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Conserved domains on  [gi|224922791|ref|NP_001139287|]
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N-acetylglucosamine-6-phosphate deacetylase isoform 2 [Homo sapiens]

Protein Classification

N-acetylglucosamine-6-phosphate deacetylase( domain architecture ID 10096248)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
13-428 7.04e-165

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: 474.76  E-value: 7.04e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  13 LQFTNCRILRGGKLLREDLWVRGGRILDPEKLFFEERRvaDERRDCGGRILAPGFIDVQINGGFGVDFSQATEDvgsGVA 92
Cdd:cd00854    1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEA--DEIIDLKGQYLVPGFIDIHIHGGGGADFMDGTAE---ALK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  93 LVARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDLL 172
Cdd:cd00854   76 TIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELKKWL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 173 ATYGplDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVGLLT 252
Cdd:cd00854  156 EAAG--GLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAAL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 253 SDrlpagRCIFYGMIADGTHTNPAALRIAHRAHP-QGLVLVTDAIPALGLGNGRHTLGQQEVEVDGLTAYVAgerpdplg 331
Cdd:cd00854  234 SD-----DDVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLA-------- 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 332 prsqpacqvahdppracplcsqgTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGADAD 411
Cdd:cd00854  301 -----------------------DGTLAGSTLTMDQAVRNMVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDAD 357
                        410
                 ....*....|....*..
gi 224922791 412 FVVLDDSLHVQATYISG 428
Cdd:cd00854  358 LVVLDDDLNVKATWING 374
 
Name Accession Description Interval E-value
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
13-428 7.04e-165

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: 474.76  E-value: 7.04e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  13 LQFTNCRILRGGKLLREDLWVRGGRILDPEKLFFEERRvaDERRDCGGRILAPGFIDVQINGGFGVDFSQATEDvgsGVA 92
Cdd:cd00854    1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEA--DEIIDLKGQYLVPGFIDIHIHGGGGADFMDGTAE---ALK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  93 LVARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDLL 172
Cdd:cd00854   76 TIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELKKWL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 173 ATYGplDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVGLLT 252
Cdd:cd00854  156 EAAG--GLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAAL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 253 SDrlpagRCIFYGMIADGTHTNPAALRIAHRAHP-QGLVLVTDAIPALGLGNGRHTLGQQEVEVDGLTAYVAgerpdplg 331
Cdd:cd00854  234 SD-----DDVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLA-------- 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 332 prsqpacqvahdppracplcsqgTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGADAD 411
Cdd:cd00854  301 -----------------------DGTLAGSTLTMDQAVRNMVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDAD 357
                        410
                 ....*....|....*..
gi 224922791 412 FVVLDDSLHVQATYISG 428
Cdd:cd00854  358 LVVLDDDLNVKATWING 374
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
15-428 1.87e-136

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 402.17  E-value: 1.87e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  15 FTNCRILRGGKLLRE-DLWVRGGRILDpeklFFEERRVADERRDCGGRILAPGFIDVQINGGFGVDFSQATEDvgsGVAL 93
Cdd:COG1820    2 ITNARIFTGDGVLEDgALLIEDGRIAA----IGPGAEPDAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGTPE---ALRT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  94 VARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDLLA 173
Cdd:COG1820   75 IARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGGGAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 174 TYGplDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVG-LLT 252
Cdd:COG1820  155 AAG--GLIKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGaALD 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 253 SDRLPAgrcifyGMIADGTHTNPAALRIAHRA-HPQGLVLVTDAIPALGLGNGRHTLGQQEVEVDGLTAYVAgerpdplg 331
Cdd:COG1820  233 DDDVYA------ELIADGIHVHPAAVRLALRAkGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLA-------- 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 332 prsqpacqvahdppracplcsqgTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGADAD 411
Cdd:COG1820  299 -----------------------DGTLAGSTLTMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDAD 355
                        410
                 ....*....|....*..
gi 224922791 412 FVVLDDSLHVQATYISG 428
Cdd:COG1820  356 LVVLDDDLNVRATWVGG 372
nagA TIGR00221
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
15-428 4.29e-79

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


Pssm-ID: 272968  Cd Length: 380  Bit Score: 254.76  E-value: 4.29e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791   15 FTNCRILRGGKLLRED-LWVRGGRILD--PEKlffeERRVADERRDCGGRILAPGFIDVQINGGFGVDFSQATEdvgSGV 91
Cdd:TIGR00221   7 LKDIAIVTGNEVIDNGaVGINDGKISTvsTEA----ELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDASF---ETL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791   92 ALVARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDL 171
Cdd:TIGR00221  80 EIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKNAQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFKKF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  172 LATYGplDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVG-L 250
Cdd:TIGR00221 160 LCEAG--GVITKVTLAPEEDQHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGaV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  251 LTSDRlpagrcIFYGMIADGTHTNPAALRIAHRAHPQG-LVLVTDAIPALGLGNGRHTLGQQEVevdgltaYVAGERpdp 329
Cdd:TIGR00221 238 LDHDD------VYTEIIADGIHIHPLNIRLAKKLKGDSkLCLVTDSMAAAGAKDGVFIFGGKTV-------YIREGT--- 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  330 lgprsqpacqvahdppracplCSQGTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGAD 409
Cdd:TIGR00221 302 ---------------------CLDSNGTLAGSSLTMIEGARNLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKD 360
                         410
                  ....*....|....*....
gi 224922791  410 ADFVVLDDSLHVQATYISG 428
Cdd:TIGR00221 361 ANLVVFTPDFEVILTIVNG 379
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
15-428 1.16e-63

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 214.07  E-value: 1.16e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  15 FTNCRILRGGKLLRED-LWVRGGRIldpEKLFFEERRVAD-ERRDCGGRILAPGFIDVQINGGFGVDFSQATEDVG-SGV 91
Cdd:PRK11170   4 LTNGRIYTGHEVLDDHaVVIADGLI---EAVCPVAELPPGiEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISvETL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  92 ALVARRILSHGVTSFCPTLVTSPPEVYHKVVpQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDL 171
Cdd:PRK11170  81 EIMQKANEKSGCTSFLPTLITSSDELMKQAV-RVMREYLAKHPNQALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 172 LATygpLDNVRIVTLAPELGRShEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVGLL 251
Cdd:PRK11170 160 CEN---ADVITKVTLAPEMVDA-EVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 252 --TSDrlpagrcIFYGMIADGTHTNPAALRIAHRAHPQGLVLVTDAIPALGLGNGRHTLGqqevevdGLTAYVagerpdp 329
Cdd:PRK11170 236 ldEPD-------VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFA-------GKTIYY------- 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 330 lgprsqpacqvaHDppracPLCSQGTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGAD 409
Cdd:PRK11170 295 ------------RD-----GLCVDENGTLSGSALTMIEAVRNLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKV 357
                        410
                 ....*....|....*....
gi 224922791 410 ADFVVLDDSLHVQATYISG 428
Cdd:PRK11170 358 ANLTAFTRDFKITKTIVNG 376
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
62-416 3.67e-11

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: 64.83  E-value: 3.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791   62 ILAPGFIDVQINGGFGVDFSQAT--EDVGSGVALVARRILSHGVTSFCPTLVTSPP------EVYHKVVPQIPVksGGPH 133
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVppEFAYEALRLGITTMLKSGTTTVLDMGATTSTgieallEAAEELPLGLRF--LGPG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  134 GAGVLGLHLEGPFISREKrgAHPEAHLRSFEAD-AFQDLLATYGPldnvriVTLAPELGRshEVIRALTARG--ICVSLG 210
Cdd:pfam01979  79 CSLDTDGELEGRKALREK--LKAGAEFIKGMADgVVFVGLAPHGA------PTFSDDELK--AALEEAKKYGlpVAIHAL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  211 HSVADLRAAEDAVWSGATFITHLFNAMLPFHHRdpgivglltsdrlpagrcIFYGMIADGTHTNPA-ALRIAHRAHPQGL 289
Cdd:pfam01979 149 ETKGEVEDAIAAFGGGIEHGTHLEVAESGGLLD------------------IIKLILAHGVHLSPTeANLLAEHLKGAGV 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  290 VLVTDAIPALGLG-NGRHTLGQQEVEVdgltayvagerpdPLGPRSQpacqvahdppracplcsqgtktLSGSIAPMDVC 368
Cdd:pfam01979 211 AHCPFSNSKLRSGrIALRKALEDGVKV-------------GLGTDGA----------------------GSGNSLNMLEE 255
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 224922791  369 VR-----HFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD 416
Cdd:pfam01979 256 LRlalelQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVD 308
 
Name Accession Description Interval E-value
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
13-428 7.04e-165

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: 474.76  E-value: 7.04e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  13 LQFTNCRILRGGKLLREDLWVRGGRILDPEKLFFEERRvaDERRDCGGRILAPGFIDVQINGGFGVDFSQATEDvgsGVA 92
Cdd:cd00854    1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEA--DEIIDLKGQYLVPGFIDIHIHGGGGADFMDGTAE---ALK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  93 LVARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDLL 172
Cdd:cd00854   76 TIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELKKWL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 173 ATYGplDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVGLLT 252
Cdd:cd00854  156 EAAG--GLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAAL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 253 SDrlpagRCIFYGMIADGTHTNPAALRIAHRAHP-QGLVLVTDAIPALGLGNGRHTLGQQEVEVDGLTAYVAgerpdplg 331
Cdd:cd00854  234 SD-----DDVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLA-------- 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 332 prsqpacqvahdppracplcsqgTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGADAD 411
Cdd:cd00854  301 -----------------------DGTLAGSTLTMDQAVRNMVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDAD 357
                        410
                 ....*....|....*..
gi 224922791 412 FVVLDDSLHVQATYISG 428
Cdd:cd00854  358 LVVLDDDLNVKATWING 374
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
15-428 1.87e-136

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 402.17  E-value: 1.87e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  15 FTNCRILRGGKLLRE-DLWVRGGRILDpeklFFEERRVADERRDCGGRILAPGFIDVQINGGFGVDFSQATEDvgsGVAL 93
Cdd:COG1820    2 ITNARIFTGDGVLEDgALLIEDGRIAA----IGPGAEPDAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGTPE---ALRT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  94 VARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDLLA 173
Cdd:COG1820   75 IARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGGGAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 174 TYGplDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVG-LLT 252
Cdd:COG1820  155 AAG--GLIKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGaALD 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 253 SDRLPAgrcifyGMIADGTHTNPAALRIAHRA-HPQGLVLVTDAIPALGLGNGRHTLGQQEVEVDGLTAYVAgerpdplg 331
Cdd:COG1820  233 DDDVYA------ELIADGIHVHPAAVRLALRAkGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLA-------- 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 332 prsqpacqvahdppracplcsqgTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGADAD 411
Cdd:COG1820  299 -----------------------DGTLAGSTLTMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDAD 355
                        410
                 ....*....|....*..
gi 224922791 412 FVVLDDSLHVQATYISG 428
Cdd:COG1820  356 LVVLDDDLNVRATWVGG 372
nagA TIGR00221
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
15-428 4.29e-79

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


Pssm-ID: 272968  Cd Length: 380  Bit Score: 254.76  E-value: 4.29e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791   15 FTNCRILRGGKLLRED-LWVRGGRILD--PEKlffeERRVADERRDCGGRILAPGFIDVQINGGFGVDFSQATEdvgSGV 91
Cdd:TIGR00221   7 LKDIAIVTGNEVIDNGaVGINDGKISTvsTEA----ELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDASF---ETL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791   92 ALVARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDL 171
Cdd:TIGR00221  80 EIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKNAQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFKKF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  172 LATYGplDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVG-L 250
Cdd:TIGR00221 160 LCEAG--GVITKVTLAPEEDQHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGaV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  251 LTSDRlpagrcIFYGMIADGTHTNPAALRIAHRAHPQG-LVLVTDAIPALGLGNGRHTLGQQEVevdgltaYVAGERpdp 329
Cdd:TIGR00221 238 LDHDD------VYTEIIADGIHIHPLNIRLAKKLKGDSkLCLVTDSMAAAGAKDGVFIFGGKTV-------YIREGT--- 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  330 lgprsqpacqvahdppracplCSQGTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGAD 409
Cdd:TIGR00221 302 ---------------------CLDSNGTLAGSSLTMIEGARNLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKD 360
                         410
                  ....*....|....*....
gi 224922791  410 ADFVVLDDSLHVQATYISG 428
Cdd:TIGR00221 361 ANLVVFTPDFEVILTIVNG 379
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
15-428 1.16e-63

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 214.07  E-value: 1.16e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  15 FTNCRILRGGKLLRED-LWVRGGRIldpEKLFFEERRVAD-ERRDCGGRILAPGFIDVQINGGFGVDFSQATEDVG-SGV 91
Cdd:PRK11170   4 LTNGRIYTGHEVLDDHaVVIADGLI---EAVCPVAELPPGiEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISvETL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  92 ALVARRILSHGVTSFCPTLVTSPPEVYHKVVpQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDL 171
Cdd:PRK11170  81 EIMQKANEKSGCTSFLPTLITSSDELMKQAV-RVMREYLAKHPNQALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 172 LATygpLDNVRIVTLAPELGRShEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVGLL 251
Cdd:PRK11170 160 CEN---ADVITKVTLAPEMVDA-EVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 252 --TSDrlpagrcIFYGMIADGTHTNPAALRIAHRAHPQGLVLVTDAIPALGLGNGRHTLGqqevevdGLTAYVagerpdp 329
Cdd:PRK11170 236 ldEPD-------VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFA-------GKTIYY------- 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 330 lgprsqpacqvaHDppracPLCSQGTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGAD 409
Cdd:PRK11170 295 ------------RD-----GLCVDENGTLSGSALTMIEAVRNLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKV 357
                        410
                 ....*....|....*....
gi 224922791 410 ADFVVLDDSLHVQATYISG 428
Cdd:PRK11170 358 ANLTAFTRDFKITKTIVNG 376
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
62-416 3.67e-11

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: 64.83  E-value: 3.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791   62 ILAPGFIDVQINGGFGVDFSQAT--EDVGSGVALVARRILSHGVTSFCPTLVTSPP------EVYHKVVPQIPVksGGPH 133
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVppEFAYEALRLGITTMLKSGTTTVLDMGATTSTgieallEAAEELPLGLRF--LGPG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  134 GAGVLGLHLEGPFISREKrgAHPEAHLRSFEAD-AFQDLLATYGPldnvriVTLAPELGRshEVIRALTARG--ICVSLG 210
Cdd:pfam01979  79 CSLDTDGELEGRKALREK--LKAGAEFIKGMADgVVFVGLAPHGA------PTFSDDELK--AALEEAKKYGlpVAIHAL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  211 HSVADLRAAEDAVWSGATFITHLFNAMLPFHHRdpgivglltsdrlpagrcIFYGMIADGTHTNPA-ALRIAHRAHPQGL 289
Cdd:pfam01979 149 ETKGEVEDAIAAFGGGIEHGTHLEVAESGGLLD------------------IIKLILAHGVHLSPTeANLLAEHLKGAGV 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  290 VLVTDAIPALGLG-NGRHTLGQQEVEVdgltayvagerpdPLGPRSQpacqvahdppracplcsqgtktLSGSIAPMDVC 368
Cdd:pfam01979 211 AHCPFSNSKLRSGrIALRKALEDGVKV-------------GLGTDGA----------------------GSGNSLNMLEE 255
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 224922791  369 VR-----HFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD 416
Cdd:pfam01979 256 LRlalelQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVD 308
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
7-416 8.05e-07

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 51.50  E-value: 8.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791   7 AAGARVLQFTNCRIL--RGGKLLRE-DLWVRGGRILDPEKLFFEERRVADERRDCGGRILAPGFID--VQI-NGGFGVDF 80
Cdd:COG1228    4 PAQAGTLLITNATLVdgTGGGVIENgTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDahTHLgLGGGRAVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  81 SQATEDVGSGVALV------ARRILSHGVTSfcptlvtsppevyhkVVpqipVKSGGPHG----------AGVLGLHL-- 142
Cdd:COG1228   84 FEAGGGITPTVDLVnpadkrLRRALAAGVTT---------------VR----DLPGGPLGlrdaiiagesKLLPGPRVla 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 143 EGPFISREKrGAH---PE---AHLRS-FEADA-FQDLLATYGPLDnvrivtlapelgRSHEVIRALT----ARGICVSlG 210
Cdd:COG1228  145 AGPALSLTG-GAHargPEearAALRElLAEGAdYIKVFAEGGAPD------------FSLEELRAILeaahALGLPVA-A 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 211 HsVADLRAAEDAVWSGATFITHL-------FNAMLpfhHRDPGIVGLLTSDRLPAGRCIFYGMIADGTHTNPAALRIAHR 283
Cdd:COG1228  211 H-AHQADDIRLAVEAGVDSIEHGtylddevADLLA---EAGTVVLVPTLSLFLALLEGAAAPVAAKARKVREAALANARR 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 284 AHPQGlVLVtdaipALGlgngrhTlgqqevevDGLTAYVAGerpdplgpRSQPACqvahdppracplcsqgtktlsgsia 363
Cdd:COG1228  287 LHDAG-VPV-----ALG------T--------DAGVGVPPG--------RSLHRE------------------------- 313
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 224922791 364 pMDVCVRHflqatGCSMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD 416
Cdd:COG1228  314 -LALAVEA-----GLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLD 360
AdeC cd01295
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ...
365-428 3.44e-06

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: 49.53  E-value: 3.44e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224922791 365 MDVCVRHFLQAtGCSMESALEAASLHPAQLLGLEKsKGTLDFGADADFVVLDD--SLHVQATYISG 428
Cdd:cd01295  223 LDYIVRRAIEA-GIPPEDAIQMATINPAECYGLHD-LGAIAPGRIADIVILDDleNFNITTVLAKG 286
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
351-416 1.57e-05

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: 47.25  E-value: 1.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224922791 351 CSQGTKTLSGSIAPMDVCVRHFlqatGCSMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD 416
Cdd:cd01296  287 FNPGSSPTSSMPLVMHLACRLM----RMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
15-125 2.88e-05

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: 46.62  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  15 FTNCRILRGGKLLREDLWVRGGRILDPEKLFFEERrvADERRDCGGRILAPGFIDVQINggFGVDFSQATEDVGSG-VAL 93
Cdd:COG0044    2 IKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPE--AAEVIDATGLLVLPGLIDLHVH--LREPGLEHKEDIETGtRAA 77
                         90       100       110
                 ....*....|....*....|....*....|..
gi 224922791  94 VArrilsHGVTSFCPTLVTSPPEVYHKVVPQI 125
Cdd:COG0044   78 AA-----GGVTTVVDMPNTNPVTDTPEALEFK 104
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
365-432 5.70e-05

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 45.86  E-value: 5.70e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 365 MDVCVRHFLQAtGCSMESALEAASLHPAQLLGLeKSKGTLDFGADADFVVLDD--SLHVQATYISGPVLA 432
Cdd:COG1001  272 IDHVVRRAIEL-GLDPVTAIQMATLNAAEHFGL-KDLGAIAPGRRADIVLLDDleDFKVEKVYADGKLVA 339
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
367-428 8.12e-05

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: 44.99  E-value: 8.12e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224922791 367 VCVRHflqatGCSMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD-DSLH----VQATYISG 428
Cdd:cd01309  294 KAVKY-----GLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNgDPLEptskPEQVYIDG 355
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
379-428 1.13e-04

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 45.17  E-value: 1.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224922791 379 SMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLDDSL-----------HVQATYISG 428
Cdd:COG1574  468 TVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPltvppeeikdiKVLLTVVGG 528
Amidohydro_3 pfam07969
Amidohydrolase family;
379-417 1.29e-04

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 44.83  E-value: 1.29e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 224922791  379 SMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLDD 417
Cdd:pfam07969 400 SLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDD 438
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
388-417 6.59e-04

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: 42.28  E-value: 6.59e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 224922791 388 SLHPAQLLGLEKSKGTLDFGADADFVVLDD 417
Cdd:cd01315  363 CENPAKLFGLSHQKGRIAVGYDADFVVWDP 392
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
383-445 1.49e-03

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: 41.35  E-value: 1.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224922791 383 ALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD-DSLHVQATY--ISGPVLAGCGDPAwcwRAVW 445
Cdd:COG0402  345 ALEMATLGGARALGLDDEIGSLEPGKRADLVVLDlDAPHLAPLHdpLSALVYAADGRDV---RTVW 407
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
365-417 2.10e-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: 40.77  E-value: 2.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 224922791 365 MDVCVRHFLqATGCSMESALEAASLHPAQLLGLeKSKGTLDFGADADFVVLDD 417
Cdd:cd01307  265 LATTLSKLL-ALGMPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFDL 315
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
354-416 2.93e-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: 39.97  E-value: 2.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224922791 354 GTKTLSGSIAPMDVcVRHFLQAT---------GCSMEsALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD 416
Cdd:cd01299  263 GVKIAFGTDAGFPV-PPHGWNARelellvkagGTPAE-ALRAATANAAELLGLSDELGVIEAGKLADLLVVD 332
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
360-431 4.18e-03

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: 39.68  E-value: 4.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224922791 360 GSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKsKGTLDFGADADFVVLDDSLHVQATYISGPVL 431
Cdd:cd01308  304 GSVDTLLREVREAVKCGDIPLEVALRVITSNVARILKLRK-KGEIQPGFDADLVILDKDLDINSVIAKGQIM 374
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
23-425 4.51e-03

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: 39.59  E-value: 4.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  23 GGKLLREDLWVRGGRI------LDPEklffeerrvADERRDCGGRILAPGFIDVQINGGfgvdfSQATEDVGsgvalvAR 96
Cdd:cd01297   14 GAPPFTADVGIRDGRIaaigpiLSTS---------AREVIDAAGLVVAPGFIDVHTHYD-----GQVFWDPD------LR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  97 RILSHGVT---------SFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEgpfiSREKRGAHPEAhlrsfEADA 167
Cdd:cd01297   74 PSSRQGVTtvvlgncgvSPAPANPDDLARLIMLMEGLVALGEGLPWGWATFAEYLD----ALEARPPAVNV-----AALV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 168 FQDLLATYGPLDNVRIVTlAPELGRSHEVIR-ALTARGICVS--------LGHSVADLRA-AEDAVWSGATFITHLFNam 237
Cdd:cd01297  145 GHAALRRAVMGLDAREAT-EEELAKMRELLReALEAGALGIStglayaprLYAGTAELVAlARVAARYGGVYQTHVRY-- 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 238 lPFHHRDPGIVGLLTSDRLpAGR----CIFYGMIADGTHTNPAALRIAHRAHPQGLVLVTDAIP--ALGLGNGRHTLGQQ 311
Cdd:cd01297  222 -EGDSILEALDELLRLGRE-TGRpvhiSHLKSAGAPNWGKIDRLLALIEAARAEGLQVTADVYPygAGSEDDVRRIMAHP 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791 312 EVEV--DGltayvagerpdplGPRSQPACQVAHDPPRACPLCSQGTKTLsgsiapmdvcvrhflqatgcSMESALEAASL 389
Cdd:cd01297  300 VVMGgsDG-------------GALGKPHPRSYGDFTRVLGHYVRERKLL--------------------SLEEAVRKMTG 346
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 224922791 390 HPAQLLGLeKSKGTLDFGADADFVVLD-DSLHVQATY 425
Cdd:cd01297  347 LPARVFGL-ADRGRIAPGYRADIVVFDpDTLADRATF 382
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
15-104 5.93e-03

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 39.39  E-value: 5.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224922791  15 FTNCRILRGGKLLREDLWVRGGRILDPEklffEERRVADERRDCGGRILAPGFIDV---QINGGF----GVDFsqateDV 87
Cdd:PRK15446   6 LSNARLVLPDEVVDGSLLIEDGRIAAID----PGASALPGAIDAEGDYLLPGLVDLhtdNLEKHLaprpGVDW-----PA 76
                         90
                 ....*....|....*..
gi 224922791  88 GSGVALVARRILSHGVT 104
Cdd:PRK15446  77 DAALAAHDAQLAAAGIT 93
PRK06189 PRK06189
allantoinase; Provisional
374-416 6.16e-03

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 39.30  E-value: 6.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 224922791 374 QATGCSMESALEAASLHPAQLLGLEKsKGTLDFGADADFVVLD 416
Cdd:PRK06189 349 IERGIPLETIARLLATNPAKRFGLPQ-KGRLEVGADADFVLVD 390
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
379-416 7.18e-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: 39.12  E-value: 7.18e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 224922791 379 SMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD 416
Cdd:cd01314  357 TLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWD 394
 
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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