|
Name |
Accession |
Description |
Interval |
E-value |
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
1-567 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 1206.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 1 MADISRRAYADMFGPTTGDKVRLADSELWIEVEDDLTIYGEEVKFGGGKVIRDGMGQGQ-MTADDCVDLVLTNALIVDHW 79
Cdd:PRK13207 1 MAKISRRAYAEMYGPTTGDRVRLADTELWIEVEKDFTTYGEEVKFGGGKVIRDGMGQSQrARADGAVDTVITNALILDHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 80 GIVKADIGVKNGRIFAVGKAGNPDIQPGVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMIGGGT 159
Cdd:PRK13207 81 GIVKADIGIKDGRIVAIGKAGNPDIQDGVDIIIGPGTEVIAGEGLIVTAGGIDTHIHFICPQQIEEALASGVTTMIGGGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 160 GPAAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPAALREQIAAGAIGLKIHEDWGATPAAINCSLEVAEEM 239
Cdd:PRK13207 161 GPATGTNATTCTPGPWHIHRMLQAADAFPMNIGFLGKGNASLPEALEEQIEAGAIGLKLHEDWGATPAAIDNCLSVADEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 240 DIQVALHSDTLNESGFVEDTLAAIAGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDMLMVC 319
Cdd:PRK13207 241 DVQVAIHTDTLNESGFVEDTIAAFKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDMLMVC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 320 HHLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVIIRTWQVAHRMKVQRGALPEETGDNDNFR 399
Cdd:PRK13207 321 HHLDPSIPEDVAFAESRIRRETIAAEDILHDLGAISMISSDSQAMGRVGEVIIRTWQTAHKMKVQRGPLPGDSGRNDNFR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 400 VKRYVAKYTINPALTHGIAHEVGSIETGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYRPMFGS 479
Cdd:PRK13207 401 VKRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWKPAFFGVKPELVLKGGMIAWAPMGDPNASIPTPQPVHYRPMFGA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 480 LGAARHSTRLTFVSQAAHANGIPQQLNLQSATAVVKGCRTVKKADMIHNALQPNITVDSQTYEVRVDGELITSEPADVLP 559
Cdd:PRK13207 481 YGGALAATSVTFVSQAALDAGIPEKLGLKKRLVPVKNTRGITKADMKLNDATPKIEVDPETYEVRADGELLTCEPATVLP 560
|
....*...
gi 1513190841 560 MAQRYFLF 567
Cdd:PRK13207 561 LAQRYFLF 568
|
|
| UreC |
COG0804 |
Urease alpha subunit [Amino acid transport and metabolism]; |
1-567 |
0e+00 |
|
Urease alpha subunit [Amino acid transport and metabolism];
Pssm-ID: 440567 [Multi-domain] Cd Length: 570 Bit Score: 1198.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 1 MADISRRAYADMFGPTTGDKVRLADSELWIEVEDDLTIYGEEVKFGGGKVIRDGMGQGQMT-ADDCVDLVLTNALIVDHW 79
Cdd:COG0804 1 MAKISRKAYADLYGPTTGDRVRLADTDLFIEVEKDLTTYGDEVKFGGGKVIRDGMGQSQTTrAEGALDLVITNAVILDHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 80 GIVKADIGVKNGRIFAVGKAGNPDIQPGVT--IPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMIGG 157
Cdd:COG0804 81 GIVKADIGIKDGRIVGIGKAGNPDTMDGVDpdLVIGPGTEVIAGEGLILTAGGIDTHIHFICPQQIEEALASGITTMIGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 158 GTGPAAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPAALREQIAAGAIGLKIHEDWGATPAAINCSLEVAE 237
Cdd:COG0804 161 GTGPAEGTNATTCTPGPWNIARMLEAADALPMNIGFLGKGNASSPEALEEQIRAGACGLKLHEDWGATPAAIDACLSVAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 238 EMDIQVALHSDTLNESGFVEDTLAAIAGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDMLM 317
Cdd:COG0804 241 EYDVQVAIHTDTLNESGFVEDTIAAIKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDMLM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 318 VCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVIIRTWQVAHRMKVQRGALPEETGDNDN 397
Cdd:COG0804 321 VCHHLDPSIPEDVAFAESRIRPETIAAEDVLHDLGAISMMSSDSQAMGRVGEVITRTWQTAHKMKKQRGPLPGDSGRNDN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 398 FRVKRYVAKYTINPALTHGIAHEVGSIETGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYRPMF 477
Cdd:COG0804 401 FRVKRYVAKYTINPAIAHGISHEVGSVEVGKLADLVLWDPAFFGVKPELVIKGGMIAWAQMGDPNASIPTPQPVHYRPMF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 478 GSLGAARHSTRLTFVSQAAHANGIPQQLNLQSATAVVKGCRTVKKADMIHNALQPNITVDSQTYEVRVDGELITSEPADV 557
Cdd:COG0804 481 GAYGKALAATSVTFVSQAALEAGIAERLGLRKRLLPVKNTRNIGKADMVLNDATPDIEVDPETYEVRVDGELLTCEPATE 560
|
570
....*....|
gi 1513190841 558 LPMAQRYFLF 567
Cdd:COG0804 561 LPLAQRYFLF 570
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
3-566 |
0e+00 |
|
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.
Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 1089.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 3 DISRRAYADMFGPTTGDKVRLADSELWIEVEDDLTIYGEEVKFGGGKVIRDGMGQGQ-MTADDCVDLVLTNALIVDHWGI 81
Cdd:cd00375 1 KISREAYADMYGPTTGDKVRLGDTDLWIEVEKDYTTYGDEVKFGGGKVLRDGMGQSSgYTREDVLDLVITNALIIDYTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 82 VKADIGVKNGRIFAVGKAGNPDIQPGVT--IPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMIGGGT 159
Cdd:cd00375 81 YKADIGIKDGRIVAIGKAGNPDIMDGVTpnMIVGPSTEVIAGEGKIVTAGGIDTHVHFICPQQIEEALASGITTMIGGGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 160 GPAAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPAALREQIAAGAIGLKIHEDWGATPAAINCSLEVAEEM 239
Cdd:cd00375 161 GPAAGTKATTCTPGPWNIKRMLQAADGLPVNIGFLGKGNGSSPDALAEQIEAGACGLKLHEDWGATPAAIDTCLSVADEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 240 DIQVALHSDTLNESGFVEDTLAAIAGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDMLMVC 319
Cdd:cd00375 241 DVQVAIHTDTLNESGFVEDTIAAIKGRTIHTYHTEGAGGGHAPDIIKVAGHPNVLPSSTNPTRPFTVNTLDEHLDMLMVC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 320 HHLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVIIRTWQVAHRMKVQRGALPEETGDNDNFR 399
Cdd:cd00375 321 HHLDPNIPEDVAFAESRIRAETIAAEDVLHDLGAISIMSSDSQAMGRVGEVILRTWQTAHKMKAQRGPLPEDSGDADNFR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 400 VKRYVAKYTINPALTHGIAHEVGSIETGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYRPMFGS 479
Cdd:cd00375 401 VKRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWEPAFFGVKPEMVLKGGFIAYAQMGDPNASIPTPQPVMMRPMFGA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 480 LGAARHSTRLTFVSQAAHANGIPQQLNLQSATAVVKGCRTVKKADMIHNALQPNITVDSQTYEVRVDGELITSEPADVLP 559
Cdd:cd00375 481 HGKAPAATSVTFVSQASLDAGIAEELGLRRRVVAVKNCRGVGKKDMKLNSATPDIEVDPETYEVRVDGELLTCEPADELP 560
|
....*..
gi 1513190841 560 MAQRYFL 566
Cdd:cd00375 561 LAQRYFL 567
|
|
| urease_alph |
TIGR01792 |
urease, alpha subunit; This model describes the urease alpha subunit UreC (designated beta or ... |
3-567 |
0e+00 |
|
urease, alpha subunit; This model describes the urease alpha subunit UreC (designated beta or B chain, UreB in Helicobacter species). Accessory proteins for incorporation of the nickel cofactor are usually found in addition to the urease alpha, beta, and gamma subunits. The trusted cutoff is set above the scores of many reported fragments and of a putative second urease alpha chain in Streptomyces coelicolor. [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 273810 [Multi-domain] Cd Length: 567 Bit Score: 947.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 3 DISRRAYADMFGPTTGDKVRLADSELWIEVEDDLTIYGEEVKFGGGKVIRDGMGQG-QMTAD-DCVDLVLTNALIVDHWG 80
Cdd:TIGR01792 1 KMSREQYASLYGPTTGDKVRLGDTDLFVEVEKDLTTYGDESKFGGGKVLRDGMGQNaTLTRNaGVLDLVITNALILDWTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 81 IVKADIGVKNGRIFAVGKAGNPDIQPGVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMIGGGTG 160
Cdd:TIGR01792 81 IYKADIGIKNGRIVGIGKAGNPDTMDGVDMIVGASTEAISGEGKIVTAGGIDTHVHYISPQQVQAALDNGITTLIGGGTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 161 PAAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPAALREQIAAGAIGLKIHEDWGATPAAINCSLEVAEEMD 240
Cdd:TIGR01792 161 PADGTNATTCTPGPWYLHRMLQAADGLPINFGFTGKGSGSGPAALIEQIEAGACGLKVHEDWGATPAAIDNALSVADEYD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 241 IQVALHSDTLNESGFVEDTLAAIAGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDMLMVCH 320
Cdd:TIGR01792 241 VQVAVHTDTLNESGFVEDTIAAFKGRTIHTYHTEGAGGGHAPDIIVVVGYNNILPSSTNPTLPYTVNTIDEHLDMLMVCH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 321 HLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVIIRTWQVAHRMKVQRGALPEETGDNDNFRV 400
Cdd:TIGR01792 321 HLNPKIPEDVAFAESRIRKETIAAEDVLQDMGAISMISSDSQAMGRIGEVVTRCWQTADKMKKQRGPLPGDSPGNDNNRV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 401 KRYVAKYTINPALTHGIAHEVGSIETGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYRPMFGSL 480
Cdd:TIGR01792 401 KRYVAKYTINPAITHGISDYIGSIEVGKLADLVLWEPAFFGVKPDMVLKGGLIAWAIMGDPNASIPTPQPVLYRPMFGAY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 481 GAARHSTRLTFVSQAAHANGIPQQLNLQSATAVVKGCRTVKKADMIHNALQPNITVDSQTYEVRVDGELITSEPADVLPM 560
Cdd:TIGR01792 481 GRALQSTSITFVSQAAYDKGIKERLGLQKLLLPVHNTRSIGKADMKLNSATPKIEVDPQTYDVKVDGVLITVEPADELPL 560
|
....*..
gi 1513190841 561 AQRYFLF 567
Cdd:TIGR01792 561 TQRYFLF 567
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
1-567 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 909.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 1 MADISRRAYADMFGPTTGDKVRLADSELWIEVEDDLT----IYGEEVKFGGGKVIRDGMGQGQMT-ADDCVDLVLTNALI 75
Cdd:PRK13206 1 MTRLSRERYAALYGPTTGDRIRLADTDLLIEVTEDRSggpgLAGDEAVFGGGKVIRESMGQGRATrAEGAPDTVITGAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 76 VDHWGIVKADIGVKNGRIFAVGKAGNPDIQPGV--TIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTT 153
Cdd:PRK13206 81 LDHWGIVKADVGIRDGRIVAIGKAGNPDIMDGVhpDLVIGPSTEIIAGNGRILTAGAIDCHVHFICPQIVDEALAAGITT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 154 MIGGGTGPAAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPAALREQIAAGAIGLKIHEDWGATPAAINCSL 233
Cdd:PRK13206 161 LIGGGTGPAEGSKATTVTPGAWHLARMLEALDGWPVNVALLGKGNTVSAEALWEQLRGGAGGFKLHEDWGSTPAAIDACL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 234 EVAEEMDIQVALHSDTLNESGFVEDTLAAIAGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHL 313
Cdd:PRK13206 241 RVADAAGVQVALHSDTLNEAGFVEDTLAAIAGRSIHAYHTEGAGGGHAPDIITVASHPNVLPSSTNPTRPHTVNTLDEHL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 314 DMLMVCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVIIRTWQVAHRMKVQRGALPEETG 393
Cdd:PRK13206 321 DMLMVCHHLNPAVPEDLAFAESRIRPSTIAAEDVLHDMGAISMIGSDSQAMGRIGEVVLRTWQTAHVMKRRRGALPGDGR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 394 dNDNFRVKRYVAKYTINPALTHGIAHEVGSIETGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHY 473
Cdd:PRK13206 401 -ADNNRARRYVAKYTICPAVAHGIDHEIGSVEVGKLADLVLWEPAFFGVRPHAVLKGGAIAWAAMGDANASIPTPQPVLP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 474 RPMFGSLGAARHSTRLTFVSQAAHANGIPQQLNLQSATAVVKGCRTVKKADMIHNALQPNITVDSQTYEVRVDGELITSE 553
Cdd:PRK13206 480 RPMFGAAPAAAAATSVHFVAPQAIEDGLADRLGLRRRLVPVADTRAVGKADMPLNDALPDIEVDPDTFTVRIDGEVWEPQ 559
|
570
....*....|....
gi 1513190841 554 PADVLPMAQRYFLF 567
Cdd:PRK13206 560 PAAELPMAQRYFLF 573
|
|
| PLN02303 |
PLN02303 |
urease |
4-567 |
0e+00 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 887.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 4 ISRRAYADMFGPTTGDKVRLADSELWIEVEDDLTIYGEEVKFGGGKVIRDGMGQGQM-TADDCVDLVLTNALIVDHWGIV 82
Cdd:PLN02303 271 ISREKYANMYGPTTGDKIRLGDTNLYAEIEKDFTVYGDECKFGGGKVLRDGMGQATGyGAADSLDTVITNAVIIDYTGIY 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 83 KADIGVKNGRIFAVGKAGNPDIQPGVT--IPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMIGGGTG 160
Cdd:PLN02303 351 KADIGIKDGLIVGIGKAGNPDVMDGVTsnMIVGVNTEVIAGEGMIVTAGGIDCHVHFICPQLATEAIASGITTLVGGGTG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 161 PAAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPAALREQIAAGAIGLKIHEDWGATPAAINCSLEVAEEMD 240
Cdd:PLN02303 431 PAHGTCATTCTPAPSHMKLMLQSTDDLPLNFGFTGKGNTAKPEGLHEIIKAGAMGLKLHEDWGTTPAAIDNCLDVAEEYD 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 241 IQVALHSDTLNESGFVEDTLAAIAGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDMLMVCH 320
Cdd:PLN02303 511 IQVTIHTDTLNESGCVEHSIAAFKGRTIHTYHSEGAGGGHAPDIIKVCGVKNVLPSSTNPTRPYTKNTIDEHLDMLMVCH 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 321 HLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVIIRTWQVAHRMKVQRGALPEETGDNDNFRV 400
Cdd:PLN02303 591 HLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSDSQAMGRIGEVITRTWQTAHKMKSQRGALEPRGADNDNFRI 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 401 KRYVAKYTINPALTHGIAHEVGSIETGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYRPMFGSL 480
Cdd:PLN02303 671 KRYIAKYTINPAIAHGMSHFVGSVEVGKLADLVLWKPAFFGAKPEMVIKGGQIAWAQMGDPNASIPTPEPVIMRPMFGAF 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 481 GAARHSTRLTFVSQAAHANGIPQQLNLQSATAVVKGCRTVKKADMIHNALQPNITVDSQTYEVRVDGELITSEPADVLPM 560
Cdd:PLN02303 751 GKAGSSNSIAFVSKAALDAGVKQLYGLTKRVEAVGNVRGLTKLDMKLNDALPVITVDPETYEVTADGEVLTCAPATSVPL 830
|
....*..
gi 1513190841 561 AQRYFLF 567
Cdd:PLN02303 831 SRNYFLF 837
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
1-566 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 882.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 1 MADISRRAYADMFGPTTGDKVRLADSELWIEVEDDLTIYGEEVKFGGGKVIRDGMG--QGQMTADDCVDLVLTNALIVDH 78
Cdd:PRK13308 1 MATIDRRAYAELYGPTTGDRVRLADTSLLAEVEHDHTVYGDECLFGGGKTLRDGMGmaPGVTSADGALDFVLCNVTVIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 79 -WGIVKADIGVKNGRIFAVGKAGNPDIQPGVT--IPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMI 155
Cdd:PRK13308 81 vLGIVKGDIGIRDGRIVGIGKAGNPDIMDGVDprLVVGPGTDVRPAEGLIATPGAIDVHVHFDSAQLVDHALASGITTML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 156 GGGTGPAagtnATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPAALREQIAAGAIGLKIHEDWGATPAAINCSLEV 235
Cdd:PRK13308 161 GGGLGPT----VGIDSGGPFNTGRMLQAAEAWPVNFGFLGRGNSSKPAALIEQVEAGACGLKIHEDWGAMPAAIDTCLEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 236 AEEMDIQVALHSDTLNESGFVEDTLAAIAGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDM 315
Cdd:PRK13308 237 ADEYDFQVQLHTDTLNESGFVEDTLAAIGGRTIHMYHTEGAGGGHAPDIIRVVGEPHCLPSSTNPTNPYTVNTFDEHLDM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 316 LMVCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVIIRTWQVAHRMKVQRGALPEETG-D 394
Cdd:PRK13308 317 TMVCHHLNPDVPEDVAFAESRIRAQTIAAEDVLHDIGAISMLGSDSQGMGRIAEVIARTWQLASKMKDQRGPLPEDRGtF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 395 NDNFRVKRYVAKYTINPALTHGIAHEVGSIETGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYR 474
Cdd:PRK13308 397 ADNARIKRYIAKYTINPAITFGIDDHIGSLEPGKLADIVLWRPAFFGIKPELVIKGGFPAWAAMGDANGSLMTCEPMLQR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 475 PMFGSLGAARHSTRLTFVSQAAHANGIPQQLNLQSATAVVKGCRTVKKADMIHNALQPNITVDSQTYEVRVDGELITSEP 554
Cdd:PRK13308 477 PQWGAFGRAKQALSVCFVSPLAIEAGLGERLGLRKRLLPVRGTRTLTKADMLHNDACPDIRVDPQTFEVFVDGELVTCEP 556
|
570
....*....|..
gi 1513190841 555 ADVLPMAQRYFL 566
Cdd:PRK13308 557 ATELPLAQRYML 568
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
4-567 |
0e+00 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 834.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 4 ISRRAYADMFGPTTGDKVRLADSELWIEVEDDLTIYGEEVKFGGGKVIRDGMGQGQMTADDCVDLVLTNALIVDHWGIVK 83
Cdd:PRK13985 3 ISRKEYVSMYGPTTGDKVRLGDTDLIAEVEHDYTIYGEELKFGGGKTLREGMSQSNNPSKEELDLIITNALIIDYTGIYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 84 ADIGVKNGRIFAVGKAGNPDIQPGVT--IPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMIGGGTGP 161
Cdd:PRK13985 83 ADIGIKDGKIAGIGKGGNKDMQDGVKnnLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTAFASGVTTMIGGGTGP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 162 AAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPAALREQIAAGAIGLKIHEDWGATPAAINCSLEVAEEMDI 241
Cdd:PRK13985 163 ADGTNATTITPGRRNLKWMLRAAEEYSMNLGFLGKGNSSNDASLADQIEAGAIGFKIHEDWGTTPSAINHALDVADKYDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 242 QVALHSDTLNESGFVEDTLAAIAGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDMLMVCHH 321
Cdd:PRK13985 243 QVAIHTDTLNEAGCVEDTMAAIAGRTMHTFHTEGAGGGHAPDIIKVAGEHNILPASTNPTIPFTVNTEAEHMDMLMVCHH 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 322 LDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVIIRTWQVAHRMKVQRGALPEETGDNDNFRVK 401
Cdd:PRK13985 323 LDKSIKEDVQFADSRIRPQTIAAEDTLHDMGIFSITSSDSQAMGRVGEVITRTWQTADKNKKEFGRLKEEKGDNDNFRIK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 402 RYVAKYTINPALTHGIAHEVGSIETGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYRPMFGSLG 481
Cdd:PRK13985 403 RYLSKYTINPAIAHGISEYVGSVEVGKVADLVLWSPAFFGVKPNMIIKGGFIALSQMGDANASIPTPQPVYYREMFAHHG 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 482 AARHSTRLTFVSQAAHANGIPQQLNLQSATAVVKGCRTVKKADMIHNALQPNITVDSQTYEVRVDGELITSEPADVLPMA 561
Cdd:PRK13985 483 KAKYDANITFVSQAAYDKGIKEELGLERQVLPVKNCRNITKKDMQFNDTTAHIEVNPETYHVFVDGKEVTSKPANKVSLA 562
|
....*.
gi 1513190841 562 QRYFLF 567
Cdd:PRK13985 563 QLFSIF 568
|
|
| ureC |
PRK13309 |
urease subunit alpha; Reviewed |
1-566 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183966 [Multi-domain] Cd Length: 572 Bit Score: 755.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 1 MADISRRAYADMFGPTTGDKVRLADSELWIEVEDDLTIYGEEVKFGGGKVIRDGMGQ-GQMTADD-CVDLVLTNALIVD- 77
Cdd:PRK13309 1 MPQISRQEYAGLFGPTTGDKIRLGDTNLFIEIEKDLRGYGDESVYGGGKSLRDGMGAnNNLTRDNgVLDLVITNVTIVDa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 78 HWGIVKADIGVKNGRIFAVGKAGNPDIQPGVT--IPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMI 155
Cdd:PRK13309 81 RLGVIKADVGIRDGKIVGIGKSGNPSTMDGVTqgMVVGVSTDAISGEHLILTAAGIDTHIHLISPQQAYHALSNGVTTFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 156 GGGTGPAAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPAALREQIAAGAIGLKIHEDWGATPAAINCSLEV 235
Cdd:PRK13309 161 GGGIGPTDGTNGTTVTPGPWNIRQMLRSIEGLPVNVGILGKGNSYGRGPLLEQAIAGVAGYKVHEDWGATAAALRHALRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 236 AEEMDIQVALHSDTLNESGFVEDTLAAIAGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDM 315
Cdd:PRK13309 241 ADEVDIQVAVHTDSLNECGYVEDTIDAFEGRTIHTFHTEGAGGGHAPDIIKVASQTNVLPSSTNPTLPYGVNSQAELFDM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 316 LMVCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVIIRTWQVAHRMKVQRGALPEETGDN 395
Cdd:PRK13309 321 IMVCHNLNPNVPADVAFAESRVRPETIAAENVLHDMGVISMFSSDSQAMGRVGENWLRAIQTADAMKAARGKLPEDAAGN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 396 DNFRVKRYVAKYTINPALTHGIAHEVGSIETGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYRP 475
Cdd:PRK13309 401 DNFRVLRYVAKITINPAITQGVSHVIGSVEVGKMADLVLWEPRFFGAKPKMVIKGGMINWAAMGDPNASLPTPQPVFYRP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 476 MFGSLGAARHSTRLTFVSQAAHANGIPQQLNLQSATAVVKGCRTVKKADMIHNALQPNITVDSQTYEVRVDGELITSEPA 555
Cdd:PRK13309 481 MFGAMGKTLQDTCVTFVSQAALDDGVKEKAGLDRQVIAVKNCRTISKRDLVRNSQTPNIEVDPETFAVKVDGVHATVKPI 560
|
570
....*....|.
gi 1513190841 556 DVLPMAQRYFL 566
Cdd:PRK13309 561 ATASLNQRYFF 571
|
|
| Urease_alpha |
pfam00449 |
Urease alpha-subunit, N-terminal domain; The N-terminal domain is a composite domain and plays ... |
4-119 |
5.94e-73 |
|
Urease alpha-subunit, N-terminal domain; The N-terminal domain is a composite domain and plays a major trimer stabilising role by contacting the catalytic domain of the symmetry related alpha-subunit.
Pssm-ID: 425689 [Multi-domain] Cd Length: 120 Bit Score: 228.53 E-value: 5.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 4 ISRRAYADMFGPTTGDKVRLADSELWIEVEDDLTIYGEEVKFGGGKVIRDGMGQGQM-TADDCVDLVLTNALIVDHWGIV 82
Cdd:pfam00449 2 ISREAYADMYGPTTGDRIRLGDTDLFIEVEKDLTVYGDEVKFGGGKVIRDGMGQSQGrTRDDALDLVITNALILDYTGIV 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 1513190841 83 KADIGVKNGRIFAVGKAGNPDIQPGVT--IPIGAATEVI 119
Cdd:pfam00449 82 KADIGIKDGRIVGIGKAGNPDTMDGVTpgMVIGPSTEVI 120
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
125-454 |
1.99e-68 |
|
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: 224.30 E-value: 1.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 125 IVTAGGIDTHIHW---------ICPQQAEEALVSGVTTMIGGGTGPAAGTNATTCTpgpwYIARMLQAADTLPVNIGLLG 195
Cdd:pfam01979 1 IVLPGLIDAHVHLemgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTST----GIEALLEAAEELPLGLRFLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 196 K-------GNGSNPAALREQIAAGA------------IGLKIHEDWGATPAAINCSLEVAEEMDIQVALHsdTLNESGFV 256
Cdd:pfam01979 77 PgcsldtdGELEGRKALREKLKAGAefikgmadgvvfVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIH--ALETKGEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 257 EDTLAAIAGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTnptlpyTVNTIDEHLDMLMVCHhldpdiaedVAFAESR 336
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLSPT------EANLLAEHLKGAGVAH---------CPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 337 IRRETIAAEDVLHDiGAFSLTSSDSQAMGRVGEVIIRTwqvahrmkvqRGALPEETGDNDNFRVKRYVAKYTINPALTHG 416
Cdd:pfam01979 220 LRSGRIALRKALED-GVKVGLGTDGAGSGNSLNMLEEL----------RLALELQFDPEGGLSPLEALRMATINPAKALG 288
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1513190841 417 IAHEVGSIETGKLADLVVWS----PAFFGVKPATIVKGGMIA 454
Cdd:pfam01979 289 LDDKVGSIEVGKDADLVVVDldplAAFFGLKPDGNVKKVIVK 330
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
67-436 |
8.82e-18 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 85.40 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 67 DLVLTNALIVDHWG---IVKADIGVKNGRIFAVGKAGnpdiqpgvTIPIGAATEVIAAEGKIVTAGGIDTHIH------- 136
Cdd:COG1228 9 TLLITNATLVDGTGggvIENGTVLVEDGKIAAVGPAA--------DLAVPAGAEVIDATGKTVLPGLIDAHTHlglgggr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 137 -----------------WICPQQAEEALVSGVTTMIGGGTGPAAGTNAT-----TCTPGPwyiaRMLQAADTLPVNIGLL 194
Cdd:COG1228 81 avefeagggitptvdlvNPADKRLRRALAAGVTTVRDLPGGPLGLRDAIiagesKLLPGP----RVLAAGPALSLTGGAH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 195 GKGNGSNPAALREQIAAGAIGLKIHEDWGA---TPAAINCSLEVAEEMDIQVALHSDTLNESgfvedTLAAIAG-RTIHt 270
Cdd:COG1228 157 ARGPEEARAALRELLAEGADYIKVFAEGGApdfSLEELRAILEAAHALGLPVAAHAHQADDI-----RLAVEAGvDSIE- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 271 fHtegaGGGHAPDIITACAHPNilPSSTNPTLPYTVNtidehldmlmvchhLDPDIAEDVAFAESRIRRETIAAEDVLHD 350
Cdd:COG1228 231 -H----GTYLDDEVADLLAEAG--TVVLVPTLSLFLA--------------LLEGAAAPVAAKARKVREAALANARRLHD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 351 IGAFSLTSSDSQAMGRVGEviiRTWQVAHRMkVQRGALPEETgdndnfrvkryVAKYTINPALTHGIAHEVGSIETGKLA 430
Cdd:COG1228 290 AGVPVALGTDAGVGVPPGR---SLHRELALA-VEAGLTPEEA-----------LRAATINAAKALGLDDDVGSLEPGKLA 354
|
....*.
gi 1513190841 431 DLVVWS 436
Cdd:COG1228 355 DLVLLD 360
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
69-218 |
7.25e-16 |
|
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: 80.14 E-value: 7.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 69 VLTNALIVDHWGIVKADIGVKNGRIFAVGKAgnpdiqpgvtIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEE--- 145
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPD----------LAAPEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKedi 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 146 ------ALVSGVTTMIgggtgPAAGTNATTCTPG--PWYIARmlqAADTLPVNIGLLG---KGNGSNPAALREQIAAGAI 214
Cdd:COG0044 71 etgtraAAAGGVTTVV-----DMPNTNPVTDTPEalEFKLAR---AEEKALVDVGPHGaltKGLGENLAELGALAEAGAV 142
|
....
gi 1513190841 215 GLKI 218
Cdd:COG0044 143 AFKV 146
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
67-155 |
6.01e-12 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 68.20 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 67 DLVLTNALIVD-HWG-IVKADIGVKNGRIFAVGKAgnpdiqpgvtipIGAATEVIAAEGKIVTAGGIDTHIH----WICP 140
Cdd:COG1001 6 DLVIKNGRLVNvFTGeILEGDIAIAGGRIAGVGDY------------IGEATEVIDAAGRYLVPGFIDGHVHiessMVTP 73
|
90
....*....|....*.
gi 1513190841 141 QQ-AEEALVSGVTTMI 155
Cdd:COG1001 74 AEfARAVLPHGTTTVI 89
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
67-155 |
8.23e-11 |
|
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: 64.24 E-value: 8.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 67 DLVLTNALIVDHWG--IVKADIGVKNGRIFAVGKAGNPDiqpgvtipigaATEVIAAEGKIVTAGGIDTHIHW----ICP 140
Cdd:cd01297 1 DLVIRNGTVVDGTGapPFTADVGIRDGRIAAIGPILSTS-----------AREVIDAAGLVVAPGFIDVHTHYdgqvFWD 69
|
90
....*....|....*
gi 1513190841 141 QQAEEALVSGVTTMI 155
Cdd:cd01297 70 PDLRPSSRQGVTTVV 84
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
67-217 |
1.79e-10 |
|
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: 63.08 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 67 DLVLTNALIVDHWGIVKADIGVKNGRIFAVGKagnpdiqpgvTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAE-- 144
Cdd:cd01315 1 DLVIKNGRVVTPDGVREADIAVKGGKIAAIGP----------DIANTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEwe 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 145 -------EALVSGVTTMIgggtgpAAGTNATTCTPGPWYIARMLQAA-DTLPVNIGLLGKGNGSNPAALREQIAAGAIGL 216
Cdd:cd01315 71 gfetgtkAAAAGGITTII------DMPLNSIPPTTTVENLEAKLEAAqGKLHVDVGFWGGLVPGNLDQLRPLDEAGVVGF 144
|
.
gi 1513190841 217 K 217
Cdd:cd01315 145 K 145
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
68-155 |
4.26e-10 |
|
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: 61.85 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 68 LVLTNALIVDHWGIVKADIGVKNGRIFAVGKagnpdiqpgvTIPIGAATEVIAAEGKIVTAGGIDTHIHWICP------- 140
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGP----------NLEAPGGVEVIDATGKYVLPGGIDPHTHLELPfmgtvta 70
|
90
....*....|....*...
gi 1513190841 141 ---QQAEEALVSGVTTMI 155
Cdd:cd01314 71 ddfESGTRAAAAGGTTTI 88
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
67-136 |
3.98e-09 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 58.78 E-value: 3.98e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 67 DLVLTNALIVDHWGIVKADIGVKNGRIFAVGKAGNPDiqpgvtipigaATEVIAAEGKIVTAGGIDTHIH 136
Cdd:PRK09060 6 DLILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGAS-----------AGEVIDCRGLHVLPGVIDSQVH 64
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
67-136 |
6.44e-09 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 58.56 E-value: 6.44e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 67 DLVLTNALIVDHWGIVKADIGVKNGRIFAVGKAgnpdiqpgvtipIGAATEVIAAEGKIVTAGGIDTHIH 136
Cdd:PRK13404 5 DLVIRGGTVVTATDTFQADIGIRGGRIAALGEG------------LGPGAREIDATGRLVLPGGVDSHCH 62
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
67-136 |
8.04e-09 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 57.87 E-value: 8.04e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 67 DLVLTNALIVDHWGIVKADIGVKNGRIFAVGKagnpdiqpgvtipiGAATEVIAAEGKIVTAGGIDTHIH 136
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGA--------------NLGDEVIDATGKYVMPGGIDPHTH 57
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
67-217 |
2.78e-07 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 53.17 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 67 DLVLTNALIVDHWGIVKADIGVKNGRIFAVGkagnPDIQpgvtipiGAATEVIAAEGKIVTAGGIDTHIHWICPQQAE-E 145
Cdd:PRK06189 4 DLIIRGGKVVTPEGVYRADIGIKNGKIAEIA----PEIS-------SPAREIIDADGLYVFPGMIDVHVHFNEPGRTHwE 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1513190841 146 ALVSGVTTMIGGGTGPAAGT--NATTCTPGPWYIARMLQAADTLP-VNIGLLGKGNGSNPAALREQIAAGAIGLK 217
Cdd:PRK06189 73 GFATGSAALAAGGCTTYFDMplNSIPPTVTREALDAKAELARQKSaVDFALWGGLVPGNLEHLRELAEAGVIGFK 147
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
68-136 |
6.02e-07 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 51.77 E-value: 6.02e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1513190841 68 LVLTNALIVDHWGIVKA--DIGVKNGRIFAVGKagnpdiqpgvTIPIGAATEVIAAEGKIVTAGGIDTHIH 136
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAG----------DIDGSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
67-155 |
8.82e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 51.58 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 67 DLVLTNALIVDHWGIVKADIGVKNGRIFAVGKAgnpdiqpgvtIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEE- 145
Cdd:PRK02382 3 DALLKDGRVYYNNSLQPRDVRIDGGKITAVGKD----------LDGSSSEEVIDARGMLLLPGGIDVHVHFREPGYTHKe 72
|
90
....*....|....*...
gi 1513190841 146 --------ALVSGVTTMI 155
Cdd:PRK02382 73 twytgsrsAAAGGVTTVV 90
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
68-136 |
2.16e-06 |
|
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: 49.88 E-value: 2.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513190841 68 LVLTNALIVDHWGIVKADIGVKNGRIFAVGKAgnpdiqpgvtIPIGAATEVIAAEGKIVTAGGIDTHIH 136
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPE----------DELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
407-447 |
5.29e-06 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 49.03 E-value: 5.29e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1513190841 407 YTINPALTHGIAHEVGSIETGKLADLVVWSPAFFGVKPATI 447
Cdd:COG1574 476 YTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEI 516
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
407-434 |
2.04e-05 |
|
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: 47.30 E-value: 2.04e-05
10 20
....*....|....*....|....*...
gi 1513190841 407 YTINPALTHGIAHEVGSIETGKLADLVV 434
Cdd:cd01300 452 YTIGAAYAIGEEDEKGSLEPGKLADFVV 479
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
408-436 |
2.27e-05 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 46.92 E-value: 2.27e-05
10 20
....*....|....*....|....*....
gi 1513190841 408 TINPALTHGIAHEVGSIETGKLADLVVWS 436
Cdd:cd01309 310 TINPAKILGIEDRVGSLEPGKDADLVVWN 338
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
69-136 |
2.37e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 46.63 E-value: 2.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513190841 69 VLTNALIVDHWGIVK-ADIGVKNGRIFAVGKAGNPDIqpgvtipigaatEVIAAEGKIVTAGGIDTHIH 136
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPGAEPDA------------EVIDLGGGYLAPGFIDLHVH 57
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
58-155 |
2.52e-05 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 47.00 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 58 GQMTADDCVDLVLTNALIVDHWGIVKA--DIGVKNGRIFAVGkagnpdiqpgvTIPIGAATeVIAAEGKIVTAGGIDTHI 135
Cdd:PRK09061 11 LMPASMAPYDLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVG-----------TAAIEGDR-TIDATGLVVAPGFIDLHA 78
|
90 100
....*....|....*....|
gi 1513190841 136 HWICPQQAEEALVSGVTTMI 155
Cdd:PRK09061 79 HGQSVAAYRMQAFDGVTTAL 98
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
117-448 |
3.75e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 46.37 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 117 EVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMIGGGTGPAAGTNATTCTPG------PWYIARMLQAADTL--- 187
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVLPNAVVKGQAGRTPKGRWLVGegwdeaQFAETRFPYALADLdev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 188 ----PVNIG-LLGKGNGSNPAALRE-------QIAAGAIGLKIHEDWGAT-------PAAINCSLEVAEEMDIQVALH-- 246
Cdd:pfam07969 81 apdgPVLLRaLHTHAAVANSAALDLagitkatEDPPGGEIARDANGEGLTgllregaYALPPLLAREAEAAAVAAALAal 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 247 -------SDTLNESGFVEDTLAAIAGRTIHTFHTEGA----------------------GGGHAPDIITACAHPNILPSS 297
Cdd:pfam07969 161 pgfgitsVDGGGGNVHSLDDYEPLRELTAAEKLKELLdaperlglphsiyelrigamklFADGVLGSRTAALTEPYFDAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 298 TNPTLPYTVNTIDEHLDM-----LMVCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVII 372
Cdd:pfam07969 241 GTGWPDFEDEALAELVAAarergLDVAIHAIGDATIDTALDAFEAVAEKLGNQGRVRIEHAQGVVPYTYSQIERVAALGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 373 R---------TWQVAHRMKVQRGALPE--------ETGDNDNF----------------------------------RVK 401
Cdd:pfam07969 321 AagvqpvfdpLWGDWLQDRLGAERARGltpvkellNAGVKVALgsdapvgpfdpwprigaavmrqtagggevlgpdeELS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1513190841 402 RY--VAKYTINPALTHGIAHEVGSIETGKLADLVVWSPAFFGVKPATIV 448
Cdd:pfam07969 401 LEeaLALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIA 449
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
67-435 |
4.40e-05 |
|
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: 45.97 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 67 DLVLTNALIVDHWG----IVKADIGVKNGRIFAVGKAGNPDIQPgvtipigAATEVIAAEGKIVTAGGIDTHIH------ 136
Cdd:COG0402 1 DLLIRGAWVLTMDPaggvLEDGAVLVEDGRIAAVGPGAELPARY-------PAAEVIDAGGKLVLPGLVNTHTHlpqtll 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 137 -----------W-----------ICPQQAE--------EALVSGVTTMigggtgpaagtnATTCTPGPWYIARMLQAADT 186
Cdd:COG0402 74 rgladdlplldWleeyiwplearLDPEDVYagallalaEMLRSGTTTV------------ADFYYVHPESADALAEAAAE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 187 LPVNiGLLGKG--NGSNPAALREQIAAG-AIGLKIHEDW----------GATP-AAINCSLEV-------AEEMDIQVAL 245
Cdd:COG0402 142 AGIR-AVLGRGlmDRGFPDGLREDADEGlADSERLIERWhgaadgrirvALAPhAPYTVSPELlraaaalARELGLPLHT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 246 HsdtLNES-GFVEDTLAAIAGRTIHTFHTEGAGGGHapdiiTACAHpnilpsstnptlpytvntidehldmlmvCHHLDP 324
Cdd:COG0402 221 H---LAETrDEVEWVLELYGKRPVEYLDELGLLGPR-----TLLAH----------------------------CVHLTD 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 325 DiaeDVA-FAESRIrreTIA---------------AEDVLH---------DIGAfsltSSDSQAMgrvgeviIRTWQVAh 379
Cdd:COG0402 265 E---EIAlLAETGA---SVAhcptsnlklgsgiapVPRLLAagvrvglgtDGAA----SNNSLDM-------FEEMRLA- 326
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1513190841 380 rMKVQRGAlpeeTGDNDNFRVKRYVAKYTINPALTHGIAHEVGSIETGKLADLVVW 435
Cdd:COG0402 327 -ALLQRLR----GGDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVL 377
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
85-155 |
4.66e-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: 45.78 E-value: 4.66e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513190841 85 DIGVKNGRIFAVGKAGNPDiqpgvtipigAATEVIAAEGKIVTAGGIDTHIHwiCPQQAEE--------ALVSGVTTMI 155
Cdd:cd01307 1 DVAIENGKIAAVGAALAAP----------AATQIVDAGGCYVSPGWIDLHVH--VYQGGTRygdrpdmiGVKSGVTTVV 67
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
68-136 |
6.55e-05 |
|
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: 45.66 E-value: 6.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1513190841 68 LVLTNALIV---DHWGIVKADIGVKNGRIFAVGKAGNPDIQPGVtipigaatEVIAAEGKIVTAGGIDTHIH 136
Cdd:cd01298 1 ILIRNGTIVttdPRRVLEDGDVLVEDGRIVAVGPALPLPAYPAD--------EVIDAKGKVVMPGLVNTHTH 64
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
68-136 |
1.68e-04 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 44.03 E-value: 1.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 68 LVLTNALIVDHWGI-VKADIGVKNGRIFAVGKAGNPDiqpgvtipigaATEVIAAEGKIVTAGGIDTHIH 136
Cdd:PRK09357 3 ILIKNGRVIDPKGLdEVADVLIDDGKIAAIGENIEAE-----------GAEVIDATGLVVAPGLVDLHVH 61
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
67-136 |
1.71e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 44.40 E-value: 1.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513190841 67 DLVLTNALIV---DHWGIVKAdIGVKNGRIFAVGkaGNPDIQPGvtipIGAATEVIAAEGKIVTAGGIDTHIH 136
Cdd:COG1574 9 DLLLTNGRIYtmdPAQPVAEA-VAVRDGRIVAVG--SDAEVRAL----AGPATEVIDLGGKTVLPGFIDAHVH 74
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
408-450 |
2.19e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 43.55 E-value: 2.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1513190841 408 TINPALTHGIAHEVGSIETGKLADLVVWSPAfFGVKpATIVKG 450
Cdd:COG1820 332 SLNPARALGLDDRKGSIAPGKDADLVVLDDD-LNVR-ATWVGG 372
|
|
| PLN02795 |
PLN02795 |
allantoinase |
69-217 |
2.44e-04 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 44.00 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 69 VLTNALIVDHWGIVKADIGVKNGRIFAVGKAGN-PDIQPGVtipigaatEVIAAEGKIVTAGGIDTHIHWICPQQAE--- 144
Cdd:PLN02795 47 VLYSKRVVTPAGVIPGAVEVEGGRIVSVTKEEEaPKSQKKP--------HVLDYGNAVVMPGLIDVHVHLNEPGRTEweg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 145 ------EALVSGVTTMIGGGTGPaagtNATTCTPGPwYIARMLQAADTLPVNIGLLGK---GNGSNPAALREQIAAGAIG 215
Cdd:PLN02795 119 fptgtkAAAAGGITTLVDMPLNS----FPSTTSVET-LELKIEAAKGKLYVDVGFWGGlvpENAHNASVLEELLDAGALG 193
|
..
gi 1513190841 216 LK 217
Cdd:PLN02795 194 LK 195
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
67-136 |
2.95e-04 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 43.47 E-value: 2.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 67 DLVLTNALIVDhwGIVKADIGVKNGRIFAVGkagnPDIQpgvtipiGAATEVIAAEGKIVTAGGIDTHIH 136
Cdd:PRK07572 3 DLIVRNANLPD--GRTGIDIGIAGGRIAAVE----PGLQ-------AEAAEEIDAAGRLVSPPFVDPHFH 59
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
67-155 |
4.28e-04 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 42.92 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 67 DLVLTNALIVDHWGIVKADIGVKNGRIFAVGKAgnpdiqpgvtipIGAATEVIAAEGKIVTAGGIDTHIHWICPQQA--- 143
Cdd:PRK08044 4 DLIIKNGTVILENEARVVDIAVKGGKIAAIGQD------------LGDAKEVMDASGLVVSPGMVDAHTHISEPGRShwe 71
|
90
....*....|....*...
gi 1513190841 144 ------EEALVSGVTTMI 155
Cdd:PRK08044 72 gyetgtRAAAKGGITTMI 89
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
83-136 |
8.91e-04 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 42.02 E-value: 8.91e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1513190841 83 KADIGVKNGRIFAVGKAGNPDiqpgvtipigaatEVIAAEGKIVTAGGIDTHIH 136
Cdd:cd01304 17 KMDIFIRDGKIVESSSGAKPA-------------KVIDASGKVVMAGGVDMHSH 57
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
408-451 |
1.58e-03 |
|
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: 41.09 E-value: 1.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1513190841 408 TINPALTHGIAHEVGSIETGKLADLVVWS-------PAFFGVKP-ATIVKGG 451
Cdd:cd01296 320 TINAAAALGLGETVGSLEVGKQADLVILDapsyehlAYRFGVNLvEYVIKNG 371
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
67-155 |
1.80e-03 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 40.90 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 67 DLVLTNALIVD--HWGIVKADIGVKNGRIFavgkagnpdiqPGVTIPIGAATEVIAAEGKIVTAGGIDTHIHwICPQQAE 144
Cdd:PRK12394 4 DILITNGHIIDpaRNINEINNLRIINDIIV-----------DADKYPVASETRIIHADGCIVTPGLIDYHAH-VFYDGTE 71
|
90
....*....|....*...
gi 1513190841 145 EA-------LVSGVTTMI 155
Cdd:PRK12394 72 GGvrpdmymPPNGVTTVV 89
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
84-155 |
2.04e-03 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 40.98 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 84 ADIGVKNGRIFAVGkagnPDIqpgvtiPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEE----------ALVSGVTT 153
Cdd:PLN02942 23 ADVYVEDGIIVAVA----PNL------KVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTEtiddffsgqaAALAGGTT 92
|
..
gi 1513190841 154 MI 155
Cdd:PLN02942 93 MH 94
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
86-136 |
3.06e-03 |
|
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: 39.93 E-value: 3.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1513190841 86 IGVKNGRIFAVGKAgnpdiqPGVTIPIGAATEVIAAEGKIVTAGGIDTHIH 136
Cdd:cd01296 1 IAIRDGRIAAVGPA------ASLPAPGPAAAEEIDAGGRAVTPGLVDCHTH 45
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
83-138 |
3.48e-03 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 40.07 E-value: 3.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1513190841 83 KADIGVKNGRIFAVGkagnpdiqPGVTIPIGAATEVIAAEGKIVTAGGIDTHIHWI 138
Cdd:cd01308 17 KKDILIAGGKILAIE--------DQLNLPGYENVTVVDLHGKILVPGFIDQHVHII 64
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|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
81-136 |
3.70e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 39.75 E-value: 3.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1513190841 81 IVKADIGVKNGRIFAVGKAgnpDIQpgvtipigaATEVIAAEGKIVTAGGIDTHIH 136
Cdd:PRK04250 12 IVEGGIGIENGRISKISLR---DLK---------GKEVIKVKGGIILPGLIDVHVH 55
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
85-136 |
3.76e-03 |
|
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: 39.98 E-value: 3.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1513190841 85 DIGVKNGRIFAVGkaGNPDIQPGvtipIGAATEVIAAEGKIVTAGGIDTHIH 136
Cdd:cd01300 1 AVAVRDGRIVAVG--SDAEAKAL----KGPATEVIDLKGKTVLPGFIDSHSH 46
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
68-136 |
4.01e-03 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 39.85 E-value: 4.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513190841 68 LVLTNALIVDHWGIVKADIGVKNGRIFAVGKAgnpdiqpgvtIPIGAATEVIAAEGKIVTAGGIDTHIH 136
Cdd:PRK09236 4 ILIKNARIVNEGKIFEGDVLIENGRIAKIASS----------ISAKSADTVIDAAGRYLLPGMIDDQVH 62
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
70-136 |
4.22e-03 |
|
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: 39.54 E-value: 4.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1513190841 70 LTNALIVDhWGIVKADIGVKNGRIFAVGKAGnpdiqpgvtiPIGAATEVIAAEGKIVTAGGIDTHIH 136
Cdd:cd01293 2 LRNARLAD-GGTALVDIAIEDGRIAAIGPAL----------AVPPDAEEVDAKGRLVLPAFVDPHIH 57
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|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
69-136 |
6.75e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 39.22 E-value: 6.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1513190841 69 VLTNALIV----DHWGIVKADIGVKNGRIFAVGkagnPDIQPGvtipigaATEVIAAEGKIVTAGGIDTHIH 136
Cdd:PRK08204 5 LIRGGTVLtmdpAIGDLPRGDILIEGDRIAAVA----PSIEAP-------DAEVVDARGMIVMPGLVDTHRH 65
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|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
131-305 |
9.62e-03 |
|
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: 38.08 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 131 IDTHIH---------------------------WICPQQAEEALVSGVTTMIGGGTGPAAgtnattcTPGPWYIARMLQA 183
Cdd:cd01292 2 IDTHVHldgsalrgtrlnlelkeaeelspedlyEDTLRALEALLAGGVTTVVDMGSTPPP-------TTTKAAIEAVAEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513190841 184 ADTLPVNIGLLGKG------------NGSNPAALREQIAAGAIGLKIHEDWGAT---PAAINCSLEVAEEMDIQVALH-S 247
Cdd:cd01292 75 ARASAGIRVVLGLGipgvpaavdedaEALLLELLRRGLELGAVGLKLAGPYTATglsDESLRRVLEEARKLGLPVVIHaG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1513190841 248 DTLNESGFVEDTLAAI-AGRTIHTFHtegaGGGHAPDIITACAHPNILPSSTNPTLPYT 305
Cdd:cd01292 155 ELPDPTRALEDLVALLrLGGRVVIGH----VSHLDPELLELLKEAGVSLEVCPLSNYLL 209
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