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Conserved domains on  [gi|585136213|gb|AHJ24681|]
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N-acetylglucosamine-6-phosphate deacetylase [Bifidobacterium breve S27]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
22-411 1.98e-138

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


:

Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 400.24  E-value: 1.98e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  22 AIRDARKVDARGIEEHAWIVADaNGAIAARGTSDDDfeaacrangigTDAVIDASGKIMTPGYVDIHSHGAWEKSFDDG- 100
Cdd:COG1820    1 AITNARIFTGDGVLEDGALLIE-DGRIAAIGPGAEP-----------DAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGt 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 101 PDGIDVARAGHAMHGTTRQVCSLITNPIDVQCENLRNVRAKMDQR--PDILGAHLEGPFLALSRKGAHDPECLKDPVPEI 178
Cdd:COG1820   69 PEALRTIARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGggAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 179 VDRMLEAADGCLRQITIAPELPHGLQAIRSFATAGTVPAVGHCDADYETARRAFDEGAGLMTHMFNAMNGLHHRKPGPIP 258
Cdd:COG1820  149 LDRLLEAAGGLIKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 259 AAVEDPRVTIELICDGFHVQDPMLRLGLG-FAPHRIAFVTDAMAATDCPDGAYKLGALDVDVVDGHARLKsNGAIAGSTL 337
Cdd:COG1820  229 AALDDDDVYAELIADGIHVHPAAVRLALRaKGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLA-DGTLAGSTL 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585136213 338 TLEHAVQRAVLELGMSPVEAIEAATLTPARAFGFDRpypvtgaPLGLLAPGYAADVLLTDPaDWSVQHAWCAGR 411
Cdd:COG1820  308 TMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDD-------RKGSIAPGKDADLVVLDD-DLNVRATWVGGE 373
 
Name Accession Description Interval E-value
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
22-411 1.98e-138

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 400.24  E-value: 1.98e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  22 AIRDARKVDARGIEEHAWIVADaNGAIAARGTSDDDfeaacrangigTDAVIDASGKIMTPGYVDIHSHGAWEKSFDDG- 100
Cdd:COG1820    1 AITNARIFTGDGVLEDGALLIE-DGRIAAIGPGAEP-----------DAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGt 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 101 PDGIDVARAGHAMHGTTRQVCSLITNPIDVQCENLRNVRAKMDQR--PDILGAHLEGPFLALSRKGAHDPECLKDPVPEI 178
Cdd:COG1820   69 PEALRTIARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGggAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 179 VDRMLEAADGCLRQITIAPELPHGLQAIRSFATAGTVPAVGHCDADYETARRAFDEGAGLMTHMFNAMNGLHHRKPGPIP 258
Cdd:COG1820  149 LDRLLEAAGGLIKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 259 AAVEDPRVTIELICDGFHVQDPMLRLGLG-FAPHRIAFVTDAMAATDCPDGAYKLGALDVDVVDGHARLKsNGAIAGSTL 337
Cdd:COG1820  229 AALDDDDVYAELIADGIHVHPAAVRLALRaKGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLA-DGTLAGSTL 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585136213 338 TLEHAVQRAVLELGMSPVEAIEAATLTPARAFGFDRpypvtgaPLGLLAPGYAADVLLTDPaDWSVQHAWCAGR 411
Cdd:COG1820  308 TMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDD-------RKGSIAPGKDADLVVLDD-DLNVRATWVGGE 373
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
22-410 1.96e-137

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: 397.72  E-value: 1.96e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  22 AIRDARKVDARGIEEHAWIVADanGAIAARGTSDDDFEaacrangigTDAVIDASGKIMTPGYVDIHSHGAWEKSFDDG- 100
Cdd:cd00854    2 IIKNARILTPGGLEDGAVLVED--GKIVAIGPEDELEE---------ADEIIDLKGQYLVPGFIDIHIHGGGGADFMDGt 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 101 PDGIDVARAGHAMHGTTRQVCSLITNPIDVQCENLRNVRAKMDQ--RPDILGAHLEGPFLALSRKGAHDPECLKDPVPEI 178
Cdd:cd00854   71 AEALKTIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEgqGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 179 VDRMLEAADGCLRQITIAPELPHGLQAIRSFATAGTVPAVGHCDADYETARRAFDEGAGLMTHMFNAMNGLHHRKPGPIP 258
Cdd:cd00854  151 LKKWLEAAGGLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 259 AAVEDPRVTIELICDGFHVQDPMLRLGLGFAP-HRIAFVTDAMAATDCPDGAYKLGALDVDVVDGHARLkSNGAIAGSTL 337
Cdd:cd00854  231 AALSDDDVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARL-ADGTLAGSTL 309
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585136213 338 TLEHAVQRAVLELGMSPVEAIEAATLTPARAFGFDRpypvtgaPLGLLAPGYAADVLLTDPaDWSVQHAWCAG 410
Cdd:cd00854  310 TMDQAVRNMVKWGGCPLEEAVRMASLNPAKLLGLDD-------RKGSLKPGKDADLVVLDD-DLNVKATWING 374
nagA TIGR00221
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
73-411 3.23e-64

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


Pssm-ID: 272968  Cd Length: 380  Bit Score: 210.46  E-value: 3.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213   73 IDASGKIMTPGYVDIHSHGAWEKSFDDGP-DGIDVARAGHAMHGTTRQVCSLITNPIDVQCENLRNVRAKMDQRP--DIL 149
Cdd:TIGR00221  47 IDLPGNVLTPGFIDIHIHGCGGVDTNDASfETLEIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKnaQAL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  150 GAHLEGPFLALSRKGAHDPECLKDPVPEIVDRMLEAADGCLRQITIAPELPHGLQAIRSFATAGTVPAVGHCDADYETAR 229
Cdd:TIGR00221 127 GLHLEGPFLSPEKKGAHPPEYIREPDVELFKKFLCEAGGVITKVTLAPEEDQHFELIRHLKDAGIIVSAGHTNATYELAK 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  230 RAFDEGAGLMTHMFNAMNGLHHRKPGPIPAAVEDPRVTIELICDGFHVqDP----MLRLGLGFAphRIAFVTDAMAATDC 305
Cdd:TIGR00221 207 AAFKAGATHATHLYNAMSPIHHREPGVIGAVLDHDDVYTEIIADGIHI-HPlnirLAKKLKGDS--KLCLVTDSMAAAGA 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  306 PDGAYKLGALDVDVVDGHArLKSNGAIAGSTLTLEHAVQRAVLELGMSPVEAIEAATLTPARAFG-FDRpypvtgapLGL 384
Cdd:TIGR00221 284 KDGVFIFGGKTVYIREGTC-LDSNGTLAGSSLTMIEGARNLVEFTNISLTDAARMSSLNPARALGiDDR--------LGS 354
                         330       340
                  ....*....|....*....|....*..
gi 585136213  385 LAPGYAADVLLTDPaDWSVQHAWCAGR 411
Cdd:TIGR00221 355 VTVGKDANLVVFTP-DFEVILTIVNGN 380
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
34-391 1.71e-54

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 185.18  E-value: 1.71e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  34 IEEHAWIVAdaNGAIaargtsdddfEAACRANGIGTD-AVIDASGKIMTPGYVDIHSHGAWEKSFDDGPDGIDVaRAGHA 112
Cdd:PRK11170  16 LDDHAVVIA--DGLI----------EAVCPVAELPPGiEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISV-ETLEI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 113 MH------GTTRQVCSLITNPIDVQCENLRNVRAKMDQRPD-ILGAHLEGPFLALSRKGAHDPECLKDPVPEIVDRMLEA 185
Cdd:PRK11170  83 MQkaneksGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNqALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFLCEN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 186 ADgCLRQITIAPELPhGLQAIRSFATAGTVPAVGHCDADYETARRAFDEGAGLMTHMFNAMNGLHHRKPGPIPAAVEDPR 265
Cdd:PRK11170 163 AD-VITKVTLAPEMV-DAEVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 266 VTIELICDGFHVQDPMLRLGLGFAPHRIAFVTDAMAatdcPDGA-------------YKLGaLDVDvvdgharlkSNGAI 332
Cdd:PRK11170 241 VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATA----PAGAnieqfifagktiyYRDG-LCVD---------ENGTL 306
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 585136213 333 AGSTLTLEHAVQRAVLELGMSPVEAIEAATLTPARAFGFDrpypvtgAPLGLLAPGYAA 391
Cdd:PRK11170 307 SGSALTMIEAVRNLVEHVGIALDEALRMATLYPARAIGVD-------KRLGSIEAGKVA 358
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
79-398 3.74e-14

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: 72.92  E-value: 3.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213   79 IMTPGYVDIHSHGAWEKSFDDGPDGIDVARAghAMHGTTRQVCSLITNPID---VQCENLRNVRAKMDQRPDILGAHLEG 155
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYEA--LRLGITTMLKSGTTTVLDmgaTTSTGIEALLEAAEELPLGLRFLGPG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  156 PFLALSRKGAHDPECLKDPVPEIVDRMLEAADGCLRQITIAPEL---PHGLQAIRSFATAGTVPAVGHC---DADYETAR 229
Cdd:pfam01979  79 CSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLAPHGAPtfsDDELKAALEEAKKYGLPVAIHAletKGEVEDAI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  230 RAFDEGAGLMTHMFNAMNGLHHRKPGPIPAA-----VEDPRVTIELICDGF--HVQDPMLRLGLGFAPHR--------IA 294
Cdd:pfam01979 159 AAFGGGIEHGTHLEVAESGGLLDIIKLILAHgvhlsPTEANLLAEHLKGAGvaHCPFSNSKLRSGRIALRkaledgvkVG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  295 FVTDAMAATDCPdgayklgaldvdvvdgharlksNGAIAGSTLTLEHAVQRAvlelGMSPVEAIEAATLTPARAFGFDRp 374
Cdd:pfam01979 239 LGTDGAGSGNSL----------------------NMLEELRLALELQFDPEG----GLSPLEALRMATINPAKALGLDD- 291
                         330       340
                  ....*....|....*....|....
gi 585136213  375 ypvtgaPLGLLAPGYAADVLLTDP 398
Cdd:pfam01979 292 ------KVGSIEVGKDADLVVVDL 309
 
Name Accession Description Interval E-value
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
22-411 1.98e-138

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 400.24  E-value: 1.98e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  22 AIRDARKVDARGIEEHAWIVADaNGAIAARGTSDDDfeaacrangigTDAVIDASGKIMTPGYVDIHSHGAWEKSFDDG- 100
Cdd:COG1820    1 AITNARIFTGDGVLEDGALLIE-DGRIAAIGPGAEP-----------DAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGt 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 101 PDGIDVARAGHAMHGTTRQVCSLITNPIDVQCENLRNVRAKMDQR--PDILGAHLEGPFLALSRKGAHDPECLKDPVPEI 178
Cdd:COG1820   69 PEALRTIARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGggAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 179 VDRMLEAADGCLRQITIAPELPHGLQAIRSFATAGTVPAVGHCDADYETARRAFDEGAGLMTHMFNAMNGLHHRKPGPIP 258
Cdd:COG1820  149 LDRLLEAAGGLIKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 259 AAVEDPRVTIELICDGFHVQDPMLRLGLG-FAPHRIAFVTDAMAATDCPDGAYKLGALDVDVVDGHARLKsNGAIAGSTL 337
Cdd:COG1820  229 AALDDDDVYAELIADGIHVHPAAVRLALRaKGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLA-DGTLAGSTL 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585136213 338 TLEHAVQRAVLELGMSPVEAIEAATLTPARAFGFDRpypvtgaPLGLLAPGYAADVLLTDPaDWSVQHAWCAGR 411
Cdd:COG1820  308 TMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDD-------RKGSIAPGKDADLVVLDD-DLNVRATWVGGE 373
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
22-410 1.96e-137

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: 397.72  E-value: 1.96e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  22 AIRDARKVDARGIEEHAWIVADanGAIAARGTSDDDFEaacrangigTDAVIDASGKIMTPGYVDIHSHGAWEKSFDDG- 100
Cdd:cd00854    2 IIKNARILTPGGLEDGAVLVED--GKIVAIGPEDELEE---------ADEIIDLKGQYLVPGFIDIHIHGGGGADFMDGt 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 101 PDGIDVARAGHAMHGTTRQVCSLITNPIDVQCENLRNVRAKMDQ--RPDILGAHLEGPFLALSRKGAHDPECLKDPVPEI 178
Cdd:cd00854   71 AEALKTIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEgqGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 179 VDRMLEAADGCLRQITIAPELPHGLQAIRSFATAGTVPAVGHCDADYETARRAFDEGAGLMTHMFNAMNGLHHRKPGPIP 258
Cdd:cd00854  151 LKKWLEAAGGLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 259 AAVEDPRVTIELICDGFHVQDPMLRLGLGFAP-HRIAFVTDAMAATDCPDGAYKLGALDVDVVDGHARLkSNGAIAGSTL 337
Cdd:cd00854  231 AALSDDDVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARL-ADGTLAGSTL 309
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585136213 338 TLEHAVQRAVLELGMSPVEAIEAATLTPARAFGFDRpypvtgaPLGLLAPGYAADVLLTDPaDWSVQHAWCAG 410
Cdd:cd00854  310 TMDQAVRNMVKWGGCPLEEAVRMASLNPAKLLGLDD-------RKGSLKPGKDADLVVLDD-DLNVKATWING 374
nagA TIGR00221
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
73-411 3.23e-64

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


Pssm-ID: 272968  Cd Length: 380  Bit Score: 210.46  E-value: 3.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213   73 IDASGKIMTPGYVDIHSHGAWEKSFDDGP-DGIDVARAGHAMHGTTRQVCSLITNPIDVQCENLRNVRAKMDQRP--DIL 149
Cdd:TIGR00221  47 IDLPGNVLTPGFIDIHIHGCGGVDTNDASfETLEIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKnaQAL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  150 GAHLEGPFLALSRKGAHDPECLKDPVPEIVDRMLEAADGCLRQITIAPELPHGLQAIRSFATAGTVPAVGHCDADYETAR 229
Cdd:TIGR00221 127 GLHLEGPFLSPEKKGAHPPEYIREPDVELFKKFLCEAGGVITKVTLAPEEDQHFELIRHLKDAGIIVSAGHTNATYELAK 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  230 RAFDEGAGLMTHMFNAMNGLHHRKPGPIPAAVEDPRVTIELICDGFHVqDP----MLRLGLGFAphRIAFVTDAMAATDC 305
Cdd:TIGR00221 207 AAFKAGATHATHLYNAMSPIHHREPGVIGAVLDHDDVYTEIIADGIHI-HPlnirLAKKLKGDS--KLCLVTDSMAAAGA 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  306 PDGAYKLGALDVDVVDGHArLKSNGAIAGSTLTLEHAVQRAVLELGMSPVEAIEAATLTPARAFG-FDRpypvtgapLGL 384
Cdd:TIGR00221 284 KDGVFIFGGKTVYIREGTC-LDSNGTLAGSSLTMIEGARNLVEFTNISLTDAARMSSLNPARALGiDDR--------LGS 354
                         330       340
                  ....*....|....*....|....*..
gi 585136213  385 LAPGYAADVLLTDPaDWSVQHAWCAGR 411
Cdd:TIGR00221 355 VTVGKDANLVVFTP-DFEVILTIVNGN 380
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
34-391 1.71e-54

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 185.18  E-value: 1.71e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  34 IEEHAWIVAdaNGAIaargtsdddfEAACRANGIGTD-AVIDASGKIMTPGYVDIHSHGAWEKSFDDGPDGIDVaRAGHA 112
Cdd:PRK11170  16 LDDHAVVIA--DGLI----------EAVCPVAELPPGiEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISV-ETLEI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 113 MH------GTTRQVCSLITNPIDVQCENLRNVRAKMDQRPD-ILGAHLEGPFLALSRKGAHDPECLKDPVPEIVDRMLEA 185
Cdd:PRK11170  83 MQkaneksGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNqALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFLCEN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 186 ADgCLRQITIAPELPhGLQAIRSFATAGTVPAVGHCDADYETARRAFDEGAGLMTHMFNAMNGLHHRKPGPIPAAVEDPR 265
Cdd:PRK11170 163 AD-VITKVTLAPEMV-DAEVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 266 VTIELICDGFHVQDPMLRLGLGFAPHRIAFVTDAMAatdcPDGA-------------YKLGaLDVDvvdgharlkSNGAI 332
Cdd:PRK11170 241 VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATA----PAGAnieqfifagktiyYRDG-LCVD---------ENGTL 306
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 585136213 333 AGSTLTLEHAVQRAVLELGMSPVEAIEAATLTPARAFGFDrpypvtgAPLGLLAPGYAA 391
Cdd:PRK11170 307 SGSALTMIEAVRNLVEHVGIALDEALRMATLYPARAIGVD-------KRLGSIEAGKVA 358
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
79-398 3.74e-14

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: 72.92  E-value: 3.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213   79 IMTPGYVDIHSHGAWEKSFDDGPDGIDVARAghAMHGTTRQVCSLITNPID---VQCENLRNVRAKMDQRPDILGAHLEG 155
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYEA--LRLGITTMLKSGTTTVLDmgaTTSTGIEALLEAAEELPLGLRFLGPG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  156 PFLALSRKGAHDPECLKDPVPEIVDRMLEAADGCLRQITIAPEL---PHGLQAIRSFATAGTVPAVGHC---DADYETAR 229
Cdd:pfam01979  79 CSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLAPHGAPtfsDDELKAALEEAKKYGLPVAIHAletKGEVEDAI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  230 RAFDEGAGLMTHMFNAMNGLHHRKPGPIPAA-----VEDPRVTIELICDGF--HVQDPMLRLGLGFAPHR--------IA 294
Cdd:pfam01979 159 AAFGGGIEHGTHLEVAESGGLLDIIKLILAHgvhlsPTEANLLAEHLKGAGvaHCPFSNSKLRSGRIALRkaledgvkVG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  295 FVTDAMAATDCPdgayklgaldvdvvdgharlksNGAIAGSTLTLEHAVQRAvlelGMSPVEAIEAATLTPARAFGFDRp 374
Cdd:pfam01979 239 LGTDGAGSGNSL----------------------NMLEELRLALELQFDPEG----GLSPLEALRMATINPAKALGLDD- 291
                         330       340
                  ....*....|....*....|....
gi 585136213  375 ypvtgaPLGLLAPGYAADVLLTDP 398
Cdd:pfam01979 292 ------KVGSIEVGKDADLVVVDL 309
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
290-413 6.71e-14

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 73.21  E-value: 6.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 290 PHRIAFVTDamaatdcpdgayklgalDVDVVDgharLKSNGAIagstltlEHAVQRAVlELGMSPVEAIEAATLTPARAF 369
Cdd:COG1001  251 SRRCALCTD-----------------DRHPDD----LLEEGHI-------DHVVRRAI-ELGLDPVTAIQMATLNAAEHF 301
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 585136213 370 GFDRpypvtgapLGLLAPGYAAD-VLLTDPADWSVQHAWCAGRRI 413
Cdd:COG1001  302 GLKD--------LGAIAPGRRADiVLLDDLEDFKVEKVYADGKLV 338
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
17-397 4.13e-11

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 64.21  E-value: 4.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  17 APSAFAIRDARKVDARG--IEEHAWIVADaNGAIAARGTSDDDFEAAcrangigTDAVIDASGKIMTPGYVDIHSH---- 90
Cdd:COG1228    6 QAGTLLITNATLVDGTGggVIENGTVLVE-DGKIAAVGPAADLAVPA-------GAEVIDATGKTVLPGLIDAHTHlglg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  91 ----GAWEKSFDDGPDGIDVARAGHA-----MHGTTRqVCSLITNPIDVQCENLRNvRAKMDQRPDILGAhleGPFLALS 161
Cdd:COG1228   78 ggraVEFEAGGGITPTVDLVNPADKRlrralAAGVTT-VRDLPGGPLGLRDAIIAG-ESKLLPGPRVLAA---GPALSLT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 162 rKGAHD---PECLKdpvpeIVDRMLEA--------ADGCLRQITIAPelphgLQAIRSFATAGTVPAVGHCDADyETARR 230
Cdd:COG1228  153 -GGAHArgpEEARA-----ALRELLAEgadyikvfAEGGAPDFSLEE-----LRAILEAAHALGLPVAAHAHQA-DDIRL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 231 AFDEGAGLMTHmfnamnglhhrkpgpIPAAVEDprvTIELICD-GFHVQDPMLRLGLGFAPHRIAFVTDAMAATDC--PD 307
Cdd:COG1228  221 AVEAGVDSIEH---------------GTYLDDE---VADLLAEaGTVVLVPTLSLFLALLEGAAAPVAAKARKVREaaLA 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 308 GAYKLGALDVDVV---DGharlkSNGAIAGSTLTLEhaVQRAVlELGMSPVEAIEAATLTPARAFGFDrpypvtgAPLGL 384
Cdd:COG1228  283 NARRLHDAGVPVAlgtDA-----GVGVPPGRSLHRE--LALAV-EAGLTPEEALRAATINAAKALGLD-------DDVGS 347
                        410
                 ....*....|...
gi 585136213 385 LAPGYAADVLLTD 397
Cdd:COG1228  348 LEPGKLADLVLLD 360
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
23-400 1.34e-08

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: 56.54  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  23 IRDARKVDARGieeHAWIVAD---ANGAIAARGTSDddfeaacranGIGTDAVIDASGKIMTPGYVDIHSHgaweksfDD 99
Cdd:cd01297    4 IRNGTVVDGTG---APPFTADvgiRDGRIAAIGPIL----------STSAREVIDAAGLVVAPGFIDVHTH-------YD 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 100 GPDGIDVARAGHAMHGTTRQV---CSLITNPIDVQcenlrnVRAKMDQRPDILGAHLEG---------PFLALSRKGAHD 167
Cdd:cd01297   64 GQVFWDPDLRPSSRQGVTTVVlgnCGVSPAPANPD------DLARLIMLMEGLVALGEGlpwgwatfaEYLDALEARPPA 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 168 PE--CL---------------KDPVPEIVDRMLEAADGCLRQ----ITIAPELPHGLQA----IRSFATagtvpAVGHCD 222
Cdd:cd01297  138 VNvaALvghaalrravmgldaREATEEELAKMRELLREALEAgalgISTGLAYAPRLYAgtaeLVALAR-----VAARYG 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 223 ADYETARR--------AFDE--------GAGLMTHMFNAMNGLHHRKPGPIPAAVEDPRVtielicDGFHVQDPMLRLGL 286
Cdd:cd01297  213 GVYQTHVRyegdsileALDEllrlgretGRPVHISHLKSAGAPNWGKIDRLLALIEAARA------EGLQVTADVYPYGA 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 287 GFAPHRIAFVTDAmAATDCPDGayklGALDVdvvdGHARLksngaIAGSTLTLEHAV-QRAVLelgmSPVEAIEAATLTP 365
Cdd:cd01297  287 GSEDDVRRIMAHP-VVMGGSDG----GALGK----PHPRS-----YGDFTRVLGHYVrERKLL----SLEEAVRKMTGLP 348
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 585136213 366 ARAFG-FDRpypvtgaplGLLAPGYAADVLLTDPAD 400
Cdd:cd01297  349 ARVFGlADR---------GRIAPGYRADIVVFDPDT 375
AdeC cd01295
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ...
282-405 1.62e-08

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: 56.08  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 282 LRLGLGFAPHRIAFVTDamaatdcpdgayklgalDVDVVDgharLKSNGAIagstltlEHAVQRAVlELGMSPVEAIEAA 361
Cdd:cd01295  194 LPAITEKNFRRFMFCTD-----------------DVHPDD----LLSEGHL-------DYIVRRAI-EAGIPPEDAIQMA 244
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 585136213 362 TLTPARAFGFDrpypvtgaPLGLLAPGYAAD-VLLTDPADWSVQH 405
Cdd:cd01295  245 TINPAECYGLH--------DLGAIAPGRIADiVILDDLENFNITT 281
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
72-397 1.36e-06

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: 49.98  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  72 VIDASGKIMTPGYVDIHSHGAWEKS----FDDGPDGIDVARAGHAMHGTTRqvcSLITNPIDVQCENLRNVRaKMDQRPD 147
Cdd:cd01299    3 VIDLGGKTLMPGLIDAHTHLGSDPGdlplDLALPVEYRTIRATRQARAALR---AGFTTVRDAGGADYGLLR-DAIDAGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 148 ILGAHLEGPFLALSRKGAHDPEcLKDPVPEIVDRMLEAADG---CLRQitIAPELPHGLQAIRSFATAGTV---PAVGHC 221
Cdd:cd01299   79 IPGPRVFASGRALSQTGGHGDP-RGLSGLFPAGGLAAVVDGveeVRAA--VREQLRRGADQIKIMATGGVLspgDPPPDT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 222 DADYETARRAFDEgaglmTHMFNAMNGLHHRKPGPIPAAVEDPRVTIElicDGFHVQDP----MLRLGLGFAPHRI---A 294
Cdd:cd01299  156 QFSEEELRAIVDE-----AHKAGLYVAAHAYGAEAIRRAIRAGVDTIE---HGFLIDDEtielMKEKGIFLVPTLAtyeA 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 295 FVTDAMAATDCPDGAYKLGALDVDVVDGHARLKSNGA--IAGS---TLTLEHAVQRAVLEL----GMSPVEAIEAATLTP 365
Cdd:cd01299  228 LAAEGAAPGLPADSAEKVALVLEAGRDALRRAHKAGVkiAFGTdagFPVPPHGWNARELELlvkaGGTPAEALRAATANA 307
                        330       340       350
                 ....*....|....*....|....*....|..
gi 585136213 366 ARAFGFDrpypvtgAPLGLLAPGYAADVLLTD 397
Cdd:cd01299  308 AELLGLS-------DELGVIEAGKLADLLVVD 332
pyrC PRK09357
dihydroorotase; Validated
23-90 3.07e-05

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 45.96  E-value: 3.07e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585136213  23 IRDARKVDARGIEEHAWIVADaNGAIAARGTsDDDFEAacrangigtDAVIDASGKIMTPGYVDIHSH 90
Cdd:PRK09357   5 IKNGRVIDPKGLDEVADVLID-DGKIAAIGE-NIEAEG---------AEVIDATGLVVAPGLVDLHVH 61
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
23-90 4.22e-05

N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 45.55  E-value: 4.22e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 585136213  23 IRDARKVDARGieeHAWIVAD---ANGAIAARGTSDDdfEAACRangigtdaVIDASGKIMTPGYVDIHSH 90
Cdd:COG3653    6 IRGGTVVDGTG---APPFRADvaiKGGRIVAVGDLAA--AEAAR--------VIDATGLVVAPGFIDIHTH 63
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
41-118 7.44e-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: 44.56  E-value: 7.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  41 VADANGAIAARGTSDDDfeaacRANGIGTDAVIDASGKIMTPGYVDIHSHGAWEKSFDD-------GPDGIDVARAGHAM 113
Cdd:cd01296    1 IAIRDGRIAAVGPAASL-----PAPGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDefaarlaGASYEEILAAGGGI 75

                 ....*
gi 585136213 114 HGTTR 118
Cdd:cd01296   76 LSTVR 80
PRK09061 PRK09061
D-glutamate deacylase; Validated
14-91 7.84e-05

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 44.69  E-value: 7.84e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585136213  14 MEGAPSAFAIRDARKVD-ARGIEEHAwIVADANGAIAARGTsdddfeaacraNGIGTDAVIDASGKIMTPGYVDIHSHG 91
Cdd:PRK09061  14 ASMAPYDLVIRNGRVVDpETGLDAVR-DVGIKGGKIAAVGT-----------AAIEGDRTIDATGLVVAPGFIDLHAHG 80
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
23-90 9.42e-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: 44.31  E-value: 9.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585136213  23 IRDARKVDARGIEEhAWIVADaNGAIAARGTSDDDFEAacrangigtDAVIDASGKIMTPGYVDIHSH 90
Cdd:COG0044    2 IKNGRVVDPGGLER-ADVLIE-DGRIAAIGPDLAAPEA---------AEVIDATGLLVLPGLIDLHVH 58
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
23-108 1.17e-04

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 44.00  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  23 IRDARKVD-ARGIEEHAwIVADANGAIAARGTSDDDFEAAcrangigtdAVIDASGKIMTPGYVDIHSHgAWEKSFDDG- 100
Cdd:COG3964    4 IKGGRVIDpANGIDGVM-DIAIKDGKIAAVAKDIDAAEAK---------KVIDASGLYVTPGLIDLHTH-VFPGGTDYGv 72

                 ....*....
gi 585136213 101 -PDGIDVAR 108
Cdd:COG3964   73 dPDGVGVRS 81
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
23-108 1.52e-04

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 43.69  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  23 IRDARKVDARGIEEHAWIVADANGAIAARGTSDDDFEAAcrangigtdAVIDASGKIMTPGYVDIHSHgAWEKSFDDG-- 100
Cdd:PRK09237   3 LRGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDGSQAK---------KVIDLSGLYVSPGWIDLHVH-VYPGSTPYGde 72

                 ....*...
gi 585136213 101 PDGIDVAR 108
Cdd:PRK09237  73 PDEVGVRS 80
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
348-393 1.67e-04

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 43.62  E-value: 1.67e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 585136213 348 LELGMSPVEAIEAATLTPARAFGFDRpypvtgapLGLLAPGYAADV 393
Cdd:COG3964  292 LALGMPLEEVIAAVTWNPARAIGLPE--------LGTLSVGADADI 329
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
352-414 1.78e-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: 40.20  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 352 MSPVEAIEAATLTPARAFGFDrpypvtgAPLGLLAPGYAADVLLTDPADWS-------------------VQHAWCAGRR 412
Cdd:COG0402  340 LSAREALEMATLGGARALGLD-------DEIGSLEPGKRADLVVLDLDAPHlaplhdplsalvyaadgrdVRTVWVAGRV 412

                 ..
gi 585136213 413 IK 414
Cdd:COG0402  413 VV 414
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
30-90 1.86e-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: 40.20  E-value: 1.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 585136213  30 DARGIEEHAWIVADaNGAIAARGTSDDDFEAAcrangiGTDAVIDASGKIMTPGYVDIHSH 90
Cdd:COG0402   14 PAGGVLEDGAVLVE-DGRIAAVGPGAELPARY------PAAEVIDAGGKLVLPGLVNTHTH 67
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
72-413 2.18e-03

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


Pssm-ID: 238634 [Multi-domain]  Cd Length: 359  Bit Score: 39.99  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  72 VIDASGKIMTPGYVDIHSH-----GAWEKSFDDGPDGIDV----ARAGHAM----HGTTRQVCSLIT---------NPID 129
Cdd:cd01309   19 VIDAKGKHVTPGLIDAHSHlgldeEGGVRETSDANEETDPvtphVRAIDGInpddEAFKRARAGGVTtvqvlpgsaNLIG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 130 VQCENLRNVRAKMDQrpDILGAHLeGPFLALsrkGAHDPECLKDPVPEIVDRMLEAADgcLRQITI-APELPHGLQAIRS 208
Cdd:cd01309   99 GQGVVIKTDGGTIED--MFIKAPA-GLKMAL---GENPKRVYGGKGKEPATRMGVAAL--LRDAFIkAQEYGRKYDLGKN 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 209 FATAGTVPavghcDADYETARRAFDEGAGLMTHMfnamnglhHRkPGPIPAAV-----EDPRVTIELICDGFHVQDPMLR 283
Cdd:cd01309  171 AKKDPPER-----DLKLEALLPVLKGEIPVRIHA--------HR-ADDILTAIriakeFGIKITIEHGAEGYKLADELAK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 284 LGlgfaphriafvtdAMAATDCPDGAYKLGALDVDVVDGHARLKSNGAIAGStLTLEHAV---QRAVLEL------GMSP 354
Cdd:cd01309  237 HG-------------IPVIYGPTLTLPKKVEEVNDAIDTNAYLLKKGGVAFA-ISSDHPVlniRNLNLEAakavkyGLSY 302
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585136213 355 VEAIEAATLTPARAFGFDRpypvtgaPLGLLAPGYAADVLL--TDP--ADWSVQHAWCAGRRI 413
Cdd:cd01309  303 EEALKAITINPAKILGIED-------RVGSLEPGKDADLVVwnGDPlePTSKPEQVYIDGRLV 358
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
40-393 2.45e-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: 39.62  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213  40 IVADANGAIAARGtSDDDFEAACRangigtdaVIDASGKIMTPGYVDIHSHGAWE-KSFDDGPDGIDVARAghamhgttr 118
Cdd:cd01307    1 DVAIENGKIAAVG-AALAAPAATQ--------IVDAGGCYVSPGWIDLHVHVYQGgTRYGDRPDMIGVKSG--------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 119 qvcslITNPIDV---QCENLRNVRAKM--DQRPDILGahlegpFLALSRKGAHdpECLKDPVPEIVDrmleaADGCLRQI 193
Cdd:cd01307   63 -----VTTVVDAgsaGADNIDGFRYTVieRSATRVYA------FLNISRVGLV--AQDELPDPDNID-----EDAVVAAA 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 194 TIAPELPHGLQA---IRSFATAGTVPA-----------------VGHCDADYETARRAFDEGaGLMTHMFNamnglhhRK 253
Cdd:cd01307  125 REYPDVIVGLKArasKSVVGEWGIKPLelakkiakeadlplmvhIGSPPPILDEVVPLLRRG-DVLTHCFN-------GK 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 254 PGPIPAAVEDPRVTIE------LICD--------GFHVQDPMLRLGLgfAPHRIAfvtdamaatdcpdgayklgaldvdv 319
Cdd:cd01307  197 PNGIVDEEGEVLPLVRrarergVIFDvghgtasfSFRVARAAIAAGL--LPDTIS------------------------- 249
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585136213 320 VDGHARLKSNGAIAGSTLTLEhavqrAVLELGMSPVEAIEAATLTPARAFGFDRpypvtgapLGLLAPGYAADV 393
Cdd:cd01307  250 SDIHGRNRTNGPVYALATTLS-----KLLALGMPLEEVIEAVTANPARMLGLAE--------IGTLAVGYDADL 310
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
341-413 4.73e-03

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 39.01  E-value: 4.73e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 585136213 341 HAVQRAVLELGMSPVEAIEAATLTPARAFGF-DRpypvtgaplGLLAPGYAADVLLTDPADWS--VQHAWCAGRRI 413
Cdd:PRK15446 313 DAAFRLADDGGLDLPQAVALVTANPARAAGLdDR---------GEIAPGKRADLVRVRRAGGLpvVRAVWRGGRRV 379
FwdA COG1229
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
70-90 4.94e-03

Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];


Pssm-ID: 440842  Cd Length: 554  Bit Score: 39.02  E-value: 4.94e-03
                         10        20
                 ....*....|....*....|.
gi 585136213  70 DAVIDASGKIMTPGYVDIHSH 90
Cdd:COG1229   41 AKVIDASGKVVMAGGVDIHTH 61
 
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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