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Conserved domains on  [gi|1721653017|gb|QEC41835|]
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amidohydrolase family protein [Pseudobacter ginsenosidimutans]

Protein Classification

amidohydrolase( domain architecture ID 10785420)

amidohydrolase is a metal-dependent hydrolase such as 5-methylthioadenosine/S-adenosylhomocysteine deaminase, which catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 16-384 8.46e-52

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: 178.48  E-value: 8.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  16 FKADQLFTGTS---LLSGGEVLIttQQGVIEAIVPAAEA-----GEEVQELAG-ILCPGFVNAHCHLELSHMKGRIPPGS 86
Cdd:COG0402     4 IRGAWVLTMDPaggVLEDGAVLV--EDGRIAAVGPGAELparypAAEVIDAGGkLVLPGLVNTHTHLPQTLLRGLADDLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  87 GMvDFLLGVMQQ--RNFPQEEVQAAIARAETAMWDSGIVAVGDICN----TADTI--AAKSMG-RLLYrnFIETMGF--- 154
Cdd:COG0402    82 LL-DWLEEYIWPleARLDPEDVYAGALLALAEMLRSGTTTVADFYYvhpeSADALaeAAAEAGiRAVL--GRGLMDRgfp 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 155 --IPATAPQRFAFAKTVFEQFEAAMPGRNSIV--PHAPYSVSPELLQLIADF--PGNQYLSIHNQESIAETQFLKDGTGg 228
Cdd:COG0402   159 dgLREDADEGLADSERLIERWHGAADGRIRVAlaPHAPYTVSPELLRAAAALarELGLPLHTHLAETRDEVEWVLELYG- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 229 MR---RLYDFlgidlsfyrpsGLSSPQLmlppfsqqqqmVLVHDVHTEASDLQWMQE-EAlpalFFCLCPNANLYIGNGL 304
Cdd:COG0402   238 KRpveYLDEL-----------GLLGPRT-----------LLAHCVHLTDEEIALLAEtGA----SVAHCPTSNLKLGSGI 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 305 PDIELLRMQGANIVLGTDSLSSNQQLSILEEVKT------IASEFPD-IPTAELLQWGTFNGAKALGFEAQFGSFEKGKQ 377
Cdd:COG0402   292 APVPRLLAAGVRVGLGTDGAASNNSLDMFEEMRLaallqrLRGGDPTaLSAREALEMATLGGARALGLDDEIGSLEPGKR 371


                  ....*..
gi 1721653017 378 PGIVLID 384
Cdd:COG0402   372 ADLVVLD 378
 
Name Accession Description Interval E-value
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 16-384 8.46e-52

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: 178.48  E-value: 8.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  16 FKADQLFTGTS---LLSGGEVLIttQQGVIEAIVPAAEA-----GEEVQELAG-ILCPGFVNAHCHLELSHMKGRIPPGS 86
Cdd:COG0402     4 IRGAWVLTMDPaggVLEDGAVLV--EDGRIAAVGPGAELparypAAEVIDAGGkLVLPGLVNTHTHLPQTLLRGLADDLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  87 GMvDFLLGVMQQ--RNFPQEEVQAAIARAETAMWDSGIVAVGDICN----TADTI--AAKSMG-RLLYrnFIETMGF--- 154
Cdd:COG0402    82 LL-DWLEEYIWPleARLDPEDVYAGALLALAEMLRSGTTTVADFYYvhpeSADALaeAAAEAGiRAVL--GRGLMDRgfp 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 155 --IPATAPQRFAFAKTVFEQFEAAMPGRNSIV--PHAPYSVSPELLQLIADF--PGNQYLSIHNQESIAETQFLKDGTGg 228
Cdd:COG0402   159 dgLREDADEGLADSERLIERWHGAADGRIRVAlaPHAPYTVSPELLRAAAALarELGLPLHTHLAETRDEVEWVLELYG- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 229 MR---RLYDFlgidlsfyrpsGLSSPQLmlppfsqqqqmVLVHDVHTEASDLQWMQE-EAlpalFFCLCPNANLYIGNGL 304
Cdd:COG0402   238 KRpveYLDEL-----------GLLGPRT-----------LLAHCVHLTDEEIALLAEtGA----SVAHCPTSNLKLGSGI 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 305 PDIELLRMQGANIVLGTDSLSSNQQLSILEEVKT------IASEFPD-IPTAELLQWGTFNGAKALGFEAQFGSFEKGKQ 377
Cdd:COG0402   292 APVPRLLAAGVRVGLGTDGAASNNSLDMFEEMRLaallqrLRGGDPTaLSAREALEMATLGGARALGLDDEIGSLEPGKR 371


                  ....*..
gi 1721653017 378 PGIVLID 384
Cdd:COG0402   372 ADLVVLD 378
Met_dep_hydrolase_D cd01312
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 60-395 1.00e-43

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


Pssm-ID: 238637 [Multi-domain]  Cd Length: 381  Bit Score: 156.07  E-value: 1.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  60 GILCPGFVNAHCHLELSHMKGRIPPGSgMVDFLLGVMQQRNFPQ-EEVQAAIARAETAMWDSGIVAVGDICN--TADTIA 136
Cdd:cd01312    27 GVLLPGLINAHTHLEFSANVAQFTYGR-FRAWLLSVINSRDELLkQPWEEAIRQGIRQMLESGTTSIGAISSdgSLLPAL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 137 AKSMGRLLYrnFIETMGfipaTAPQRFAF-AKTVFEQFEAAMPGRNS-----IVPHAPYSVSPELLQLIADFPG--NQYL 208
Cdd:cd01312   106 ASSGLRGVF--FNEVIG----SNPSAIDFkGETFLERFKRSKSFESQlfipaISPHAPYSVHPELAQDLIDLAKklNLPL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 209 SIHNQESIAETQFLKDGTGGMRRLYD-FLGIDlsfyRPSGLSSPQLMLPPFSQQQQMV-LVHDVHTEASDLQWMQEEALp 286
Cdd:cd01312   180 STHFLESKEEREWLEESKGWFKHFWEsFLKLP----KPKKLATAIDFLDMLGGLGTRVsFVHCVYANLEEAEILASRGA- 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 287 alFFCLCPNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNQQLSILEEVKTIASEFPDIP----TAELLQWGTFNGAKA 362
Cdd:cd01312   255 --SIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDGLSSNISLSLLDELRALLDLHPEEDllelASELLLMATLGGARA 332

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1721653017 363 LGFEAqfGSFEKGKQPGIVLIDNAGDSFEKSSA 395
Cdd:cd01312   333 LGLNN--GEIEAGKRADFAVFELPGPGIKEQAP 363
PRK08418 PRK08418
metal-dependent hydrolase;
60-384 9.09e-34

metal-dependent hydrolase;


Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 130.09  E-value: 9.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  60 GILCPGFVNAHCHLELSHMKGRIPPGSGMVdFLLGVMQQRNFPQEEVQ-AAIARAETAMWDSGIVAVGDICNTAD--TIA 136
Cdd:PRK08418   54 SVLLPAFINPHTHLEFSANKTTLDYGDFIP-WLGSVINHREDLLEKCKgALIQQAINEMLKSGVGTIGAISSFGIdlEIC 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 137 AKSMGRLLYrnFIETMGFIPATAPQRFAFAKTVFEQ---FEAAM--PGrnsIVPHAPYSVSPELLQLIADFPGNQYL--S 209
Cdd:PRK08418  133 AKSPLRVVF--FNEILGSNASAVDELYQDFLARFEEskkFKSKKfiPA---IAIHSPYSVHPILAKKALQLAKKENLlvS 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 210 IHNQESIAETQFLKDGTGGMRRLYD-FLGIdlsfyrPSGLSSPQLMLPPFSQQQQMvLVHDVHTEASDLQWMQEealpaL 288
Cdd:PRK08418  208 THFLESKAEREWLEESKGWFKKFFEkFLKE------PKPLYTPKEFLELFKGLRTL-FTHCVYASEEELEKIKS-----K 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 289 FFCL--CPNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNQQLSILEEVKT---IASEFPDIPTA-ELLQWGTFNGAKA 362
Cdd:PRK08418  276 NASIthCPFSNRLLSNKALDLEKAKKAGINYSIATDGLSSNISLSLLDELRAallTHANMPLLELAkILLLSATRYGAKA 355

                         330       340
                  ....*....|....*....|..
gi 1721653017 363 LGFEAqfGSFEKGKQPGIVLID 384
Cdd:PRK08418  356 LGLNN--GEIKEGKDADLSVFE 375
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 61-384 7.95e-27

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: 109.51  E-value: 7.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  61 ILCPGFVNAHCHLELSHMKGRippgsgmvdfllgvmqqrNFPQEEVQAAIARAETAMWDSGIVAVGDICNTADT---IAA 137
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGI------------------PVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTgieALL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 138 KSMGRLLYRNFIETMGFIPATaPQRFAFAKTVFEQFEAAM-------PGRNSIV--PHAPYSVSPELLQLI---ADFPGN 205
Cdd:pfam01979  63 EAAEELPLGLRFLGPGCSLDT-DGELEGRKALREKLKAGAefikgmaDGVVFVGlaPHGAPTFSDDELKAAleeAKKYGL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 206 QyLSIHNQESIAETQFLKDGTGGMRRLYDFLgidlsfyrpSGLSSPQLMLPpfsqqQQMVLVHDVHTEASDLQWMqEEAL 285
Cdd:pfam01979 142 P-VAIHALETKGEVEDAIAAFGGGIEHGTHL---------EVAESGGLLDI-----IKLILAHGVHLSPTEANLL-AEHL 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 286 PALFFCLCPNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNQQLSILEE----VKTIASEFPDIPTAELLQWGTFNGAK 361
Cdd:pfam01979 206 KGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEElrlaLELQFDPEGGLSPLEALRMATINPAK 285

                         330       340
                  ....*....|....*....|...
gi 1721653017 362 ALGFEAQFGSFEKGKQPGIVLID 384
Cdd:pfam01979 286 ALGLDDKVGSIEVGKDADLVVVD 308
 
Name Accession Description Interval E-value
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 16-384 8.46e-52

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: 178.48  E-value: 8.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  16 FKADQLFTGTS---LLSGGEVLIttQQGVIEAIVPAAEA-----GEEVQELAG-ILCPGFVNAHCHLELSHMKGRIPPGS 86
Cdd:COG0402     4 IRGAWVLTMDPaggVLEDGAVLV--EDGRIAAVGPGAELparypAAEVIDAGGkLVLPGLVNTHTHLPQTLLRGLADDLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  87 GMvDFLLGVMQQ--RNFPQEEVQAAIARAETAMWDSGIVAVGDICN----TADTI--AAKSMG-RLLYrnFIETMGF--- 154
Cdd:COG0402    82 LL-DWLEEYIWPleARLDPEDVYAGALLALAEMLRSGTTTVADFYYvhpeSADALaeAAAEAGiRAVL--GRGLMDRgfp 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 155 --IPATAPQRFAFAKTVFEQFEAAMPGRNSIV--PHAPYSVSPELLQLIADF--PGNQYLSIHNQESIAETQFLKDGTGg 228
Cdd:COG0402   159 dgLREDADEGLADSERLIERWHGAADGRIRVAlaPHAPYTVSPELLRAAAALarELGLPLHTHLAETRDEVEWVLELYG- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 229 MR---RLYDFlgidlsfyrpsGLSSPQLmlppfsqqqqmVLVHDVHTEASDLQWMQE-EAlpalFFCLCPNANLYIGNGL 304
Cdd:COG0402   238 KRpveYLDEL-----------GLLGPRT-----------LLAHCVHLTDEEIALLAEtGA----SVAHCPTSNLKLGSGI 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 305 PDIELLRMQGANIVLGTDSLSSNQQLSILEEVKT------IASEFPD-IPTAELLQWGTFNGAKALGFEAQFGSFEKGKQ 377
Cdd:COG0402   292 APVPRLLAAGVRVGLGTDGAASNNSLDMFEEMRLaallqrLRGGDPTaLSAREALEMATLGGARALGLDDEIGSLEPGKR 371


                  ....*..
gi 1721653017 378 PGIVLID 384
Cdd:COG0402   372 ADLVVLD 378
Met_dep_hydrolase_D cd01312
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 60-395 1.00e-43

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


Pssm-ID: 238637 [Multi-domain]  Cd Length: 381  Bit Score: 156.07  E-value: 1.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  60 GILCPGFVNAHCHLELSHMKGRIPPGSgMVDFLLGVMQQRNFPQ-EEVQAAIARAETAMWDSGIVAVGDICN--TADTIA 136
Cdd:cd01312    27 GVLLPGLINAHTHLEFSANVAQFTYGR-FRAWLLSVINSRDELLkQPWEEAIRQGIRQMLESGTTSIGAISSdgSLLPAL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 137 AKSMGRLLYrnFIETMGfipaTAPQRFAF-AKTVFEQFEAAMPGRNS-----IVPHAPYSVSPELLQLIADFPG--NQYL 208
Cdd:cd01312   106 ASSGLRGVF--FNEVIG----SNPSAIDFkGETFLERFKRSKSFESQlfipaISPHAPYSVHPELAQDLIDLAKklNLPL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 209 SIHNQESIAETQFLKDGTGGMRRLYD-FLGIDlsfyRPSGLSSPQLMLPPFSQQQQMV-LVHDVHTEASDLQWMQEEALp 286
Cdd:cd01312   180 STHFLESKEEREWLEESKGWFKHFWEsFLKLP----KPKKLATAIDFLDMLGGLGTRVsFVHCVYANLEEAEILASRGA- 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 287 alFFCLCPNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNQQLSILEEVKTIASEFPDIP----TAELLQWGTFNGAKA 362
Cdd:cd01312   255 --SIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDGLSSNISLSLLDELRALLDLHPEEDllelASELLLMATLGGARA 332

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1721653017 363 LGFEAqfGSFEKGKQPGIVLIDNAGDSFEKSSA 395
Cdd:cd01312   333 LGLNN--GEIEAGKRADFAVFELPGPGIKEQAP 363
PRK08418 PRK08418
metal-dependent hydrolase;
60-384 9.09e-34

metal-dependent hydrolase;


Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 130.09  E-value: 9.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  60 GILCPGFVNAHCHLELSHMKGRIPPGSGMVdFLLGVMQQRNFPQEEVQ-AAIARAETAMWDSGIVAVGDICNTAD--TIA 136
Cdd:PRK08418   54 SVLLPAFINPHTHLEFSANKTTLDYGDFIP-WLGSVINHREDLLEKCKgALIQQAINEMLKSGVGTIGAISSFGIdlEIC 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 137 AKSMGRLLYrnFIETMGFIPATAPQRFAFAKTVFEQ---FEAAM--PGrnsIVPHAPYSVSPELLQLIADFPGNQYL--S 209
Cdd:PRK08418  133 AKSPLRVVF--FNEILGSNASAVDELYQDFLARFEEskkFKSKKfiPA---IAIHSPYSVHPILAKKALQLAKKENLlvS 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 210 IHNQESIAETQFLKDGTGGMRRLYD-FLGIdlsfyrPSGLSSPQLMLPPFSQQQQMvLVHDVHTEASDLQWMQEealpaL 288
Cdd:PRK08418  208 THFLESKAEREWLEESKGWFKKFFEkFLKE------PKPLYTPKEFLELFKGLRTL-FTHCVYASEEELEKIKS-----K 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 289 FFCL--CPNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNQQLSILEEVKT---IASEFPDIPTA-ELLQWGTFNGAKA 362
Cdd:PRK08418  276 NASIthCPFSNRLLSNKALDLEKAKKAGINYSIATDGLSSNISLSLLDELRAallTHANMPLLELAkILLLSATRYGAKA 355

                         330       340
                  ....*....|....*....|..
gi 1721653017 363 LGFEAqfGSFEKGKQPGIVLID 384
Cdd:PRK08418  356 LGLNN--GEIKEGKDADLSVFE 375
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 28-384 7.89e-30

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


Pssm-ID: 238623 [Multi-domain]  Cd Length: 411  Bit Score: 119.23  E-value: 7.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  28 LSGGEVLIttQQGVIEAIVPAAEA----GEEVQELAG-ILCPGFVNAHCHLELSHMKGrIPPGSGMVDFLLGVMQ--QRN 100
Cdd:cd01298    17 LEDGDVLV--EDGRIVAVGPALPLpaypADEVIDAKGkVVMPGLVNTHTHLAMTLLRG-LADDLPLMEWLKDLIWplERL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 101 FPQEEVQAA--IARAEtaMWDSGIVAVGDICNTADTIAAKSMGRL-----LYRNFIETMGFIPATAPQRFAFAKTVFEQF 173
Cdd:cd01298    94 LTEEDVYLGalLALAE--MIRSGTTTFADMYFFYPDAVAEAAEELgiravLGRGIMDLGTEDVEETEEALAEAERLIREW 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 174 EAAMPGRNSIV--PHAPYSVSPELLQLIADFpGNQY---LSIHNQESIAETQFLKDGTGgmRRLYDFLGiDLsfyrpsGL 248
Cdd:cd01298   172 HGAADGRIRVAlaPHAPYTCSDELLREVAEL-AREYgvpLHIHLAETEDEVEESLEKYG--KRPVEYLE-EL------GL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 249 SSPQLmlppfsqqqqmVLVHDVHTEASDLQWMqeeALPALFFCLCPNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNQ 328
Cdd:cd01298   242 LGPDV-----------VLAHCVWLTDEEIELL---AETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDGAASNN 307

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721653017 329 QLSILEEVKTIA----SEFPD---IPTAELLQWGTFNGAKALGFEaQFGSFEKGKQPGIVLID 384
Cdd:cd01298   308 NLDMFEEMRLAAllqkLAHGDptaLPAEEALEMATIGGAKALGLD-EIGSLEVGKKADLILID 369
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 61-384 7.95e-27

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: 109.51  E-value: 7.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  61 ILCPGFVNAHCHLELSHMKGRippgsgmvdfllgvmqqrNFPQEEVQAAIARAETAMWDSGIVAVGDICNTADT---IAA 137
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGI------------------PVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTgieALL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 138 KSMGRLLYRNFIETMGFIPATaPQRFAFAKTVFEQFEAAM-------PGRNSIV--PHAPYSVSPELLQLI---ADFPGN 205
Cdd:pfam01979  63 EAAEELPLGLRFLGPGCSLDT-DGELEGRKALREKLKAGAefikgmaDGVVFVGlaPHGAPTFSDDELKAAleeAKKYGL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 206 QyLSIHNQESIAETQFLKDGTGGMRRLYDFLgidlsfyrpSGLSSPQLMLPpfsqqQQMVLVHDVHTEASDLQWMqEEAL 285
Cdd:pfam01979 142 P-VAIHALETKGEVEDAIAAFGGGIEHGTHL---------EVAESGGLLDI-----IKLILAHGVHLSPTEANLL-AEHL 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 286 PALFFCLCPNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNQQLSILEE----VKTIASEFPDIPTAELLQWGTFNGAK 361
Cdd:pfam01979 206 KGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEElrlaLELQFDPEGGLSPLEALRMATINPAK 285

                         330       340
                  ....*....|....*....|...
gi 1721653017 362 ALGFEAQFGSFEKGKQPGIVLID 384
Cdd:pfam01979 286 ALGLDDKVGSIEVGKDADLVVVD 308
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
38-384 2.95e-24

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 103.84  E-value: 2.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  38 QQGVIEAIVPAAEA-----GEEVQELAG-ILCPGFVNAHCHLELSHMKGrippgsgMVDFLlgvmqqrnfPQEE-VQAAI 110
Cdd:PRK09045   34 RDGRIVAILPRAEAraryaAAETVELPDhVLIPGLINAHTHAAMSLLRG-------LADDL---------PLMTwLQDHI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 111 ARAETAMWDSGIVAVGdicntadTIAAksMGRLLyRNFIET---MGFIPATAPQRF------------------AFAKTV 169
Cdd:PRK09045   98 WPAEGAWVSEEFVRDG-------TLLA--IAEML-RGGTTCfndMYFFPEAAAEAAhqagmraqigmpvldfptAWASDA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 170 FEQFEAAMPGRN----------SIVPHAPYSVSPELLQLIADFPGNQYLSIHN---------QESIAETqflkdgtgGMR 230
Cdd:PRK09045  168 DEYLAKGLELHDqwrhhplistAFAPHAPYTVSDENLERIRTLAEQLDLPIHIhlhetaqeiADSLKQH--------GQR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 231 ---RLYDFlgidlsfyrpsGLSSPQLmlppfsqqqqmVLVHDVHTEASDLQWMQEEALPALFfclCPNANLYIGNGLPDI 307
Cdd:PRK09045  240 plaRLARL-----------GLLGPRL-----------IAVHMTQLTDAEIALLAETGCSVVH---CPESNLKLASGFCPV 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 308 ELLRMQGANIVLGTDSLSSNQQLSILEEVKTIA------SEFPD-IPTAELLQWGTFNGAKALGFEAQFGSFEKGKQPGI 380
Cdd:PRK09045  295 AKLLQAGVNVALGTDGAASNNDLDLFGEMRTAAllakavAGDATaLPAHTALRMATLNGARALGLDDEIGSLEPGKQADL 374


                  ....
gi 1721653017 381 VLID 384
Cdd:PRK09045  375 VAVD 378
PRK06687 PRK06687
TRZ/ATZ family protein;
50-387 2.48e-15

TRZ/ATZ family protein;


Pssm-ID: 180657 [Multi-domain]  Cd Length: 419  Bit Score: 76.97  E-value: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  50 EAGEEVQELAGI-LCPGFVNAHCHLELSHMKGrIPPGSGMVDFLLGVM--QQRNFPQEEVQAAIARAETAMWDSGIVAVG 126
Cdd:PRK06687   43 EQAEQIIDYQGAwIMPGLVNCHTHSAMTGLRG-IRDDSNLHEWLNDYIwpAESEFTPDMTTNAVKEALTEMLQSGTTTFN 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 127 DICN----TADTI--AAKSMGRLLYrnFIETMGFIPA-TAPQRFAFAKTVFEQFeAAMPGRN---SIVPHAPYSVSPELL 196
Cdd:PRK06687  122 DMYNpngvDIQQIyqVVKTSKMRCY--FSPTLFSSETeTTAETISRTRSIIDEI-LKYKNPNfkvMVAPHSPYSCSRDLL 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 197 QLIADFPGNQYLSIHNQesIAETQflkdgtggmrrlyDFLGIDLSFY--RPSGLSSPQLMLppfsqQQQMVLVHDVHTEA 274
Cdd:PRK06687  199 EASLEMAKELNIPLHVH--VAETK-------------EESGIILKRYgkRPLAFLEELGYL-----DHPSVFAHGVELNE 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 275 SDLQWMqeeALPALFFCLCPNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNQQLSILEEVKTIA----------SEFP 344
Cdd:PRK06687  259 REIERL---ASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDSVASNNNLDMFEEGRTAAllqkmksgdaSQFP 335

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1721653017 345 dIPTAelLQWGTFNGAKALGFEAQFGSFEKGKQPGIVLIDNAG 387
Cdd:PRK06687  336 -IETA--LKVLTIEGAKALGMENQIGSLEVGKQADFLVIQPQG 375
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
 50-384 1.46e-13

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 71.76  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  50 EAGEEVQELAG-ILCPGFVNAHCHLELSHMKG---RIPPGSGMVDFLLGVmqQRNFPQEEVQAAIARAETAMWDSGIVAV 125
Cdd:PRK08393   39 KPADTVIDASGsVVSPGFINAHTHSPMVLLRGladDVPLMEWLQNYIWPR--ERKLKRKDIYWGAYLGLLEMIKSGTTTF 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 126 GDICNTADTIAaKSMGRLLYRNFIeTMGFIPATAPQRFAFAKTVFEQFEAAMPGRNS------IVPHAPYSVSPELLQLI 199
Cdd:PRK08393  117 VDMYFHMEEVA-KATLEVGLRGYL-SYGMVDLGDEEKREKEIKETEKLMEFIEKLNSprvhfvFGPHAPYTCSLALLKWV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 200 ADFPG--NQYLSIHnqesIAETqflKDGTGGMRRLYdflgidlsfyrpsGLSSPQLMLPPFSQQQQMVLVHDVHTEASDL 277
Cdd:PRK08393  195 REKARewNKLITIH----LSET---MDEIKQIREKY-------------GKSPVVLLDEIGFLNEDVIAAHGVWLSSRDI 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 278 QWMQEEALPALFfclCPNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNQQLSILEEVK------TIASEFPDIPTAE- 350
Cdd:PRK08393  255 RILASAGVTVAH---NPASNMKLGSGVMPLRKLLNAGVNVALGTDGAASNNNLDMLREMKlaallhKVHNLDPTIADAEt 331

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1721653017 351 LLQWGTFNGAKALGFEAqfGSFEKGKQPGIVLID 384
Cdd:PRK08393  332 VFRMATQNGAKALGLKA--GVIKEGYLADIAVID 363
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 28-384 1.46e-13

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 71.70  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  28 LSGGEVLIttQQGVIEAIVPAAE--AGEEVQELAGILCPGFVNAHCHLELSHMKG---RIPPGSGMVDFLLGVMQQRNfp 102
Cdd:PRK06038   19 LKKGSVVI--EDGTITEVSESTPgdADTVIDAKGSVVMPGLVNTHTHAAMTLFRGyadDLPLAEWLNDHIWPAEAKLT-- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 103 QEEVQAAIARAETAMWDSGIVAVGD----ICNTADTIAAKSMGRLLYRNFIETmgFIPATAPQRFAFAKTVFEQFEAAMP 178
Cdd:PRK06038   95 AEDVYAGSLLACLEMIKSGTTSFADmyfyMDEVAKAVEESGLRAALSYGMIDL--GDDEKGEAELKEGKRFVKEWHGAAD 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 179 GRNSIV--PHAPYSVSPELLQLIADFPGNQYLSIHNQESIAETQFLKdgtggMRRLYDFLGI----DLSFYRPSGLSSpq 252
Cdd:PRK06038  173 GRIKVMygPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQ-----MKEQYGMCSVnyldDIGFLGPDVLAA-- 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 253 lmlppfsqqqqmvlvHDVHTEASDLQWMQEEALPALFfclCPNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNQQLSI 332
Cdd:PRK06038  246 ---------------HCVWLSDGDIEILRERGVNVSH---NPVSNMKLASGIAPVPKLLERGVNVSLGTDGCASNNNLDM 307

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1721653017 333 LEEVKTIA------SEFPD-IPTAELLQWGTFNGAKALGFEAqfGSFEKGKQPGIVLID 384
Cdd:PRK06038  308 FEEMKTAAllhkvnTMDPTaLPARQVLEMATVNGAKALGINT--GMLKEGYLADIIIVD 364
PRK15493 PRK15493
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
53-386 6.21e-13

bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;


Pssm-ID: 185390 [Multi-domain]  Cd Length: 435  Bit Score: 69.70  E-value: 6.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  53 EEVQELAG-ILCPGFVNAHCHLELSHMKGripPGSGMVdfLLGVMQQRNFPQEEV---QAAIARAETA---MWDSGIVAV 125
Cdd:PRK15493   47 DEVIDMKGkWVLPGLVNTHTHVVMSLLRG---IGDDML--LQPWLETRIWPLESQftpELAVASTELGlleMVKSGTTSF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 126 GDICNTADTIAAKSMgrllyrNFIETMGFIPATAPQRFAFA-----KTVFEQFEAAMPG--------RNSIVPHAPYSVS 192
Cdd:PRK15493  122 SDMFNPIGVDQDAIM------ETVSRSGMRAAVSRTLFSFGtkedeKKAIEEAEKYVKRyynesgmlTTMVAPHSPYTCS 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 193 PELLQLIADFP--GNQYLSIHNQESIAETQFLKDGTGgmRRLYDFLGIDLSFYRPSGLSSPQLMlppFSQQQQMVLVHDV 270
Cdd:PRK15493  196 TELLEECARIAveNQTMVHIHLSETEREVRDIEAQYG--KRPVEYAASCGLFKRPTVIAHGVVL---NDNERAFLAEHDV 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 271 HTEASdlqwmqeealpalffclcPNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNQQLSILEEV-------KTIASEF 343
Cdd:PRK15493  271 RVAHN------------------PNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEEMriatllqKGIHQDA 332

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1721653017 344 PDIPTAELLQWGTFNGAKALGFEaQFGSFEKGKQPGIVLIDNA 386
Cdd:PRK15493  333 TALPVETALTLATKGAAEVIGMK-QTGSLEVGKCADFITIDPS 374
Met_dep_hydrolase_E cd01313
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 34-399 6.95e-13

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


Pssm-ID: 238638 [Multi-domain]  Cd Length: 418  Bit Score: 69.79  E-value: 6.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  34 LITTQQGVIEAIVPAAeAGEEVQELAGILCPGFVNAHCHLELSHMKGRI---PPGSG--------MVDFLLGVMQqrnfp 102
Cdd:cd01313    13 IEVDADGRIAAVNPDT-ATEAVALLGGALLPGMPNLHSHAFQRAMAGLTeyrGSAADsfwtwrelMYRFAARLTP----- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 103 qEEVQAAIARAETAMWDSGIVAVGDI------------CNTAD----TIAAKS---MGRLLYRNFIETMGF-IPATAPQR 162
Cdd:cd01313    87 -EQIEAIARQLYIEMLLAGITAVGEFhyvhhdpdgtpyADPAElaqrVIAAASdagIGITLLPVLYARAGFgGPAPNPGQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 163 FAFAKTVFEQFE------AAMPGRNSIV----PHAPYSVSPELLQLIADFPGNQY-LSIHNQESIAETQFLKDGTGGmrr 231
Cdd:cd01313   166 RRFINGYEDFLGllekalRAVKEHAAARigvaPHSLRAVPAEQLAALAALASEKApVHIHLAEQPKEVDDCLAAHGR--- 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 232 lydflgidlsfyRPSglsspQLMLPPFSQQQQMVLVHDVHTEASDLQWMQEEALPAlffCLCPNANLYIGNGLPDIELLR 311
Cdd:cd01313   243 ------------RPV-----ELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVV---GLCPTTEANLGDGIFPAAALL 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 312 MQGANIVLGTDslsSNQQLSILEEVK--------------TIASEFPDIPtAELLQWGTFNGAKALGFEAqfGSFEKGKQ 377
Cdd:cd01313   303 AAGGRIGIGSD---SNARIDLLEELRqleysqrlrdrarnVLATAGGSSA-RALLDAALAGGAQALGLAT--GALEAGAR 376

                         410       420
                  ....*....|....*....|..
gi 1721653017 378 PGIVLIDNAGDSFEKSSAKRIL 399
Cdd:cd01313   377 ADLLSLDLDHPSLAGALPDTLL 398
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
31-384 1.06e-11

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 66.18  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  31 GEVLIttQQGVIEAIVPAAEAGE--EVQELAG-ILCPGFVNAHCH------------LEL-SHMKGRIPPGSGMVD---- 90
Cdd:PRK07228   22 GDVLI--EDDRIAAVGDRLDLEDydDHIDATGkVVIPGLIQGHIHlcqtlfrgiaddLELlDWLKDRIWPLEAAHDaesm 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  91 ---FLLGVMQqrnFPQEEVQAAI--------ARAETAMWDSGIVAVGDIC--------------NTADTIAA-------- 137
Cdd:PRK07228  100 yysALLGIGE---LIESGTTTIVdmesvhhtDSAFEAAGESGIRAVLGKVmmdygddvpeglqeDTEASLAEsvrllekw 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 138 --KSMGRLLYrnfietmgfipATAPqRFAFaktvfeqfeaampgrnsivphapySVSPELLQLIADFPGNQYLSIHNQ-- 213
Cdd:PRK07228  177 hgADNGRIRY-----------AFTP-RFAV------------------------SCTEELLRGVRDLADEYGVRIHTHas 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 214 ESIAETQFLKDGTGgMRrlydflgiDLSFYRPSGLSSPQLmlppfsqqqqmVLVHDVHTEASDLQWMQEEALPAlffCLC 293
Cdd:PRK07228  221 ENRGEIETVEEETG-MR--------NIHYLDEVGLTGEDL-----------ILAHCVWLDEEEREILAETGTHV---THC 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 294 PNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNQQLSILEEVKTIAS-EFPD------IPTAELLQWGTFNGAKALGFE 366
Cdd:PRK07228  278 PSSNLKLASGIAPVPDLLERGINVALGADGAPCNNTLDPFTEMRQAALiQKVDrlgptaMPARTVFEMATLGGAKAAGFE 357

                         410
                  ....*....|....*...
gi 1721653017 367 AQFGSFEKGKQPGIVLID 384
Cdd:PRK07228  358 DEIGSLEEGKKADLAILD 375
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 16-391 2.40e-11

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 64.60  E-value: 2.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  16 FKADQLFTGTS--LLSGGEVLIttQQGVIEAIVPAAE----AGEEVQELAG-ILCPGFVNAHCHLELShmkgrippGSGM 88
Cdd:COG1228    12 ITNATLVDGTGggVIENGTVLV--EDGKIAAVGPAADlavpAGAEVIDATGkTVLPGLIDAHTHLGLG--------GGRA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  89 VDFLLGvmQQRNFPQEEVQAAIARAETAMwDSGIVAV-----GDICNTADTIAAKSM---GRLLYRN--FIE-TMGFIPA 157
Cdd:COG1228    82 VEFEAG--GGITPTVDLVNPADKRLRRAL-AAGVTTVrdlpgGPLGLRDAIIAGESKllpGPRVLAAgpALSlTGGAHAR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 158 TAPQRFAFAKTVFEQ---FEAAMPGRNSIVPhapysvSPELLQLIAD--FPGNQYLSIHnqesiAetqflkDGTGGMRRL 232
Cdd:COG1228   159 GPEEARAALRELLAEgadYIKVFAEGGAPDF------SLEELRAILEaaHALGLPVAAH-----A------HQADDIRLA 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 233 YDFlGIDlsfyrpsglsspqlmlppfsqqqqmVLVHDVHTEASDLQWMQEE----ALPALFFCLC----------PNANL 298
Cdd:COG1228   222 VEA-GVD-------------------------SIEHGTYLDDEVADLLAEAgtvvLVPTLSLFLAllegaaapvaAKARK 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 299 YIGNGLPDIELLRMQGANIVLGTDSLSSNQQ-LSILEEVKtIASEFpDIPTAELLQWGTFNGAKALGFEAQFGSFEKGKQ 377
Cdd:COG1228   276 VREAALANARRLHDAGVPVALGTDAGVGVPPgRSLHRELA-LAVEA-GLTPEEALRAATINAAKALGLDDDVGSLEPGKL 353

                         410
                  ....*....|....
gi 1721653017 378 PGIVLIDnaGDSFE 391
Cdd:COG1228   354 ADLVLLD--GDPLE 365
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 40-389 8.23e-11

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


Pssm-ID: 238628 [Multi-domain]  Cd Length: 429  Bit Score: 63.07  E-value: 8.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  40 GVIEAIVPAAEAGEEVQELAG-ILCPGFVNAHCHLELSHMKGrIPPGSGMVDFLlgvmQQRNFPQEEVQAAIARAE---- 114
Cdd:cd01303    40 GAAETLKRAAKPGARVIDSPNqFILPGFIDTHIHAPQYANIG-SGLGEPLLDWL----ETYTFPEEAKFADPAYARevyg 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 115 ------------TAMWDSGI-----VAVGDICNTAD--TIAAK-SMGRLLYRNFIETmgfipatAPQRFAFAKTVFEQfe 174
Cdd:cd01303   115 rfldellrngttTACYFATIhpestEALFEEAAKRGqrAIAGKvCMDRNAPEYYRDT-------AESSYRDTKRLIER-- 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 175 aaMPGRNSIVPH------APySVSPELL----QLIADFPGnqylsIHNQESIAETqflKDGTGGMRRLYDFLGIDLSFYR 244
Cdd:cd01303   186 --WHGKSGRVKPaitprfAP-SCSEELLaalgKLAKEHPD-----LHIQTHISEN---LDEIAWVKELFPGARDYLDVYD 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 245 PSGLSSPQlmlppfsqqqqMVLVHDVHTEASDLQWMQEEALPALFfclCPNANLYIGNGLPDIELLRMQGANIVLGTDsL 324
Cdd:cd01303   255 KYGLLTEK-----------TVLAHCVHLSEEEFNLLKERGASVAH---CPTSNLFLGSGLFDVRKLLDAGIKVGLGTD-V 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721653017 325 SSNQQLSILEE----VKTIAS-EFP-----DIPTAELLQWGTFNGAKALGFEAQFGSFEKGKQPGIVLIDNAGDS 389
Cdd:cd01303   320 GGGTSFSMLDTlrqaYKVSRLlGYElgghaKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATP 394
PRK12393 PRK12393
amidohydrolase; Provisional
 35-384 4.36e-10

amidohydrolase; Provisional


Pssm-ID: 237088 [Multi-domain]  Cd Length: 457  Bit Score: 61.24  E-value: 4.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  35 ITTQQGVIEAIVP-AAEAGEEVQELAG-ILCPGFVNAHCHLELSHMKGrIPPG--SGMVDFLLGVMQQR--NFPQE--EV 106
Cdd:PRK12393   28 IRIRDGRIAAIGAlTPLPGERVIDATDcVVYPGWVNTHHHLFQSLLKG-VPAGinQSLTAWLAAVPYRFraRFDEDlfRL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 107 QAAIARAETAMwdSGIVAVGD---------ICNTADTI--AAKSMG-RLLY--------RNFiETmGFIPATAPQRF--- 163
Cdd:PRK12393  107 AARIGLVELLR--SGCTTVADhhylyhpgmPFDTGDILfdEAEALGmRFVLcrggatqtRGD-HP-GLPTALRPETLdqm 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 164 -AFAKTVFEQFEAAMPG---RNSIVPHAP-YSVSPELLQLIADFPGNQYLSIHNQESiaETQFLKDGTG---GMRRL--- 232
Cdd:PRK12393  183 lADVERLVSRYHDASPDslrRVVVAPTTPtFSLPPELLREVARAARGMGLRLHSHLS--ETVDYVDFCRekyGMTPVqfv 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 233 --YDFLGIDLSFyrpsglsspqlmlppfsqqqqmvlVHDVHTEASDLQWMqeeALPALFFCLCPNANLYIGNGLPDIELL 310
Cdd:PRK12393  261 aeHDWLGPDVWF------------------------AHLVKLDAEEIALL---AQTGTGIAHCPQSNGRLGSGIAPALAM 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 311 RMQGANIVLGTDSLSSNQQLSILEEVKTI-----ASEFPDIPTAE-LLQWGTFNGAKALGFEAqFGSFEKGKQPGIVLID 384
Cdd:PRK12393  314 EAAGVPVSLGVDGAASNESADMLSEAHAAwllhrAEGGADATTVEdVVHWGTAGGARVLGLDA-IGTLAVGQAADLAIYD 392
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 66-362 7.59e-10

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is 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 family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


Pssm-ID: 238617 [Multi-domain]  Cd Length: 275  Bit Score: 59.27  E-value: 7.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  66 FVNAHCHLELSHMKGRIPPGSGMVDFLLGVmqqrnfpqEEVQAAIARAETAMWDSGIVAVGDICNTADTIAAKSMGRLLY 145
Cdd:cd01292     1 FIDTHVHLDGSALRGTRLNLELKEAEELSP--------EDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 146 RNFIETMGFI------PATAPQRFAFAKTVFEQFEAAMPGRNSIVPHAPYS------VSPELLQLIAdfpgnQYLSIHNQ 213
Cdd:cd01292    73 EAARASAGIRvvlglgIPGVPAAVDEDAEALLLELLRRGLELGAVGLKLAGpytatgLSDESLRRVL-----EEARKLGL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 214 ESIAETQFLKDGTGGMRRLYDFLGIDLSFyrpsglsspqlmlppfsqqqqmVLVHDVHTEASDLQWMQEEALPalfFCLC 293
Cdd:cd01292   148 PVVIHAGELPDPTRALEDLVALLRLGGRV----------------------VIGHVSHLDPELLELLKEAGVS---LEVC 202

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721653017 294 PNANLY---IGNGLPDIELLRMQGANIVLGTDSLSSNQQLSILEEVKTIASEF-PDIPTAELLQWGTFNGAKA 362
Cdd:cd01292   203 PLSNYLlgrDGEGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLrLGLSLEEALRLATINPARA 275
PRK07213 PRK07213
chlorohydrolase; Provisional
 266-392 6.26e-09

chlorohydrolase; Provisional


Pssm-ID: 235969 [Multi-domain]  Cd Length: 375  Bit Score: 57.36  E-value: 6.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 266 LVHDVHTEASDLQWMQEEALPALffcLCPNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNQQlSILEEVKTIAsEFPD 345
Cdd:PRK07213  231 IVHATHPSNDDLELLKENNIPVV---VCPRANASFNVGLPPLNEMLEKGILLGIGTDNFMANSP-SIFREMEFIY-KLYH 305

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1721653017 346 IPTAELLQWGTFNGAKALGFEaQFGSFEKGKQPGIVLIDNAGDSFEK 392
Cdd:PRK07213  306 IEPKEILKMATINGAKILGLI-NVGLIEEGFKADFTFIKPTNIKFSK 351
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
16-72 1.69e-08

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 55.88  E-value: 1.69e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1721653017  16 FKADQLFTGTSLLSGGEVLIttQQGVIEAIVPAAEAGEEVQELAG-ILCPGFVNAHCH 72
Cdd:COG1820     2 ITNARIFTGDGVLEDGALLI--EDGRIAAIGPGAEPDAEVIDLGGgYLAPGFIDLHVH 57
PRK09228 PRK09228
guanine deaminase; Provisional
 34-384 2.31e-08

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 55.58  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  34 LITTQQGVIEAIVPAAE------AGEEVQELAG-ILCPGFVNAHCHLELSHMKGriPPGSGMVDFLlgvmQQRNFPQEev 106
Cdd:PRK09228   33 LLLVEDGRIVAAGPYAElraqlpADAEVTDYRGkLILPGFIDTHIHYPQTDMIA--SYGEQLLDWL----NTYTFPEE-- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 107 qaaiAR-AETAMwdsgivavgdicntADTIAAKSMGRLLyRNFIETMgfipatapqrFAFAkTVFEQ-----FEAAM--- 177
Cdd:PRK09228  105 ----RRfADPAY--------------AREVAEFFLDELL-RNGTTTA----------LVFG-TVHPQsvdalFEAAEarn 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 178 --------------P------------------------GRNS--IVPH-APYSvSPELL----QLIADFPGnQYLSIHN 212
Cdd:PRK09228  155 mrmiagkvlmdrnaPdglrdtaesgyddskalierwhgkGRLLyaITPRfAPTS-TPEQLeaagALAREHPD-VWIQTHL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 213 QESIAETQFLKDgtggmrrLY----DFLGIdlsfYRPSGLSSPQLmlppfsqqqqmVLVHDVHTEASDLQWMQEEALPAL 288
Cdd:PRK09228  233 SENLDEIAWVKE-------LFpearDYLDV----YERYGLLGPRA-----------VFAHCIHLEDRERRRLAETGAAIA 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 289 FfclCPNANLYIGNGLPDIELLRMQGANIVLGTD-----SLSSNQQLsiLEEVKTIASEFPDIPTAELLQWGTFNGAKAL 363
Cdd:PRK09228  291 F---CPTSNLFLGSGLFDLKRADAAGVRVGLGTDvgggtSFSMLQTM--NEAYKVQQLQGYRLSPFQAFYLATLGGARAL 365

                         410       420
                  ....*....|....*....|.
gi 1721653017 364 GFEAQFGSFEKGKQPGIVLID 384
Cdd:PRK09228  366 GLDDRIGNLAPGKEADFVVLD 386
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
 295-384 5.58e-08

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 54.50  E-value: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 295 NANLYIGNGLPDIELLRmQGANIVLGTDSLSSNQQLSILEEVK----TIASEFPD---IPTAELLQWGTFNGAKALGFEA 367
Cdd:PRK06380  268 NFKLGTGGSPPIPEMLD-NGINVTIGTDSNGSNNSLDMFEAMKfsalSVKNERWDasiIKAQEILDFATINAAKALELNA 346

                          90
                  ....*....|....*..
gi 1721653017 368 qfGSFEKGKQPGIVLID 384
Cdd:PRK06380  347 --GSIEVGKLADLVILD 361
PRK05985 PRK05985
cytosine deaminase; Provisional
 19-77 4.76e-07

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 51.47  E-value: 4.76e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721653017  19 DQLFTGTSLLSGGEVLITTQQGVIEAIVPA--AEAGEEVQELAG-ILCPGFVNAHCHLELSH 77
Cdd:PRK05985    3 DLLFRNVRPAGGAAVDILIRDGRIAAIGPAlaAPPGAEVEDGGGaLALPGLVDGHIHLDKTF 64
PRK08204 PRK08204
hypothetical protein; Provisional
 290-384 1.36e-06

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 50.00  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 290 FCLCPNANLYIGNGLPDIELLRMQGANIVLGTDSLSS--------------------NQQLsiLEEVKTIASEFPdIPTA 349
Cdd:PRK08204  269 FSVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTStggdmftqmrfalqaerardNAVH--LREGGMPPPRLT-LTAR 345

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1721653017 350 ELLQWGTFNGAKALGFEAQFGSFEKGKQPGIVLID 384
Cdd:PRK08204  346 QVLEWATIEGARALGLEDRIGSLTPGKQADLVLID 380
archeal_chlorohydrolases cd01305
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ...
 265-362 1.85e-06

Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are 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. They 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. Some members of this subgroup are predicted to be chlorohyrolases.


Pssm-ID: 238630 [Multi-domain]  Cd Length: 263  Bit Score: 48.94  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 265 VLVHDVHTEASDLQWMQEEALPALffcLCPNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNqQLSILEEVKTIASEF- 343
Cdd:cd01305   167 LLVHGTHLTDEDLELVRENGVPVV---LCPRSNLYFGVGIPPVAELLKLGIKVLLGTDNVMVN-EPDMWAEMEFLAKYSr 242

                          90       100
                  ....*....|....*....|..
gi 1721653017 344 ---PDIPTaELLQWGTFNGAKA 362
Cdd:cd01305   243 lqgYLSPL-EILRMATVNAAEF 263
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 268-384 2.30e-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: 46.10  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 268 HDVHTEASDLQWMQEEALPALffcLCPNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNQQLSILEEVKTIASEFPDIP 347
Cdd:cd01296   235 HLEHTSDEGIAALAEAGTVAV---LLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPGSSPTSSMPLVMHLACRLMRMT 311

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1721653017 348 TAELLQWGTFNGAKALGFEAQFGSFEKGKQPGIVLID 384
Cdd:cd01296   312 PEEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 21-150 3.35e-05

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


Pssm-ID: 238618 [Multi-domain]  Cd Length: 398  Bit Score: 45.70  E-value: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  21 LFTGTSLLSGGEVL--ITTQQGVIEAIVPA--AEAGEEVQELAG-ILCPGFVNAHCHLELSHMKGRIPPGSGmvDFLLGV 95
Cdd:cd01293     1 LLRNARLADGGTALvdIAIEDGRIAAIGPAlaVPPDAEEVDAKGrLVLPAFVDPHIHLDKTFTGGRWPNNSG--GTLLEA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721653017  96 MQ-----QRNFPQEEVQaaiARAETAM---WDSGIVAVG---DICNTADTIAAKSMGRLL--YRNFIE 150
Cdd:cd01293    79 IIaweerKLLLTAEDVK---ERAERALelaIAHGTTAIRthvDVDPAAGLKALEALLELReeWADLID 143
PRK09229 PRK09229
N-formimino-L-glutamate deiminase; Validated
 20-384 1.44e-04

N-formimino-L-glutamate deiminase; Validated


Pssm-ID: 236420 [Multi-domain]  Cd Length: 456  Bit Score: 43.68  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  20 QLFTGTSLLSGG---EVLIT-TQQGVIEAIVPAAeAGEEVQELAGILCPGFVNAHCHL------ELSHMKGRiPPGS--- 86
Cdd:PRK09229    4 TLFAERALLPDGwarNVRLTvDADGRIAAVEPGA-APAGAERLAGPVLPGMPNLHSHAfqramaGLTEVRGP-PQDSfws 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  87 ---GMVDFLlgvmqQRNFPqEEVQAAIARAETAMWDSGIVAVG---------------DICNTADTIAAKS----MGRLL 144
Cdd:PRK09229   82 wreLMYRFA-----LRLTP-DQLEAIARQLYVEMLEAGYTSVGefhylhhdpdgtpyaDPAEMALRIVAAAraagIGLTL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 145 YRNFIETMGF--IPATAPQ-RF-----AFAKTVfEQFEAAMPG----RNSIVPHAPYSVSPELLQ-LIADFPGNQYLSIH 211
Cdd:PRK09229  156 LPVLYAHSGFggQPPNPGQrRFindpdGFLRLL-EALRRALAAlpgaRLGLAPHSLRAVTPDQLAaVLALAAPDGPVHIH 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 212 nqesIAETQflkdgtggmRRLYDFLgidlsfyRPSGLSSPQLMLPPFSQQQQMVLVHDVHTEASDLQWMQEEALPAlffC 291
Cdd:PRK09229  235 ----IAEQT---------KEVDDCL-------AWSGARPVEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVA---G 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 292 LCP--NANLyiGNGLPDIELLRMQGANIVLGTDSLSSnqqLSILEEVKT--------------IASEFPDIPTAELLQWG 355
Cdd:PRK09229  292 LCPttEANL--GDGIFPAVDYLAAGGRFGIGSDSHVS---IDLVEELRLleygqrlrdrrrnvLAAAAQPSVGRRLFDAA 366

                         410       420
                  ....*....|....*....|....*....
gi 1721653017 356 TFNGAKALGFEAqfGSFEKGKQPGIVLID 384
Cdd:PRK09229  367 LAGGAQALGRAI--GGLAVGARADLVVLD 393
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 307-391 2.27e-04

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: 43.07  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 307 IELLRMQGANIVLGTDSLSSNQQLSILEEVKTIASefpDIPTAELLQWGTFNGAKALGFEAQFGSFEKGKQPGIVLIDna 386
Cdd:cd01309   264 AYLLKKGGVAFAISSDHPVLNIRNLNLEAAKAVKY---GLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWN-- 338


                  ....*
gi 1721653017 387 GDSFE 391
Cdd:cd01309   339 GDPLE 343
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
17-78 8.74e-04

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 41.24  E-value: 8.74e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017  17 KADQLFTGTSLL---SG----GEVLITtqQGVIEAIVPAAEAGEEVQELAG-ILCPGFVNAHCHLELSHM 78
Cdd:COG1001     4 PADLVIKNGRLVnvfTGeileGDIAIA--GGRIAGVGDYIGEATEVIDAAGrYLVPGFIDGHVHIESSMV 71
PRK07583 PRK07583
cytosine deaminase;
35-83 1.25e-03

cytosine deaminase;


Pssm-ID: 236062  Cd Length: 438  Bit Score: 40.74  E-value: 1.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1721653017  35 ITTQQGVIEAIVPAAEAGEEVQ--ELAG-ILCPGFVNAHCHLELSHMKGRIP 83
Cdd:PRK07583   43 IEIADGKIAAILPAGGAPDELPavDLKGrMVWPCFVDMHTHLDKGHIWPRSP 94
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 303-384 1.43e-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: 40.35  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 303 GLPDIELLRMQGANIVLGTDSLSSNqqlsILEEvkTIASEFPD-----IPTAELLQWGTFNGAKALGFEAQFGSFEKGKQ 377
Cdd:cd01299   252 GRDALRRAHKAGVKIAFGTDAGFPV----PPHG--WNARELELlvkagGTPAEALRAATANAAELLGLSDELGVIEAGKL 325


                  ....*..
gi 1721653017 378 PGIVLID 384
Cdd:cd01299   326 ADLLVVD 332
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 21-67 3.64e-03

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 39.19  E-value: 3.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1721653017  21 LFTGTSLLSGGEVLIttQQGVIEAIVPAAE--AGEEVQELAG-ILCPGFV 67
Cdd:PRK11170    9 IYTGHEVLDDHAVVI--ADGLIEAVCPVAElpPGIEQRDLNGaILSPGFI 56
pyrC PRK09357
dihydroorotase; Validated
 31-73 5.08e-03

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 38.64  E-value: 5.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1721653017  31 GEVLIttQQGVIEAIVPA-AEAGEEVQELAG-ILCPGFVNAHCHL 73
Cdd:PRK09357   20 ADVLI--DDGKIAAIGENiEAEGAEVIDATGlVVAPGLVDLHVHL 62
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 291-384 7.52e-03

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 38.29  E-value: 7.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721653017 291 CLCPNANLYIGNGLPDIELLRMQGANIVLGTDSLSSNQQLSILEEVKTI-----ASEFPDIPTA-ELLQWGTFNGAKALG 364
Cdd:PRK08203  290 AHCPCSNMRLASGIAPVRELRAAGVPVGLGVDGSASNDGSNLIGEARQAlllqrLRYGPDAMTArEALEWATLGGARVLG 369

                          90       100
                  ....*....|....*....|
gi 1721653017 365 fEAQFGSFEKGKQPGIVLID 384
Cdd:PRK08203  370 -RDDIGSLAPGKLADLALFD 388
 
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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