|
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: 1205.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 1 MAEISRQAYADMFGPTTGDKVRLADSELWIEVENDLTVYGEEVKFGGGKVIRDGMGQGQ-MTADDCVDLVLTNALIVDHW 79
Cdd:PRK13207 1 MAKISRRAYAEMYGPTTGDRVRLADTELWIEVEKDFTTYGEEVKFGGGKVIRDGMGQSQrARADGAVDTVITNALILDHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 80 GIVKADIGVKNGRIFAVGKAGNPDIQPGVTIPIGAATEAIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMIGGGT 159
Cdd:PRK13207 81 GIVKADIGIKDGRIVAIGKAGNPDIQDGVDIIIGPGTEVIAGEGLIVTAGGIDTHIHFICPQQIEEALASGVTTMIGGGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 160 GPAAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPDALREQIAAGAIGLKIHEDWGATPAAINCSLEVAEEM 239
Cdd:PRK13207 161 GPATGTNATTCTPGPWHIHRMLQAADAFPMNIGFLGKGNASLPEALEEQIEAGAIGLKLHEDWGATPAAIDNCLSVADEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 240 DIQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDMLMVC 319
Cdd:PRK13207 241 DVQVAIHTDTLNESGFVEDTIAAFKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDMLMVC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 320 HHLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALPEETGDNDNFR 399
Cdd:PRK13207 321 HHLDPSIPEDVAFAESRIRRETIAAEDILHDLGAISMISSDSQAMGRVGEVIIRTWQTAHKMKVQRGPLPGDSGRNDNFR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 400 VKRYIAKYTINPALTHGIAHEVGSIEAGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYRPMFGA 479
Cdd:PRK13207 401 VKRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWKPAFFGVKPELVLKGGMIAWAPMGDPNASIPTPQPVHYRPMFGA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 480 LGAARHATRLTFVSQAADAQGIAQQLNLQSATAVVKGCRTVKKADMIHNGLQPNITVDSQTYEVRVDGELITSEPADVLP 559
Cdd:PRK13207 481 YGGALAATSVTFVSQAALDAGIPEKLGLKKRLVPVKNTRGITKADMKLNDATPKIEVDPETYEVRADGELLTCEPATVLP 560
|
....*...
gi 1732753225 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: 1195.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 1 MAEISRQAYADMFGPTTGDKVRLADSELWIEVENDLTVYGEEVKFGGGKVIRDGMGQGQMT-ADDCVDLVLTNALIVDHW 79
Cdd:COG0804 1 MAKISRKAYADLYGPTTGDRVRLADTDLFIEVEKDLTTYGDEVKFGGGKVIRDGMGQSQTTrAEGALDLVITNAVILDHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 80 GIVKADIGVKNGRIFAVGKAGNPDIQPGVT--IPIGAATEAIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMIGG 157
Cdd:COG0804 81 GIVKADIGIKDGRIVGIGKAGNPDTMDGVDpdLVIGPGTEVIAGEGLILTAGGIDTHIHFICPQQIEEALASGITTMIGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 158 GTGPAAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPDALREQIAAGAIGLKIHEDWGATPAAINCSLEVAE 237
Cdd:COG0804 161 GTGPAEGTNATTCTPGPWNIARMLEAADALPMNIGFLGKGNASSPEALEEQIRAGACGLKLHEDWGATPAAIDACLSVAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 238 EMDIQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDMLM 317
Cdd:COG0804 241 EYDVQVAIHTDTLNESGFVEDTIAAIKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDMLM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 318 VCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALPEETGDNDN 397
Cdd:COG0804 321 VCHHLDPSIPEDVAFAESRIRPETIAAEDVLHDLGAISMMSSDSQAMGRVGEVITRTWQTAHKMKKQRGPLPGDSGRNDN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 398 FRVKRYIAKYTINPALTHGIAHEVGSIEAGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYRPMF 477
Cdd:COG0804 401 FRVKRYVAKYTINPAIAHGISHEVGSVEVGKLADLVLWDPAFFGVKPELVIKGGMIAWAQMGDPNASIPTPQPVHYRPMF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 478 GALGAARHATRLTFVSQAADAQGIAQQLNLQSATAVVKGCRTVKKADMIHNGLQPNITVDSQTYEVRVDGELITSEPADV 557
Cdd:COG0804 481 GAYGKALAATSVTFVSQAALEAGIAERLGLRKRLLPVKNTRNIGKADMVLNDATPDIEVDPETYEVRVDGELLTCEPATE 560
|
570
....*....|
gi 1732753225 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: 1093.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 3 EISRQAYADMFGPTTGDKVRLADSELWIEVENDLTVYGEEVKFGGGKVIRDGMGQGQ-MTADDCVDLVLTNALIVDHWGI 81
Cdd:cd00375 1 KISREAYADMYGPTTGDKVRLGDTDLWIEVEKDYTTYGDEVKFGGGKVLRDGMGQSSgYTREDVLDLVITNALIIDYTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 82 VKADIGVKNGRIFAVGKAGNPDIQPGVT--IPIGAATEAIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMIGGGT 159
Cdd:cd00375 81 YKADIGIKDGRIVAIGKAGNPDIMDGVTpnMIVGPSTEVIAGEGKIVTAGGIDTHVHFICPQQIEEALASGITTMIGGGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 160 GPAAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPDALREQIAAGAIGLKIHEDWGATPAAINCSLEVAEEM 239
Cdd:cd00375 161 GPAAGTKATTCTPGPWNIKRMLQAADGLPVNIGFLGKGNGSSPDALAEQIEAGACGLKLHEDWGATPAAIDTCLSVADEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 240 DIQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDMLMVC 319
Cdd:cd00375 241 DVQVAIHTDTLNESGFVEDTIAAIKGRTIHTYHTEGAGGGHAPDIIKVAGHPNVLPSSTNPTRPFTVNTLDEHLDMLMVC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 320 HHLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALPEETGDNDNFR 399
Cdd:cd00375 321 HHLDPNIPEDVAFAESRIRAETIAAEDVLHDLGAISIMSSDSQAMGRVGEVILRTWQTAHKMKAQRGPLPEDSGDADNFR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 400 VKRYIAKYTINPALTHGIAHEVGSIEAGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYRPMFGA 479
Cdd:cd00375 401 VKRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWEPAFFGVKPEMVLKGGFIAYAQMGDPNASIPTPQPVMMRPMFGA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 480 LGAARHATRLTFVSQAADAQGIAQQLNLQSATAVVKGCRTVKKADMIHNGLQPNITVDSQTYEVRVDGELITSEPADVLP 559
Cdd:cd00375 481 HGKAPAATSVTFVSQASLDAGIAEELGLRRRVVAVKNCRGVGKKDMKLNSATPDIEVDPETYEVRVDGELLTCEPADELP 560
|
....*..
gi 1732753225 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: 946.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 3 EISRQAYADMFGPTTGDKVRLADSELWIEVENDLTVYGEEVKFGGGKVIRDGMGQG-QMTAD-DCVDLVLTNALIVDHWG 80
Cdd:TIGR01792 1 KMSREQYASLYGPTTGDKVRLGDTDLFVEVEKDLTTYGDESKFGGGKVLRDGMGQNaTLTRNaGVLDLVITNALILDWTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 81 IVKADIGVKNGRIFAVGKAGNPDIQPGVTIPIGAATEAIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMIGGGTG 160
Cdd:TIGR01792 81 IYKADIGIKNGRIVGIGKAGNPDTMDGVDMIVGASTEAISGEGKIVTAGGIDTHVHYISPQQVQAALDNGITTLIGGGTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 161 PAAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPDALREQIAAGAIGLKIHEDWGATPAAINCSLEVAEEMD 240
Cdd:TIGR01792 161 PADGTNATTCTPGPWYLHRMLQAADGLPINFGFTGKGSGSGPAALIEQIEAGACGLKVHEDWGATPAAIDNALSVADEYD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 241 IQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDMLMVCH 320
Cdd:TIGR01792 241 VQVAVHTDTLNESGFVEDTIAAFKGRTIHTYHTEGAGGGHAPDIIVVVGYNNILPSSTNPTLPYTVNTIDEHLDMLMVCH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 321 HLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALPEETGDNDNFRV 400
Cdd:TIGR01792 321 HLNPKIPEDVAFAESRIRKETIAAEDVLQDMGAISMISSDSQAMGRIGEVVTRCWQTADKMKKQRGPLPGDSPGNDNNRV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 401 KRYIAKYTINPALTHGIAHEVGSIEAGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYRPMFGAL 480
Cdd:TIGR01792 401 KRYVAKYTINPAITHGISDYIGSIEVGKLADLVLWEPAFFGVKPDMVLKGGLIAWAIMGDPNASIPTPQPVLYRPMFGAY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 481 GAARHATRLTFVSQAADAQGIAQQLNLQSATAVVKGCRTVKKADMIHNGLQPNITVDSQTYEVRVDGELITSEPADVLPM 560
Cdd:TIGR01792 481 GRALQSTSITFVSQAAYDKGIKERLGLQKLLLPVHNTRSIGKADMKLNSATPKIEVDPQTYDVKVDGVLITVEPADELPL 560
|
....*..
gi 1732753225 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: 907.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 1 MAEISRQAYADMFGPTTGDKVRLADSELWIEVENDLTV----YGEEVKFGGGKVIRDGMGQGQMT-ADDCVDLVLTNALI 75
Cdd:PRK13206 1 MTRLSRERYAALYGPTTGDRIRLADTDLLIEVTEDRSGgpglAGDEAVFGGGKVIRESMGQGRATrAEGAPDTVITGAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 76 VDHWGIVKADIGVKNGRIFAVGKAGNPDIQPGV--TIPIGAATEAIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTT 153
Cdd:PRK13206 81 LDHWGIVKADVGIRDGRIVAIGKAGNPDIMDGVhpDLVIGPSTEIIAGNGRILTAGAIDCHVHFICPQIVDEALAAGITT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 154 MIGGGTGPAAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPDALREQIAAGAIGLKIHEDWGATPAAINCSL 233
Cdd:PRK13206 161 LIGGGTGPAEGSKATTVTPGAWHLARMLEALDGWPVNVALLGKGNTVSAEALWEQLRGGAGGFKLHEDWGSTPAAIDACL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 234 EVAEEMDIQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHL 313
Cdd:PRK13206 241 RVADAAGVQVALHSDTLNEAGFVEDTLAAIAGRSIHAYHTEGAGGGHAPDIITVASHPNVLPSSTNPTRPHTVNTLDEHL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 314 DMLMVCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALPEETG 393
Cdd:PRK13206 321 DMLMVCHHLNPAVPEDLAFAESRIRPSTIAAEDVLHDMGAISMIGSDSQAMGRIGEVVLRTWQTAHVMKRRRGALPGDGR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 394 dNDNFRVKRYIAKYTINPALTHGIAHEVGSIEAGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHY 473
Cdd:PRK13206 401 -ADNNRARRYVAKYTICPAVAHGIDHEIGSVEVGKLADLVLWEPAFFGVRPHAVLKGGAIAWAAMGDANASIPTPQPVLP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 474 RPMFGALGAARHATRLTFVSQAADAQGIAQQLNLQSATAVVKGCRTVKKADMIHNGLQPNITVDSQTYEVRVDGELITSE 553
Cdd:PRK13206 480 RPMFGAAPAAAAATSVHFVAPQAIEDGLADRLGLRRRLVPVADTRAVGKADMPLNDALPDIEVDPDTFTVRIDGEVWEPQ 559
|
570
....*....|....
gi 1732753225 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: 895.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 4 ISRQAYADMFGPTTGDKVRLADSELWIEVENDLTVYGEEVKFGGGKVIRDGMGQGQM-TADDCVDLVLTNALIVDHWGIV 82
Cdd:PLN02303 271 ISREKYANMYGPTTGDKIRLGDTNLYAEIEKDFTVYGDECKFGGGKVLRDGMGQATGyGAADSLDTVITNAVIIDYTGIY 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 83 KADIGVKNGRIFAVGKAGNPDIQPGVT--IPIGAATEAIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMIGGGTG 160
Cdd:PLN02303 351 KADIGIKDGLIVGIGKAGNPDVMDGVTsnMIVGVNTEVIAGEGMIVTAGGIDCHVHFICPQLATEAIASGITTLVGGGTG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 161 PAAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPDALREQIAAGAIGLKIHEDWGATPAAINCSLEVAEEMD 240
Cdd:PLN02303 431 PAHGTCATTCTPAPSHMKLMLQSTDDLPLNFGFTGKGNTAKPEGLHEIIKAGAMGLKLHEDWGTTPAAIDNCLDVAEEYD 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 241 IQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDMLMVCH 320
Cdd:PLN02303 511 IQVTIHTDTLNESGCVEHSIAAFKGRTIHTYHSEGAGGGHAPDIIKVCGVKNVLPSSTNPTRPYTKNTIDEHLDMLMVCH 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 321 HLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALPEETGDNDNFRV 400
Cdd:PLN02303 591 HLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSDSQAMGRIGEVITRTWQTAHKMKSQRGALEPRGADNDNFRI 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 401 KRYIAKYTINPALTHGIAHEVGSIEAGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYRPMFGAL 480
Cdd:PLN02303 671 KRYIAKYTINPAIAHGMSHFVGSVEVGKLADLVLWKPAFFGAKPEMVIKGGQIAWAQMGDPNASIPTPEPVIMRPMFGAF 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 481 GAARHATRLTFVSQAADAQGIAQQLNLQSATAVVKGCRTVKKADMIHNGLQPNITVDSQTYEVRVDGELITSEPADVLPM 560
Cdd:PLN02303 751 GKAGSSNSIAFVSKAALDAGVKQLYGLTKRVEAVGNVRGLTKLDMKLNDALPVITVDPETYEVTADGEVLTCAPATSVPL 830
|
....*..
gi 1732753225 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: 877.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 1 MAEISRQAYADMFGPTTGDKVRLADSELWIEVENDLTVYGEEVKFGGGKVIRDGMG--QGQMTADDCVDLVLTNALIVDH 78
Cdd:PRK13308 1 MATIDRRAYAELYGPTTGDRVRLADTSLLAEVEHDHTVYGDECLFGGGKTLRDGMGmaPGVTSADGALDFVLCNVTVIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 79 -WGIVKADIGVKNGRIFAVGKAGNPDIQPGVT--IPIGAATEAIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMI 155
Cdd:PRK13308 81 vLGIVKGDIGIRDGRIVGIGKAGNPDIMDGVDprLVVGPGTDVRPAEGLIATPGAIDVHVHFDSAQLVDHALASGITTML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 156 GGGTGPAagtnATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPDALREQIAAGAIGLKIHEDWGATPAAINCSLEV 235
Cdd:PRK13308 161 GGGLGPT----VGIDSGGPFNTGRMLQAAEAWPVNFGFLGRGNSSKPAALIEQVEAGACGLKIHEDWGAMPAAIDTCLEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 236 AEEMDIQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDM 315
Cdd:PRK13308 237 ADEYDFQVQLHTDTLNESGFVEDTLAAIGGRTIHMYHTEGAGGGHAPDIIRVVGEPHCLPSSTNPTNPYTVNTFDEHLDM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 316 LMVCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALPEETG-D 394
Cdd:PRK13308 317 TMVCHHLNPDVPEDVAFAESRIRAQTIAAEDVLHDIGAISMLGSDSQGMGRIAEVIARTWQLASKMKDQRGPLPEDRGtF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 395 NDNFRVKRYIAKYTINPALTHGIAHEVGSIEAGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYR 474
Cdd:PRK13308 397 ADNARIKRYIAKYTINPAITFGIDDHIGSLEPGKLADIVLWRPAFFGIKPELVIKGGFPAWAAMGDANGSLMTCEPMLQR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 475 PMFGALGAARHATRLTFVSQAADAQGIAQQLNLQSATAVVKGCRTVKKADMIHNGLQPNITVDSQTYEVRVDGELITSEP 554
Cdd:PRK13308 477 PQWGAFGRAKQALSVCFVSPLAIEAGLGERLGLRKRLLPVRGTRTLTKADMLHNDACPDIRVDPQTFEVFVDGELVTCEP 556
|
570
....*....|..
gi 1732753225 555 ADVLPMAQRYFL 566
Cdd:PRK13308 557 ATELPLAQRYML 568
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
3-567 |
0e+00 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 833.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 3 EISRQAYADMFGPTTGDKVRLADSELWIEVENDLTVYGEEVKFGGGKVIRDGMGQGQMTADDCVDLVLTNALIVDHWGIV 82
Cdd:PRK13985 2 KISRKEYVSMYGPTTGDKVRLGDTDLIAEVEHDYTIYGEELKFGGGKTLREGMSQSNNPSKEELDLIITNALIIDYTGIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 83 KADIGVKNGRIFAVGKAGNPDIQPGVT--IPIGAATEAIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMIGGGTG 160
Cdd:PRK13985 82 KADIGIKDGKIAGIGKGGNKDMQDGVKnnLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTAFASGVTTMIGGGTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 161 PAAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPDALREQIAAGAIGLKIHEDWGATPAAINCSLEVAEEMD 240
Cdd:PRK13985 162 PADGTNATTITPGRRNLKWMLRAAEEYSMNLGFLGKGNSSNDASLADQIEAGAIGFKIHEDWGTTPSAINHALDVADKYD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 241 IQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDMLMVCH 320
Cdd:PRK13985 242 VQVAIHTDTLNEAGCVEDTMAAIAGRTMHTFHTEGAGGGHAPDIIKVAGEHNILPASTNPTIPFTVNTEAEHMDMLMVCH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 321 HLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALPEETGDNDNFRV 400
Cdd:PRK13985 322 HLDKSIKEDVQFADSRIRPQTIAAEDTLHDMGIFSITSSDSQAMGRVGEVITRTWQTADKNKKEFGRLKEEKGDNDNFRI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 401 KRYIAKYTINPALTHGIAHEVGSIEAGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYRPMFGAL 480
Cdd:PRK13985 402 KRYLSKYTINPAIAHGISEYVGSVEVGKVADLVLWSPAFFGVKPNMIIKGGFIALSQMGDANASIPTPQPVYYREMFAHH 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 481 GAARHATRLTFVSQAADAQGIAQQLNLQSATAVVKGCRTVKKADMIHNGLQPNITVDSQTYEVRVDGELITSEPADVLPM 560
Cdd:PRK13985 482 GKAKYDANITFVSQAAYDKGIKEELGLERQVLPVKNCRNITKKDMQFNDTTAHIEVNPETYHVFVDGKEVTSKPANKVSL 561
|
....*..
gi 1732753225 561 AQRYFLF 567
Cdd:PRK13985 562 AQLFSIF 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: 759.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 1 MAEISRQAYADMFGPTTGDKVRLADSELWIEVENDLTVYGEEVKFGGGKVIRDGMGQ-GQMTADD-CVDLVLTNALIVD- 77
Cdd:PRK13309 1 MPQISRQEYAGLFGPTTGDKIRLGDTNLFIEIEKDLRGYGDESVYGGGKSLRDGMGAnNNLTRDNgVLDLVITNVTIVDa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 78 HWGIVKADIGVKNGRIFAVGKAGNPDIQPGVT--IPIGAATEAIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMI 155
Cdd:PRK13309 81 RLGVIKADVGIRDGKIVGIGKSGNPSTMDGVTqgMVVGVSTDAISGEHLILTAAGIDTHIHLISPQQAYHALSNGVTTFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 156 GGGTGPAAGTNATTCTPGPWYIARMLQAADTLPVNIGLLGKGNGSNPDALREQIAAGAIGLKIHEDWGATPAAINCSLEV 235
Cdd:PRK13309 161 GGGIGPTDGTNGTTVTPGPWNIRQMLRSIEGLPVNVGILGKGNSYGRGPLLEQAIAGVAGYKVHEDWGATAAALRHALRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 236 AEEMDIQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTVNTIDEHLDM 315
Cdd:PRK13309 241 ADEVDIQVAVHTDSLNECGYVEDTIDAFEGRTIHTFHTEGAGGGHAPDIIKVASQTNVLPSSTNPTLPYGVNSQAELFDM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 316 LMVCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDIGAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALPEETGDN 395
Cdd:PRK13309 321 IMVCHNLNPNVPADVAFAESRVRPETIAAENVLHDMGVISMFSSDSQAMGRVGENWLRAIQTADAMKAARGKLPEDAAGN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 396 DNFRVKRYIAKYTINPALTHGIAHEVGSIEAGKLADLVVWSPAFFGVKPATIVKGGMIACAPMGDINASIPTPQPVHYRP 475
Cdd:PRK13309 401 DNFRVLRYVAKITINPAITQGVSHVIGSVEVGKMADLVLWEPRFFGAKPKMVIKGGMINWAAMGDPNASLPTPQPVFYRP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 476 MFGALGAARHATRLTFVSQAADAQGIAQQLNLQSATAVVKGCRTVKKADMIHNGLQPNITVDSQTYEVRVDGELITSEPA 555
Cdd:PRK13309 481 MFGAMGKTLQDTCVTFVSQAALDDGVKEKAGLDRQVIAVKNCRTISKRDLVRNSQTPNIEVDPETFAVKVDGVHATVKPI 560
|
570
....*....|.
gi 1732753225 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 ... |
3-119 |
1.28e-72 |
|
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: 227.38 E-value: 1.28e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 3 EISRQAYADMFGPTTGDKVRLADSELWIEVENDLTVYGEEVKFGGGKVIRDGMGQGQM-TADDCVDLVLTNALIVDHWGI 81
Cdd:pfam00449 1 KISREAYADMYGPTTGDRIRLGDTDLFIEVEKDLTVYGDEVKFGGGKVIRDGMGQSQGrTRDDALDLVITNALILDYTGI 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1732753225 82 VKADIGVKNGRIFAVGKAGNPDIQPGVT--IPIGAATEAI 119
Cdd:pfam00449 81 VKADIGIKDGRIVGIGKAGNPDTMDGVTpgMVIGPSTEVI 120
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
125-454 |
9.16e-70 |
|
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: 227.77 E-value: 9.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 125 IVTAGGIDTHIHW---------ICPQQAEEALVSGVTTMIGGGTGPAAGTNATTCTpgpwYIARMLQAADTLPVNIGLLG 195
Cdd:pfam01979 1 IVLPGLIDAHVHLemgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTST----GIEALLEAAEELPLGLRFLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 196 K-------GNGSNPDALREQIAAGA------------IGLKIHEDWGATPAAINCSLEVAEEMDIQVALHsdTLNESGFV 256
Cdd:pfam01979 77 PgcsldtdGELEGRKALREKLKAGAefikgmadgvvfVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIH--ALETKGEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 257 EDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTnptlpyTVNTIDEHLDMLMVCHhldpdiaedVAFAESR 336
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLSPT------EANLLAEHLKGAGVAH---------CPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 337 IRRETIAAEDVLHDiGAFSLTSSDSQAMGRVGEVILRTwqvahrmkvqRGALPEETGDNDNFRVKRYIAKYTINPALTHG 416
Cdd:pfam01979 220 LRSGRIALRKALED-GVKVGLGTDGAGSGNSLNMLEEL----------RLALELQFDPEGGLSPLEALRMATINPAKALG 288
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1732753225 417 IAHEVGSIEAGKLADLVVWS----PAFFGVKPATIVKGGMIA 454
Cdd:pfam01979 289 LDDKVGSIEVGKDADLVVVDldplAAFFGLKPDGNVKKVIVK 330
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
67-436 |
2.06e-17 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 84.24 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 67 DLVLTNALIVDHWG---IVKADIGVKNGRIFAVGKAGnpdiqpgvTIPIGAATEAIAAEGKIVTAGGIDTHIH------- 136
Cdd:COG1228 9 TLLITNATLVDGTGggvIENGTVLVEDGKIAAVGPAA--------DLAVPAGAEVIDATGKTVLPGLIDAHTHlglgggr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 137 -----------------WICPQQAEEALVSGVTTMIGGGTGPAAGTNAT-----TCTPGPwyiaRMLQAADTLPVNIGLL 194
Cdd:COG1228 81 avefeagggitptvdlvNPADKRLRRALAAGVTTVRDLPGGPLGLRDAIiagesKLLPGP----RVLAAGPALSLTGGAH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 195 GKGNGSNPDALREQIAAGAIGLKIHEDWGA---TPAAINCSLEVAEEMDIQVALHSDTLnesgfvEDTLAAI--GGRTIH 269
Cdd:COG1228 157 ARGPEEARAALRELLAEGADYIKVFAEGGApdfSLEELRAILEAAHALGLPVAAHAHQA------DDIRLAVeaGVDSIE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 270 tfHtegaGGGHAPDIITACAHPNilPSSTNPTLPYTVNtidehldmlmvchhLDPDIAEDVAFAESRIRRETIAAEDVLH 349
Cdd:COG1228 231 --H----GTYLDDEVADLLAEAG--TVVLVPTLSLFLA--------------LLEGAAAPVAAKARKVREAALANARRLH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 350 DIGAFSLTSSDSQAMGRVGeviLRTWQVAHRMkVQRGALPEETgdndnfrvkryIAKYTINPALTHGIAHEVGSIEAGKL 429
Cdd:COG1228 289 DAGVPVALGTDAGVGVPPG---RSLHRELALA-VEAGLTPEEA-----------LRAATINAAKALGLDDDVGSLEPGKL 353
|
....*..
gi 1732753225 430 ADLVVWS 436
Cdd:COG1228 354 ADLVLLD 360
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
69-218 |
1.76e-14 |
|
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: 75.51 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 69 VLTNALIVDHWGIVKADIGVKNGRIFAVGKAgnpdiqpgvtIPIGAATEAIAAEGKIVTAGGIDTHIHWICPQQAEE--- 145
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPD----------LAAPEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKedi 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 146 ------ALVSGVTTMIgggtgPAAGTNATTCTPG--PWYIARmlqAADTLPVNIGLLG---KGNGSNPDALREQIAAGAI 214
Cdd:COG0044 71 etgtraAAAGGVTTVV-----DMPNTNPVTDTPEalEFKLAR---AEEKALVDVGPHGaltKGLGENLAELGALAEAGAV 142
|
....
gi 1732753225 215 GLKI 218
Cdd:COG0044 143 AFKV 146
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
67-155 |
7.47e-11 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 64.74 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 67 DLVLTNALIVD-HWG-IVKADIGVKNGRIFAVGKAgnpdiqpgvtipIGAATEAIAAEGKIVTAGGIDTHIH----WICP 140
Cdd:COG1001 6 DLVIKNGRLVNvFTGeILEGDIAIAGGRIAGVGDY------------IGEATEVIDAAGRYLVPGFIDGHVHiessMVTP 73
|
90
....*....|....*.
gi 1732753225 141 QQ-AEEALVSGVTTMI 155
Cdd:COG1001 74 AEfARAVLPHGTTTVI 89
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
67-217 |
1.39e-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: 63.46 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 67 DLVLTNALIVDHWGIVKADIGVKNGRIFAVGKagnpdiqpgvTIPIGAATEAIAAEGKIVTAGGIDTHIHWICPQQAE-- 144
Cdd:cd01315 1 DLVIKNGRVVTPDGVREADIAVKGGKIAAIGP----------DIANTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEwe 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 145 -------EALVSGVTTMIgggtgpAAGTNATTCTPGPWYIARMLQAA-DTLPVNIGLLGKGNGSNPDALREQIAAGAIGL 216
Cdd:cd01315 71 gfetgtkAAAAGGITTII------DMPLNSIPPTTTVENLEAKLEAAqGKLHVDVGFWGGLVPGNLDQLRPLDEAGVVGF 144
|
.
gi 1732753225 217 K 217
Cdd:cd01315 145 K 145
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
67-155 |
5.70e-10 |
|
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: 61.54 E-value: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 67 DLVLTNALIVDHWG--IVKADIGVKNGRIFAVGKAGNPDiqpgvtipigaATEAIAAEGKIVTAGGIDTHIHW----ICP 140
Cdd:cd01297 1 DLVIRNGTVVDGTGapPFTADVGIRDGRIAAIGPILSTS-----------AREVIDAAGLVVAPGFIDVHTHYdgqvFWD 69
|
90
....*....|....*
gi 1732753225 141 QQAEEALVSGVTTMI 155
Cdd:cd01297 70 PDLRPSSRQGVTTVV 84
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
68-155 |
2.40e-09 |
|
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: 59.54 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 68 LVLTNALIVDHWGIVKADIGVKNGRIFAVGKagnpdiqpgvTIPIGAATEAIAAEGKIVTAGGIDTHIHWICP------- 140
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGP----------NLEAPGGVEVIDATGKYVLPGGIDPHTHLELPfmgtvta 70
|
90
....*....|....*...
gi 1732753225 141 ---QQAEEALVSGVTTMI 155
Cdd:cd01314 71 ddfESGTRAAAAGGTTTI 88
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
67-136 |
1.90e-08 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 57.02 E-value: 1.90e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 67 DLVLTNALIVDHWGIVKADIGVKNGRIFAVGKAgnpdiqpgvtipIGAATEAIAAEGKIVTAGGIDTHIH 136
Cdd:PRK13404 5 DLVIRGGTVVTATDTFQADIGIRGGRIAALGEG------------LGPGAREIDATGRLVLPGGVDSHCH 62
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
67-136 |
2.57e-08 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 56.47 E-value: 2.57e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 67 DLVLTNALIVDHWGIVKADIGVKNGRIFAVGKAGNPDiqpgvtipigaATEAIAAEGKIVTAGGIDTHIH 136
Cdd:PRK09060 6 DLILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGAS-----------AGEVIDCRGLHVLPGVIDSQVH 64
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
67-217 |
3.69e-08 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 55.86 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 67 DLVLTNALIVDHWGIVKADIGVKNGRIFAVGkagnPDIQpgvtipiGAATEAIAAEGKIVTAGGIDTHIHWICPQQAE-E 145
Cdd:PRK06189 4 DLIIRGGKVVTPEGVYRADIGIKNGKIAEIA----PEIS-------SPAREIIDADGLYVFPGMIDVHVHFNEPGRTHwE 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732753225 146 ALVSGVTTMIGGGTGPAAGT--NATTCTPGPWYIARMLQAADTLP-VNIGLLGKGNGSNPDALREQIAAGAIGLK 217
Cdd:PRK06189 73 GFATGSAALAAGGCTTYFDMplNSIPPTVTREALDAKAELARQKSaVDFALWGGLVPGNLEHLRELAEAGVIGFK 147
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
67-136 |
6.91e-08 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 55.18 E-value: 6.91e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 67 DLVLTNALIVDHWGIVKADIGVKNGRIFAVGKagnpdiqpgvtipiGAATEAIAAEGKIVTAGGIDTHIH 136
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGA--------------NLGDEVIDATGKYVMPGGIDPHTH 57
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
67-155 |
2.22e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 50.42 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 67 DLVLTNALIVDHWGIVKADIGVKNGRIFAVGKAgnpdiqpgvtIPIGAATEAIAAEGKIVTAGGIDTHIHWICPQQAEE- 145
Cdd:PRK02382 3 DALLKDGRVYYNNSLQPRDVRIDGGKITAVGKD----------LDGSSSEEVIDARGMLLLPGGIDVHVHFREPGYTHKe 72
|
90
....*....|....*...
gi 1732753225 146 --------ALVSGVTTMI 155
Cdd:PRK02382 73 twytgsrsAAAGGVTTVV 90
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
67-435 |
2.42e-06 |
|
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: 50.21 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 67 DLVLTNALIVDHWG----IVKADIGVKNGRIFAVGKAGNPDIQPgvtipigAATEAIAAEGKIVTAGGIDTHIH------ 136
Cdd:COG0402 1 DLLIRGAWVLTMDPaggvLEDGAVLVEDGRIAAVGPGAELPARY-------PAAEVIDAGGKLVLPGLVNTHTHlpqtll 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 137 -----------W-----------ICPQQAE--------EALVSGVTTMigggtgpaagtnATTCTPGPWYIARMLQAADT 186
Cdd:COG0402 74 rgladdlplldWleeyiwplearLDPEDVYagallalaEMLRSGTTTV------------ADFYYVHPESADALAEAAAE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 187 LPVNiGLLGKG--NGSNPDALREQIAAG-AIGLKIHEDW----------GATP-AAINCSLEV-------AEEMDIQVAL 245
Cdd:COG0402 142 AGIR-AVLGRGlmDRGFPDGLREDADEGlADSERLIERWhgaadgrirvALAPhAPYTVSPELlraaaalARELGLPLHT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 246 HsdtLNES-GFVEDTLAAIGGRTIHTFHTEGAGGGHapdiiTACAHpnilpsstnptlpytvntidehldmlmvCHHLDP 324
Cdd:COG0402 221 H---LAETrDEVEWVLELYGKRPVEYLDELGLLGPR-----TLLAH----------------------------CVHLTD 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 325 DiaeDVA-FAESRIrreTIA---------------AEDVLH---------DIGAfsltSSDSQAMgrvgeviLRTWQVAh 379
Cdd:COG0402 265 E---EIAlLAETGA---SVAhcptsnlklgsgiapVPRLLAagvrvglgtDGAA----SNNSLDM-------FEEMRLA- 326
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1732753225 380 rMKVQRGAlpeeTGDNDNFRVKRYIAKYTINPALTHGIAHEVGSIEAGKLADLVVW 435
Cdd:COG0402 327 -ALLQRLR----GGDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVL 377
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
407-447 |
3.91e-06 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 49.80 E-value: 3.91e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1732753225 407 YTINPALTHGIAHEVGSIEAGKLADLVVWSPAFFGVKPATI 447
Cdd:COG1574 476 YTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEI 516
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
68-136 |
5.52e-06 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 48.69 E-value: 5.52e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732753225 68 LVLTNALIVDHWGIVKA--DIGVKNGRIFAVGKagnpdiqpgvTIPIGAATEAIAAEGKIVTAGGIDTHIH 136
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAG----------DIDGSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
68-136 |
6.49e-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: 48.73 E-value: 6.49e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732753225 68 LVLTNALIVDHWGIVKADIGVKNGRIFAVGKAgnpdiqpgvtIPIGAATEAIAAEGKIVTAGGIDTHIH 136
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPE----------DELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
404-448 |
1.07e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 48.30 E-value: 1.07e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1732753225 404 IAKYTINPALTHGIAHEVGSIEAGKLADLVVWSPAFFGVKPATIV 448
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIA 449
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
408-436 |
1.09e-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: 47.69 E-value: 1.09e-05
10 20
....*....|....*....|....*....
gi 1732753225 408 TINPALTHGIAHEVGSIEAGKLADLVVWS 436
Cdd:cd01309 310 TINPAKILGIEDRVGSLEPGKDADLVVWN 338
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
404-434 |
1.63e-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: 47.69 E-value: 1.63e-05
10 20 30
....*....|....*....|....*....|.
gi 1732753225 404 IAKYTINPALTHGIAHEVGSIEAGKLADLVV 434
Cdd:cd01300 449 LRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
58-155 |
7.01e-05 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 45.46 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 58 GQMTADDCVDLVLTNALIVDHWGIVKA--DIGVKNGRIFAVGkagnpdiqpgvTIPIGAATEaIAAEGKIVTAGGIDTHI 135
Cdd:PRK09061 11 LMPASMAPYDLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVG-----------TAAIEGDRT-IDATGLVVAPGFIDLHA 78
|
90 100
....*....|....*....|
gi 1732753225 136 HWICPQQAEEALVSGVTTMI 155
Cdd:PRK09061 79 HGQSVAAYRMQAFDGVTTAL 98
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
408-450 |
8.00e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 45.09 E-value: 8.00e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1732753225 408 TINPALTHGIAHEVGSIEAGKLADLVVWSPAfFGVKpATIVKG 450
Cdd:COG1820 332 SLNPARALGLDDRKGSIAPGKDADLVVLDDD-LNVR-ATWVGG 372
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
69-136 |
9.05e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 45.09 E-value: 9.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732753225 69 VLTNALIVDHWGIVK-ADIGVKNGRIFAVGKAGNPDIqpgvtipigaatEAIAAEGKIVTAGGIDTHIH 136
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPGAEPDA------------EVIDLGGGYLAPGFIDLHVH 57
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
68-136 |
1.87e-04 |
|
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: 44.12 E-value: 1.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732753225 68 LVLTNALIV---DHWGIVKADIGVKNGRIFAVGKAGNPDIQPGVTIpigaateaIAAEGKIVTAGGIDTHIH 136
Cdd:cd01298 1 ILIRNGTIVttdPRRVLEDGDVLVEDGRIVAVGPALPLPAYPADEV--------IDAKGKVVMPGLVNTHTH 64
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
85-155 |
2.09e-04 |
|
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: 43.86 E-value: 2.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732753225 85 DIGVKNGRIFAVGKAGNPDiqpgvtipigAATEAIAAEGKIVTAGGIDTHIHwiCPQQAEE--------ALVSGVTTMI 155
Cdd:cd01307 1 DVAIENGKIAAVGAALAAP----------AATQIVDAGGCYVSPGWIDLHVH--VYQGGTRygdrpdmiGVKSGVTTVV 67
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
408-451 |
6.25e-04 |
|
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: 42.25 E-value: 6.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1732753225 408 TINPALTHGIAHEVGSIEAGKLADLVVWS-------PAFFGVKP-ATIVKGG 451
Cdd:cd01296 320 TINAAAALGLGETVGSLEVGKQADLVILDapsyehlAYRFGVNLvEYVIKNG 371
|
|
| PLN02795 |
PLN02795 |
allantoinase |
69-217 |
9.33e-04 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 42.07 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 69 VLTNALIVDHWGIVKADIGVKNGRIFAVGKAGN-PDIQPGV-TIPIGAAteaiaaegkIVTAGGIDTHIHWICPQQAE-- 144
Cdd:PLN02795 47 VLYSKRVVTPAGVIPGAVEVEGGRIVSVTKEEEaPKSQKKPhVLDYGNA---------VVMPGLIDVHVHLNEPGRTEwe 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 145 -------EALVSGVTTMIGGGTGPaagtNATTCTPGPwYIARMLQAADTLPVNIGLLGK---GNGSNPDALREQIAAGAI 214
Cdd:PLN02795 118 gfptgtkAAAAGGITTLVDMPLNS----FPSTTSVET-LELKIEAAKGKLYVDVGFWGGlvpENAHNASVLEELLDAGAL 192
|
...
gi 1732753225 215 GLK 217
Cdd:PLN02795 193 GLK 195
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
67-136 |
1.08e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 41.54 E-value: 1.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 67 DLVLTNALIVDhwGIVKADIGVKNGRIFAVGkagnPDIQpgvtipiGAATEAIAAEGKIVTAGGIDTHIH 136
Cdd:PRK07572 3 DLIVRNANLPD--GRTGIDIGIAGGRIAAVE----PGLQ-------AEAAEEIDAAGRLVSPPFVDPHFH 59
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
68-136 |
1.57e-03 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 40.95 E-value: 1.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 68 LVLTNALIVDHWGI-VKADIGVKNGRIFAVGKAGNPDiqpgvtipigaATEAIAAEGKIVTAGGIDTHIH 136
Cdd:PRK09357 3 ILIKNGRVIDPKGLdEVADVLIDDGKIAAIGENIEAE-----------GAEVIDATGLVVAPGLVDLHVH 61
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
67-155 |
2.11e-03 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 40.61 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 67 DLVLTNALIVDHWGIVKADIGVKNGRIFAVGKAgnpdiqpgvtipIGAATEAIAAEGKIVTAGGIDTHIHWICPQQA--- 143
Cdd:PRK08044 4 DLIIKNGTVILENEARVVDIAVKGGKIAAIGQD------------LGDAKEVMDASGLVVSPGMVDAHTHISEPGRShwe 71
|
90
....*....|....*...
gi 1732753225 144 ------EEALVSGVTTMI 155
Cdd:PRK08044 72 gyetgtRAAAKGGITTMI 89
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
67-136 |
2.31e-03 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 40.55 E-value: 2.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732753225 67 DLVLTNALIV---DHWGIVKAdIGVKNGRIFAVGkaGNPDIQPGvtipIGAATEAIAAEGKIVTAGGIDTHIH 136
Cdd:COG1574 9 DLLLTNGRIYtmdPAQPVAEA-VAVRDGRIVAVG--SDAEVRAL----AGPATEVIDLGGKTVLPGFIDAHVH 74
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
83-136 |
5.09e-03 |
|
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: 39.70 E-value: 5.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1732753225 83 KADIGVKNGRIFAVGKAGNPDiqpgvtipigaatEAIAAEGKIVTAGGIDTHIH 136
Cdd:cd01304 17 KMDIFIRDGKIVESSSGAKPA-------------KVIDASGKVVMAGGVDMHSH 57
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
70-136 |
6.52e-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: 39.15 E-value: 6.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732753225 70 LTNALIVDhWGIVKADIGVKNGRIFAVGKAGnpdiqpgvtiPIGAATEAIAAEGKIVTAGGIDTHIH 136
Cdd:cd01293 2 LRNARLAD-GGTALVDIAIEDGRIAAIGPAL----------AVPPDAEEVDAKGRLVLPAFVDPHIH 57
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
67-155 |
6.66e-03 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 38.97 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 67 DLVLTNALIVD--HWGIVKADIGVKNGRIFavgkagnpdiqPGVTIPIGAATEAIAAEGKIVTAGGIDTHIHwICPQQAE 144
Cdd:PRK12394 4 DILITNGHIIDpaRNINEINNLRIINDIIV-----------DADKYPVASETRIIHADGCIVTPGLIDYHAH-VFYDGTE 71
|
90
....*....|....*...
gi 1732753225 145 EA-------LVSGVTTMI 155
Cdd:PRK12394 72 GGvrpdmymPPNGVTTVV 89
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
131-305 |
8.06e-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: 38.47 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 131 IDTHIH---------------------------WICPQQAEEALVSGVTTMIGGGTGPAAgtnattcTPGPWYIARMLQA 183
Cdd:cd01292 2 IDTHVHldgsalrgtrlnlelkeaeelspedlyEDTLRALEALLAGGVTTVVDMGSTPPP-------TTTKAAIEAVAEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732753225 184 ADTLPVNIGLLGKG------------NGSNPDALREQIAAGAIGLKIHEDWGAT---PAAINCSLEVAEEMDIQVALH-S 247
Cdd:cd01292 75 ARASAGIRVVLGLGipgvpaavdedaEALLLELLRRGLELGAVGLKLAGPYTATglsDESLRRVLEEARKLGLPVVIHaG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1732753225 248 DTLNESGFVEDTLAAIG-GRTIHTFHtegaGGGHAPDIITACAHPNILPSSTNPTLPYT 305
Cdd:cd01292 155 ELPDPTRALEDLVALLRlGGRVVIGH----VSHLDPELLELLKEAGVSLEVCPLSNYLL 209
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
86-136 |
8.07e-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: 38.78 E-value: 8.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1732753225 86 IGVKNGRIFAVGKAgnpdiqPGVTIPIGAATEAIAAEGKIVTAGGIDTHIH 136
Cdd:cd01296 1 IAIRDGRIAAVGPA------ASLPAPGPAAAEEIDAGGRAVTPGLVDCHTH 45
|
|
| |
