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Conserved domains on  [gi|254675292|ref|NP_082184|]
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probable imidazolonepropionase [Mus musculus]

Protein Classification

imidazolonepropionase( domain architecture ID 10101315)

imidazolonepropionase catalyzes the formation of N-formimidoyl-L-glutamate through the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 43-420 0e+00

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: 538.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  43 VVGTDGLIKAVGPAAVIQKqfSGETFEERIDCSGKCVLPGLVDAHTHPVWAGERVHEFAMKLAGATYMDIHQAGGGINFT 122
Cdd:cd01296    1 IAIRDGRIAAVGPAASLPA--PGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 123 VEHTRQASEEELFCSFQQRLQCMMRAGTTLVECKSGYGLNLETELKMLRVIERARRELHLSLSATYCGAHSVPKGKTAVE 202
Cdd:cd01296   79 VRATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGRE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 203 AA-DDIISHHLPRLKElsrngDLHVDNIDVFCEKGVFDLDTTRRILEGGKKMGLQINFHGDELHPMKAAELGAELGAQAI 281
Cdd:cd01296  159 EYiDLVIEEVLPAVAE-----ENLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 282 SHLEEVSDEGIAAMAAARCSAVLLPTTAYMLRLKQPRARKMLDEGVIVALGSDFNPNAYCF-SMPMVMHLACVNMRMSMP 360
Cdd:cd01296  234 DHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPGSSPTsSMPLVMHLACRLMRMTPE 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 361 EALAAATINAAYALGKSHTHGSLEVGKQGDAIIINASRWEHLIYQFGGHHelIDYVITKG 420
Cdd:cd01296  314 EALTAATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNL--VEYVIKNG 371
 
Name Accession Description Interval E-value
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 43-420 0e+00

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: 538.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  43 VVGTDGLIKAVGPAAVIQKqfSGETFEERIDCSGKCVLPGLVDAHTHPVWAGERVHEFAMKLAGATYMDIHQAGGGINFT 122
Cdd:cd01296    1 IAIRDGRIAAVGPAASLPA--PGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 123 VEHTRQASEEELFCSFQQRLQCMMRAGTTLVECKSGYGLNLETELKMLRVIERARRELHLSLSATYCGAHSVPKGKTAVE 202
Cdd:cd01296   79 VRATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGRE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 203 AA-DDIISHHLPRLKElsrngDLHVDNIDVFCEKGVFDLDTTRRILEGGKKMGLQINFHGDELHPMKAAELGAELGAQAI 281
Cdd:cd01296  159 EYiDLVIEEVLPAVAE-----ENLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 282 SHLEEVSDEGIAAMAAARCSAVLLPTTAYMLRLKQPRARKMLDEGVIVALGSDFNPNAYCF-SMPMVMHLACVNMRMSMP 360
Cdd:cd01296  234 DHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPGSSPTsSMPLVMHLACRLMRMTPE 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 361 EALAAATINAAYALGKSHTHGSLEVGKQGDAIIINASRWEHLIYQFGGHHelIDYVITKG 420
Cdd:cd01296  314 EALTAATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNL--VEYVIKNG 371
hutI TIGR01224
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ...
 38-422 2.16e-137

imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273512 [Multi-domain]  Cd Length: 377  Bit Score: 398.32  E-value: 2.16e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292   38 EGASVVVgTDGLIKAVGPAAviqkQFSGETFEERIDCSGKCVLPGLVDAHTHPVWAGERVHEFAMKLAGATYMDIHQAGG 117
Cdd:TIGR01224   2 EDAVILI-HGGKIVWIGQLA----ALPGEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  118 GINFTVEHTRQASEEELFCSFQQRLQCMMRAGTTLVECKSGYGLNLETELKMLRVIERARRELHLSLSATYCGAHSVPKG 197
Cdd:TIGR01224  77 GILSTVRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  198 KTAVEAA--DDIISHHLPRLKElsrngDLHVDNIDVFCEKGVFDLDTTRRILEGGKKMGLQINFHGDELHPMKAAELGAE 275
Cdd:TIGR01224 157 FQGRPDDyvDGICEELIPQVAE-----EGLASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAK 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  276 LGAQAISHLEEVSDEGIAAMAAARCSAVLLPTTAYMLRLKQPRARKMLDEGVIVALGSDFNP-NAYCFSMPMVMHLACVN 354
Cdd:TIGR01224 232 LGAVSADHLEHASDAGIKALAEAGTVAVLLPGTTFYLRETYPPARQLIDYGVPVALATDLNPgSSPTLSMQLIMSLACRL 311

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675292  355 MRMSMPEALAAATINAAYALGKSHTHGSLEVGKQGDAIIINASRWEHLIYQFGGHHelIDYVITKGKV 422
Cdd:TIGR01224 312 MKMTPEEALHAATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPYHYGVNH--VHAVIKNGNI 377
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 6-426 8.29e-51

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 175.92  E-value: 8.29e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292   6 RLLLENAQQVVLVCARgerFLTGsalRSLAVLEGASVVVgTDGLIKAVGPAAVIQKQFSGETfeerIDCSGKCVLPGLVD 85
Cdd:COG1228    1 KKAPAQAGTLLITNAT---LVDG---TGGGVIENGTVLV-EDGKIAAVGPAADLAVPAGAEV----IDATGKTVLPGLID 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  86 AHTHPVWAGERVHEFAMklagatymdihqaGGGINFTVEHTRQASEeelfcsfqqRLQCMMRAGTTLVECKSGYGLNL-- 163
Cdd:COG1228   70 AHTHLGLGGGRAVEFEA-------------GGGITPTVDLVNPADK---------RLRRALAAGVTTVRDLPGGPLGLrd 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 164 ---ETELKML---RVIERARrelhlSLSATYcGAHSvpKGKTAVEAAddiishhlprLKELSRNGdlhVDNIDVFCEKG- 236
Cdd:COG1228  128 aiiAGESKLLpgpRVLAAGP-----ALSLTG-GAHA--RGPEEARAA----------LRELLAEG---ADYIKVFAEGGa 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 237 -VFDLDTTRRILEGGKKMGLQINFHGDELHPMKAAelgAELGAQAISHLEEVSDEGIAAMAAaRCSAVLLPTTAYMLRL- 314
Cdd:COG1228  187 pDFSLEELRAILEAAHALGLPVAAHAHQADDIRLA---VEAGVDSIEHGTYLDDEVADLLAE-AGTVVLVPTLSLFLALl 262

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 315 -----------------KQPRARKMLDEGVIVALGSDFN-PNAYCFSMPMVMHLAcVNMRMSMPEALAAATINAAYALGK 376
Cdd:COG1228  263 egaaapvaakarkvreaALANARRLHDAGVPVALGTDAGvGVPPGRSLHRELALA-VEAGLTPEEALRAATINAAKALGL 341

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 254675292 377 SHTHGSLEVGKQGDAIIINASRWEHLIYqfgghHELIDYVITKGKVIYKK 426
Cdd:COG1228  342 DDDVGSLEPGKLADLVLLDGDPLEDIAY-----LEDVRAVMKDGRVVDRS 386
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 79-423 1.18e-07

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: 53.27  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292   79 VLPGLVDAHTHpvwagervhefamklagatymdihqagggINFTVEHTRQASEEELFCSFQQRLQCMMRAGTTLVeCKSG 158
Cdd:pfam01979   2 VLPGLIDAHVH-----------------------------LEMGLLRGIPVPPEFAYEALRLGITTMLKSGTTTV-LDMG 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  159 YGLNLETELkMLRVIERARRELHL-----SLSATYCGAHSVPKGKTAVEAADDIISHHLPRLK-ELSRNGDLHvdnidvf 232
Cdd:pfam01979  52 ATTSTGIEA-LLEAAEELPLGLRFlgpgcSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFvGLAPHGAPT------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  233 cekgvFDLDTTRRILEGGKKMGLQINFHGDEL-HPMKAAELGAELGAQAISHLE---------------------EVSDE 290
Cdd:pfam01979 124 -----FSDDELKAALEEAKKYGLPVAIHALETkGEVEDAIAAFGGGIEHGTHLEvaesgglldiiklilahgvhlSPTEA 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  291 GIAAMAAARCSAVLLPTTAYMLRLKQPRARKMLDEGVIVALGSDFNPNAYCFSMPMVMHLAC-----VNMRMSMPEALAA 365
Cdd:pfam01979 199 NLLAEHLKGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALelqfdPEGGLSPLEALRM 278

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 254675292  366 ATINAAYALGKSHTHGSLEVGKQGDAIIINASRWEHLIYQFGGhhELIDYVITKGKVI 423
Cdd:pfam01979 279 ATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPD--GNVKKVIVKGKIV 334
PRK09228 PRK09228
guanine deaminase; Provisional
 39-89 2.41e-05

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 46.34  E-value: 2.41e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 254675292  39 GASVVvgTDGLIKAVGPAAVIQKQFSGETfeERIDCSGKCVLPGLVDAHTH 89
Cdd:PRK09228  32 GLLLV--EDGRIVAAGPYAELRAQLPADA--EVTDYRGKLILPGFIDTHIH 78
 
Name Accession Description Interval E-value
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 43-420 0e+00

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: 538.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  43 VVGTDGLIKAVGPAAVIQKqfSGETFEERIDCSGKCVLPGLVDAHTHPVWAGERVHEFAMKLAGATYMDIHQAGGGINFT 122
Cdd:cd01296    1 IAIRDGRIAAVGPAASLPA--PGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 123 VEHTRQASEEELFCSFQQRLQCMMRAGTTLVECKSGYGLNLETELKMLRVIERARRELHLSLSATYCGAHSVPKGKTAVE 202
Cdd:cd01296   79 VRATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGRE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 203 AA-DDIISHHLPRLKElsrngDLHVDNIDVFCEKGVFDLDTTRRILEGGKKMGLQINFHGDELHPMKAAELGAELGAQAI 281
Cdd:cd01296  159 EYiDLVIEEVLPAVAE-----ENLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 282 SHLEEVSDEGIAAMAAARCSAVLLPTTAYMLRLKQPRARKMLDEGVIVALGSDFNPNAYCF-SMPMVMHLACVNMRMSMP 360
Cdd:cd01296  234 DHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPGSSPTsSMPLVMHLACRLMRMTPE 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 361 EALAAATINAAYALGKSHTHGSLEVGKQGDAIIINASRWEHLIYQFGGHHelIDYVITKG 420
Cdd:cd01296  314 EALTAATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNL--VEYVIKNG 371
hutI TIGR01224
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ...
 38-422 2.16e-137

imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273512 [Multi-domain]  Cd Length: 377  Bit Score: 398.32  E-value: 2.16e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292   38 EGASVVVgTDGLIKAVGPAAviqkQFSGETFEERIDCSGKCVLPGLVDAHTHPVWAGERVHEFAMKLAGATYMDIHQAGG 117
Cdd:TIGR01224   2 EDAVILI-HGGKIVWIGQLA----ALPGEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  118 GINFTVEHTRQASEEELFCSFQQRLQCMMRAGTTLVECKSGYGLNLETELKMLRVIERARRELHLSLSATYCGAHSVPKG 197
Cdd:TIGR01224  77 GILSTVRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  198 KTAVEAA--DDIISHHLPRLKElsrngDLHVDNIDVFCEKGVFDLDTTRRILEGGKKMGLQINFHGDELHPMKAAELGAE 275
Cdd:TIGR01224 157 FQGRPDDyvDGICEELIPQVAE-----EGLASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAK 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  276 LGAQAISHLEEVSDEGIAAMAAARCSAVLLPTTAYMLRLKQPRARKMLDEGVIVALGSDFNP-NAYCFSMPMVMHLACVN 354
Cdd:TIGR01224 232 LGAVSADHLEHASDAGIKALAEAGTVAVLLPGTTFYLRETYPPARQLIDYGVPVALATDLNPgSSPTLSMQLIMSLACRL 311

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675292  355 MRMSMPEALAAATINAAYALGKSHTHGSLEVGKQGDAIIINASRWEHLIYQFGGHHelIDYVITKGKV 422
Cdd:TIGR01224 312 MKMTPEEALHAATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPYHYGVNH--VHAVIKNGNI 377
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 6-426 8.29e-51

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 175.92  E-value: 8.29e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292   6 RLLLENAQQVVLVCARgerFLTGsalRSLAVLEGASVVVgTDGLIKAVGPAAVIQKQFSGETfeerIDCSGKCVLPGLVD 85
Cdd:COG1228    1 KKAPAQAGTLLITNAT---LVDG---TGGGVIENGTVLV-EDGKIAAVGPAADLAVPAGAEV----IDATGKTVLPGLID 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  86 AHTHPVWAGERVHEFAMklagatymdihqaGGGINFTVEHTRQASEeelfcsfqqRLQCMMRAGTTLVECKSGYGLNL-- 163
Cdd:COG1228   70 AHTHLGLGGGRAVEFEA-------------GGGITPTVDLVNPADK---------RLRRALAAGVTTVRDLPGGPLGLrd 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 164 ---ETELKML---RVIERARrelhlSLSATYcGAHSvpKGKTAVEAAddiishhlprLKELSRNGdlhVDNIDVFCEKG- 236
Cdd:COG1228  128 aiiAGESKLLpgpRVLAAGP-----ALSLTG-GAHA--RGPEEARAA----------LRELLAEG---ADYIKVFAEGGa 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 237 -VFDLDTTRRILEGGKKMGLQINFHGDELHPMKAAelgAELGAQAISHLEEVSDEGIAAMAAaRCSAVLLPTTAYMLRL- 314
Cdd:COG1228  187 pDFSLEELRAILEAAHALGLPVAAHAHQADDIRLA---VEAGVDSIEHGTYLDDEVADLLAE-AGTVVLVPTLSLFLALl 262

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 315 -----------------KQPRARKMLDEGVIVALGSDFN-PNAYCFSMPMVMHLAcVNMRMSMPEALAAATINAAYALGK 376
Cdd:COG1228  263 egaaapvaakarkvreaALANARRLHDAGVPVALGTDAGvGVPPGRSLHRELALA-VEAGLTPEEALRAATINAAKALGL 341

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 254675292 377 SHTHGSLEVGKQGDAIIINASRWEHLIYqfgghHELIDYVITKGKVIYKK 426
Cdd:COG1228  342 DDDVGSLEPGKLADLVLLDGDPLEDIAY-----LEDVRAVMKDGRVVDRS 386
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 21-425 5.64e-17

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: 82.18  E-value: 5.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  21 RGERFLTGSAlrSLAVLEGASVVVgTDGLIKAVGPAAVIQKQFSGEtfeERIDCSGKCVLPGLVDAHTHpvwagerVHEF 100
Cdd:COG0402    5 RGAWVLTMDP--AGGVLEDGAVLV-EDGRIAAVGPGAELPARYPAA---EVIDAGGKLVLPGLVNTHTH-------LPQT 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 101 AMK--LAGATYMDIHQagggiNFTVEHTRQASEEELFCSFQQRLQCMMRAGTTLVeCKSGYGLNLETElkmlrVIERARR 178
Cdd:COG0402   72 LLRglADDLPLLDWLE-----EYIWPLEARLDPEDVYAGALLALAEMLRSGTTTV-ADFYYVHPESAD-----ALAEAAA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 179 ELHLSLSATY-CGAHSVPKGktAVEAADDIISHHLPRLKEL--SRNGDLHVdnidVFCEKGVF--DLDTTRRILEGGKKM 253
Cdd:COG0402  141 EAGIRAVLGRgLMDRGFPDG--LREDADEGLADSERLIERWhgAADGRIRV----ALAPHAPYtvSPELLRAAAALAREL 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 254 GLQINFH----------GDELHPMKAAELGAELG--------AQAIsHLeevSDEGIAAMAAARCSAVLLPTTAYMLRLK 315
Cdd:COG0402  215 GLPLHTHlaetrdevewVLELYGKRPVEYLDELGllgprtllAHCV-HL---TDEEIALLAETGASVAHCPTSNLKLGSG 290

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 316 QPRARKMLDEGVIVALGSDFNPNAYCFSMPMVMHLACVNMR--------MSMPEALAAATINAAYALGKSHTHGSLEVGK 387
Cdd:COG0402  291 IAPVPRLLAAGVRVGLGTDGAASNNSLDMFEEMRLAALLQRlrggdptaLSAREALEMATLGGARALGLDDEIGSLEPGK 370

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 254675292 388 QGDAIIINASRWE---------HLIYQFGGHHelIDYVITKGKVIYK 425
Cdd:COG0402  371 RADLVVLDLDAPHlaplhdplsALVYAADGRD--VRTVWVAGRVVVR 415
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
41-95 7.21e-11

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 64.05  E-value: 7.21e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 254675292  41 SVVVgTDGLIKAVGPAAVIQKQFSGETfeERIDCSGKCVLPGLVDAHTHPVWAGE 95
Cdd:COG1574   29 AVAV-RDGRIVAVGSDAEVRALAGPAT--EVIDLGGKTVLPGFIDAHVHLLGGGL 80
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 7-426 1.94e-08

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: 56.06  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292   7 LLLENAQQVVLVCARgerfltgsalrslaVLEGASVVVgTDGLIKAVGPAAViQKQFSGEtfeERIDCSGKCVLPGLVDA 86
Cdd:cd01298    1 ILIRNGTIVTTDPRR--------------VLEDGDVLV-EDGRIVAVGPALP-LPAYPAD---EVIDAKGKVVMPGLVNT 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  87 HTHpvwagervheFAMKL-----AGATYMDIHQ------AGggiNFTVEHTRQASeeelfcsfqqRLQC--MMRAGTTLV 153
Cdd:cd01298   62 HTH----------LAMTLlrglaDDLPLMEWLKdliwplER---LLTEEDVYLGA----------LLALaeMIRSGTTTF 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 154 ecksgyglnLETELKMLRVIERARREL----HLSLSATYCGAHSVPKGKTAVEAADDIIS-HHLPRlkelsrNGDLHVdn 228
Cdd:cd01298  119 ---------ADMYFFYPDAVAEAAEELgiraVLGRGIMDLGTEDVEETEEALAEAERLIReWHGAA------DGRIRV-- 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 229 idVFCEKGVFDL--DTTRRILEGGKKMGLQINFHG----DELHPMKA----------AELGAeLGAQAI-SHLEEVSDEG 291
Cdd:cd01298  182 --ALAPHAPYTCsdELLREVAELAREYGVPLHIHLaeteDEVEESLEkygkrpveylEELGL-LGPDVVlAHCVWLTDEE 258

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 292 IAAMAAARCSAVLLPTTAYMLRLKQPRARKMLDEGVIVALGSD-----------------------FNPNAYCFSMPMVM 348
Cdd:cd01298  259 IELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDgaasnnnldmfeemrlaallqklAHGDPTALPAEEAL 338

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 349 HLACVNMR--MSMPEAlaaatinaayalgkshthGSLEVGKQGDAIIINASR---------WEHLIYqfGGHHELIDYVI 417
Cdd:cd01298  339 EMATIGGAkaLGLDEI------------------GSLEVGKKADLILIDLDGphllpvhdpISHLVY--SANGGDVDTVI 398


                 ....*....
gi 254675292 418 TKGKVIYKK 426
Cdd:cd01298  399 VNGRVVMED 407
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 43-94 2.29e-08

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


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 55.78  E-value: 2.29e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 254675292  43 VVGTDGLIKAVGPAAVIQKQFSGETfeERIDCSGKCVLPGLVDAHTHPVWAG 94
Cdd:cd01300    2 VAVRDGRIVAVGSDAEAKALKGPAT--EVIDLKGKTVLPGFIDSHSHLLLGG 51
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 83-351 6.12e-08

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: 53.88  E-value: 6.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  83 LVDAHTHPVWAGERvhefamklagatymdihqaGGGINFTVEHTRQASEEELFCSFQQRLQCMMRAGTTLVECKSGYGLN 162
Cdd:cd01292    1 FIDTHVHLDGSALR-------------------GTRLNLELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPP 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 163 LETELKMLRVIERARRELHLSLSATYCGAHSVPKGktaveaaDDIISHHLPRLKELSRNGDLHVDNIDVFCEKGVFDLDT 242
Cdd:cd01292   62 TTTKAAIEAVAEAARASAGIRVVLGLGIPGVPAAV-------DEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDES 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 243 TRRILEGGKKMGLQINFH----GDELHPMKAAELGAELGAQ-AISHLEEVSDEGIAAMAAARCSAVLLPTTAYMLRLK-- 315
Cdd:cd01292  135 LRRVLEEARKLGLPVVIHagelPDPTRALEDLVALLRLGGRvVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRDge 214

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 254675292 316 -QPRARKMLDEGVIVALGSDFNPNAYCFSMPMVMHLA 351
Cdd:cd01292  215 gAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLL 251
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 40-89 8.69e-08

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: 53.94  E-value: 8.69e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 254675292  40 ASVVVgTDGLIKAVGPAAviqkqfSGETFEERIDCSGKCVLPGLVDAHTH 89
Cdd:COG0044   16 ADVLI-EDGRIAAIGPDL------AAPEAAEVIDATGLLVLPGLIDLHVH 58
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 79-423 1.18e-07

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: 53.27  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292   79 VLPGLVDAHTHpvwagervhefamklagatymdihqagggINFTVEHTRQASEEELFCSFQQRLQCMMRAGTTLVeCKSG 158
Cdd:pfam01979   2 VLPGLIDAHVH-----------------------------LEMGLLRGIPVPPEFAYEALRLGITTMLKSGTTTV-LDMG 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  159 YGLNLETELkMLRVIERARRELHL-----SLSATYCGAHSVPKGKTAVEAADDIISHHLPRLK-ELSRNGDLHvdnidvf 232
Cdd:pfam01979  52 ATTSTGIEA-LLEAAEELPLGLRFlgpgcSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFvGLAPHGAPT------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  233 cekgvFDLDTTRRILEGGKKMGLQINFHGDEL-HPMKAAELGAELGAQAISHLE---------------------EVSDE 290
Cdd:pfam01979 124 -----FSDDELKAALEEAKKYGLPVAIHALETkGEVEDAIAAFGGGIEHGTHLEvaesgglldiiklilahgvhlSPTEA 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  291 GIAAMAAARCSAVLLPTTAYMLRLKQPRARKMLDEGVIVALGSDFNPNAYCFSMPMVMHLAC-----VNMRMSMPEALAA 365
Cdd:pfam01979 199 NLLAEHLKGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALelqfdPEGGLSPLEALRM 278

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 254675292  366 ATINAAYALGKSHTHGSLEVGKQGDAIIINASRWEHLIYQFGGhhELIDYVITKGKVI 423
Cdd:pfam01979 279 ATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPD--GNVKKVIVKGKIV 334
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 38-423 4.28e-06

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: 48.78  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  38 EGASV-VVGTDGLIKAVGPAAviqkqfSGETFEERIDCSGKCVLPGLVDAHTH----PVWAGERVHEFAMKLAGAtymdI 112
Cdd:cd01293   11 GTALVdIAIEDGRIAAIGPAL------AVPPDAEEVDAKGRLVLPAFVDPHIHldktFTGGRWPNNSGGTLLEAI----I 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 113 HQAGGGINFTVEHTRQASEeelfcsfqQRLQCMMRAGTTL----VECKSGYGLNLetelkmLRVIERARRE----LHLSL 184
Cdd:cd01293   81 AWEERKLLLTAEDVKERAE--------RALELAIAHGTTAirthVDVDPAAGLKA------LEALLELREEwadlIDLQI 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 185 SA-----TYCGAHSVPKGKTAVEAADDIIShHLPRLkELSRNGDLHVDNIdvfcekgvFDLdttrrilegGKKMGLQINF 259
Cdd:cd01293  147 VAfpqhgLLSTPGGEELMREALKMGADVVG-GIPPA-EIDEDGEESLDTL--------FEL---------AQEHGLDIDL 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 260 HGDE------LHPMKAAELGAELGAQ---AISHL-------EEVSDEGIAAMAAARCSAVLLPTTAYMLRLKQ------- 316
Cdd:cd01293  208 HLDEtddpgsRTLEELAEEAERRGMQgrvTCSHAtalgslpEAEVSRLADLLAEAGISVVSLPPINLYLQGREdttpkrr 287

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292 317 --PRARKMLDEGVIVALGSD-----FNPNAyCFSMPMVMHLACVNMRMSMPEALAAAT----INAAYALGKshTHGSLEV 385
Cdd:cd01293  288 gvTPVKELRAAGVNVALGSDnvrdpWYPFG-SGDMLEVANLAAHIAQLGTPEDLALALdlitGNAARALGL--EDYGIKV 364

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 254675292 386 GKQGDAIIINASRWEHLIYqfGGHHELIdyVITKGKVI 423
Cdd:cd01293  365 GCPADLVLLDAEDVAEAVA--RQPPRRV--VIRKGRVV 398
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 47-89 6.24e-06

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


Pssm-ID: 238639 [Multi-domain]  Cd Length: 447  Bit Score: 48.37  E-value: 6.24e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 254675292  47 DGLIKAVGPAaviqkqFSGETFEERIDCSGKCVLPGLVDAHTH 89
Cdd:cd01314   23 DGKIVAIGPN------LEAPGGVEVIDATGKYVLPGGIDPHTH 59
PRK09228 PRK09228
guanine deaminase; Provisional
 39-89 2.41e-05

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 46.34  E-value: 2.41e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 254675292  39 GASVVvgTDGLIKAVGPAAVIQKQFSGETfeERIDCSGKCVLPGLVDAHTH 89
Cdd:PRK09228  32 GLLLV--EDGRIVAAGPYAELRAQLPADA--EVTDYRGKLILPGFIDTHIH 78
PRK08323 PRK08323
phenylhydantoinase; Validated
 47-89 4.54e-05

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 45.55  E-value: 4.54e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 254675292  47 DGLIKAVGPAAViqkqfsgetfEERIDCSGKCVLPGLVDAHTH 89
Cdd:PRK08323  25 DGKIAAIGANLG----------DEVIDATGKYVMPGGIDPHTH 57
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
21-89 4.80e-05

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 45.09  E-value: 4.80e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675292  21 RGERFLTGSAlrslaVLEGASVVVgTDGLIKAVGPAAviqkqfsgETFEERIDCSGKCVLPGLVDAHTH 89
Cdd:COG1820    3 TNARIFTGDG-----VLEDGALLI-EDGRIAAIGPGA--------EPDAEVIDLGGGYLAPGFIDLHVH 57
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
 47-111 4.80e-05

D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.


Pssm-ID: 273937 [Multi-domain]  Cd Length: 454  Bit Score: 45.45  E-value: 4.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675292   47 DGLIKAVGPAAVIQKQFsgetfeERIDCSGKCVLPGLVDAHTHpvwagervheFAMKLAGATYMD 111
Cdd:TIGR02033  23 GGKIVAVGDNLIPPDAV------EVIDATGKYVLPGGIDVHTH----------LEMPFGGTTTAD 71
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
 43-98 5.50e-05

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: 45.01  E-value: 5.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 254675292  43 VVGTDGLIKAVGpaAVIQkqfsGETFEERIDCSGKCVLPGLVDAHTHPVWAGERVH 98
Cdd:cd01307    2 VAIENGKIAAVG--AALA----APAATQIVDAGGCYVSPGWIDLHVHVYQGGTRYG 51
pyrC PRK09357
dihydroorotase; Validated
 47-89 1.23e-04

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 44.03  E-value: 1.23e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 254675292  47 DGLIKAVGPAAviqkqfsGETFEERIDCSGKCVLPGLVDAHTH 89
Cdd:PRK09357  26 DGKIAAIGENI-------EAEGAEVIDATGLVVAPGLVDLHVH 61
PRK07203 PRK07203
putative aminohydrolase SsnA;
36-89 1.61e-04

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 43.77  E-value: 1.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 254675292  36 VLEGASVVVgTDGLIKAVGPAAVIQKQFSGETFeerIDCSGKCVLPGLVDAHTH 89
Cdd:PRK07203  18 VIEDGAIAI-EGNVIVEIGTTDELKAKYPDAEF---IDAKGKLIMPGLINSHNH 67
PRK08204 PRK08204
hypothetical protein; Provisional
 37-92 2.04e-04

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 43.45  E-value: 2.04e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 254675292  37 LEGASVVVgTDGLIKAVGPAavIQKqfsGETfeERIDCSGKCVLPGLVDAHTHpVW 92
Cdd:PRK08204  21 LPRGDILI-EGDRIAAVAPS--IEA---PDA--EVVDARGMIVMPGLVDTHRH-TW 67
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 36-89 2.45e-04

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


Pssm-ID: 238622 [Multi-domain]  Cd Length: 415  Bit Score: 43.05  E-value: 2.45e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675292  36 VLEGASVVVGT------------DGLIKAVGPAaviqkqfSGETFEERIDCSGKCVLPGLVDAHTH 89
Cdd:cd01297    3 VIRNGTVVDGTgappftadvgirDGRIAAIGPI-------LSTSAREVIDAAGLVVAPGFIDVHTH 61
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 70-92 2.85e-04

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


Pssm-ID: 238624 [Multi-domain]  Cd Length: 342  Bit Score: 42.67  E-value: 2.85e-04
                         10        20
                 ....*....|....*....|...
gi 254675292  70 ERIDCSGKCVLPGLVDAHTHPVW 92
Cdd:cd01299    2 QVIDLGGKTLMPGLIDAHTHLGS 24
PRK02382 PRK02382
dihydroorotase; Provisional
 37-89 2.90e-04

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 43.10  E-value: 2.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 254675292  37 LEGASVVVgTDGLIKAVGpaaviqKQFSGETFEERIDCSGKCVLPGLVDAHTH 89
Cdd:PRK02382  17 LQPRDVRI-DGGKITAVG------KDLDGSSSEEVIDARGMLLLPGGIDVHVH 62
PRK05985 PRK05985
cytosine deaminase; Provisional
 47-90 2.96e-04

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 42.61  E-value: 2.96e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 254675292  47 DGLIKAVGPAaviqkqFSGETFEERIDCSGKCVLPGLVDAHTHP 90
Cdd:PRK05985  23 DGRIAAIGPA------LAAPPGAEVEDGGGALALPGLVDGHIHL 60
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
35-89 3.06e-04

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 42.98  E-value: 3.06e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 254675292  35 AVLEGASVVVgTDGLIKAVGPAAVIQKQFsgeTFEERIDCSGKCVLPGLVDAHTH 89
Cdd:PRK09045  24 VVLEDHAVAI-RDGRIVAILPRAEARARY---AAAETVELPDHVLIPGLINAHTH 74
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
46-94 3.11e-04

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 42.85  E-value: 3.11e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 254675292  46 TDGLIKAVGPAAVIQKQfsgetfEERIDCSGKCVLPGLVDAHTHpVWAG 94
Cdd:COG3964   25 KDGKIAAVAKDIDAAEA------KKVIDASGLYVTPGLIDLHTH-VFPG 66
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 21-89 4.57e-04

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


Pssm-ID: 238640 [Multi-domain]  Cd Length: 447  Bit Score: 42.28  E-value: 4.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675292  21 RGERFLTGSALRSlavlegASVVVgTDGLIKAVGPAaviqkqFSGETFEERIDCSGKCVLPGLVDAHTH 89
Cdd:cd01315    5 KNGRVVTPDGVRE------ADIAV-KGGKIAAIGPD------IANTEAEEVIDAGGLVVMPGLIDTHVH 60
Amidohydro_3 pfam07969
Amidohydrolase family;
317-424 5.44e-04

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 42.13  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  317 PRARKMLDEGVIVALGSDFNPNAYC---FSMPMVMHLACVNM-------RMSMPEALAAATINAAYALGKSHTHGSLEVG 386
Cdd:pfam07969 349 TPVKELLNAGVKVALGSDAPVGPFDpwpRIGAAVMRQTAGGGevlgpdeELSLEEALALYTSGPAKALGLEDRKGTLGVG 428

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 254675292  387 KQGDAIIINASRW----EHLiyqfggHHELIDYVITKGKVIY 424
Cdd:pfam07969 429 KDADLVVLDDDPLtvdpPAI------ADIRVRLTVVDGRVVY 464
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 37-89 8.59e-04

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: 41.41  E-value: 8.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 254675292  37 LEGASVVVgTDGLIKAVGPaaviqkQFSGETFEERIDCSGKCVLPGLVDAHTH 89
Cdd:cd00854   14 LEDGAVLV-EDGKIVAIGP------EDELEEADEIIDLKGQYLVPGFIDIHIH 59
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
47-135 8.67e-04

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 41.37  E-value: 8.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  47 DGLIKAVGPAAviqkqfSGETFEERIDCSGKCVLPGLVDAHTHPVWAGERVH----EFAMKLAGATYMDihqAG--GGIN 120
Cdd:PRK09237  25 DGKIAAVAGDI------DGSQAKKVIDLSGLYVSPGWIDLHVHVYPGSTPYGdepdEVGVRSGVTTVVD---AGsaGADN 95

                         90
                 ....*....|....*..
gi 254675292 121 FT--VEHTRQASEEELF 135
Cdd:PRK09237  96 FDdfRKLTIEASKTRVL 112
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 4-88 9.38e-04

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 41.32  E-value: 9.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292   4 SHRLLLENAQqVVLvcarGERFLTGSalrslavlegasvVVGTDGLIKAVGPAAVIQKQFsgetfeerIDCSGKCVLPGL 83
Cdd:PRK15446   1 MMEMILSNAR-LVL----PDEVVDGS-------------LLIEDGRIAAIDPGASALPGA--------IDAEGDYLLPGL 54


                 ....*
gi 254675292  84 VDAHT 88
Cdd:PRK15446  55 VDLHT 59
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 43-89 1.06e-03

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 40.99  E-value: 1.06e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 254675292  43 VVGTDGLIKAVGPAAVIqkqfsGETFEERIDCSGKCVLPGLVDAHTH 89
Cdd:PRK08203  26 LVVEGGRIVEVGPGGAL-----PQPADEVFDARGHVVTPGLVNTHHH 67
PRK09059 PRK09059
dihydroorotase; Validated
 37-119 1.28e-03

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 40.79  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  37 LEGASVVVGTDGLIKAVGPAAVIQKQFSGEtfeERIDCSGKCVLPGLVDAHthpVWAGERVHEFAMKLAGATYMdihQAG 116
Cdd:PRK09059  19 LDEIGTVLIEDGVIVAAGKGAGNQGAPEGA---EIVDCAGKAVAPGLVDAR---VFVGEPGAEHRETIASASRA---AAA 89


                 ...
gi 254675292 117 GGI 119
Cdd:PRK09059  90 GGV 92
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 47-89 1.94e-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: 1.94e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 254675292  47 DGLIKAVGPAavIQKQFSGEtfeeRIDCSGKCVLPGLVDAHTH 89
Cdd:cd01309    1 DGKIVAVGAE--ITTPADAE----VIDAKGKHVTPGLIDAHSH 37
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 69-89 2.10e-03

Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.


Pssm-ID: 238642 [Multi-domain]  Cd Length: 374  Bit Score: 39.91  E-value: 2.10e-03
                         10        20
                 ....*....|....*....|.
gi 254675292  69 EERIDCSGKCVLPGLVDAHTH 89
Cdd:cd01317    2 AEVIDAEGKILAPGLVDLHVH 22
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
36-91 2.17e-03

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 39.98  E-value: 2.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 254675292  36 VLEGASVVVgtDGLIKAVGPAAVIQKqfsgetFEERIDCSGKCVLPGLVDAHTHPV 91
Cdd:PRK07228  19 IVDGDVLIE--DDRIAAVGDRLDLED------YDDHIDATGKVVIPGLIQGHIHLC 66
PLN02942 PLN02942
dihydropyrimidinase
 38-112 2.80e-03

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 39.83  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675292  38 EGASVVVgTDGLIKAVGPAAviqKQFSGETFeerIDCSGKCVLPGLVDAHTH---PVWAGERVHEF----AMKLAGATYM 110
Cdd:PLN02942  21 ELADVYV-EDGIIVAVAPNL---KVPDDVRV---IDATGKFVMPGGIDPHTHlamPFMGTETIDDFfsgqAAALAGGTTM 93


                 ..
gi 254675292 111 DI 112
Cdd:PLN02942  94 HI 95
Amidohydro_3 pfam07969
Amidohydrolase family;
72-97 4.12e-03

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 39.44  E-value: 4.12e-03
                          10        20
                  ....*....|....*....|....*.
gi 254675292   72 IDCSGKCVLPGLVDAHTHPVWAGERV 97
Cdd:pfam07969   3 IDAKGRLVLPGFVDPHTHLDGGGLNL 28
PRK09060 PRK09060
dihydroorotase; Validated
 36-89 5.08e-03

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 39.13  E-value: 5.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675292  36 VLEGASVV---------VG-TDGLIKAVGpaaviqkQFSGETFEERIDCSGKCVLPGLVDAHTH 89
Cdd:PRK09060   8 ILKGGTVVnpdgegradIGiRDGRIAAIG-------DLSGASAGEVIDCRGLHVLPGVIDSQVH 64
 
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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