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Conserved domains on  [gi|2163461419|ref|WP_231472576|]
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N-acetylglucosamine-6-phosphate deacetylase [Enterococcus casseliflavus]

Protein Classification

N-acetylglucosamine-6-phosphate deacetylase( domain architecture ID 10788057)

N-acetylglucosamine-6-phosphate deacetylase catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate, which is the first committed step in the biosynthetic pathway to amino-sugar

CATH:  3.20.20.140|2.30.40.10
EC:  3.5.1.25
Gene Ontology:  GO:0008448|GO:0046872|GO:0005975|GO:0046349
PubMed:  17567048|17567047|9144792
SCOP:  4002805|4002851

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
4-376 0e+00

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


:

Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 506.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419   4 YIYADKFFLKSAVHGPGYLEVKEGKFGAIVDEVPAGADVEDYSGKWVAPGLVDTHIHGFMNHDVMDNDAEGIKAMSEGLL 83
Cdd:COG1820     1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEPDAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGTPEALRTIARAHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  84 SCGVTSFLPTTLTSSKERLRDVAETVGKVKDEVTGAKIQGIYFEGPFFTEEHKGAQNPIYFGDPDIDTFHEWQEASGGII 163
Cdd:COG1820    81 RHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGGGAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLEAAGGLI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 164 KKIALAPEREGVKEFVSQVTKEGVVVALGHSNGTLQEAQTAVEAGASVFVHAFNGMRGLNHREPGMVGALLSLKEVFSEL 243
Cdd:COG1820   161 KLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDDDVYAEL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 244 ICDGHHVHPQAAEILMEKAGHDHVALITDCMMAGGMPDGDYILGEFPVVVKDGTARMETGNLAGSILKLKEAVKNVVEWG 323
Cdd:COG1820   241 IADGIHVHPAAVRLALRAKGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVRNLVEWT 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2163461419 324 IATPQEAVMMASLIPAISCKIDHACGMIKQGRPADFIVLDQEMNLAATYLDGV 376
Cdd:COG1820   321 GLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
 
Name Accession Description Interval E-value
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
4-376 0e+00

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 506.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419   4 YIYADKFFLKSAVHGPGYLEVKEGKFGAIVDEVPAGADVEDYSGKWVAPGLVDTHIHGFMNHDVMDNDAEGIKAMSEGLL 83
Cdd:COG1820     1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEPDAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGTPEALRTIARAHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  84 SCGVTSFLPTTLTSSKERLRDVAETVGKVKDEVTGAKIQGIYFEGPFFTEEHKGAQNPIYFGDPDIDTFHEWQEASGGII 163
Cdd:COG1820    81 RHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGGGAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLEAAGGLI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 164 KKIALAPEREGVKEFVSQVTKEGVVVALGHSNGTLQEAQTAVEAGASVFVHAFNGMRGLNHREPGMVGALLSLKEVFSEL 243
Cdd:COG1820   161 KLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDDDVYAEL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 244 ICDGHHVHPQAAEILMEKAGHDHVALITDCMMAGGMPDGDYILGEFPVVVKDGTARMETGNLAGSILKLKEAVKNVVEWG 323
Cdd:COG1820   241 IADGIHVHPAAVRLALRAKGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVRNLVEWT 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2163461419 324 IATPQEAVMMASLIPAISCKIDHACGMIKQGRPADFIVLDQEMNLAATYLDGV 376
Cdd:COG1820   321 GLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 4-375 1.19e-160

N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 455.50  E-value: 1.19e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419   4 YIYADKFFLKSAVHGPGYLEVKEGKFGAIV--DEVPAGADVEDYSGKWVAPGLVDTHIHGFMNHDVMDNDAEGIKAMSEG 81
Cdd:cd00854     1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGpeDELEEADEIIDLKGQYLVPGFIDIHIHGGGGADFMDGTAEALKTIAEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  82 LLSCGVTSFLPTTLTSSKERLRDVAETVGKVKDEVTGAKIQGIYFEGPFFTEEHKGAQNPIYFGDPDIDTFHEWQEASGG 161
Cdd:cd00854    81 LAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELKKWLEAAGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 162 IIKKIALAPEREGVKEFVSQVTKEGVVVALGHSNGTLQEAQTAVEAGASVFVHAFNGMRGLNHREPGMVGALLSLKEVFS 241
Cdd:cd00854   161 LIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAALSDDDVYA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 242 ELICDGHHVHPQAAEILMEKAGHDHVALITDCMMAGGMPDGDYILGEFPVVVKDGTARMETGNLAGSILKLKEAVKNVVE 321
Cdd:cd00854   241 ELIADGIHVHPAAVRLAYRAKGADKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLADGTLAGSTLTMDQAVRNMVK 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2163461419 322 WGIATPQEAVMMASLIPAISCKIDHACGMIKQGRPADFIVLDQEMNLAATYLDG 375
Cdd:cd00854   321 WGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
nagA TIGR00221
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
 20-375 6.34e-87

N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]


Pssm-ID: 272968  Cd Length: 380  Bit Score: 267.85  E-value: 6.34e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  20 GYLEVKEGKFGAIV--DEVPAGADVEDYSGKWVAPGLVDTHIHGFMNHDVMDNDAEGIKAMSEGLLSCGVTSFLPTTLTS 97
Cdd:TIGR00221  22 GAVGINDGKISTVSteAELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDASFETLEIMSERLPKSGCTSFLPTLITQ 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  98 S----KERLRDVAETVGKVKdevtGAKIQGIYFEGPFFTEEHKGAQNPIYFGDPDIDTFHEWQEASGGIIKKIALAPERE 173
Cdd:TIGR00221 102 PdeniKQAVKNMREYLAKEK----NAQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFKKFLCEAGGVITKVTLAPEED 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 174 GVKEFVSQVTKEGVVVALGHSNGTLQEAQTAVEAGASVFVHAFNGMRGLNHREPGMVGALLSLKEVFSELICDGHHVHPQ 253
Cdd:TIGR00221 178 QHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGAVLDHDDVYTEIIADGIHIHPL 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 254 AAEILMEKAGHDHVALITDCMMAGGMPDGDYILGEFPVVVKDGTARMETGNLAGSILKLKEAVKNVVEWGIATPQEAVMM 333
Cdd:TIGR00221 258 NIRLAKKLKGDSKLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDSNGTLAGSSLTMIEGARNLVEFTNISLTDAARM 337

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2163461419 334 ASLIPAISCKIDHACGMIKQGRPADFIVLDQEMNLAATYLDG 375
Cdd:TIGR00221 338 SSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNG 379
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 24-375 2.70e-59

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 196.73  E-value: 2.70e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  24 VKEGKFGAI--VDEVPAGADVEDYSGKWVAPGLVDTHIHGFMNhdVMDND------AEGIKAMSEGLLSCGVTSFLPTTL 95
Cdd:PRK11170   23 IADGLIEAVcpVAELPPGIEQRDLNGAILSPGFIDLQLNGCGG--VQFNDtaeaisVETLEIMQKANEKSGCTSFLPTLI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  96 TSSKERLRDVAETVgkvKDEVTGAKIQ--GIYFEGPFFTEEHKGAQNPIYFGDPD---IDTFHEwqeaSGGIIKKIALAP 170
Cdd:PRK11170  101 TSSDELMKQAVRVM---REYLAKHPNQalGLHLEGPYLNLVKKGTHNPEFIRKPDaemVDFLCE----NADVITKVTLAP 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 171 EREGVkEFVSQVTKEGVVVALGHSNGTLQEAQTAVEAGASVFVHAFNGMRGLNHREPGMVGALLSLKEVFSELICDGHHV 250
Cdd:PRK11170  174 EMVDA-EVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPDVYCGIIADGLHV 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 251 HpqAAEI-LMEKAGHDHVALITDCMMAGGMPDGDYILGEFPVVVKDGTARMETGNLAGSILKLKEAVKNVVEW-GIATpQ 328
Cdd:PRK11170  253 D--YANIrNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIEAVRNLVEHvGIAL-D 329

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2163461419 329 EAVMMASLIPAISCKIDHACGMIKQGRPADFIVLDQEMNLAATYLDG 375
Cdd:PRK11170  330 EALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRDFKITKTIVNG 376
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 49-373 1.71e-15

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 76.77  E-value: 1.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  49 WVAPGLVDTHIHGFMNHDVMDND-----AEGIKAMSEGLLSCGVTSFLPTTLTSSKERLRdVAETVGKVkdevtgakIQG 123
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVppefaYEALRLGITTMLKSGTTTVLDMGATTSTGIEA-LLEAAEEL--------PLG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 124 IYFEGPFFTEEHKGAQNPIYFGDPDIDTFHEWQEASGGIIKKIALAPE------REGVKEFVSQVTKEGVVVA--LGHSN 195
Cdd:pfam01979  72 LRFLGPGCSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLAPHgaptfsDDELKAALEEAKKYGLPVAihALETK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 196 GTLQEAQTAVEAGASVFVHAFNGMRGlnhrepgmvGALLSLKEVFSelicDGHHVHPQAAEILMEKAGHDHVALITD--- 272
Cdd:pfam01979 152 GEVEDAIAAFGGGIEHGTHLEVAESG---------GLLDIIKLILA----HGVHLSPTEANLLAEHLKGAGVAHCPFsns 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 273 ------CMMAGGMPDGDYIlgefpVVVKDGTARMETGNLAGSiLKLKEAVKNVVEWGIaTPQEAVMMASLIPAISCKIDH 346
Cdd:pfam01979 219 klrsgrIALRKALEDGVKV-----GLGTDGAGSGNSLNMLEE-LRLALELQFDPEGGL-SPLEALRMATINPAKALGLDD 291

                         330       340
                  ....*....|....*....|....*..
gi 2163461419 347 ACGMIKQGRPADFIVLDQEMNLAATYL 373
Cdd:pfam01979 292 KVGSIEVGKDADLVVVDLDPLAAFFGL 318
 
Name Accession Description Interval E-value
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
4-376 0e+00

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 506.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419   4 YIYADKFFLKSAVHGPGYLEVKEGKFGAIVDEVPAGADVEDYSGKWVAPGLVDTHIHGFMNHDVMDNDAEGIKAMSEGLL 83
Cdd:COG1820     1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEPDAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGTPEALRTIARAHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  84 SCGVTSFLPTTLTSSKERLRDVAETVGKVKDEVTGAKIQGIYFEGPFFTEEHKGAQNPIYFGDPDIDTFHEWQEASGGII 163
Cdd:COG1820    81 RHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGGGAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLEAAGGLI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 164 KKIALAPEREGVKEFVSQVTKEGVVVALGHSNGTLQEAQTAVEAGASVFVHAFNGMRGLNHREPGMVGALLSLKEVFSEL 243
Cdd:COG1820   161 KLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDDDVYAEL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 244 ICDGHHVHPQAAEILMEKAGHDHVALITDCMMAGGMPDGDYILGEFPVVVKDGTARMETGNLAGSILKLKEAVKNVVEWG 323
Cdd:COG1820   241 IADGIHVHPAAVRLALRAKGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVRNLVEWT 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2163461419 324 IATPQEAVMMASLIPAISCKIDHACGMIKQGRPADFIVLDQEMNLAATYLDGV 376
Cdd:COG1820   321 GLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 4-375 1.19e-160

N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 455.50  E-value: 1.19e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419   4 YIYADKFFLKSAVHGPGYLEVKEGKFGAIV--DEVPAGADVEDYSGKWVAPGLVDTHIHGFMNHDVMDNDAEGIKAMSEG 81
Cdd:cd00854     1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGpeDELEEADEIIDLKGQYLVPGFIDIHIHGGGGADFMDGTAEALKTIAEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  82 LLSCGVTSFLPTTLTSSKERLRDVAETVGKVKDEVTGAKIQGIYFEGPFFTEEHKGAQNPIYFGDPDIDTFHEWQEASGG 161
Cdd:cd00854    81 LAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELKKWLEAAGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 162 IIKKIALAPEREGVKEFVSQVTKEGVVVALGHSNGTLQEAQTAVEAGASVFVHAFNGMRGLNHREPGMVGALLSLKEVFS 241
Cdd:cd00854   161 LIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAALSDDDVYA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 242 ELICDGHHVHPQAAEILMEKAGHDHVALITDCMMAGGMPDGDYILGEFPVVVKDGTARMETGNLAGSILKLKEAVKNVVE 321
Cdd:cd00854   241 ELIADGIHVHPAAVRLAYRAKGADKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLADGTLAGSTLTMDQAVRNMVK 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2163461419 322 WGIATPQEAVMMASLIPAISCKIDHACGMIKQGRPADFIVLDQEMNLAATYLDG 375
Cdd:cd00854   321 WGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
nagA TIGR00221
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
 20-375 6.34e-87

N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]


Pssm-ID: 272968  Cd Length: 380  Bit Score: 267.85  E-value: 6.34e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  20 GYLEVKEGKFGAIV--DEVPAGADVEDYSGKWVAPGLVDTHIHGFMNHDVMDNDAEGIKAMSEGLLSCGVTSFLPTTLTS 97
Cdd:TIGR00221  22 GAVGINDGKISTVSteAELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDASFETLEIMSERLPKSGCTSFLPTLITQ 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  98 S----KERLRDVAETVGKVKdevtGAKIQGIYFEGPFFTEEHKGAQNPIYFGDPDIDTFHEWQEASGGIIKKIALAPERE 173
Cdd:TIGR00221 102 PdeniKQAVKNMREYLAKEK----NAQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFKKFLCEAGGVITKVTLAPEED 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 174 GVKEFVSQVTKEGVVVALGHSNGTLQEAQTAVEAGASVFVHAFNGMRGLNHREPGMVGALLSLKEVFSELICDGHHVHPQ 253
Cdd:TIGR00221 178 QHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGAVLDHDDVYTEIIADGIHIHPL 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 254 AAEILMEKAGHDHVALITDCMMAGGMPDGDYILGEFPVVVKDGTARMETGNLAGSILKLKEAVKNVVEWGIATPQEAVMM 333
Cdd:TIGR00221 258 NIRLAKKLKGDSKLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDSNGTLAGSSLTMIEGARNLVEFTNISLTDAARM 337

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2163461419 334 ASLIPAISCKIDHACGMIKQGRPADFIVLDQEMNLAATYLDG 375
Cdd:TIGR00221 338 SSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNG 379
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 24-375 2.70e-59

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 196.73  E-value: 2.70e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  24 VKEGKFGAI--VDEVPAGADVEDYSGKWVAPGLVDTHIHGFMNhdVMDND------AEGIKAMSEGLLSCGVTSFLPTTL 95
Cdd:PRK11170   23 IADGLIEAVcpVAELPPGIEQRDLNGAILSPGFIDLQLNGCGG--VQFNDtaeaisVETLEIMQKANEKSGCTSFLPTLI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  96 TSSKERLRDVAETVgkvKDEVTGAKIQ--GIYFEGPFFTEEHKGAQNPIYFGDPD---IDTFHEwqeaSGGIIKKIALAP 170
Cdd:PRK11170  101 TSSDELMKQAVRVM---REYLAKHPNQalGLHLEGPYLNLVKKGTHNPEFIRKPDaemVDFLCE----NADVITKVTLAP 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 171 EREGVkEFVSQVTKEGVVVALGHSNGTLQEAQTAVEAGASVFVHAFNGMRGLNHREPGMVGALLSLKEVFSELICDGHHV 250
Cdd:PRK11170  174 EMVDA-EVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPDVYCGIIADGLHV 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 251 HpqAAEI-LMEKAGHDHVALITDCMMAGGMPDGDYILGEFPVVVKDGTARMETGNLAGSILKLKEAVKNVVEW-GIATpQ 328
Cdd:PRK11170  253 D--YANIrNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIEAVRNLVEHvGIAL-D 329

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2163461419 329 EAVMMASLIPAISCKIDHACGMIKQGRPADFIVLDQEMNLAATYLDG 375
Cdd:PRK11170  330 EALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRDFKITKTIVNG 376
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 49-373 1.71e-15

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 76.77  E-value: 1.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  49 WVAPGLVDTHIHGFMNHDVMDND-----AEGIKAMSEGLLSCGVTSFLPTTLTSSKERLRdVAETVGKVkdevtgakIQG 123
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVppefaYEALRLGITTMLKSGTTTVLDMGATTSTGIEA-LLEAAEEL--------PLG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 124 IYFEGPFFTEEHKGAQNPIYFGDPDIDTFHEWQEASGGIIKKIALAPE------REGVKEFVSQVTKEGVVVA--LGHSN 195
Cdd:pfam01979  72 LRFLGPGCSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLAPHgaptfsDDELKAALEEAKKYGLPVAihALETK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 196 GTLQEAQTAVEAGASVFVHAFNGMRGlnhrepgmvGALLSLKEVFSelicDGHHVHPQAAEILMEKAGHDHVALITD--- 272
Cdd:pfam01979 152 GEVEDAIAAFGGGIEHGTHLEVAESG---------GLLDIIKLILA----HGVHLSPTEANLLAEHLKGAGVAHCPFsns 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 273 ------CMMAGGMPDGDYIlgefpVVVKDGTARMETGNLAGSiLKLKEAVKNVVEWGIaTPQEAVMMASLIPAISCKIDH 346
Cdd:pfam01979 219 klrsgrIALRKALEDGVKV-----GLGTDGAGSGNSLNMLEE-LRLALELQFDPEGGL-SPLEALRMATINPAKALGLDD 291

                         330       340
                  ....*....|....*....|....*..
gi 2163461419 347 ACGMIKQGRPADFIVLDQEMNLAATYL 373
Cdd:pfam01979 292 KVGSIEVGKDADLVVVDLDPLAAFFGL 318
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 15-363 1.47e-10

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 62.29  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  15 AVHGPGYLEVKEGKFGAIVD----EVPAGADVEDYSGKWVAPGLVDTHIHGFMNHDVMDNDAEG---------IKAMSEG 81
Cdd:COG1228    24 GVIENGTVLVEDGKIAAVGPaadlAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGggitptvdlVNPADKR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  82 L---LSCGVTSFLptTLTSSKERLRDVAetvgkvkDEVTGAKIQG--IYFEGPFFTeehkgAQNPIYFGDPD--IDTFHE 154
Cdd:COG1228   104 LrraLAAGVTTVR--DLPGGPLGLRDAI-------IAGESKLLPGprVLAAGPALS-----LTGGAHARGPEeaRAALRE 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 155 WQEASGGIIKKIA----LAPEREGVKEFVSQVTKEGVVVAlGHSNGtLQEAQTAVEAGASVFVHAF------------NG 218
Cdd:COG1228   170 LLAEGADYIKVFAeggaPDFSLEELRAILEAAHALGLPVA-AHAHQ-ADDIRLAVEAGVDSIEHGTylddevadllaeAG 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 219 MRGLNhrePGMVGALLSLKEVFSELICDGHHVHPQAAEIL--MEKAGHdHVALITDCmmAGGMPDGDYILGEFpvvvkdg 296
Cdd:COG1228   248 TVVLV---PTLSLFLALLEGAAAPVAAKARKVREAALANArrLHDAGV-PVALGTDA--GVGVPPGRSLHREL------- 314

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163461419 297 tarmetgNLAgsilklkeavknvVEWGIaTPQEAVMMASLIPAISCKIDHACGMIKQGRPADFIVLD 363
Cdd:COG1228   315 -------ALA-------------VEAGL-TPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLD 360
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 19-109 2.40e-06

L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.


Pssm-ID: 238640 [Multi-domain]  Cd Length: 447  Bit Score: 49.21  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  19 PGYLEVKEGKFGAIVDEV--PAGADVEDYSGKWVAPGLVDTHIHgfMNhDVMDNDAEGIKAMSEGLLSCGVTSFL----- 91
Cdd:cd01315    17 EADIAVKGGKIAAIGPDIanTEAEEVIDAGGLVVMPGLIDTHVH--IN-EPGRTEWEGFETGTKAAAAGGITTIIdmpln 93

                          90       100
                  ....*....|....*....|
gi 2163461419  92 --PTTLTssKERLRDVAETV 109
Cdd:cd01315    94 siPPTTT--VENLEAKLEAA 111
PRK09228 PRK09228
guanine deaminase; Provisional
 27-83 2.75e-06

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 49.03  E-value: 2.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2163461419  27 GKFGAIVDEVPAGADVEDYSGKWVAPGLVDTHIHgFMNHDVmdndaegIKAMSEGLL 83
Cdd:PRK09228   45 GPYAELRAQLPADAEVTDYRGKLILPGFIDTHIH-YPQTDM-------IASYGEQLL 93
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 20-63 2.09e-05

Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440171 [Multi-domain]  Cd Length: 416  Bit Score: 46.36  E-value: 2.09e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2163461419  20 GYLEVKEGKFGAI-----VDEVPAGADVEDYSGKWVAPGLVDTHIHGFM 63
Cdd:COG0402    22 GAVLVEDGRIAAVgpgaeLPARYPAAEVIDAGGKLVLPGLVNTHTHLPQ 70
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 20-63 8.32e-05

TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.


Pssm-ID: 238623 [Multi-domain]  Cd Length: 411  Bit Score: 44.50  E-value: 8.32e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2163461419  20 GYLEVKEGKFGAIVDEVPA----GADVEDYSGKWVAPGLVDTHIHGFM 63
Cdd:cd01298    20 GDVLVEDGRIVAVGPALPLpaypADEVIDAKGKVVMPGLVNTHTHLAM 67
PRK06189 PRK06189
allantoinase; Provisional
 24-107 1.48e-04

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 43.54  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  24 VKEGKFGAIVDEVPAGADVE-DYSGKWVAPGLVDTHIH----GFmnhdvmdNDAEGIKAMSEGLLSCGVTSFL------- 91
Cdd:PRK06189   25 IKNGKIAEIAPEISSPAREIiDADGLYVFPGMIDVHVHfnepGR-------THWEGFATGSAALAAGGCTTYFdmplnsi 97

                          90
                  ....*....|....*.
gi 2163461419  92 PTTLTssKERLRDVAE 107
Cdd:PRK06189   98 PPTVT--REALDAKAE 111
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 44-363 2.46e-04

Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238624 [Multi-domain]  Cd Length: 342  Bit Score: 42.67  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  44 DYSGKWVAPGLVDTHIHGFMNhdvmDNDAEGIKAMSEGLLSCGVTSFLPTTLTSSKERLRDVAETV-GKVKDEVTGAKIQ 122
Cdd:cd01299     5 DLGGKTLMPGLIDAHTHLGSD----PGDLPLDLALPVEYRTIRATRQARAALRAGFTTVRDAGGADyGLLRDAIDAGLIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 123 G--IYFEGPFFTEeHKGaqNPIYFGDPDIDTFHEWQEASGGiikkialapeREGVKEFVSQVTKEGV----VVA------ 190
Cdd:cd01299    81 GprVFASGRALSQ-TGG--HGDPRGLSGLFPAGGLAAVVDG----------VEEVRAAVREQLRRGAdqikIMAtggvls 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 191 ----LGHSNGTLQEAQTAVE----AGASVFVHAF----------NGMRGLNHrepgmvgallslkevfselicdGHHVHP 252
Cdd:cd01299   148 pgdpPPDTQFSEEELRAIVDeahkAGLYVAAHAYgaeairrairAGVDTIEH----------------------GFLIDD 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 253 QAAEiLMEKAGhdhvALITDCMMAGGMPDGDYILGEFP--------VVVKDGTARMETGNLAG--------SILKLKEAV 316
Cdd:cd01299   206 ETIE-LMKEKG----IFLVPTLATYEALAAEGAAPGLPadsaekvaLVLEAGRDALRRAHKAGvkiafgtdAGFPVPPHG 280

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2163461419 317 KNV------VEWGIaTPQEAVMMASLIPAISCKIDHACGMIKQGRPADFIVLD 363
Cdd:cd01299   281 WNArelellVKAGG-TPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVD 332
Amidohydro_3 pfam07969
Amidohydrolase family;
171-379 2.60e-04

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 42.90  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 171 EREGVKEFVSQVTKEGVVVALgHSNGTLQEAQTAVEAGASVFVHAFNGMRGLNHrEPGMVGALLSLKEVFSEL-ICDG-H 248
Cdd:pfam07969 248 EDEALAELVAAARERGLDVAI-HAIGDATIDTALDAFEAVAEKLGNQGRVRIEH-AQGVVPYTYSQIERVAALgGAAGvQ 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419 249 HVH-PQAAEILMEKAGHDHVALITDC--MMAGGMPDG---DYILG---EFPVVvkdGTARMETGNLAGSILKLKEAVknv 319
Cdd:pfam07969 326 PVFdPLWGDWLQDRLGAERARGLTPVkeLLNAGVKVAlgsDAPVGpfdPWPRI---GAAVMRQTAGGGEVLGPDEEL--- 399

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163461419 320 vewgiaTPQEAVMMASLIPAISCKIDHACGMIKQGRPADFIVLD------QEMNLA-----ATYLDGVCRY 379
Cdd:pfam07969 400 ------SLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDddpltvDPPAIAdirvrLTVVDGRVVY 464
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 17-107 3.09e-04

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439814 [Multi-domain]  Cd Length: 439  Bit Score: 42.39  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  17 HGPGYLEVKEGKFGAIVD--EVPAGADVEDYSGKWVAPGLVDTHIH----GFMnhdvmdnDAEGIKAmseGLLSC---GV 87
Cdd:COG0044    13 LERADVLIEDGRIAAIGPdlAAPEAAEVIDATGLLVLPGLIDLHVHlrepGLE-------HKEDIET---GTRAAaagGV 82

                          90       100
                  ....*....|....*....|....
gi 2163461419  88 TSFL--PTTL--TSSKERLRDVAE 107
Cdd:COG0044    83 TTVVdmPNTNpvTDTPEALEFKLA 106
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
24-62 3.21e-04

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 42.53  E-value: 3.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2163461419  24 VKEGKFGAIVDEVPAGADVE--DYSGKWVAPGLVDTHIHGF 62
Cdd:PRK09237   23 IEDGKIAAVAGDIDGSQAKKviDLSGLYVSPGWIDLHVHVY 63
pyrC PRK09357
dihydroorotase; Validated
 24-60 3.30e-04

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 42.49  E-value: 3.30e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2163461419  24 VKEGKFGAIV-DEVPAGADVEDYSGKWVAPGLVDTHIH 60
Cdd:PRK09357   24 IDDGKIAAIGeNIEAEGAEVIDATGLVVAPGLVDLHVH 61
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 24-89 4.10e-04

D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.


Pssm-ID: 238622 [Multi-domain]  Cd Length: 415  Bit Score: 42.28  E-value: 4.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163461419  24 VKEGKFGAIVDEVPAGAD-VEDYSGKWVAPGLVDTHIHGfmnhdvmDNDAEGIKAMSEgLLSCGVTS 89
Cdd:cd01297    24 IRDGRIAAIGPILSTSAReVIDAAGLVVAPGFIDVHTHY-------DGQVFWDPDLRP-SSRQGVTT 82
PRK05985 PRK05985
cytosine deaminase; Provisional
 24-60 7.78e-04

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 41.07  E-value: 7.78e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2163461419  24 VKEGKFGAIVD--EVPAGADVEDYSGKWVAPGLVDTHIH 60
Cdd:PRK05985   21 IRDGRIAAIGPalAAPPGAEVEDGGGALALPGLVDGHIH 59
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 22-60 1.09e-03

Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.


Pssm-ID: 238618 [Multi-domain]  Cd Length: 398  Bit Score: 40.69  E-value: 1.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2163461419  22 LEVKEGKFGAIV--DEVPAGADVEDYSGKWVAPGLVDTHIH 60
Cdd:cd01293    17 IAIEDGRIAAIGpaLAVPPDAEEVDAKGRLVLPAFVDPHIH 57
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 24-108 1.66e-03

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 40.45  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  24 VKEGKFGAIVDEVPAGADVEDYSGKWVAPGLVDTHIH-------GFMNHDvmdnDAE-GIKAMSEGllscGVTSFLPTTL 95
Cdd:PRK13404   26 IRGGRIAALGEGLGPGAREIDATGRLVLPGGVDSHCHidqpsgdGIMMAD----DFYtGTVSAAFG----GTTTVIPFAA 97

                          90
                  ....*....|...
gi 2163461419  96 TSSKERLRDVAET 108
Cdd:PRK13404   98 QHRGQSLREAVED 110
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 22-108 2.79e-03

D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.


Pssm-ID: 238639 [Multi-domain]  Cd Length: 447  Bit Score: 39.51  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163461419  22 LEVKEGKFGAIVD--EVPAGADVEDYSGKWVAPGLVDTHIH---GFMNHDVMDNDAEGIKAMSEGllscGVTSFLPTTLT 96
Cdd:cd01314    19 ILIEDGKIVAIGPnlEAPGGVEVIDATGKYVLPGGIDPHTHlelPFMGTVTADDFESGTRAAAAG----GTTTIIDFAIP 94

                          90
                  ....*....|..
gi 2163461419  97 SSKERLRDVAET 108
Cdd:cd01314    95 NKGQSLLEAVEK 106
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
24-62 3.81e-03

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 38.99  E-value: 3.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2163461419  24 VKEGKFGAIVDEVPAGADVE--DYSGKWVAPGLVDTHIHGF 62
Cdd:COG3964    24 IKDGKIAAVAKDIDAAEAKKviDASGLYVTPGLIDLHTHVF 64
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
24-60 3.93e-03

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 39.31  E-value: 3.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2163461419  24 VKEGKFGAIVDEVPAGADVEDYSGKWVAPGLVDTHIH 60
Cdd:COG1001    29 IAGGRIAGVGDYIGEATEVIDAAGRYLVPGFIDGHVH 65
PLN02795 PLN02795
allantoinase
 5-60 4.50e-03

allantoinase


Pssm-ID: 178392 [Multi-domain]  Cd Length: 505  Bit Score: 38.99  E-value: 4.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163461419   5 IYADKFFLKSAVhGPGYLEVKEGKFGAIVDEVPA-----GADVEDYSGKWVAPGLVDTHIH 60
Cdd:PLN02795   48 LYSKRVVTPAGV-IPGAVEVEGGRIVSVTKEEEApksqkKPHVLDYGNAVVMPGLIDVHVH 107
PRK08044 PRK08044
allantoinase AllB;
24-60 4.85e-03

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 38.68  E-value: 4.85e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2163461419  24 VKEGKFGAIVDEVPAGADVEDYSGKWVAPGLVDTHIH 60
Cdd:PRK08044   25 VKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTH 61
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
326-381 5.14e-03

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 38.63  E-value: 5.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163461419 326 TPQEAVMMASLIPAISCKIDHACGMIKQGRPADFIVLDQ------EMNLA-----ATYLDGVCRYQA 381
Cdd:COG1574   468 TVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRdpltvpPEEIKdikvlLTVVGGRVVYEA 534
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
 27-62 5.92e-03

Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238632 [Multi-domain]  Cd Length: 338  Bit Score: 38.46  E-value: 5.92e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2163461419  27 GKFGAIVDEVPAGAD--VEDYSGKWVAPGLVDTHIHGF 62
Cdd:cd01307     7 GKIAAVGAALAAPAAtqIVDAGGCYVSPGWIDLHVHVY 44
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 27-60 7.14e-03

Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.


Pssm-ID: 238628 [Multi-domain]  Cd Length: 429  Bit Score: 38.41  E-value: 7.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2163461419  27 GKFGAIVDEVPAGADVEDYSGKWVAPGLVDTHIH 60
Cdd:cd01303    40 GAAETLKRAAKPGARVIDSPNQFILPGFIDTHIH 73
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 26-60 9.08e-03

Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238634 [Multi-domain]  Cd Length: 359  Bit Score: 37.68  E-value: 9.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2163461419  26 EGKFGAIV--DEVPAGADVEDYSGKWVAPGLVDTHIH 60
Cdd:cd01309     1 DGKIVAVGaeITTPADAEVIDAKGKHVTPGLIDAHSH 37
 
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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