEHIFKAAIEEKIKIFILGGGSNILINDEEeIDFPIIYTGHLNKIE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  94 VSDDAIIAGSGAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGDLLKFTNQELEL 173
Cdd:PRK14650   91 IHDNQIVAECGTNFEDLCKFALQNELSGLEFIYGLPGTLGGAIWMNARCFGNEISEILDKITFIDEKGKTICKKFKKEEF 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 174 DYRNSIVQQQHLVVLEAAFTLAPGQLDDIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHF--AGKLIQDSNLQGHRIG 251
Cdd:PRK14650  171 KYKISPFQNKNTFILKATLNLKKGNKKHIEEIMKQNKQIRINKGHYLFPSSGSTFKNNKAFLkpTGQIIEECKLKGLSIG 250

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1403656416 252 GVEVSKKHAGFMVNVDNGTATDYENLIHHVQQVVKEKFDVELHREVRIIG 301
Cdd:PRK14650  251 GATVSHYHGNFIININNATSKDIKTLIEKVKTEVQIKTGFLLEEEVLYIG 300
murB PRK13904
UDP-N-acetylmuramate dehydrogenase;
114-300 5.47e-41

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184384 [Multi-domain]  Cd Length: 257  Bit Score: 143.14  E-value: 5.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 114 ARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDyALCVNeQGDLLKftnQELELDYRNSIVQQqhlVVLEAAFT 193
Cdd:PRK13904   84 AKKNNLGGFEFLGKLPGTLGGLVKMNAGLKEYEISNNLE-SICTN-GGWIEK---EDIGFGYRSSGING---VILEARFK 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 194 LAPGQLDDIQakmDDLTERRESkQPLEyPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSKKHAGFMVNVDNGTATD 273
Cdd:PRK13904  156 KTHGFDEELL---EAFKSMRKN-QPKG-PSFGSCFKNPKGDYAGRLIEAVGLKGYCKGGAGFSEEHANFLVNLGGATFED 230

                         170       180
                  ....*....|....*....|....*..
gi 1403656416 274 YENLIHHVQQVVKEKFDVELHREVRII 300
Cdd:PRK13904  231 ALDLIELAKKRVLEEFGINLEEEVIIL 257
PRK14651 PRK14651
UDP-N-acetylmuramate dehydrogenase;
24-292 6.22e-37

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237776 [Multi-domain]  Cd Length: 273  Bit Score: 133.02  E-value: 6.22e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  24 PLKHYTYTKTGGNADFYLSPTKNEEVQAIvryarqhDIPVTYLGNGSNIIIREGGIRGIVISLLSlnHIAVSDDAIIAGS 103
Cdd:PRK14651    8 PLARYTTLGVGGPAELWTVETHEQLAEAT-------EAPYRVLGGGSNLLVSDAGVPERVIRLGG--EFAEWDLDGWVGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 104 GAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGdLLKFTNQELELDYRNSIVQQQ 183
Cdd:PRK14651   79 GVPLPGLVRRAARLGLSGLEGLVGIPAQVGGAVKMNAGTRFGEMADALHTVEIVHDGG-FHQYSPDELGFGYRHSGLPPG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 184 HlVVLEAAFTLAPGQLDDIQAKMDDLTERRESKQPLEYPSCGsvFQRPPGHFAGKLIQDSNLQGHRIGGVEVSKKHAGFM 263
Cdd:PRK14651  158 H-VVTRVRLKLRPSTPEAVLAKMALVDAARKGQPKKKSAGCA--FKNPPGDSAGRLIDEAGLKGTRVGDAMISPEHGNFI 234

                         250       260
                  ....*....|....*....|....*....
gi 1403656416 264 VNVDNGTATDYENLIHHVQQVVKEKFDVE 292
Cdd:PRK14651  235 VNLGGATAADVHALLRRVRARVGLPLELE 263
PRK14648 PRK14648
UDP-N-acetylmuramate dehydrogenase;
12-302 6.68e-36

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173111 [Multi-domain]  Cd Length: 354  Bit Score: 132.15  E-value: 6.68e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  12 KLVPRDIIKINEPLKHYTYTKTGGNADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGGIRGIVISLL---S 88
Cdd:PRK14648    5 RIRARRITRRNVPLAERCSFRIGGAAQFWAEPRSCTQLRALIEEAQRARIPLSLIGGGSNVLIADEGVPGLMLSLRrfrS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  89 LNHIAVSDDAII--AGSGAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCV--------- 157
Cdd:PRK14648   85 LHTQTQRDGSVLvhAGAGLPVAALLAFCAHHALRGLETFAGLPGSVGGAAYMNARCYGRAIADCFHSARTLvlhpvrsra 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 158 -----------NEQGDLL-----KFTNQELEL--------DYRNSIVQQQHLVVLEAA--------FTLAPGQLDDIQAK 205
Cdd:PRK14648  165 kelpevrknaqDKRGECLgldggPFTCSSFQTvfaragdwGYKRSPFQSPHGVELHAGrrlilslcVRLTPGNPAQIRKH 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 206 MDDLTERRESKQPLEYPSCGSVFQRPP--GHFAGKLIQDSNLQGHRIGGVEVSKKHAGFMVNVDNGTATDYENLIHHVQQ 283
Cdd:PRK14648  245 MQEKIADRISKGQFRFPSAGSAFKNNPafGKPSGILIEEAGLRGTSCGAAQVAPWHGNLIINTGNATAHQVRTLLRVVRQ 324

                         330
                  ....*....|....*....
gi 1403656416 284 VVKEKFDVELHREVRIIGD 302
Cdd:PRK14648  325 RVFETHGVWLEREIIFSGE 343
murB PRK00046
UDP-N-acetylmuramate dehydrogenase;
19-300 1.08e-33

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 234593 [Multi-domain]  Cd Length: 334  Bit Score: 125.64  E-value: 1.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  19 IKINEPLKHYTytkTGG---NADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGgIRGIVI--SLLSLNHIA 93
Cdd:PRK00046    3 LQMNHSLKPLN---TFGidaRARHLVEAESEEQLLEALADARAAGLPVLVLGGGSNVLFTED-FDGTVLlnRIKGIEVLS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  94 VSDDAII--AGSGAAIIDVSKAARDHALTGLE-FACgIPGSIGGAVYMNAGAYGGEVKDCIDYALCVN-EQGDLLKFTNQ 169
Cdd:PRK00046   79 EDDDAWYlhVGAGENWHDLVLWTLQQGMPGLEnLAL-IPGTVGAAPIQNIGAYGVELKDVCDYVEALDlATGEFVRLSAA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 170 ELELDYRNSIVQQQHL---VVLEAAFTLA----P----GQLDDIQAK-------MDDLTERRESK--QPLEYPSCGSVFQ 229
Cdd:PRK00046  158 ECRFGYRDSIFKHEYPdryAITAVGFRLPkqwqPvldyGDLARLDPDtvtaqdvFDAVCAIRRSKlpDPKVLGNAGSFFK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 230 RP--------------PG--HF----------AGKLIQDSNLQGHRIGGVEVSKKHAGFMVNVDNGTATDYENLIHHVQQ 283
Cdd:PRK00046  238 NPvvsaeqfeallaqyPDipHYpqadgsvklaAGWLIDQCGLKGFQIGGAAVHEKQALVLVNYGNATGADVLALARHIQQ 317

                         330
                  ....*....|....*..
gi 1403656416 284 VVKEKFDVELHREVRII 300
Cdd:PRK00046  318 DVREKFGVELEPEPRFI 334
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 37-167 6.71e-29

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: 107.67  E-value: 6.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  37 ADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGGIRGIVISLLSLNHIAVSDDA---IIAGSGAAIIDVSKA 113
Cdd:pfam01565   1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQTGGIVLDLSRLNGILEIDPEdgtATVEAGVTLGDLVRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1403656416 114 ARDHALT-GLEFACGIPGSIGGAVYMNAGAYGGE----VKDCIDYALCVNEQGDLLKFT 167
Cdd:pfam01565  81 LAAKGLLlGLDPGSGIPGTVGGAIATNAGGYGSEkyglTRDNVLGLEVVLADGEVVRLG 139
murB PRK13903
UDP-N-acetylmuramate dehydrogenase;
24-301 8.39e-23

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237552 [Multi-domain]  Cd Length: 363  Bit Score: 96.57  E-value: 8.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  24 PLKHYTYTKTGGNADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIIIREGGIRGIVIsllslnHIAVSD------- 96
Cdd:PRK13903   20 PLAPLTTLRVGGPARRLVTCTSTEELVAAVRELDAAGEPLLVLGGGSNLVIADDGFDGTVV------RVATRGvtvdcgg 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  97 DAIIAGSGAAIIDVSKAARDHALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCI------DYALcvneqGDLLKFTNQE 170
Cdd:PRK13903   94 GLVRAEAGAVWDDVVARTVEAGLGGLECLSGIPGSAGATPVQNVGAYGQEVSDTItrvrllDRRT-----GEVRWVPAAD 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 171 LELDYRNSIVQQQ-HLVVLEAAFTLAPG-------------QLDDIQAKMDDLTERRE-------SKQPLEYP------S 223
Cdd:PRK13903  169 LGFGYRTSVLKHSdRAVVLEVEFQLDPSglsaplrygelarALGVEPGERVPPAAVREavlalraGKGMVLDPadhdtwS 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416 224 CGSVFQRP----------------------------PGHF---AGKLIQDSNL-QGHRIGG--VEVSKKHAGFMVNVDNG 269
Cdd:PRK13903  249 AGSFFTNPvvspavaerlaarvaerlgdpvprypagDGGVklsAAWLIERAGFgKGYPGGGapARLSTKHTLALTNRGGA 328

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1403656416 270 TATDYENLIHHVQQVVKEKFDVELHREVRIIG 301
Cdd:PRK13903  329 TTADLVALAREVRDGVRDAFGVTLVPEPVLVG 360
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
1-144 1.06e-12

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


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 68.00  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416   1 MSQEDILTDLKKLVPRDIIKINEPLKHYTYTKTG---GNADFYLSPTKNEEVQAIVRYARQHDIPVTYLGNGSNIiirEG 77
Cdd:COG0277     1 MLTAALLAALRAILAGRVLTDPADRAAYARDGNSlyrGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGL---AG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  78 GI----RGIVISLLSLNHI-AVSDDA--IIAGSGAAIIDVSKAARDHaltGLEFACGiPGS-----IGGAVYMNAG---- 141
Cdd:COG0277    78 GAvpldGGVVLDLSRMNRIlEVDPEDrtATVEAGVTLADLNAALAPH---GLFFPPD-PSSqgtatIGGNIATNAGgprs 153


                  ....
gi 1403656416 142 -AYG 144
Cdd:COG0277   154 lKYG 157
PRK11230 PRK11230
glycolate oxidase subunit GlcD; Provisional
 43-165 1.02e-03

glycolate oxidase subunit GlcD; Provisional


Pssm-ID: 183043 [Multi-domain]  Cd Length: 499  Bit Score: 40.53  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403656416  43 PTKNEEVQAIVRYARQHDIPVTYLGNGSNIiirEGGI----RGIVISLLSLNHI-AVSDDAIIA--GSGAAIIDVSKAAR 115
Cdd:PRK11230   62 PKQMEQVQALLAVCHRLRVPVVARGAGTGL---SGGAlpleKGVLLVMARFNRIlDINPVGRRArvQPGVRNLAISQAAA 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1403656416 116 DHAL-----TGLEFACgipgSIGGAVYMNAGAYggevkDCIDYALCVNeqgDLLK 165
Cdd:PRK11230  139 PHGLyyapdPSSQIAC----SIGGNVAENAGGV-----HCLKYGLTVH---NLLK 181
 
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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