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Conserved domains on  [gi|311033395|sp|Q96NU7|]
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RecName: Full=Probable imidazolonepropionase; AltName: Full=Amidohydrolase domain-containing protein 1

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: 532.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  43 VVGKDGFIKAIGPADVIQRqfSGETFEEIIDCSGKCILPGLVDAHTHPVWAGERVHEFAMKLAGATYMEIHQAGGGIHFT 122
Cdd:cd01296    1 IAIRDGRIAAVGPAASLPA--PGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 123 VERTRQATEEELFRSLQQRLQCMMRAGTTLVECKSGYGLDLETELKMLRVIERARRELDIGISATYCGAHSVPKGKTATE 202
Cdd:cd01296   79 VRATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGRE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 203 AA-DDIINNHLPKLKELGrngeiHVDNIDVFCEKGVFDLDSTRRILQRGKDIGLQINFHGDELHPMKAAELGAELGAQAI 281
Cdd:cd01296  159 EYiDLVIEEVLPAVAEEN-----LADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 282 SHLEEVSDEGIVAMATARCSAILLPTTAYMLRLKQPRARKMLDEGVIVALGSDFNPNAYCF-SMPMVMHLACVNMRMSMP 360
Cdd:cd01296  234 DHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPGSSPTsSMPLVMHLACRLMRMTPE 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 361 EALAAATINAAYALGKSHTHGSLEVGKQGDLIIINSSRWEHLIYQFGGHHelIEYVIAKG 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: 532.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  43 VVGKDGFIKAIGPADVIQRqfSGETFEEIIDCSGKCILPGLVDAHTHPVWAGERVHEFAMKLAGATYMEIHQAGGGIHFT 122
Cdd:cd01296    1 IAIRDGRIAAVGPAASLPA--PGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 123 VERTRQATEEELFRSLQQRLQCMMRAGTTLVECKSGYGLDLETELKMLRVIERARRELDIGISATYCGAHSVPKGKTATE 202
Cdd:cd01296   79 VRATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGRE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 203 AA-DDIINNHLPKLKELGrngeiHVDNIDVFCEKGVFDLDSTRRILQRGKDIGLQINFHGDELHPMKAAELGAELGAQAI 281
Cdd:cd01296  159 EYiDLVIEEVLPAVAEEN-----LADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 282 SHLEEVSDEGIVAMATARCSAILLPTTAYMLRLKQPRARKMLDEGVIVALGSDFNPNAYCF-SMPMVMHLACVNMRMSMP 360
Cdd:cd01296  234 DHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPGSSPTsSMPLVMHLACRLMRMTPE 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 361 EALAAATINAAYALGKSHTHGSLEVGKQGDLIIINSSRWEHLIYQFGGHHelIEYVIAKG 420
Cdd:cd01296  314 EALTAATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNL--VEYVIKNG 371
hutI TIGR01224
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ...
 38-422 2.46e-140

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: 406.03  E-value: 2.46e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395   38 EGASLVVgKDGFIKAIGPadviQRQFSGETFEEIIDCSGKCILPGLVDAHTHPVWAGERVHEFAMKLAGATYMEIHQAGG 117
Cdd:TIGR01224   2 EDAVILI-HGGKIVWIGQ----LAALPGEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  118 GIHFTVERTRQATEEELFRSLQQRLQCMMRAGTTLVECKSGYGLDLETELKMLRVIERARRELDIGISATYCGAHSVPKG 197
Cdd:TIGR01224  77 GILSTVRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  198 KTATEAA--DDIINNHLPKLKElgrngEIHVDNIDVFCEKGVFDLDSTRRILQRGKDIGLQINFHGDELHPMKAAELGAE 275
Cdd:TIGR01224 157 FQGRPDDyvDGICEELIPQVAE-----EGLASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAK 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  276 LGAQAISHLEEVSDEGIVAMATARCSAILLPTTAYMLRLKQPRARKMLDEGVIVALGSDFNP-NAYCFSMPMVMHLACVN 354
Cdd:TIGR01224 232 LGAVSADHLEHASDAGIKALAEAGTVAVLLPGTTFYLRETYPPARQLIDYGVPVALATDLNPgSSPTLSMQLIMSLACRL 311

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311033395  355 MRMSMPEALAAATINAAYALGKSHTHGSLEVGKQGDLIIINSSRWEHLIYQFGGHHelIEYVIAKGKL 422
Cdd:TIGR01224 312 MKMTPEEALHAATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPYHYGVNH--VHAVIKNGNI 377
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 35-426 3.27e-52

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 179.39  E-value: 3.27e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  35 AVLEGASLVVgKDGFIKAIGPADVIQRQFSGEtfeeIIDCSGKCILPGLVDAHTHPVWAGERVHEFAMklagatymeihq 114
Cdd:COG1228   24 GVIENGTVLV-EDGKIAAVGPAADLAVPAGAE----VIDATGKTVLPGLIDAHTHLGLGGGRAVEFEA------------ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 115 aGGGIHFTVERTRQATEeelfrslqqRLQCMMRAGTTLVECKSGYGLDL-----ETELKML---RVIERARreldiGISA 186
Cdd:COG1228   87 -GGGITPTVDLVNPADK---------RLRRALAAGVTTVRDLPGGPLGLrdaiiAGESKLLpgpRVLAAGP-----ALSL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 187 TYcGAHsvpkGKTATEAADdiinnHLPKLKELGrngeihVDNIDVFCEKG--VFDLDSTRRILQRGKDIGLQINFHGDEL 264
Cdd:COG1228  152 TG-GAH----ARGPEEARA-----ALRELLAEG------ADYIKVFAEGGapDFSLEELRAILEAAHALGLPVAAHAHQA 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 265 HPMKAAelgAELGAQAISHLEEVSDEGIVAMAtARCSAILLPTTAYMLRL------------------KQPRARKMLDEG 326
Cdd:COG1228  216 DDIRLA---VEAGVDSIEHGTYLDDEVADLLA-EAGTVVLVPTLSLFLALlegaaapvaakarkvreaALANARRLHDAG 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 327 VIVALGSDFN-PNAYCFSMPMVMHLAcVNMRMSMPEALAAATINAAYALGKSHTHGSLEVGKQGDLIIINSSRWEHLIYq 405
Cdd:COG1228  292 VPVALGTDAGvGVPPGRSLHRELALA-VEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY- 369

                        410       420
                 ....*....|....*....|.
gi 311033395 406 fgghHELIEYVIAKGKLIYKT 426
Cdd:COG1228  370 ----LEDVRAVMKDGRVVDRS 386
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 79-423 4.12e-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: 51.73  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395   79 ILPGLVDAHTHpvwagervhefamklagatymeihqagggIHFTVERTRQATEEELFRSLQQRLQCMMRAGTTLVeCKSG 158
Cdd:pfam01979   2 VLPGLIDAHVH-----------------------------LEMGLLRGIPVPPEFAYEALRLGITTMLKSGTTTV-LDMG 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  159 YGldleTELKMLRVIErARRELDIGIsaTYCGAHSVPKGKTATEAADDIINNHLPKL-KELGRNGEIHVDNIDVFcEKGV 237
Cdd:pfam01979  52 AT----TSTGIEALLE-AAEELPLGL--RFLGPGCSLDTDGELEGRKALREKLKAGAeFIKGMADGVVFVGLAPH-GAPT 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  238 FDLDSTRRILQRGKDIGLQINFHGDEL-HPMKAAELGAELGAQAISHLE---EVSDEGIVAMATARC------SAILLPT 307
Cdd:pfam01979 124 FSDDELKAALEEAKKYGLPVAIHALETkGEVEDAIAAFGGGIEHGTHLEvaeSGGLLDIIKLILAHGvhlsptEANLLAE 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  308 TAYMLRL------------KQPRARKMLDEGVIVALGSDFNPNAYCFSMPMVMHLAC-----VNMRMSMPEALAAATINA 370
Cdd:pfam01979 204 HLKGAGVahcpfsnsklrsGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALelqfdPEGGLSPLEALRMATINP 283

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 311033395  371 AYALGKSHTHGSLEVGKQGDLIIINSSRWEHLIYQFGGhhELIEYVIAKGKLI 423
Cdd:pfam01979 284 AKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPD--GNVKKVIVKGKIV 334
PRK09228 PRK09228
guanine deaminase; Provisional
 42-89 7.82e-06

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 47.88  E-value: 7.82e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 311033395  42 LVVGKDGFIKAIGPADVIQRQFSGETfeEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK09228  33 LLLVEDGRIVAAGPYAELRAQLPADA--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: 532.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  43 VVGKDGFIKAIGPADVIQRqfSGETFEEIIDCSGKCILPGLVDAHTHPVWAGERVHEFAMKLAGATYMEIHQAGGGIHFT 122
Cdd:cd01296    1 IAIRDGRIAAVGPAASLPA--PGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILST 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 123 VERTRQATEEELFRSLQQRLQCMMRAGTTLVECKSGYGLDLETELKMLRVIERARRELDIGISATYCGAHSVPKGKTATE 202
Cdd:cd01296   79 VRATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGRE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 203 AA-DDIINNHLPKLKELGrngeiHVDNIDVFCEKGVFDLDSTRRILQRGKDIGLQINFHGDELHPMKAAELGAELGAQAI 281
Cdd:cd01296  159 EYiDLVIEEVLPAVAEEN-----LADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 282 SHLEEVSDEGIVAMATARCSAILLPTTAYMLRLKQPRARKMLDEGVIVALGSDFNPNAYCF-SMPMVMHLACVNMRMSMP 360
Cdd:cd01296  234 DHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPGSSPTsSMPLVMHLACRLMRMTPE 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 361 EALAAATINAAYALGKSHTHGSLEVGKQGDLIIINSSRWEHLIYQFGGHHelIEYVIAKG 420
Cdd:cd01296  314 EALTAATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNL--VEYVIKNG 371
hutI TIGR01224
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ...
 38-422 2.46e-140

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: 406.03  E-value: 2.46e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395   38 EGASLVVgKDGFIKAIGPadviQRQFSGETFEEIIDCSGKCILPGLVDAHTHPVWAGERVHEFAMKLAGATYMEIHQAGG 117
Cdd:TIGR01224   2 EDAVILI-HGGKIVWIGQ----LAALPGEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  118 GIHFTVERTRQATEEELFRSLQQRLQCMMRAGTTLVECKSGYGLDLETELKMLRVIERARRELDIGISATYCGAHSVPKG 197
Cdd:TIGR01224  77 GILSTVRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  198 KTATEAA--DDIINNHLPKLKElgrngEIHVDNIDVFCEKGVFDLDSTRRILQRGKDIGLQINFHGDELHPMKAAELGAE 275
Cdd:TIGR01224 157 FQGRPDDyvDGICEELIPQVAE-----EGLASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAK 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  276 LGAQAISHLEEVSDEGIVAMATARCSAILLPTTAYMLRLKQPRARKMLDEGVIVALGSDFNP-NAYCFSMPMVMHLACVN 354
Cdd:TIGR01224 232 LGAVSADHLEHASDAGIKALAEAGTVAVLLPGTTFYLRETYPPARQLIDYGVPVALATDLNPgSSPTLSMQLIMSLACRL 311

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311033395  355 MRMSMPEALAAATINAAYALGKSHTHGSLEVGKQGDLIIINSSRWEHLIYQFGGHHelIEYVIAKGKL 422
Cdd:TIGR01224 312 MKMTPEEALHAATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPYHYGVNH--VHAVIKNGNI 377
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 35-426 3.27e-52

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 179.39  E-value: 3.27e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  35 AVLEGASLVVgKDGFIKAIGPADVIQRQFSGEtfeeIIDCSGKCILPGLVDAHTHPVWAGERVHEFAMklagatymeihq 114
Cdd:COG1228   24 GVIENGTVLV-EDGKIAAVGPAADLAVPAGAE----VIDATGKTVLPGLIDAHTHLGLGGGRAVEFEA------------ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 115 aGGGIHFTVERTRQATEeelfrslqqRLQCMMRAGTTLVECKSGYGLDL-----ETELKML---RVIERARreldiGISA 186
Cdd:COG1228   87 -GGGITPTVDLVNPADK---------RLRRALAAGVTTVRDLPGGPLGLrdaiiAGESKLLpgpRVLAAGP-----ALSL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 187 TYcGAHsvpkGKTATEAADdiinnHLPKLKELGrngeihVDNIDVFCEKG--VFDLDSTRRILQRGKDIGLQINFHGDEL 264
Cdd:COG1228  152 TG-GAH----ARGPEEARA-----ALRELLAEG------ADYIKVFAEGGapDFSLEELRAILEAAHALGLPVAAHAHQA 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 265 HPMKAAelgAELGAQAISHLEEVSDEGIVAMAtARCSAILLPTTAYMLRL------------------KQPRARKMLDEG 326
Cdd:COG1228  216 DDIRLA---VEAGVDSIEHGTYLDDEVADLLA-EAGTVVLVPTLSLFLALlegaaapvaakarkvreaALANARRLHDAG 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 327 VIVALGSDFN-PNAYCFSMPMVMHLAcVNMRMSMPEALAAATINAAYALGKSHTHGSLEVGKQGDLIIINSSRWEHLIYq 405
Cdd:COG1228  292 VPVALGTDAGvGVPPGRSLHRELALA-VEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY- 369

                        410       420
                 ....*....|....*....|.
gi 311033395 406 fgghHELIEYVIAKGKLIYKT 426
Cdd:COG1228  370 ----LEDVRAVMKDGRVVDRS 386
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 24-425 1.48e-18

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: 87.19  E-value: 1.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  24 RFLARDAL-----RSLAVLEGASLVVgKDGFIKAIGPADVIQRQFSGEtfeEIIDCSGKCILPGLVDAHTHpvwagervh 98
Cdd:COG0402    1 DLLIRGAWvltmdPAGGVLEDGAVLV-EDGRIAAVGPGAELPARYPAA---EVIDAGGKLVLPGLVNTHTH--------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  99 eFAMKL--AGATYMEIHQAGGGIHFTVERtrQATEEELFRSLQQRLQCMMRAGTTLVecksgygLDLETELK--MLRVIE 174
Cdd:COG0402   68 -LPQTLlrGLADDLPLLDWLEEYIWPLEA--RLDPEDVYAGALLALAEMLRSGTTTV-------ADFYYVHPesADALAE 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 175 RARrelDIGISATYC-GAHSVPKGKTATEAADDIINNHLPKLKEL--GRNGEIHVdnidVFCEKGVF--DLDSTRRI--L 247
Cdd:COG0402  138 AAA---EAGIRAVLGrGLMDRGFPDGLREDADEGLADSERLIERWhgAADGRIRV----ALAPHAPYtvSPELLRAAaaL 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 248 QRGKDIGLQINFHGD--------ELHPMKAAELGAELG--------AQAIsHLeevSDEGIVAMATARCSAILLPTTAYM 311
Cdd:COG0402  211 ARELGLPLHTHLAETrdevewvlELYGKRPVEYLDELGllgprtllAHCV-HL---TDEEIALLAETGASVAHCPTSNLK 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 312 LRLKQPRARKMLDEGVIVALGSDFNPNAYCFSMPMVMHLACVNMR--------MSMPEALAAATINAAYALGKSHTHGSL 383
Cdd:COG0402  287 LGSGIAPVPRLLAAGVRVGLGTDGAASNNSLDMFEEMRLAALLQRlrggdptaLSAREALEMATLGGARALGLDDEIGSL 366

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 311033395 384 EVGKQGDLIIINSSRWE---------HLIYQFGGHHelIEYVIAKGKLIYK 425
Cdd:COG0402  367 EPGKRADLVVLDLDAPHlaplhdplsALVYAADGRD--VRTVWVAGRVVVR 415
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 43-423 2.58e-11

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: 64.96  E-value: 2.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  43 VVGKDGFIKAIGPADviqrqfSGETFEEIIDCSGKCILPGLVDAHTH--PVWAGERVHEFamklAGATYMEIHQAgggih 120
Cdd:cd01293   17 IAIEDGRIAAIGPAL------AVPPDAEEVDAKGRLVLPAFVDPHIHldKTFTGGRWPNN----SGGTLLEAIIA----- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 121 fTVERTRQATEEELFRSLQQRLQCMMRAGTTL----VECksgyglDLETELKMLRVIERARRE----LDIGISA-----T 187
Cdd:cd01293   82 -WEERKLLLTAEDVKERAERALELAIAHGTTAirthVDV------DPAAGLKALEALLELREEwadlIDLQIVAfpqhgL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 188 YCGAHSVPKGKTATEAADDIINNhLPKLkELGRNGEIHVDNIdvfcekgvFDLDStrrilQRGKDIGLQINFHGDEL--H 265
Cdd:cd01293  155 LSTPGGEELMREALKMGADVVGG-IPPA-EIDEDGEESLDTL--------FELAQ-----EHGLDIDLHLDETDDPGsrT 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 266 PMKAAELGAELGAQ---AISHL-------EEVSDEGIVAMATARCSAILLPTTAYMLRLKQ---------PRARKMLDEG 326
Cdd:cd01293  220 LEELAEEAERRGMQgrvTCSHAtalgslpEAEVSRLADLLAEAGISVVSLPPINLYLQGREdttpkrrgvTPVKELRAAG 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 327 VIVALGSD-----FNPNAyCFSMPMVMHLACVNMRMSMPEALAAAT----INAAYALGKshTHGSLEVGKQGDLIIINSS 397
Cdd:cd01293  300 VNVALGSDnvrdpWYPFG-SGDMLEVANLAAHIAQLGTPEDLALALdlitGNAARALGL--EDYGIKVGCPADLVLLDAE 376

                        410       420
                 ....*....|....*....|....*.
gi 311033395 398 RWEHLIYqfGGHHELIeyVIAKGKLI 423
Cdd:cd01293  377 DVAEAVA--RQPPRRV--VIRKGRVV 398
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 83-351 8.74e-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: 8.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  83 LVDAHTHPVWAGERVHEFAMKLAGATYMEIHQagggihfTVERTRQATEEelfrslqqrlqcMMRAGTTLVECKSGYGLD 162
Cdd:cd01292    1 FIDTHVHLDGSALRGTRLNLELKEAEELSPED-------LYEDTLRALEA------------LLAGGVTTVVDMGSTPPP 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 163 LETELKMLRVIERARRELDIGISATYCGAHSVPKGKTATEAaddiinnHLPKLKELGRNGEIHVDNIDVFCEKGVFDLDS 242
Cdd:cd01292   62 TTTKAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEA-------LLLELLRRGLELGAVGLKLAGPYTATGLSDES 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 243 TRRILQRGKDIGLQINFH----GDELHPMKAAELGAELGAQ-AISHLEEVSDEGIVAMATARCSAILLPTTAYMLRLK-- 315
Cdd:cd01292  135 LRRVLEEARKLGLPVVIHagelPDPTRALEDLVALLRLGGRvVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRDge 214

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 311033395 316 -QPRARKMLDEGVIVALGSDFNPNAYCFSMPMVMHLA 351
Cdd:cd01292  215 gAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLL 251
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
46-95 1.12e-09

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 60.20  E-value: 1.12e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 311033395  46 KDGFIKAIGPADVIQRQFSGETfeEIIDCSGKCILPGLVDAHTHPVWAGE 95
Cdd:COG1574   33 RDGRIVAVGSDAEVRALAGPAT--EVIDLGGKTVLPGFIDAHVHLLGGGL 80
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 7-425 3.98e-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: 54.90  E-value: 3.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395   7 LLLENAQQVVLVCARgerflardalrslaVLEGASLVVgKDGFIKAIGPADViQRQFSGEtfeEIIDCSGKCILPGLVDA 86
Cdd:cd01298    1 ILIRNGTIVTTDPRR--------------VLEDGDVLV-EDGRIVAVGPALP-LPAYPAD---EVIDAKGKVVMPGLVNT 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  87 HTHpvwagervheFAMKL-----AGATYMEIHQAgggihfTVERTRQATEEELFRsLQQRLQC--MMRAGTTLVecksgy 159
Cdd:cd01298   62 HTH----------LAMTLlrglaDDLPLMEWLKD------LIWPLERLLTEEDVY-LGALLALaeMIRSGTTTF------ 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 160 gldLETELKMLRVIERARRELdiGISATYCGAhSVPKGKTATEAADDIINNHLPKLKE--LGRNGEIHVdnidVFCEKGV 237
Cdd:cd01298  119 ---ADMYFFYPDAVAEAAEEL--GIRAVLGRG-IMDLGTEDVEETEEALAEAERLIREwhGAADGRIRV----ALAPHAP 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 238 FDL--DSTRRILQRGKDIGLQINFHG----DELHPMKA----------AELGAeLGAQAI-SHLEEVSDEGIVAMATARC 300
Cdd:cd01298  189 YTCsdELLREVAELAREYGVPLHIHLaeteDEVEESLEkygkrpveylEELGL-LGPDVVlAHCVWLTDEEIELLAETGT 267

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 301 SAILLPTTAYMLRLKQPRARKMLDEGVIVALGSD-----------------------FNPNAYCFSMPMVMHLACVNMR- 356
Cdd:cd01298  268 GVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDgaasnnnldmfeemrlaallqklAHGDPTALPAEEALEMATIGGAk 347

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 311033395 357 -MSMPEAlaaatinaayalgkshthGSLEVGKQGDLIIINSSR---------WEHLIYqfGGHHELIEYVIAKGKLIYK 425
Cdd:cd01298  348 aLGLDEI------------------GSLEVGKKADLILIDLDGphllpvhdpISHLVY--SANGGDVDTVIVNGRVVME 406
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 46-89 5.16e-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: 54.71  E-value: 5.16e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 311033395  46 KDGFIKAIGPADviqrqfSGETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:COG0044   21 EDGRIAAIGPDL------AAPEAAEVIDATGLLVLPGLIDLHVH 58
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 43-94 1.10e-07

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: 53.85  E-value: 1.10e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 311033395  43 VVGKDGFIKAIGPADVIQRQFSGETfeEIIDCSGKCILPGLVDAHTHPVWAG 94
Cdd:cd01300    2 VAVRDGRIVAVGSDAEAKALKGPAT--EVIDLKGKTVLPGFIDSHSHLLLGG 51
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 79-423 4.12e-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: 51.73  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395   79 ILPGLVDAHTHpvwagervhefamklagatymeihqagggIHFTVERTRQATEEELFRSLQQRLQCMMRAGTTLVeCKSG 158
Cdd:pfam01979   2 VLPGLIDAHVH-----------------------------LEMGLLRGIPVPPEFAYEALRLGITTMLKSGTTTV-LDMG 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  159 YGldleTELKMLRVIErARRELDIGIsaTYCGAHSVPKGKTATEAADDIINNHLPKL-KELGRNGEIHVDNIDVFcEKGV 237
Cdd:pfam01979  52 AT----TSTGIEALLE-AAEELPLGL--RFLGPGCSLDTDGELEGRKALREKLKAGAeFIKGMADGVVFVGLAPH-GAPT 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  238 FDLDSTRRILQRGKDIGLQINFHGDEL-HPMKAAELGAELGAQAISHLE---EVSDEGIVAMATARC------SAILLPT 307
Cdd:pfam01979 124 FSDDELKAALEEAKKYGLPVAIHALETkGEVEDAIAAFGGGIEHGTHLEvaeSGGLLDIIKLILAHGvhlsptEANLLAE 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  308 TAYMLRL------------KQPRARKMLDEGVIVALGSDFNPNAYCFSMPMVMHLAC-----VNMRMSMPEALAAATINA 370
Cdd:pfam01979 204 HLKGAGVahcpfsnsklrsGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALelqfdPEGGLSPLEALRMATINP 283

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 311033395  371 AYALGKSHTHGSLEVGKQGDLIIINSSRWEHLIYQFGGhhELIEYVIAKGKLI 423
Cdd:pfam01979 284 AKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPD--GNVKKVIVKGKIV 334
Amidohydro_3 pfam07969
Amidohydrolase family;
158-424 1.33e-06

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 50.22  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  158 GYGLDLETELKMLRVIERAR-RELDIGISATycgahsvpkGKTATEAADDIINNHLPKLKELGRNGEIHVDNIdvfcekG 236
Cdd:pfam07969 241 GTGWPDFEDEALAELVAAAReRGLDVAIHAI---------GDATIDTALDAFEAVAEKLGNQGRVRIEHAQGV------V 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  237 VFDLDSTRRILQRGKDIGLQINFHgdelhPMKAAELGAELGAQAISHLeevsdegivamatarcsaillpttaymlrlkq 316
Cdd:pfam07969 306 PYTYSQIERVAALGGAAGVQPVFD-----PLWGDWLQDRLGAERARGL-------------------------------- 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  317 PRARKMLDEGVIVALGSDFNPNAYC---FSMPMVMHLACVNM-------RMSMPEALAAATINAAYALGKSHTHGSLEVG 386
Cdd:pfam07969 349 TPVKELLNAGVKVALGSDAPVGPFDpwpRIGAAVMRQTAGGGevlgpdeELSLEEALALYTSGPAKALGLEDRKGTLGVG 428

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 311033395  387 KQGDLIIINSSRW----EHLiyqfggHHELIEYVIAKGKLIY 424
Cdd:pfam07969 429 KDADLVVLDDDPLtvdpPAI------ADIRVRLTVVDGRVVY 464
PRK09228 PRK09228
guanine deaminase; Provisional
 42-89 7.82e-06

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 47.88  E-value: 7.82e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 311033395  42 LVVGKDGFIKAIGPADVIQRQFSGETfeEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK09228  33 LLLVEDGRIVAAGPYAELRAQLPADA--EVTDYRGKLILPGFIDTHIH 78
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 46-89 1.16e-05

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: 47.21  E-value: 1.16e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 311033395  46 KDGFIKAIGPAdviqrqFSGETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:cd01314   22 EDGKIVAIGPN------LEAPGGVEVIDATGKYVLPGGIDPHTH 59
pyrC PRK09357
dihydroorotase; Validated
 46-89 1.88e-05

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 46.73  E-value: 1.88e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 311033395  46 KDGFIKAIGPADviqrqfsGETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK09357  25 DDGKIAAIGENI-------EAEGAEVIDATGLVVAPGLVDLHVH 61
PRK08323 PRK08323
phenylhydantoinase; Validated
 46-89 3.06e-05

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 45.93  E-value: 3.06e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 311033395  46 KDGFIKAIGPADViqrqfsgetfEEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK08323  24 EDGKIAAIGANLG----------DEVIDATGKYVMPGGIDPHTH 57
PRK05985 PRK05985
cytosine deaminase; Provisional
 46-186 4.54e-05

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 45.31  E-value: 4.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  46 KDGFIKAIGPAdviqrqFSGETFEEIIDCSGKCILPGLVDAHTHP---VWaGERVHEfamklagatymeiHQAGGGIH-- 120
Cdd:PRK05985  22 RDGRIAAIGPA------LAAPPGAEVEDGGGALALPGLVDGHIHLdktFW-GDPWYP-------------NEPGPSLRer 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311033395 121 --FTVERTRQATEEELFRSLQQRLQCMMRaGTTLVEC----KSGYGLD-LETelkMLRVIERARRELDIGISA 186
Cdd:PRK05985  82 iaNERRRRAASGHPAAERALALARAAAAA-GTTAMRShvdvDPDAGLRhLEA---VLAARETLRGLIDIQIVA 150
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
36-89 5.24e-05

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 45.09  E-value: 5.24e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 311033395  36 VLEGASLVVgKDGFIKAIGPADviqrqfsgETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:COG1820   13 VLEDGALLI-EDGRIAAIGPGA--------EPDAEVIDLGGGYLAPGFIDLHVH 57
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 40-89 6.50e-05

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: 44.97  E-value: 6.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 311033395  40 ASLVVgKDGFIKAIGPADviqrqfSGETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:cd01315   18 ADIAV-KGGKIAAIGPDI------ANTEAEEVIDAGGLVVMPGLIDTHVH 60
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
 43-98 6.93e-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: 44.63  E-value: 6.93e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 311033395  43 VVGKDGFIKAIGPADVIQRQfsgetfEEIIDCSGKCILPGLVDAHTHPVWAGERVH 98
Cdd:cd01307    2 VAIENGKIAAVGAALAAPAA------TQIVDAGGCYVSPGWIDLHVHVYQGGTRYG 51
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 70-153 1.31e-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: 43.82  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  70 EIIDCSGKCILPGLVDAHTHPVWAGERvhefamklagatymeihqagggihfTVERTRQATEEELFRSLQQrLQCMMRAG 149
Cdd:cd01299    2 QVIDLGGKTLMPGLIDAHTHLGSDPGD-------------------------LPLDLALPVEYRTIRATRQ-ARAALRAG 55


                 ....
gi 311033395 150 TTLV 153
Cdd:cd01299   56 FTTV 59
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 37-89 1.48e-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: 43.72  E-value: 1.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 311033395  37 LEGASLVVgKDGFIKAIGPADviqrqfSGETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:cd00854   14 LEDGAVLV-EDGKIVAIGPED------ELEEADEIIDLKGQYLVPGFIDIHIH 59
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
35-89 3.37e-04

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 42.59  E-value: 3.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 311033395  35 AVLEGASLVVgKDGFIKAIGPADVIQRQFsgeTFEEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK09045  24 VVLEDHAVAI-RDGRIVAILPRAEARARY---AAAETVELPDHVLIPGLINAHTH 74
PRK06687 PRK06687
TRZ/ATZ family protein;
42-402 3.97e-04

TRZ/ATZ family protein;


Pssm-ID: 180657 [Multi-domain]  Cd Length: 419  Bit Score: 42.30  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  42 LVVGKDGFIKAIGPADviqrQFSGETFEEIIDCSGKCILPGLVDAHTHPVWAGER-------VHEfamklagatYMEIHQ 114
Cdd:PRK06687  23 ILAVKDSQIVYVGQDK----PAFLEQAEQIIDYQGAWIMPGLVNCHTHSAMTGLRgirddsnLHE---------WLNDYI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 115 AGGGIHFTVERTRQATEEELFRSLQQrlqcmmrAGTTLVECKSGYGLDLETELKMLR----------------------V 172
Cdd:PRK06687  90 WPAESEFTPDMTTNAVKEALTEMLQS-------GTTTFNDMYNPNGVDIQQIYQVVKtskmrcyfsptlfssetettaeT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 173 IERARRELDIGISATYCGAHSVPKGKTATEAADDIINNHLPKLKELgrNGEIHVDNIDVFCEKGVFDLDSTRRILQRGKD 252
Cdd:PRK06687 163 ISRTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKEL--NIPLHVHVAETKEESGIILKRYGKRPLAFLEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 253 IGL----QINFHGDELHPMKAAELGAE---LGAQAISHLEEVSDEGIVAMATARCSAILLPTTAymlrLKQPRARKMLDE 325
Cdd:PRK06687 241 LGYldhpSVFAHGVELNEREIERLASSqvaIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDS----VASNNNLDMFEE 316

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311033395 326 GVIVALGSDFNP-NAYCFSMPMVMHLACVNmrmsmpealaaatinAAYALGKSHTHGSLEVGKQGDLIIINSSRWEHL 402
Cdd:PRK06687 317 GRTAALLQKMKSgDASQFPIETALKVLTIE---------------GAKALGMENQIGSLEVGKQADFLVIQPQGKIHL 379
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
 69-425 4.13e-04

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 42.56  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  69 EEIIDCSGKCILPGLVDAHTHPVWAGER-------VHEFAMKlagatymeihqagggihfTVERTRQATEEELFRSLQQR 141
Cdd:PRK06380  42 DYIIDATGKVVMPGLINTHAHVGMTASKglfddvdLEEFLMK------------------TFKYDSKRTREGIYNSAKLG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 142 LQCMMRAGTTLVecksgygLDLETELKmlrVIERARREldIGISAtYCGAHSVPKGKTATEA-----ADDIINNHlpklk 216
Cdd:PRK06380 104 MYEMINSGITAF-------VDLYYSED---IIAKAAEE--LGIRA-FLSWAVLDEEITTQKGdplnnAENFIREH----- 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 217 elgRNGEIHVDNIDVfceKGVF--DLDSTRRILQRGKDIGLQINFHGDELHPmKAAELGAELGAQAISHLEEV---SDEG 291
Cdd:PRK06380 166 ---RNEELVTPSIGV---QGIYvaNDETYLKAKEIAEKYDTIMHMHLSETRK-EVYDHVKRTGERPVEHLEKIgflNSKL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 292 IVA---MATARCSAILL---------PTTAYMLRLK-QPRARKMLDEGVIVALGSDFNPNAYCFSMPMVMHLACV---NM 355
Cdd:PRK06380 239 IAAhcvWATYHEIKLLSkngvkvswnSVSNFKLGTGgSPPIPEMLDNGINVTIGTDSNGSNNSLDMFEAMKFSALsvkNE 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395 356 R-----MSMPEALAAATINAAYALgkSHTHGSLEVGKQGDLIIINSSRWEHLIYQ---------FGGHHELIEYVIAKGK 421
Cdd:PRK06380 319 RwdasiIKAQEILDFATINAAKAL--ELNAGSIEVGKLADLVILDARAPNMIPTRknnivsnivYSLNPLNVDHVIVNGK 396


                 ....
gi 311033395 422 LIYK 425
Cdd:PRK06380 397 ILKE 400
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
46-94 6.41e-04

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 41.69  E-value: 6.41e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 311033395  46 KDGFIKAIGPADVIQRQfsgetfEEIIDCSGKCILPGLVDAHTHpVWAG 94
Cdd:COG3964   25 KDGKIAAVAKDIDAAEA------KKVIDASGLYVTPGLIDLHTH-VFPG 66
PRK07203 PRK07203
putative aminohydrolase SsnA;
24-89 8.81e-04

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 41.46  E-value: 8.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311033395  24 RFLARDALRSlaVLEGASLVVgKDGFIKAIGPADVIQRQFSGEtfeEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK07203   8 TAITRDPAKP--VIEDGAIAI-EGNVIVEIGTTDELKAKYPDA---EFIDAKGKLIMPGLINSHNH 67
PRK09060 PRK09060
dihydroorotase; Validated
 46-89 1.00e-03

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 41.06  E-value: 1.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 311033395  46 KDGFIKAIGpadviqrQFSGETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK09060  28 RDGRIAAIG-------DLSGASAGEVIDCRGLHVLPGVIDSQVH 64
PRK02382 PRK02382
dihydroorotase; Provisional
 46-89 1.26e-03

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 40.79  E-value: 1.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 311033395  46 KDGFIKAIGpadviqRQFSGETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK02382  25 DGGKITAVG------KDLDGSSSEEVIDARGMLLLPGGIDVHVH 62
PRK08204 PRK08204
hypothetical protein; Provisional
 21-130 1.36e-03

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 40.76  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  21 RGERFLARDAlrSLAVLEGASLVVgKDGFIKAIGPAdvIQrqfSGETfeEIIDCSGKCILPGLVDAHTHpVWagervhEF 100
Cdd:PRK08204   7 RGGTVLTMDP--AIGDLPRGDILI-EGDRIAAVAPS--IE---APDA--EVVDARGMIVMPGLVDTHRH-TW------QS 69

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 311033395 101 AMKLAGA-----TYMEIHQAGGGIHFTVERTRQAT 130
Cdd:PRK08204  70 VLRGIGAdwtlqTYFREIHGNLGPMFRPEDVYIAN 104
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 69-89 1.45e-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: 40.68  E-value: 1.45e-03
                         10        20
                 ....*....|....*....|.
gi 311033395  69 EEIIDCSGKCILPGLVDAHTH 89
Cdd:cd01317    2 AEVIDAEGKILAPGLVDLHVH 22
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
46-98 1.56e-03

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 40.60  E-value: 1.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 311033395  46 KDGFIKAIGPAdviqrqFSGETFEEIIDCSGKCILPGLVDAHTHPVWAGERVH 98
Cdd:PRK09237  24 EDGKIAAVAGD------IDGSQAKKVIDLSGLYVSPGWIDLHVHVYPGSTPYG 70
PLN02942 PLN02942
dihydropyrimidinase
 43-112 2.03e-03

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 40.21  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  43 VVGKDGFIKAIGP-----ADVIqrqfsgetfeeIIDCSGKCILPGLVDAHTH---PVWAGERVHEF----AMKLAGATYM 110
Cdd:PLN02942  25 VYVEDGIIVAVAPnlkvpDDVR-----------VIDATGKFVMPGGIDPHTHlamPFMGTETIDDFfsgqAAALAGGTTM 93


                 ..
gi 311033395 111 EI 112
Cdd:PLN02942  94 HI 95
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
 47-89 2.84e-03

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: 39.68  E-value: 2.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 311033395   47 DGFIKAIGPADVIQRQFsgetfeEIIDCSGKCILPGLVDAHTH 89
Cdd:TIGR02033  23 GGKIVAVGDNLIPPDAV------EVIDATGKYVLPGGIDVHTH 59
PRK08044 PRK08044
allantoinase AllB;
34-89 3.04e-03

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 39.84  E-value: 3.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 311033395  34 LAVLEGASLVVG---KDGFIKAIGpadviqrQFSGETfEEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK08044  11 TVILENEARVVDiavKGGKIAAIG-------QDLGDA-KEVMDASGLVVSPGMVDAHTH 61
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 36-88 3.12e-03

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 39.39  E-value: 3.12e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 311033395  36 VLEGaSLVVgKDGFIKAIGPAdviqrqfsGETFEEIIDCSGKCILPGLVDAHT 88
Cdd:PRK15446  17 VVDG-SLLI-EDGRIAAIDPG--------ASALPGAIDAEGDYLLPGLVDLHT 59
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 47-89 4.29e-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: 39.22  E-value: 4.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 311033395  47 DGFIKAIG-----PADViqrqfsgetfeEIIDCSGKCILPGLVDAHTH 89
Cdd:cd01309    1 DGKIVAVGaeittPADA-----------EVIDAKGKHVTPGLIDAHSH 37
PRK09059 PRK09059
dihydroorotase; Validated
 37-119 4.57e-03

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 39.25  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  37 LEGASLVVGKDGFIKAIGPAdvIQRQFSGETfEEIIDCSGKCILPGLVDAHthpVWAGERVHEFAMKLAGATYMeihQAG 116
Cdd:PRK09059  19 LDEIGTVLIEDGVIVAAGKG--AGNQGAPEG-AEIVDCAGKAVAPGLVDAR---VFVGEPGAEHRETIASASRA---AAA 89


                 ...
gi 311033395 117 GGI 119
Cdd:PRK09059  90 GGV 92
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 20-89 5.13e-03

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


Pssm-ID: 238628 [Multi-domain]  Cd Length: 429  Bit Score: 38.80  E-value: 5.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311033395  20 ARGERFLARDALRslaVLEGASLVVGkDGFIKAIGPADVIQRQFSGETfeEIIDCSGKCILPGLVDAHTH 89
Cdd:cd01303   10 SLPELELVEDALR---VVEDGLIVVV-DGNIIAAGAAETLKRAAKPGA--RVIDSPNQFILPGFIDTHIH 73
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 37-89 6.42e-03

dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273302 [Multi-domain]  Cd Length: 411  Bit Score: 38.58  E-value: 6.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 311033395   37 LEGASLVvgKDGFIKAIG----PADviqrqfsgetfEEIIDCSGKCILPGLVDAHTH 89
Cdd:TIGR00857   4 TEVDILV--EGGRIKKIGklriPPD-----------AEVIDAKGLLVLPGFIDLHVH 47
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
36-91 8.04e-03

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 38.44  E-value: 8.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 311033395  36 VLEGASLVvgKDGFIKAIGPADVIQRqfsgetFEEIIDCSGKCILPGLVDAHTHPV 91
Cdd:PRK07228  19 IVDGDVLI--EDDRIAAVGDRLDLED------YDDHIDATGKVVIPGLIQGHIHLC 66
 
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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