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Conserved domains on  [gi|488388214|ref|WP_002457599|]
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UDP-N-acetylmuramate dehydrogenase [Staphylococcus epidermidis]

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;
1-306 0e+00

UDP-N-acetylmuramate dehydrogenase;


:

Pssm-ID: 184386 [Multi-domain]  Cd Length: 307  Bit Score: 610.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214   1 MNKNDILRGLESILPKDIIKVDEPLKRYTYTETGGKADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK13906   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  81 GIVLSLLSLNHIETSDDAIIAGSGAAIIDVSNVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDYALCVNEK 160
Cdd:PRK13906  81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 161 GDLLKLTTAELELDYRNSVVQQKHLVVLEAAFTLEPGKLDEIQAKMDDLTERRESKQPLEFPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK13906 161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488388214 241 QDSNLQGYRIGGVEVSTKHAGFMVNVDNGTATDYEALIHHVQKTVKEKFDVELNTEVRIIGEHPTD 306
Cdd:PRK13906 241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKE 306
 
Name Accession Description Interval E-value
murB PRK13906
UDP-N-acetylmuramate dehydrogenase;
1-306 0e+00

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184386 [Multi-domain]  Cd Length: 307  Bit Score: 610.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214   1 MNKNDILRGLESILPKDIIKVDEPLKRYTYTETGGKADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK13906   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  81 GIVLSLLSLNHIETSDDAIIAGSGAAIIDVSNVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDYALCVNEK 160
Cdd:PRK13906  81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 161 GDLLKLTTAELELDYRNSVVQQKHLVVLEAAFTLEPGKLDEIQAKMDDLTERRESKQPLEFPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK13906 161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488388214 241 QDSNLQGYRIGGVEVSTKHAGFMVNVDNGTATDYEALIHHVQKTVKEKFDVELNTEVRIIGEHPTD 306
Cdd:PRK13906 241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKE 306
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
23-300 3.04e-143

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: 404.40  E-value: 3.04e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  23 EPLKRYTYTETGGKADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGGIRGIVLSLLSLNHIETSDDAII-A 101
Cdd:COG0812    1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLGRLKGIEVDDGVLVtA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 102 GSGAAIIDVSNVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDYALCVNEKGDLLKLTTAELELDYRNSVVQ 181
Cdd:COG0812   81 GAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTGEVRTLSAEECGFGYRDSIFK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 182 QKHLVVLEAAFTLEPGKLDEIQAKMDDLTERRESKQPLEFPSCGSVFQRPPGHFAGKLIQDSNLQGYRIGGVEVSTKHAG 261
Cdd:COG0812  161 RERYIILSVTFRLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRIGGAQVSEKHAN 240
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 488388214 262 FMVNVDNGTATDYEALIHHVQKTVKEKFDVELNTEVRII 300
Cdd:COG0812  241 FLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
25-301 5.24e-79

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: 241.59  E-value: 5.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214   25 LKRYTYTETGGKADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGGIRGIVLSLLSLN-HIETSDDAIIAGS 103
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGIdIEDDEGEYVHVGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  104 GAAIIDVSNVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDYALCVNEKGDLLKLTTAELELDYRNSVVQQK 183
Cdd:TIGR00179  81 GENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATILLATGKTEWLTNEQLGFGYRTSIFQHK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  184 HL-VVLEAAFTLEPG---KLDE--IQAKMDDLTERRESKQPLEFPSCGSVFQRPPGHFAGKLIQDSNLQGYRIGGVEVST 257
Cdd:TIGR00179 161 YVgLVLKAEFQLTLGfgtRLDPetITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKGYQIGGAAVSK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 488388214  258 KHAGFMVNVDNGTATDYEALIHHVQKTVKEKFDVELNTEVRIIG 301
Cdd:TIGR00179 241 QHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKIIG 284
MurB_C pfam02873
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ...
202-300 4.12e-54

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: 171.38  E-value: 4.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  202 IQAKMDDLTERRESKQPLEFPSCGSVFQRPPGHFAGKLIQDSNLQGYRIGGVEVSTKHAGFMVNVDNGTATDYEALIHHV 281
Cdd:pfam02873   1 IRAAMLELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEV 80
                          90
                  ....*....|....*....
gi 488388214  282 QKTVKEKFDVELNTEVRII 300
Cdd:pfam02873  81 RERVKEKFGVELEPEVRII 99
 
Name Accession Description Interval E-value
murB PRK13906
UDP-N-acetylmuramate dehydrogenase;
1-306 0e+00

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184386 [Multi-domain]  Cd Length: 307  Bit Score: 610.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214   1 MNKNDILRGLESILPKDIIKVDEPLKRYTYTETGGKADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK13906   1 MINKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  81 GIVLSLLSLNHIETSDDAIIAGSGAAIIDVSNVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDYALCVNEK 160
Cdd:PRK13906  81 GIVISLLSLDHIEVSDDAIIAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 161 GDLLKLTTAELELDYRNSVVQQKHLVVLEAAFTLEPGKLDEIQAKMDDLTERRESKQPLEFPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK13906 161 GSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLI 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488388214 241 QDSNLQGYRIGGVEVSTKHAGFMVNVDNGTATDYEALIHHVQKTVKEKFDVELNTEVRIIGEHPTD 306
Cdd:PRK13906 241 QDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGEHPKE 306
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
10-302 1.41e-160

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 449.18  E-value: 1.41e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  10 LESILP--KDIIKVDEPLKRYTYTETGGKADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGGIRGIVLSL- 86
Cdd:PRK13905   2 LKELLPalRGRLLENEPLARYTSFRVGGPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVRDGGIRGVVIRLg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  87 LSLNHIETSDDAIIAGSGAAIIDVSNVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDYALCVNEKGDLLKL 166
Cdd:PRK13905  82 KGLNEIEVEGNRITAGAGAPLIKLARFAAEAGLSGLEFAAGIPGTVGGAVFMNAGAYGGETADVLESVEVLDRDGEIKTL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 167 TTAELELDYRNSVVQQKHLVVLEAAFTLEPGKLDEIQAKMDDLTERRESKQPLEFPSCGSVFQRPPGHFAGKLIQDSNLQ 246
Cdd:PRK13905 162 SNEELGFGYRHSALQEEGLIVLSATFQLEPGDKEEIKARMDELLARREATQPLEYPSAGSVFKNPPGHFAGKLIEEAGLK 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488388214 247 GYRIGGVEVSTKHAGFMVNVDNGTATDYEALIHHVQKTVKEKFDVELNTEVRIIGE 302
Cdd:PRK13905 242 GYRIGGAQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRIIGE 297
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
23-300 3.04e-143

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: 404.40  E-value: 3.04e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  23 EPLKRYTYTETGGKADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGGIRGIVLSLLSLNHIETSDDAII-A 101
Cdd:COG0812    1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLGRLKGIEVDDGVLVtA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 102 GSGAAIIDVSNVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDYALCVNEKGDLLKLTTAELELDYRNSVVQ 181
Cdd:COG0812   81 GAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTGEVRTLSAEECGFGYRDSIFK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 182 QKHLVVLEAAFTLEPGKLDEIQAKMDDLTERRESKQPLEFPSCGSVFQRPPGHFAGKLIQDSNLQGYRIGGVEVSTKHAG 261
Cdd:COG0812  161 RERYIILSVTFRLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRIGGAQVSEKHAN 240
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 488388214 262 FMVNVDNGTATDYEALIHHVQKTVKEKFDVELNTEVRII 300
Cdd:COG0812  241 FLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
PRK12436 PRK12436
UDP-N-acetylmuramate dehydrogenase;
1-302 1.57e-141

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 171497 [Multi-domain]  Cd Length: 305  Bit Score: 401.31  E-value: 1.57e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214   1 MNKNDILRGLESILPKDIIKVDEPLKRYTYTETGGKADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGGIR 80
Cdd:PRK12436   1 MNMQEVYEYLSTVLPEGHVKQDEMLKNHTHIKVGGKADVFVAPTNYDEIQEVIKYANKYNIPVTFLGNGSNVIIKDGGIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  81 GIVLSLLSLNHIETSDDAIIAGSGAAIIDVSNVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDYALCVNEK 160
Cdd:PRK12436  81 GITVSLIHITGVTVTGTTIVAQCGAAIIDVSRIALDHNLTGLEFACGIPGSVGGALYMNAGAYGGEISFVLTEAVVMTGD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 161 GDLLKLTTAELELDYRNSVVQQKHLVVLEAAFTLEPGKLDEIQAKMDDLTERRESKQPLEFPSCGSVFQRPPGHFAGKLI 240
Cdd:PRK12436 161 GELRTLTKEAFEFGYRKSVFANNHYIILEARFELEEGVYEEIKAKMDDLTFKRESKQPLEYPSCGSVFKRPPNNFAGKLI 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488388214 241 QDSNLQGYRIGGVEVSTKHAGFMVNVDNGTATDYEALIHHVQKTVKEKFDVELNTEVRIIGE 302
Cdd:PRK12436 241 QESGLQGKRIGGVEVSLKHAGFMVNVDNGTAQDYIDLIHFVQKTVEEKFGVKLEREVRIIGE 302
murB TIGR00179
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ...
25-301 5.24e-79

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: 241.59  E-value: 5.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214   25 LKRYTYTETGGKADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGGIRGIVLSLLSLN-HIETSDDAIIAGS 103
Cdd:TIGR00179   1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGIdIEDDEGEYVHVGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  104 GAAIIDVSNVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDYALCVNEKGDLLKLTTAELELDYRNSVVQQK 183
Cdd:TIGR00179  81 GENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATILLATGKTEWLTNEQLGFGYRTSIFQHK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  184 HL-VVLEAAFTLEPG---KLDE--IQAKMDDLTERRESKQPLEFPSCGSVFQRPPGHFAGKLIQDSNLQGYRIGGVEVST 257
Cdd:TIGR00179 161 YVgLVLKAEFQLTLGfgtRLDPetITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKGYQIGGAAVSK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 488388214  258 KHAGFMVNVDNGTATDYEALIHHVQKTVKEKFDVELNTEVRIIG 301
Cdd:TIGR00179 241 QHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKIIG 284
PRK14652 PRK14652
UDP-N-acetylmuramate dehydrogenase;
19-302 4.10e-66

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237777 [Multi-domain]  Cd Length: 302  Bit Score: 209.34  E-value: 4.10e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  19 IKVDEPLKRYTYTETGGKADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGGIRGIVLSLLSLNHIETSDDA 98
Cdd:PRK14652  18 VLRDAPLAPRTAVRVGGPADLLVRPADPDALSALLRAVRELGVPLSILGGGANTLVADAGVRGVVLRLPQDFPGESTDGG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  99 -IIAGSGAAIIDVSNVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDyALCVNEKGDLLKLTTAELELDYRN 177
Cdd:PRK14652  98 rLVLGAGAPISRLPARAHAHGLVGMEFLAGIPGTLGGAVAMNAGTKLGEMKDVVT-AVELATADGAGFVPAAALGYAYRT 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 178 SVVQQKHlVVLEAAFTLEPGKLDEIQAKMDDLTERRESKQPLEFPSCGSVFQRPPGHFAGKLIQDSNLQGYRIGGVEVST 257
Cdd:PRK14652 177 CRLPPGA-VITRVEVRLRPGDVAASEALMRADRERRRRTQPLDRPTFGSTFTNPPGDYAGRLVEAVGLKGHRVGGAIWSP 255
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 488388214 258 KHAGFMVNVDNGTATDYEALIHHVQKTVKEKFDVELNTEVRIIGE 302
Cdd:PRK14652 256 VHANFVTNLGGATARDVLALVRLARARVKERFGIALETEVRLLGE 300
PRK14653 PRK14653
UDP-N-acetylmuramate dehydrogenase;
21-299 1.08e-63

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237778 [Multi-domain]  Cd Length: 297  Bit Score: 202.76  E-value: 1.08e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  21 VDEPLKRYTYTETGGKADFYLSPTKNEEVQAIVKFAHEnSIPVTYLGNGSNIIIREGGIRGIVLSLLSLNHIETSDDAII 100
Cdd:PRK14653  18 INEEMKCHVSFKIGGPVPLFAIPNSTNGFIETINLLKE-GIEVKILGNGTNVLPKDEPMDFVVVSTERLDDIFVDNDKII 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 101 AGSGAAIIDVSNVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDYALCVNEKgDLLKLTTAELELDYRNSVV 180
Cdd:PRK14653  97 CESGLSLKKLCLVAAKNGLSGFENAYGIPGSVGGAVYMNAGAYGWETAENIVEVVAYDGK-KIIRLGKNEIKFSYRNSIF 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 181 -QQKHLVVLEAAFTLEPGKLDEIQAKMDDLTERRESKQPLEFPSCGSVFQRP-PGHFAGKLIQDSNLQGYRIGGVEVSTK 258
Cdd:PRK14653 176 kEEKDLIILRVTFKLKKGNKNEIYNLMLETMKKRVEKQPLEFPSAGSVFKRPrKDFYVGSAIEKLGLKGFSIGGAQISEK 255
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 488388214 259 HAGFMVNVDNGTATDYEALIHHVQKTVKEKFDVELNTEVRI 299
Cdd:PRK14653 256 HAGFIINYNNAKAEDVLKLIEYVKDKIYENYNVELETEIEI 296
PRK14649 PRK14649
UDP-N-acetylmuramate dehydrogenase;
22-301 9.96e-63

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173112 [Multi-domain]  Cd Length: 295  Bit Score: 200.45  E-value: 9.96e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  22 DEPLKRYTYTETGGKADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGGIRGIVLSLLS--LNHIETSDDA- 98
Cdd:PRK14649   6 NEPLAPYTSWRIGGPARYFVEPTTPDEAIAAAAWAEQRQLPLFWLGGGSNLLVRDEGFDGLVARYRGqrWELHEHGDTAe 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  99 IIAGSGAAIIDVSNVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDYALCVNEKGDLLKLTTAELELDYRNS 178
Cdd:PRK14649  86 VWVEAGAPMAGTARRLAAQGWAGLEWAEGLPGTIGGAIYGNAGCYGGDTATVLIRAWLLLNGSECVEWSVHDFAYGYRTS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 179 VVQQ--------KHLVVLEAAFTLEPGKLDEIQAKMDDLTERRESKQPLEfPSCGSVFQRPPGHFAGKLIQDSNLQGYRI 250
Cdd:PRK14649 166 VLKQlradgitwRPPLVLAARFRLHRDDPTALAARMEAIAAERKQKTPAG-SSCGSVFKNPPGDSAGRLIEAAGLKGTRI 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488388214 251 GGVEVSTKHAGFMVNVDNGTATDYEALIHHVQKTVKEKFDVELNTEVRIIG 301
Cdd:PRK14649 245 GDAEIATRHANYIINLGGARAADILRLIDLARTRVLAQFGIELELEVRIIG 295
MurB_C pfam02873
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ...
202-300 4.12e-54

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: 171.38  E-value: 4.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  202 IQAKMDDLTERRESKQPLEFPSCGSVFQRPPGHFAGKLIQDSNLQGYRIGGVEVSTKHAGFMVNVDNGTATDYEALIHHV 281
Cdd:pfam02873   1 IRAAMLELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEV 80
                          90
                  ....*....|....*....
gi 488388214  282 QKTVKEKFDVELNTEVRII 300
Cdd:pfam02873  81 RERVKEKFGVELEPEVRII 99
PRK14650 PRK14650
UDP-N-acetylmuramate dehydrogenase;
6-301 5.67e-45

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173113 [Multi-domain]  Cd Length: 302  Bit Score: 154.62  E-value: 5.67e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214   6 ILRGLESILPKDIIKVD-EPLKRYTYTETGGKADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGG-IRGIV 83
Cdd:PRK14650   1 MLKNINNFLKKINIKPQtKNLANYTTYKIGGISKLFLTPKTIKDAEHIFKAAIEEKIKIFILGGGSNILINDEEeIDFPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  84 LSLLSLNHIETSDDAIIAGSGAAIIDVSNVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDYALCVNEKGDL 163
Cdd:PRK14650  81 IYTGHLNKIEIHDNQIVAECGTNFEDLCKFALQNELSGLEFIYGLPGTLGGAIWMNARCFGNEISEILDKITFIDEKGKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 164 LKLTTAELELDYRNSVVQQKHLVVLEAAFTLEPGKLDEIQAKMDDLTERRESKQPLEFPSCGSVFQRPPGHF--AGKLIQ 241
Cdd:PRK14650 161 ICKKFKKEEFKYKISPFQNKNTFILKATLNLKKGNKKHIEEIMKQNKQIRINKGHYLFPSSGSTFKNNKAFLkpTGQIIE 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 242 DSNLQGYRIGGVEVSTKHAGFMVNVDNGTATDYEALIHHVQKTVKEKFDVELNTEVRIIG 301
Cdd:PRK14650 241 ECKLKGLSIGGATVSHYHGNFIININNATSKDIKTLIEKVKTEVQIKTGFLLEEEVLYIG 300
murB PRK13904
UDP-N-acetylmuramate dehydrogenase;
112-300 2.42e-42

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 184384 [Multi-domain]  Cd Length: 257  Bit Score: 146.61  E-value: 2.42e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 112 NVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDyALCVNeKGDLLKlttAELELDYRNSVVQQkhlVVLEAA 191
Cdd:PRK13904  82 NYAKKNNLGGFEFLGKLPGTLGGLVKMNAGLKEYEISNNLE-SICTN-GGWIEK---EDIGFGYRSSGING---VILEAR 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 192 FTLEPGKLDEIQakmDDLTERRESkQPLEfPSCGSVFQRPPGHFAGKLIQDSNLQGYRIGGVEVSTKHAGFMVNVDNGTA 271
Cdd:PRK13904 154 FKKTHGFDEELL---EAFKSMRKN-QPKG-PSFGSCFKNPKGDYAGRLIEAVGLKGYCKGGAGFSEEHANFLVNLGGATF 228
                        170       180
                 ....*....|....*....|....*....
gi 488388214 272 TDYEALIHHVQKTVKEKFDVELNTEVRII 300
Cdd:PRK13904 229 EDALDLIELAKKRVLEEFGINLEEEVIIL 257
PRK14651 PRK14651
UDP-N-acetylmuramate dehydrogenase;
24-304 4.69e-38

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237776 [Multi-domain]  Cd Length: 273  Bit Score: 135.72  E-value: 4.69e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  24 PLKRYTYTETGGKADFYLSPTKNEEVQAIvkfahenSIPVTYLGNGSNIIIREGGIRGIVLSLLSlnHIETSDDAIIAGS 103
Cdd:PRK14651   8 PLARYTTLGVGGPAELWTVETHEQLAEAT-------EAPYRVLGGGSNLLVSDAGVPERVIRLGG--EFAEWDLDGWVGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 104 GAAIIDVSNVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDYALCVNEKGdLLKLTTAELELDYRNSVVQQK 183
Cdd:PRK14651  79 GVPLPGLVRRAARLGLSGLEGLVGIPAQVGGAVKMNAGTRFGEMADALHTVEIVHDGG-FHQYSPDELGFGYRHSGLPPG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 184 HlVVLEAAFTLEPGKLDEIQAKMDDLTERRESKQPLEFPSCGsvFQRPPGHFAGKLIQDSNLQGYRIGGVEVSTKHAGFM 263
Cdd:PRK14651 158 H-VVTRVRLKLRPSTPEAVLAKMALVDAARKGQPKKKSAGCA--FKNPPGDSAGRLIDEAGLKGTRVGDAMISPEHGNFI 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 488388214 264 VNVDNGTATDYEALIHHVQktvkEKFDVELNTEVRIIGEHP 304
Cdd:PRK14651 235 VNLGGATAADVHALLRRVR----ARVGLPLELEWELWPEQL 271
PRK14648 PRK14648
UDP-N-acetylmuramate dehydrogenase;
13-302 5.27e-35

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 173111 [Multi-domain]  Cd Length: 354  Bit Score: 129.84  E-value: 5.27e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  13 ILPKDIIKVDEPLKRYTYTETGGKADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGGIRGIVLSLLSLN-- 90
Cdd:PRK14648   6 IRARRITRRNVPLAERCSFRIGGAAQFWAEPRSCTQLRALIEEAQRARIPLSLIGGGSNVLIADEGVPGLMLSLRRFRsl 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  91 HIETSDDAII---AGSGAAIIDVSNVARDHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCIDYALCV---------- 157
Cdd:PRK14648  86 HTQTQRDGSVlvhAGAGLPVAALLAFCAHHALRGLETFAGLPGSVGGAAYMNARCYGRAIADCFHSARTLvlhpvrsrak 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 158 ----------NEKGDLLKLTTAEL-------------ELDYRNSVVQQKHLVVLEAA--------FTLEPGKLDEIQAKM 206
Cdd:PRK14648 166 elpevrknaqDKRGECLGLDGGPFtcssfqtvfaragDWGYKRSPFQSPHGVELHAGrrlilslcVRLTPGNPAQIRKHM 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 207 DDLTERRESKQPLEFPSCGSVFQRPP--GHFAGKLIQDSNLQGYRIGGVEVSTKHAGFMVNVDNGTATDYEALIHHVQKT 284
Cdd:PRK14648 246 QEKIADRISKGQFRFPSAGSAFKNNPafGKPSGILIEEAGLRGTSCGAAQVAPWHGNLIINTGNATAHQVRTLLRVVRQR 325
                        330
                 ....*....|....*...
gi 488388214 285 VKEKFDVELNTEVRIIGE 302
Cdd:PRK14648 326 VFETHGVWLEREIIFSGE 343
murB PRK00046
UDP-N-acetylmuramate dehydrogenase;
36-300 4.17e-30

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 234593 [Multi-domain]  Cd Length: 334  Bit Score: 116.01  E-value: 4.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  36 KADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGgIRGIVL--SLLSLNHIETSDDAII--AGSGAAIIDVS 111
Cdd:PRK00046  20 RARHLVEAESEEQLLEALADARAAGLPVLVLGGGSNVLFTED-FDGTVLlnRIKGIEVLSEDDDAWYlhVGAGENWHDLV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 112 NVARDHVLTGLE-FACgIPGSIGGAVFMNAGAYGGEVKDCIDYALCVN-EKGDLLKLTTAELELDYRNSV----VQQKHL 185
Cdd:PRK00046  99 LWTLQQGMPGLEnLAL-IPGTVGAAPIQNIGAYGVELKDVCDYVEALDlATGEFVRLSAAECRFGYRDSIfkheYPDRYA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 186 VV-------LEAAFTLEPGKLDEIQAkmDDLTER---------RESK--QPLEFPSCGSVFQRP--------------PG 233
Cdd:PRK00046 178 ITavgfrlpKQWQPVLDYGDLARLDP--DTVTAQdvfdavcaiRRSKlpDPKVLGNAGSFFKNPvvsaeqfeallaqyPD 255
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488388214 234 --HF----------AGKLIQDSNLQGYRIGGVEVSTKHAGFMVNVDNGTATDYEALIHHVQKTVKEKFDVELNTEVRII 300
Cdd:PRK00046 256 ipHYpqadgsvklaAGWLIDQCGLKGFQIGGAAVHEKQALVLVNYGNATGADVLALARHIQQDVREKFGVELEPEPRFI 334
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
37-167 6.96e-27

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: 102.28  E-value: 6.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214   37 ADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGGIRGIVLSLLSLNHIETSDDA---IIAGSGAAIIDVSNV 113
Cdd:pfam01565   1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQTGGIVLDLSRLNGILEIDPEdgtATVEAGVTLGDLVRA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488388214  114 ARDH-VLTGLEFACGIPGSIGGAVFMNAGAYGGE----VKDCIDYALCVNEKGDLLKLT 167
Cdd:pfam01565  81 LAAKgLLLGLDPGSGIPGTVGGAIATNAGGYGSEkyglTRDNVLGLEVVLADGEVVRLG 139
murB PRK13903
UDP-N-acetylmuramate dehydrogenase;
22-301 8.29e-26

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237552 [Multi-domain]  Cd Length: 363  Bit Score: 105.04  E-value: 8.29e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  22 DEPLKRYTYTETGGKADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIIIREGGIRGIVLSLLSLN-HIETSDDAII 100
Cdd:PRK13903  18 DVPLAPLTTLRVGGPARRLVTCTSTEELVAAVRELDAAGEPLLVLGGGSNLVIADDGFDGTVVRVATRGvTVDCGGGLVR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 101 AGSGAAIIDVsnVAR--DHVLTGLEFACGIPGSIGGAVFMNAGAYGGEVKDCI------DYALcvnekGDLLKLTTAELE 172
Cdd:PRK13903  98 AEAGAVWDDV--VARtvEAGLGGLECLSGIPGSAGATPVQNVGAYGQEVSDTItrvrllDRRT-----GEVRWVPAADLG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 173 LDYRNSVVQQK-HLVVLEAAFTLEPGKLD------EIQAKMD-------DLTERRE-------SKQPLEFP------SCG 225
Cdd:PRK13903 171 FGYRTSVLKHSdRAVVLEVEFQLDPSGLSaplrygELARALGvepgervPPAAVREavlalraGKGMVLDPadhdtwSAG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214 226 SVFQRP----------------------------PGHF---AGKLIQDSNL-QGYRIGG--VEVSTKHAGFMVNVDNGTA 271
Cdd:PRK13903 251 SFFTNPvvspavaerlaarvaerlgdpvprypagDGGVklsAAWLIERAGFgKGYPGGGapARLSTKHTLALTNRGGATT 330
                        330       340       350
                 ....*....|....*....|....*....|
gi 488388214 272 TDYEALIHHVQKTVKEKFDVELNTEVRIIG 301
Cdd:PRK13903 331 ADLVALAREVRDGVRDAFGVTLVPEPVLVG 360
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
1-144 4.39e-13

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


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 69.15  E-value: 4.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214   1 MNKNDILRGLESILPKDIIKVDEPLKRYTYTETG---GKADFYLSPTKNEEVQAIVKFAHENSIPVTYLGNGSNIiirEG 77
Cdd:COG0277    1 MLTAALLAALRAILAGRVLTDPADRAAYARDGNSlyrGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGL---AG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  78 GI----RGIVLSLLSLNHIETSDDA---IIAGSGAAIIDVSNVARDHvltGLEFACGiPGS-----IGGAVFMNAG---- 141
Cdd:COG0277   78 GAvpldGGVVLDLSRMNRILEVDPEdrtATVEAGVTLADLNAALAPH---GLFFPPD-PSSqgtatIGGNIATNAGgprs 153

                 ....
gi 488388214 142 -AYG 144
Cdd:COG0277  154 lKYG 157
PRK11230 PRK11230
glycolate oxidase subunit GlcD; Provisional
2-172 3.59e-05

glycolate oxidase subunit GlcD; Provisional


Pssm-ID: 183043 [Multi-domain]  Cd Length: 499  Bit Score: 45.15  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214   2 NKNDILRGLESILPK-DIIKVDEPLKRYtytETGGKADFYLSPT------KNEEVQAIVKFAHENSIPVTYLGNGSNIii 74
Cdd:PRK11230  17 DRTSLLMALREHLPGlEILHTDEELIPY---ECDGLSAYRTRPLlvvlpkQMEQVQALLAVCHRLRVPVVARGAGTGL-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388214  75 rEGGI----RGIVLSLLSLNHI-ETSDDAIIA--GSGAAIIDVSNVARDHvltGLEFA----CGIPGSIGGAVFMNAGAY 143
Cdd:PRK11230  92 -SGGAlpleKGVLLVMARFNRIlDINPVGRRArvQPGVRNLAISQAAAPH---GLYYApdpsSQIACSIGGNVAENAGGV 167
                        170       180
                 ....*....|....*....|....*....
gi 488388214 144 ggevkDCIDYALCVNekgDLLKLTTAELE 172
Cdd:PRK11230 168 -----HCLKYGLTVH---NLLKVEILTLD 188
 
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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