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Conserved domains on  [gi|502612471|ref|WP_012849445|]
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N-acetylglucosamine-6-phosphate deacetylase [Edwardsiella piscicida]

Protein Classification

N-acetylglucosamine-6-phosphate deacetylase( domain architecture ID 10793546)

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 PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 1-379 0e+00

N-acetylglucosamine-6-phosphate deacetylase; Provisional


:

Pssm-ID: 183010  Cd Length: 382  Bit Score: 745.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471   1 MYALTHCRIYTGHDILDDHAVVIANGLIEKICPEAALAPDIATRDLGGAILAPGFIDVQLNGCGGVQFNDSEEAVSEQTL 80
Cdd:PRK11170   1 MYALTNGRIYTGHEVLDDHAVVIADGLIEAVCPVAELPPGIEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISVETL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  81 EIMQRANERAGCTSYLPTLITCSDAMMQRGITVMQSYLRRHRNQALGLHIEGPYISLEKKGTHNPRYIRRPDSAMLDFIC 160
Cdd:PRK11170  81 EIMQKANEKSGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNQALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFLC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 161 SHAEAVVKVTMAPEMSDDAAIQQLRAAGIVVSAGHSNASYEEARRGFAAGMRFATHLYNAMPAISGRAPGLMGAIFDTPE 240
Cdd:PRK11170 161 ENADVITKVTLAPEMVDAEVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 241 VYTGIIADGHHVAWPNIRMAKKLKGDHLVLVTDATAPAGSDIDSFIFAGKTVYYRNGLVVDENGTLSGSALTMIEAVQNS 320
Cdd:PRK11170 241 VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIEAVRNL 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502612471 321 VEHVGIALDEALRMATLYPARAIGVAQRLGSIEPGKVANLTAFTRDFQVTTTIVNGETV 379
Cdd:PRK11170 321 VEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRDFKITKTIVNGNEV 379
 
Name Accession Description Interval E-value
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 1-379 0e+00

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 745.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471   1 MYALTHCRIYTGHDILDDHAVVIANGLIEKICPEAALAPDIATRDLGGAILAPGFIDVQLNGCGGVQFNDSEEAVSEQTL 80
Cdd:PRK11170   1 MYALTNGRIYTGHEVLDDHAVVIADGLIEAVCPVAELPPGIEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISVETL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  81 EIMQRANERAGCTSYLPTLITCSDAMMQRGITVMQSYLRRHRNQALGLHIEGPYISLEKKGTHNPRYIRRPDSAMLDFIC 160
Cdd:PRK11170  81 EIMQKANEKSGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNQALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFLC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 161 SHAEAVVKVTMAPEMSDDAAIQQLRAAGIVVSAGHSNASYEEARRGFAAGMRFATHLYNAMPAISGRAPGLMGAIFDTPE 240
Cdd:PRK11170 161 ENADVITKVTLAPEMVDAEVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 241 VYTGIIADGHHVAWPNIRMAKKLKGDHLVLVTDATAPAGSDIDSFIFAGKTVYYRNGLVVDENGTLSGSALTMIEAVQNS 320
Cdd:PRK11170 241 VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIEAVRNL 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502612471 321 VEHVGIALDEALRMATLYPARAIGVAQRLGSIEPGKVANLTAFTRDFQVTTTIVNGETV 379
Cdd:PRK11170 321 VEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRDFKITKTIVNGNEV 379
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
3-377 2.04e-177

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 498.08  E-value: 2.04e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471   3 ALTHCRIYTGHDILDDHAVVIANGLIEKICPEAAlaPDIATRDLGGAILAPGFIDVQLNGCGGVQFNDSeeavSEQTLEI 82
Cdd:COG1820    1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAE--PDAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDG----TPEALRT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  83 MQRANERAGCTSYLPTLITCSDAMMQRGITVMQSYLRRH-RNQALGLHIEGPYISLEKKGTHNPRYIRRPDSAMLDFICS 161
Cdd:COG1820   75 IARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGgGAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 162 HAEAVVK-VTMAPEM-SDDAAIQQLRAAGIVVSAGHSNASYEEARRGFAAGMRFATHLYNAMPAISGRAPGLMGAIFDTP 239
Cdd:COG1820  155 AAGGLIKlVTLAPELpGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDD 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 240 EVYTGIIADGHHVAWPNIRMAKKLKG-DHLVLVTDATAPAGSDIDSFIFAGKTVYYRNGLVVDENGTLSGSALTMIEAVQ 318
Cdd:COG1820  235 DVYAELIADGIHVHPAAVRLALRAKGpDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVR 314

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502612471 319 NSVEHVGIALDEALRMATLYPARAIGVAQRLGSIEPGKVANLTAFTRDFQVTTTIVNGE 377
Cdd:COG1820  315 NLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
nagA TIGR00221
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
 1-376 1.86e-171

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


Pssm-ID: 272968  Cd Length: 380  Bit Score: 483.18  E-value: 1.86e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471    1 MYALTHCRIYTGHDILDDHAVVIANGLIEKICPEAALAPDIATRDLGGAILAPGFIDVQLNGCGGVQFNDSeeavSEQTL 80
Cdd:TIGR00221   4 SYLLKDIAIVTGNEVIDNGAVGINDGKISTVSTEAELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDA----SFETL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471   81 EIMQRANERAGCTSYLPTLITCSDAMMQRGITVMQSYLRRHRN-QALGLHIEGPYISLEKKGTHNPRYIRRPDSAML-DF 158
Cdd:TIGR00221  80 EIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKNaQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFkKF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  159 ICSHAEAVVKVTMAP-EMSDDAAIQQLRAAGIVVSAGHSNASYEEARRGFAAGMRFATHLYNAMPAISGRAPGLMGAIFD 237
Cdd:TIGR00221 160 LCEAGGVITKVTLAPeEDQHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGAVLD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  238 TPEVYTGIIADGHHVAWPNIRMAKKLKGDH-LVLVTDATAPAGSDIDSFIFAGKTVYYRNGLVVDENGTLSGSALTMIEA 316
Cdd:TIGR00221 240 HDDVYTEIIADGIHIHPLNIRLAKKLKGDSkLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDSNGTLAGSSLTMIEG 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  317 VQNSVEHVGIALDEALRMATLYPARAIGVAQRLGSIEPGKVANLTAFTRDFQVTTTIVNG 376
Cdd:TIGR00221 320 ARNLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNG 379
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 2-376 2.77e-139

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: 401.19  E-value: 2.77e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471   2 YALTHCRIYTGhDILDDHAVVIANGLIEKICPEAALAPDIATRDLGGAILAPGFIDVQLNGCGGVQFNDSeeavSEQTLE 81
Cdd:cd00854    1 LIIKNARILTP-GGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHGGGGADFMDG----TAEALK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  82 IMQRANERAGCTSYLPTLITCSDAMMQRGITVMQSYLRRHR-NQALGLHIEGPYISLEKKGTHNPRYIRRPD-SAMLDFI 159
Cdd:cd00854   76 TIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQgAEILGIHLEGPFISPEKKGAHPPEYLRAPDpEELKKWL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 160 CSHAEAVVKVTMAPEM-SDDAAIQQLRAAGIVVSAGHSNASYEEARRGFAAGMRFATHLYNAMPAISGRAPGLMGAIFDT 238
Cdd:cd00854  156 EAAGGLIKLVTLAPELdGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAALSD 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 239 PEVYTGIIADGHHVAWPNIRMAKKLKG-DHLVLVTDATAPAGSDIDSFIFAGKTVYYRNGLVVDENGTLSGSALTMIEAV 317
Cdd:cd00854  236 DDVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLADGTLAGSTLTMDQAV 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502612471 318 QNSVEHVGIALDEALRMATLYPARAIGVAQRLGSIEPGKVANLTAFTRDFQVTTTIVNG 376
Cdd:cd00854  316 RNMVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 50-379 2.62e-37

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: 137.63  E-value: 2.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471   50 ILAPGFIDVQLNGCGGVQFNDSE-EAVSEQTLEIMQRANERAGCTSYLPTLITCSDAMmqrgITVMQSYlrrhRNQALGL 128
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVpPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGI----EALLEAA----EELPLGL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  129 HIEGPYISLEKKGTHNPRY-IRRPDSAMLDFICSHAEAVVKVTMAPEM----SDDAAIQQLRAA-----GIVVSAGHSNA 198
Cdd:pfam01979  73 RFLGPGCSLDTDGELEGRKaLREKLKAGAEFIKGMADGVVFVGLAPHGaptfSDDELKAALEEAkkyglPVAIHALETKG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  199 SYEEARRGFAAGMRFATHLYNAMPaisgrapglmgaiFDTPEVYTGIIADGHHV-AWPNIRMAKKLKGDHLVLVTDATAP 277
Cdd:pfam01979 153 EVEDAIAAFGGGIEHGTHLEVAES-------------GGLLDIIKLILAHGVHLsPTEANLLAEHLKGAGVAHCPFSNSK 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  278 AGSDIDSF---IFAGKTVyyrnGLVVDenGTLSGSALTMIEAVQNSVE-----HVGIALDEALRMATLYPARAIGVAQRL 349
Cdd:pfam01979 220 LRSGRIALrkaLEDGVKV----GLGTD--GAGSGNSLNMLEELRLALElqfdpEGGLSPLEALRMATINPAKALGLDDKV 293

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 502612471  350 GSIEPGKVANLTAF-----------TRDFQVTTTIVNGETV 379
Cdd:pfam01979 294 GSIEVGKDADLVVVdldplaaffglKPDGNVKKVIVKGKIV 334
 
Name Accession Description Interval E-value
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 1-379 0e+00

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 745.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471   1 MYALTHCRIYTGHDILDDHAVVIANGLIEKICPEAALAPDIATRDLGGAILAPGFIDVQLNGCGGVQFNDSEEAVSEQTL 80
Cdd:PRK11170   1 MYALTNGRIYTGHEVLDDHAVVIADGLIEAVCPVAELPPGIEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISVETL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  81 EIMQRANERAGCTSYLPTLITCSDAMMQRGITVMQSYLRRHRNQALGLHIEGPYISLEKKGTHNPRYIRRPDSAMLDFIC 160
Cdd:PRK11170  81 EIMQKANEKSGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNQALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFLC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 161 SHAEAVVKVTMAPEMSDDAAIQQLRAAGIVVSAGHSNASYEEARRGFAAGMRFATHLYNAMPAISGRAPGLMGAIFDTPE 240
Cdd:PRK11170 161 ENADVITKVTLAPEMVDAEVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 241 VYTGIIADGHHVAWPNIRMAKKLKGDHLVLVTDATAPAGSDIDSFIFAGKTVYYRNGLVVDENGTLSGSALTMIEAVQNS 320
Cdd:PRK11170 241 VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIEAVRNL 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502612471 321 VEHVGIALDEALRMATLYPARAIGVAQRLGSIEPGKVANLTAFTRDFQVTTTIVNGETV 379
Cdd:PRK11170 321 VEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRDFKITKTIVNGNEV 379
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
3-377 2.04e-177

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 498.08  E-value: 2.04e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471   3 ALTHCRIYTGHDILDDHAVVIANGLIEKICPEAAlaPDIATRDLGGAILAPGFIDVQLNGCGGVQFNDSeeavSEQTLEI 82
Cdd:COG1820    1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAE--PDAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDG----TPEALRT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  83 MQRANERAGCTSYLPTLITCSDAMMQRGITVMQSYLRRH-RNQALGLHIEGPYISLEKKGTHNPRYIRRPDSAMLDFICS 161
Cdd:COG1820   75 IARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGgGAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 162 HAEAVVK-VTMAPEM-SDDAAIQQLRAAGIVVSAGHSNASYEEARRGFAAGMRFATHLYNAMPAISGRAPGLMGAIFDTP 239
Cdd:COG1820  155 AAGGLIKlVTLAPELpGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDD 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 240 EVYTGIIADGHHVAWPNIRMAKKLKG-DHLVLVTDATAPAGSDIDSFIFAGKTVYYRNGLVVDENGTLSGSALTMIEAVQ 318
Cdd:COG1820  235 DVYAELIADGIHVHPAAVRLALRAKGpDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVR 314

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502612471 319 NSVEHVGIALDEALRMATLYPARAIGVAQRLGSIEPGKVANLTAFTRDFQVTTTIVNGE 377
Cdd:COG1820  315 NLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
nagA TIGR00221
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
 1-376 1.86e-171

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


Pssm-ID: 272968  Cd Length: 380  Bit Score: 483.18  E-value: 1.86e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471    1 MYALTHCRIYTGHDILDDHAVVIANGLIEKICPEAALAPDIATRDLGGAILAPGFIDVQLNGCGGVQFNDSeeavSEQTL 80
Cdd:TIGR00221   4 SYLLKDIAIVTGNEVIDNGAVGINDGKISTVSTEAELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDA----SFETL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471   81 EIMQRANERAGCTSYLPTLITCSDAMMQRGITVMQSYLRRHRN-QALGLHIEGPYISLEKKGTHNPRYIRRPDSAML-DF 158
Cdd:TIGR00221  80 EIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKNaQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFkKF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  159 ICSHAEAVVKVTMAP-EMSDDAAIQQLRAAGIVVSAGHSNASYEEARRGFAAGMRFATHLYNAMPAISGRAPGLMGAIFD 237
Cdd:TIGR00221 160 LCEAGGVITKVTLAPeEDQHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGAVLD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  238 TPEVYTGIIADGHHVAWPNIRMAKKLKGDH-LVLVTDATAPAGSDIDSFIFAGKTVYYRNGLVVDENGTLSGSALTMIEA 316
Cdd:TIGR00221 240 HDDVYTEIIADGIHIHPLNIRLAKKLKGDSkLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDSNGTLAGSSLTMIEG 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  317 VQNSVEHVGIALDEALRMATLYPARAIGVAQRLGSIEPGKVANLTAFTRDFQVTTTIVNG 376
Cdd:TIGR00221 320 ARNLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNG 379
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 2-376 2.77e-139

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: 401.19  E-value: 2.77e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471   2 YALTHCRIYTGhDILDDHAVVIANGLIEKICPEAALAPDIATRDLGGAILAPGFIDVQLNGCGGVQFNDSeeavSEQTLE 81
Cdd:cd00854    1 LIIKNARILTP-GGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHGGGGADFMDG----TAEALK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  82 IMQRANERAGCTSYLPTLITCSDAMMQRGITVMQSYLRRHR-NQALGLHIEGPYISLEKKGTHNPRYIRRPD-SAMLDFI 159
Cdd:cd00854   76 TIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQgAEILGIHLEGPFISPEKKGAHPPEYLRAPDpEELKKWL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 160 CSHAEAVVKVTMAPEM-SDDAAIQQLRAAGIVVSAGHSNASYEEARRGFAAGMRFATHLYNAMPAISGRAPGLMGAIFDT 238
Cdd:cd00854  156 EAAGGLIKLVTLAPELdGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAALSD 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 239 PEVYTGIIADGHHVAWPNIRMAKKLKG-DHLVLVTDATAPAGSDIDSFIFAGKTVYYRNGLVVDENGTLSGSALTMIEAV 317
Cdd:cd00854  236 DDVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLADGTLAGSTLTMDQAV 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502612471 318 QNSVEHVGIALDEALRMATLYPARAIGVAQRLGSIEPGKVANLTAFTRDFQVTTTIVNG 376
Cdd:cd00854  316 RNMVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 50-379 2.62e-37

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: 137.63  E-value: 2.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471   50 ILAPGFIDVQLNGCGGVQFNDSE-EAVSEQTLEIMQRANERAGCTSYLPTLITCSDAMmqrgITVMQSYlrrhRNQALGL 128
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVpPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGI----EALLEAA----EELPLGL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  129 HIEGPYISLEKKGTHNPRY-IRRPDSAMLDFICSHAEAVVKVTMAPEM----SDDAAIQQLRAA-----GIVVSAGHSNA 198
Cdd:pfam01979  73 RFLGPGCSLDTDGELEGRKaLREKLKAGAEFIKGMADGVVFVGLAPHGaptfSDDELKAALEEAkkyglPVAIHALETKG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  199 SYEEARRGFAAGMRFATHLYNAMPaisgrapglmgaiFDTPEVYTGIIADGHHV-AWPNIRMAKKLKGDHLVLVTDATAP 277
Cdd:pfam01979 153 EVEDAIAAFGGGIEHGTHLEVAES-------------GGLLDIIKLILAHGVHLsPTEANLLAEHLKGAGVAHCPFSNSK 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  278 AGSDIDSF---IFAGKTVyyrnGLVVDenGTLSGSALTMIEAVQNSVE-----HVGIALDEALRMATLYPARAIGVAQRL 349
Cdd:pfam01979 220 LRSGRIALrkaLEDGVKV----GLGTD--GAGSGNSLNMLEELRLALElqfdpEGGLSPLEALRMATINPAKALGLDDKV 293

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 502612471  350 GSIEPGKVANLTAF-----------TRDFQVTTTIVNGETV 379
Cdd:pfam01979 294 GSIEVGKDADLVVVdldplaaffglKPDGNVKKVIVKGKIV 334
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 1-383 1.36e-19

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 89.25  E-value: 1.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471   1 MYALTHCRIYTGHD--ILDDHAVVIANGLIEKICPEAALA-PDIATR-DLGGAILAPGFID--VQLNGCGGVQFNDSEEA 74
Cdd:COG1228    9 TLLITNATLVDGTGggVIENGTVLVEDGKIAAVGPAADLAvPAGAEViDATGKTVLPGLIDahTHLGLGGGRAVEFEAGG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  75 VSEQTLEIMQRANERAgctsylptlitcsDAMMQRGIT---VMQSY---LRRHRNQALGLHIEGPYIslekkgthnpryi 148
Cdd:COG1228   89 GITPTVDLVNPADKRL-------------RRALAAGVTtvrDLPGGplgLRDAIIAGESKLLPGPRV------------- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 149 rRPDSAMLDFICSHAEAVVK--VTMAPEMSDDAAiqqlRAAGIVVSAGHSNASYEEARRGFAA----GMRFATHLY---N 219
Cdd:COG1228  143 -LAAGPALSLTGGAHARGPEeaRAALRELLAEGA----DYIKVFAEGGAPDFSLEELRAILEAahalGLPVAAHAHqadD 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 220 AMPAISGRAPGLMGAIFDTPEVYTGIIADGHHVAWPNIRMAKKLKGDHLVLVTDATAPAGSDIDSFIfagkTVYYRNGLV 299
Cdd:COG1228  218 IRLAVEAGVDSIEHGTYLDDEVADLLAEAGTVVLVPTLSLFLALLEGAAAPVAAKARKVREAALANA----RRLHDAGVP 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 300 V-----DENGTLSGSAL--TMIEAVQnsvehVGIALDEALRMATLYPARAIGVAQRLGSIEPGKVANLTAFTRD-FQVTT 371
Cdd:COG1228  294 ValgtdAGVGVPPGRSLhrELALAVE-----AGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDpLEDIA 368

                        410
                 ....*....|..
gi 502612471 372 TIVNGETVYQRG 383
Cdd:COG1228  369 YLEDVRAVMKDG 380
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
328-383 3.39e-11

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 64.43  E-value: 3.39e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612471 328 LDEALRMATLYPARAIGVAQRLGSIEPGKVANLTAFTRDF-----------QVTTTIVNGETVYQRG 383
Cdd:COG1574  469 VEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPltvppeeikdiKVLLTVVGGRVVYEAE 535
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 245-380 1.18e-09

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: 59.25  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 245 IIADGHHVAWpniRMAKKLKGDHLVLVTDATAPAGSDIDSF---IFAGKTVYYRNGLVV----DENGTLSgsALTMIEAV 317
Cdd:cd01309  219 ITIEHGAEGY---KLADELAKHGIPVIYGPTLTLPKKVEEVndaIDTNAYLLKKGGVAFaissDHPVLNI--RNLNLEAA 293

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502612471 318 QnSVEHvGIALDEALRMATLYPARAIGVAQRLGSIEPGKVANLTAFTRD-----FQVTTTIVNGETVY 380
Cdd:cd01309  294 K-AVKY-GLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDpleptSKPEQVYIDGRLVY 359
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 21-383 9.59e-09

Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.


Pssm-ID: 238633 [Multi-domain]  Cd Length: 387  Bit Score: 56.63  E-value: 9.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  21 VVIANGLIEKICPEAALA--PDIATRDLGGAILAPGFIDVQLNGCGGvqfnDSEEAVSEQTLEIMQRANERAGCTSY--- 95
Cdd:cd01308   20 ILIAGGKILAIEDQLNLPgyENVTVVDLHGKILVPGFIDQHVHIIGG----GGEGGPSTRTPEVTLSDLTTAGVTTVvgc 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471  96 ---------LPTLITCSDAMMQRGITvmqSYLRRHRNQALGLHIEGpyiSLEKKGTHNPRYIRRPDSAMLDFICShaeav 166
Cdd:cd01308   96 lgtdgisrsMEDLLAKARALEEEGIT---CFVYTGSYEVPTRTITG---SIRKDLLLIDKVIGVGEIAISDHRSS----- 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 167 vkvtmAPEMSDDAAI-QQLRAAGIVV-SAGHSNASYEEARRGFAAGMRFATH----LYNAMPAISGRAPGL--------- 231
Cdd:cd01308  165 -----QPTVEELARIaAEARVGGLLGgKAGIVHIHLGDGKRALSPIFELIEEteipITQFLPTHINRTAPLfeqgvefak 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 232 MGAIFDtpeVYTGIIADghHVAWPNIRMAKKLKgdHLVlvtdataPAGSDIDSFIFAGKTvyyrNGL--VVDENGTLSG- 308
Cdd:cd01308  240 MGGTID---LTSSIDPQ--FRKEGEVRPSEALK--RLL-------EQGVPLERITFSSDG----NGSlpKFDENGNLVGl 301

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502612471 309 ---SALTMIEAVQNSVEHVGIALDEALRMATLYPARAIGVAQRlGSIEPGKVANLTAFTRDFQVTTTIVNGETVYQRG 383
Cdd:cd01308  302 gvgSVDTLLREVREAVKCGDIPLEVALRVITSNVARILKLRKK-GEIQPGFDADLVILDKDLDINSVIAKGQIMVRNG 378
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
327-383 1.11e-08

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 56.46  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 327 ALD--EALRMATLYPARAIGVAQRLGSIEPGKVANLTAF---------------------TRDfQVTTTIVNGETVYQRG 383
Cdd:PRK09045 339 ALPahTALRMATLNGARALGLDDEIGSLEPGKQADLVAVdlsgletqpvydpvsqlvyaaGRE-QVSHVWVAGKQLLDDR 417
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 321-383 1.15e-07

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 53.26  E-value: 1.15e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502612471 321 VEHVGIALDEALRMATLYPARAIGVAQRlGSIEPGKVANLTAFTRD---FQVTTTIVNGETVYQRG 383
Cdd:PRK15446 319 ADDGGLDLPQAVALVTANPARAAGLDDR-GEIAPGKRADLVRVRRAgglPVVRAVWRGGRRVFLAG 383
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 330-382 1.53e-07

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: 52.91  E-value: 1.53e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502612471 330 EALRMATLYPARAIGVAQRLGSIEPGKVANLTAF--------------------TRDFQVTTTIVNGETVYQR 382
Cdd:COG0402  344 EALEMATLGGARALGLDDEIGSLEPGKRADLVVLdldaphlaplhdplsalvyaADGRDVRTVWVAGRVVVRD 416
Amidohydro_3 pfam07969
Amidohydrolase family;
328-380 2.32e-07

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 52.53  E-value: 2.32e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502612471  328 LDEALRMATLYPARAIGVAQRLGSIEPGKVANLTAFTRDF-----------QVTTTIVNGETVY 380
Cdd:pfam07969 401 LEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPltvdppaiadiRVRLTVVDGRVVY 464
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
325-383 6.12e-07

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 51.25  E-value: 6.12e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502612471 325 GIALDEALRMATLYPARAIGVAqRLGSIEPGKVANLTAFT--RDFQVTTTIVNGETVYQRG 383
Cdd:COG1001  283 GLDPVTAIQMATLNAAEHFGLK-DLGAIAPGRRADIVLLDdlEDFKVEKVYADGKLVAEDG 342
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
330-383 2.20e-06

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 49.23  E-value: 2.20e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502612471 330 EALRMATLYPARAIGVAQRLGSIEPGKVANLT-----------------------AFTRDfQVTTTIVNGETVYQRG 383
Cdd:PRK07228 341 TVFEMATLGGAKAAGFEDEIGSLEEGKKADLAildldglhatpshgvdvlshlvyAAHGS-DVETTMVDGKIVMEDG 416
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 328-361 8.82e-06

YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 47.69  E-value: 8.82e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 502612471 328 LDEALRMATLYPARAIGVAQRLGSIEPGKVANLT 361
Cdd:cd01300  445 LEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFV 478
AdeC cd01295
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ...
 224-384 2.19e-05

Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.


Pssm-ID: 238620 [Multi-domain]  Cd Length: 422  Bit Score: 46.06  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 224 ISGRAPGLMGA---------IFDTPEVYTGIIAD-----GHHV------AWPNIRMAKKLKG----DHLVLVTDATAPag 279
Cdd:cd01295  137 VDGHAPGLSGEelnaymaagISTDHEAMTGEEALeklrlGMYVmlregsIAKNLEALLPAITeknfRRFMFCTDDVHP-- 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 280 SDIDSfifagktvyyrnglvvdengtlSGSALTMI-EAVQNsvehvGIALDEALRMATLYPARAIGVAQrLGSIEPGKVA 358
Cdd:cd01295  215 DDLLS----------------------EGHLDYIVrRAIEA-----GIPPEDAIQMATINPAECYGLHD-LGAIAPGRIA 266

                        170       180
                 ....*....|....*....|....*...
gi 502612471 359 NLTAFT--RDFQVTTTIVNGETVYQRGG 384
Cdd:cd01295  267 DIVILDdlENFNITTVLAKGIAVVERHG 294
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 297-383 4.16e-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: 45.27  E-value: 4.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 297 GLVVDenGTLSGSALTMIEAV-QNSVEHVGIALD-------EALRMATLYPARAIGVAQrLGSIEPGKVANLTAF-TRDF 367
Cdd:cd01298  297 GLGTD--GAASNNNLDMFEEMrLAALLQKLAHGDptalpaeEALEMATIGGAKALGLDE-IGSLEVGKKADLILIdLDGP 373

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 502612471 368 -------------------QVTTTIVNGETVYQRG 383
Cdd:cd01298  374 hllpvhdpishlvysanggDVDTVIVNGRVVMEDG 408
PhnM cd01306
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ...
 322-376 1.76e-04

PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.


Pssm-ID: 238631  Cd Length: 325  Bit Score: 43.04  E-value: 1.76e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502612471 322 EHVGIALDEALRMATLYPARAIGVAQRlGSIEPGKVANLTAFTRDF---QVTTTIVNG 376
Cdd:cd01306  269 DLGGWSLPEAVALVSANPARAVGLTDR-GSIAPGKRADLILVDDMDgvpVVRTVWRGG 325
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 303-360 5.63e-04

Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 41.47  E-value: 5.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502612471 303 NGTLSGSALTMIEAVQNSvehvGIALDEALRMATLYPARAIGVAQRLGSIEPGKVANL 360
Cdd:cd01296  291 SSPTSSMPLVMHLACRLM----RMTPEEALTAATINAAAALGLGETVGSLEVGKQADL 344
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
323-379 5.92e-04

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 41.76  E-value: 5.92e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502612471 323 HVGIALDEALRMATLYPARAIGVAQrLGSIEPGKVANLTAFT-RDFQVTTTIVNGETV 379
Cdd:PRK09237 293 ALGMPLEEVIAAVTKNAADALRLPE-LGRLQVGSDADLTLFTlKDGPFTLTDSEGDSL 349
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 21-59 6.96e-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: 41.62  E-value: 6.96e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 502612471  21 VVIANGLIEKICPEAALAPDIATRDLGGAILAPGFIDVQ 59
Cdd:COG0044   18 VLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLH 56
Met_dep_hydrolase_D cd01312
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 330-363 1.46e-03

Metallo-dependent hydrolases, subgroup D 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: 238637 [Multi-domain]  Cd Length: 381  Bit Score: 40.51  E-value: 1.46e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 502612471 330 EALRMATLYPARAIGVAqrLGSIEPGKVANLTAF 363
Cdd:cd01312  320 ELLLMATLGGARALGLN--NGEIEAGKRADFAVF 351
PRK09228 PRK09228
guanine deaminase; Provisional
 18-57 1.66e-03

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 40.17  E-value: 1.66e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 502612471  18 DHAVVIANGLIEKICPEAALAP----DIATRDLGGAILAPGFID 57
Cdd:PRK09228  31 DGLLLVEDGRIVAAGPYAELRAqlpaDAEVTDYRGKLILPGFID 74
PRK05985 PRK05985
cytosine deaminase; Provisional
 19-57 1.73e-03

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 40.30  E-value: 1.73e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 502612471  19 HAVVIANGLIEKICPEAALAPDIATRDLGGAILAPGFID 57
Cdd:PRK05985  17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVD 55
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 330-360 2.56e-03

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: 39.58  E-value: 2.56e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 502612471 330 EALRMATLYPARAIGVAQRLGSIEPGKVANL 360
Cdd:cd01299  298 EALRAATANAAELLGLSDELGVIEAGKLADL 328
PRK08204 PRK08204
hypothetical protein; Provisional
 310-366 3.46e-03

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 39.22  E-value: 3.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502612471 310 ALTMIEAVQNSV---------EHVGIALDEALRMATLYPARAIGVAQRLGSIEPGKVANLTAFTRD 366
Cdd:PRK08204 317 ALQAERARDNAVhlreggmppPRLTLTARQVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDAT 382
PRK12394 PRK12394
metallo-dependent hydrolase;
325-378 6.53e-03

metallo-dependent hydrolase;


Pssm-ID: 183497 [Multi-domain]  Cd Length: 379  Bit Score: 38.20  E-value: 6.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 502612471 325 GIALDEALRMATLYPARAIGVAQRLGSIEPGKVANLTAFT-RDFQVTTTIVNGET 378
Cdd:PRK12394 300 GMALEDVINACTHTPAVLMGMAAEIGTLAPGAFADIAIFKlKNRHVEFADIHGET 354
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 297-369 7.82e-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: 38.03  E-value: 7.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502612471 297 GLVVDENGTLSGSAL-TMIEAVQNS-------VEHVGIALDEALRMATLYPARAIGVAQRLGSIEPGKVAnltaftrDFQ 368
Cdd:cd01303  314 GLGTDVGGGTSFSMLdTLRQAYKVSrllgyelGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEF-------DAV 386


                 .
gi 502612471 369 V 369
Cdd:cd01303  387 V 387
 
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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