|
Name |
Accession |
Description |
Interval |
E-value |
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
2-571 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 1117.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 2 SFKMTQSQYTSLYGPTTGDSIRLGDTNLFAQVEHDYTSYGDEVTFGGGKSIRDGMGQNPNVTRDDryVADLVITNAVIID 81
Cdd:PRK13207 1 MAKISRRAYAEMYGPTTGDRVRLADTELWIEVEKDFTTYGEEVKFGGGKVIRDGMGQSQRARADG--AVDTVITNALILD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 82 YDKVVKADIGIKNGYIFAIGQAGNPDIMDNIDIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQAEVALESGITTHIGG 161
Cdd:PRK13207 79 HWGIVKADIGIKDGRIVAIGKAGNPDIQDGVDIIIGPGTEVIAGEGLIVTAGGIDTHIHFICPQQIEEALASGVTTMIGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 162 GTGASEGTKATTVTPGPWHIHRMLEAAEQLPINVGFTGKGQAVNHTALIEQIHAGVIGLKVHEDWGATPSALDHALAVAD 241
Cdd:PRK13207 159 GTGPATGTNATTCTPGPWHIHRMLQAADAFPMNIGFLGKGNASLPEALEEQIEAGAIGLKLHEDWGATPAAIDNCLSVAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 242 EFDVQIALHADTLNEAGFMEDTMAAVKGRVLHMYHTEGAGGGHAPDLIKSASYPNILPSSTNPTLPYTQNTVDEHLDMVM 321
Cdd:PRK13207 239 EYDVQVAIHTDTLNESGFVEDTIAAFKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDMLM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 322 ITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGFLDGDAEYNDN 401
Cdd:PRK13207 319 VCHHLDPSIPEDVAFAESRIRRETIAAEDILHDLGAISMISSDSQAMGRVGEVIIRTWQTAHKMKVQRGPLPGDSGRNDN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 402 NRIKRYIAKYTINPAITHGISDYVGSIEGGKLADLVMWEPAFFGVKPELIVKGGLINAAVNGDANGSIPTSEPQKYRKMY 481
Cdd:PRK13207 399 FRVKRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWKPAFFGVKPELVLKGGMIAWAPMGDPNASIPTPQPVHYRPMF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 482 GQYGGNLQHTAITFVSKTAFESGIYRSLNLQRMVRPVHGIRNLTKKDMKNNDATPKLDVDPQTYEVFVDGEKVTSEPATE 561
Cdd:PRK13207 479 GAYGGALAATSVTFVSQAALDAGIPEKLGLKKRLVPVKNTRGITKADMKLNDATPKIEVDPETYEVRADGELLTCEPATV 558
|
570
....*....|
gi 1093480465 562 LPLTQRYFLF 571
Cdd:PRK13207 559 LPLAQRYFLF 568
|
|
| UreC |
COG0804 |
Urease alpha subunit [Amino acid transport and metabolism]; |
2-571 |
0e+00 |
|
Urease alpha subunit [Amino acid transport and metabolism];
Pssm-ID: 440567 [Multi-domain] Cd Length: 570 Bit Score: 1106.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 2 SFKMTQSQYTSLYGPTTGDSIRLGDTNLFAQVEHDYTSYGDEVTFGGGKSIRDGMGQNPNvTRDDRyVADLVITNAVIID 81
Cdd:COG0804 1 MAKISRKAYADLYGPTTGDRVRLADTDLFIEVEKDLTTYGDEVKFGGGKVIRDGMGQSQT-TRAEG-ALDLVITNAVILD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 82 YDKVVKADIGIKNGYIFAIGQAGNPDIMD--NIDIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQAEVALESGITTHI 159
Cdd:COG0804 79 HWGIVKADIGIKDGRIVGIGKAGNPDTMDgvDPDLVIGPGTEVIAGEGLILTAGGIDTHIHFICPQQIEEALASGITTMI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 160 GGGTGASEGTKATTVTPGPWHIHRMLEAAEQLPINVGFTGKGQAVNHTALIEQIHAGVIGLKVHEDWGATPSALDHALAV 239
Cdd:COG0804 159 GGGTGPAEGTNATTCTPGPWNIARMLEAADALPMNIGFLGKGNASSPEALEEQIRAGACGLKLHEDWGATPAAIDACLSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 240 ADEFDVQIALHADTLNEAGFMEDTMAAVKGRVLHMYHTEGAGGGHAPDLIKSASYPNILPSSTNPTLPYTQNTVDEHLDM 319
Cdd:COG0804 239 ADEYDVQVAIHTDTLNESGFVEDTIAAIKGRTIHTFHTEGAGGGHAPDIIKVAGEPNVLPSSTNPTRPYTVNTIDEHLDM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 320 VMITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGFLDGDAEYN 399
Cdd:COG0804 319 LMVCHHLDPSIPEDVAFAESRIRPETIAAEDVLHDLGAISMMSSDSQAMGRVGEVITRTWQTAHKMKKQRGPLPGDSGRN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 400 DNNRIKRYIAKYTINPAITHGISDYVGSIEGGKLADLVMWEPAFFGVKPELIVKGGLINAAVNGDANGSIPTSEPQKYRK 479
Cdd:COG0804 399 DNFRVKRYVAKYTINPAIAHGISHEVGSVEVGKLADLVLWDPAFFGVKPELVIKGGMIAWAQMGDPNASIPTPQPVHYRP 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 480 MYGQYGGNLQHTAITFVSKTAFESGIYRSLNLQRMVRPVHGIRNLTKKDMKNNDATPKLDVDPQTYEVFVDGEKVTSEPA 559
Cdd:COG0804 479 MFGAYGKALAATSVTFVSQAALEAGIAERLGLRKRLLPVKNTRNIGKADMVLNDATPDIEVDPETYEVRVDGELLTCEPA 558
|
570
....*....|..
gi 1093480465 560 TELPLTQRYFLF 571
Cdd:COG0804 559 TELPLAQRYFLF 570
|
|
| urease_alph |
TIGR01792 |
urease, alpha subunit; This model describes the urease alpha subunit UreC (designated beta or ... |
4-571 |
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: 1015.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 4 KMTQSQYTSLYGPTTGDSIRLGDTNLFAQVEHDYTSYGDEVTFGGGKSIRDGMGQNPNVTRDDRyVADLVITNAVIIDYD 83
Cdd:TIGR01792 1 KMSREQYASLYGPTTGDKVRLGDTDLFVEVEKDLTTYGDESKFGGGKVLRDGMGQNATLTRNAG-VLDLVITNALILDWT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 84 KVVKADIGIKNGYIFAIGQAGNPDIMDNIDIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQAEVALESGITTHIGGGT 163
Cdd:TIGR01792 80 GIYKADIGIKNGRIVGIGKAGNPDTMDGVDMIVGASTEAISGEGKIVTAGGIDTHVHYISPQQVQAALDNGITTLIGGGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 164 GASEGTKATTVTPGPWHIHRMLEAAEQLPINVGFTGKGQAVNHTALIEQIHAGVIGLKVHEDWGATPSALDHALAVADEF 243
Cdd:TIGR01792 160 GPADGTNATTCTPGPWYLHRMLQAADGLPINFGFTGKGSGSGPAALIEQIEAGACGLKVHEDWGATPAAIDNALSVADEY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 244 DVQIALHADTLNEAGFMEDTMAAVKGRVLHMYHTEGAGGGHAPDLIKSASYPNILPSSTNPTLPYTQNTVDEHLDMVMIT 323
Cdd:TIGR01792 240 DVQVAVHTDTLNESGFVEDTIAAFKGRTIHTYHTEGAGGGHAPDIIVVVGYNNILPSSTNPTLPYTVNTIDEHLDMLMVC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 324 HHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGFLDGDAEYNDNNR 403
Cdd:TIGR01792 320 HHLNPKIPEDVAFAESRIRKETIAAEDVLQDMGAISMISSDSQAMGRIGEVVTRCWQTADKMKKQRGPLPGDSPGNDNNR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 404 IKRYIAKYTINPAITHGISDYVGSIEGGKLADLVMWEPAFFGVKPELIVKGGLINAAVNGDANGSIPTSEPQKYRKMYGQ 483
Cdd:TIGR01792 400 VKRYVAKYTINPAITHGISDYIGSIEVGKLADLVLWEPAFFGVKPDMVLKGGLIAWAIMGDPNASIPTPQPVLYRPMFGA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 484 YGGNLQHTAITFVSKTAFESGIYRSLNLQRMVRPVHGIRNLTKKDMKNNDATPKLDVDPQTYEVFVDGEKVTSEPATELP 563
Cdd:TIGR01792 480 YGRALQSTSITFVSQAAYDKGIKERLGLQKLLLPVHNTRSIGKADMKLNSATPKIEVDPQTYDVKVDGVLITVEPADELP 559
|
....*...
gi 1093480465 564 LTQRYFLF 571
Cdd:TIGR01792 560 LTQRYFLF 567
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
4-570 |
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: 985.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 4 KMTQSQYTSLYGPTTGDSIRLGDTNLFAQVEHDYTSYGDEVTFGGGKSIRDGMGQNPNVTRDDryVADLVITNAVIIDYD 83
Cdd:cd00375 1 KISREAYADMYGPTTGDKVRLGDTDLWIEVEKDYTTYGDEVKFGGGKVLRDGMGQSSGYTRED--VLDLVITNALIIDYT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 84 KVVKADIGIKNGYIFAIGQAGNPDIM--DNIDIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQAEVALESGITTHIGG 161
Cdd:cd00375 79 GIYKADIGIKDGRIVAIGKAGNPDIMdgVTPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICPQQIEEALASGITTMIGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 162 GTGASEGTKATTVTPGPWHIHRMLEAAEQLPINVGFTGKGQAVNHTALIEQIHAGVIGLKVHEDWGATPSALDHALAVAD 241
Cdd:cd00375 159 GTGPAAGTKATTCTPGPWNIKRMLQAADGLPVNIGFLGKGNGSSPDALAEQIEAGACGLKLHEDWGATPAAIDTCLSVAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 242 EFDVQIALHADTLNEAGFMEDTMAAVKGRVLHMYHTEGAGGGHAPDLIKSASYPNILPSSTNPTLPYTQNTVDEHLDMVM 321
Cdd:cd00375 239 EYDVQVAIHTDTLNESGFVEDTIAAIKGRTIHTYHTEGAGGGHAPDIIKVAGHPNVLPSSTNPTRPFTVNTLDEHLDMLM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 322 ITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGFLDGDAEYNDN 401
Cdd:cd00375 319 VCHHLDPNIPEDVAFAESRIRAETIAAEDVLHDLGAISIMSSDSQAMGRVGEVILRTWQTAHKMKAQRGPLPEDSGDADN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 402 NRIKRYIAKYTINPAITHGISDYVGSIEGGKLADLVMWEPAFFGVKPELIVKGGLINAAVNGDANGSIPTSEPQKYRKMY 481
Cdd:cd00375 399 FRVKRYIAKYTINPAIAHGISHEVGSVEVGKLADLVLWEPAFFGVKPEMVLKGGFIAYAQMGDPNASIPTPQPVMMRPMF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 482 GQYGGNLQHTAITFVSKTAFESGIYRSLNLQRMVRPVHGIRNLTKKDMKNNDATPKLDVDPQTYEVFVDGEKVTSEPATE 561
Cdd:cd00375 479 GAHGKAPAATSVTFVSQASLDAGIAEELGLRRRVVAVKNCRGVGKKDMKLNSATPDIEVDPETYEVRVDGELLTCEPADE 558
|
....*....
gi 1093480465 562 LPLTQRYFL 570
Cdd:cd00375 559 LPLAQRYFL 567
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
4-571 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 849.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 4 KMTQSQYTSLYGPTTGDSIRLGDTNLFAQVEHDYT----SYGDEVTFGGGKSIRDGMGQNpNVTRDDRyVADLVITNAVI 79
Cdd:PRK13206 3 RLSRERYAALYGPTTGDRIRLADTDLLIEVTEDRSggpgLAGDEAVFGGGKVIRESMGQG-RATRAEG-APDTVITGAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 80 IDYDKVVKADIGIKNGYIFAIGQAGNPDIMDNI--DIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQAEVALESGITT 157
Cdd:PRK13206 81 LDHWGIVKADVGIRDGRIVAIGKAGNPDIMDGVhpDLVIGPSTEIIAGNGRILTAGAIDCHVHFICPQIVDEALAAGITT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 158 HIGGGTGASEGTKATTVTPGPWHIHRMLEAAEQLPINVGFTGKGQAVNHTALIEQIHAGVIGLKVHEDWGATPSALDHAL 237
Cdd:PRK13206 161 LIGGGTGPAEGSKATTVTPGAWHLARMLEALDGWPVNVALLGKGNTVSAEALWEQLRGGAGGFKLHEDWGSTPAAIDACL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 238 AVADEFDVQIALHADTLNEAGFMEDTMAAVKGRVLHMYHTEGAGGGHAPDLIKSASYPNILPSSTNPTLPYTQNTVDEHL 317
Cdd:PRK13206 241 RVADAAGVQVALHSDTLNEAGFVEDTLAAIAGRSIHAYHTEGAGGGHAPDIITVASHPNVLPSSTNPTRPHTVNTLDEHL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 318 DMVMITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGFLDGDAE 397
Cdd:PRK13206 321 DMLMVCHHLNPAVPEDLAFAESRIRPSTIAAEDVLHDMGAISMIGSDSQAMGRIGEVVLRTWQTAHVMKRRRGALPGDGR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 398 yNDNNRIKRYIAKYTINPAITHGISDYVGSIEGGKLADLVMWEPAFFGVKPELIVKGGLINAAVNGDANGSIPTSEPQKY 477
Cdd:PRK13206 401 -ADNNRARRYVAKYTICPAVAHGIDHEIGSVEVGKLADLVLWEPAFFGVRPHAVLKGGAIAWAAMGDANASIPTPQPVLP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 478 RKMYGQYGGNLQHTAITFVSKTAFESGIYRSLNLQRMVRPVHGIRNLTKKDMKNNDATPKLDVDPQTYEVFVDGEKVTSE 557
Cdd:PRK13206 480 RPMFGAAPAAAAATSVHFVAPQAIEDGLADRLGLRRRLVPVADTRAVGKADMPLNDALPDIEVDPDTFTVRIDGEVWEPQ 559
|
570
....*....|....
gi 1093480465 558 PATELPLTQRYFLF 571
Cdd:PRK13206 560 PAAELPMAQRYFLF 573
|
|
| PLN02303 |
PLN02303 |
urease |
2-571 |
0e+00 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 837.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 2 SFKMTQSQYTSLYGPTTGDSIRLGDTNLFAQVEHDYTSYGDEVTFGGGKSIRDGMGQNPNVTRDDryVADLVITNAVIID 81
Cdd:PLN02303 268 TTTISREKYANMYGPTTGDKIRLGDTNLYAEIEKDFTVYGDECKFGGGKVLRDGMGQATGYGAAD--SLDTVITNAVIID 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 82 YDKVVKADIGIKNGYIFAIGQAGNP--DIMDNIDIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQAEVALESGITTHI 159
Cdd:PLN02303 346 YTGIYKADIGIKDGLIVGIGKAGNPdvMDGVTSNMIVGVNTEVIAGEGMIVTAGGIDCHVHFICPQLATEAIASGITTLV 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 160 GGGTGASEGTKATTVTPGPWHIHRMLEAAEQLPINVGFTGKGQAVNHTALIEQIHAGVIGLKVHEDWGATPSALDHALAV 239
Cdd:PLN02303 426 GGGTGPAHGTCATTCTPAPSHMKLMLQSTDDLPLNFGFTGKGNTAKPEGLHEIIKAGAMGLKLHEDWGTTPAAIDNCLDV 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 240 ADEFDVQIALHADTLNEAGFMEDTMAAVKGRVLHMYHTEGAGGGHAPDLIKSASYPNILPSSTNPTLPYTQNTVDEHLDM 319
Cdd:PLN02303 506 AEEYDIQVTIHTDTLNESGCVEHSIAAFKGRTIHTYHSEGAGGGHAPDIIKVCGVKNVLPSSTNPTRPYTKNTIDEHLDM 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 320 VMITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGFLDGDAEYN 399
Cdd:PLN02303 586 LMVCHHLDKNIPEDVAFAESRIRAETIAAEDILHDMGAISIISSDSQAMGRIGEVITRTWQTAHKMKSQRGALEPRGADN 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 400 DNNRIKRYIAKYTINPAITHGISDYVGSIEGGKLADLVMWEPAFFGVKPELIVKGGLINAAVNGDANGSIPTSEPQKYRK 479
Cdd:PLN02303 666 DNFRIKRYIAKYTINPAIAHGMSHFVGSVEVGKLADLVLWKPAFFGAKPEMVIKGGQIAWAQMGDPNASIPTPEPVIMRP 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 480 MYGQYGGNLQHTAITFVSKTAFESGIYRSLNLQRMVRPVHGIRNLTKKDMKNNDATPKLDVDPQTYEVFVDGEKVTSEPA 559
Cdd:PLN02303 746 MFGAFGKAGSSNSIAFVSKAALDAGVKQLYGLTKRVEAVGNVRGLTKLDMKLNDALPVITVDPETYEVTADGEVLTCAPA 825
|
570
....*....|..
gi 1093480465 560 TELPLTQRYFLF 571
Cdd:PLN02303 826 TSVPLSRNYFLF 837
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
4-570 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 831.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 4 KMTQSQYTSLYGPTTGDSIRLGDTNLFAQVEHDYTSYGDEVTFGGGKSIRDGMGQNPNVTRDDRyVADLVITNAVIID-Y 82
Cdd:PRK13308 3 TIDRRAYAELYGPTTGDRVRLADTSLLAEVEHDHTVYGDECLFGGGKTLRDGMGMAPGVTSADG-ALDFVLCNVTVIDpV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 83 DKVVKADIGIKNGYIFAIGQAGNPDIMDNIDII--IGATTDIISAEGKIVTAGGIDTHVHFINPEQAEVALESGITTHIG 160
Cdd:PRK13308 82 LGIVKGDIGIRDGRIVGIGKAGNPDIMDGVDPRlvVGPGTDVRPAEGLIATPGAIDVHVHFDSAQLVDHALASGITTMLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 161 GGTGASegtkATTVTPGPWHIHRMLEAAEQLPINVGFTGKGQAVNHTALIEQIHAGVIGLKVHEDWGATPSALDHALAVA 240
Cdd:PRK13308 162 GGLGPT----VGIDSGGPFNTGRMLQAAEAWPVNFGFLGRGNSSKPAALIEQVEAGACGLKIHEDWGAMPAAIDTCLEVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 241 DEFDVQIALHADTLNEAGFMEDTMAAVKGRVLHMYHTEGAGGGHAPDLIKSASYPNILPSSTNPTLPYTQNTVDEHLDMV 320
Cdd:PRK13308 238 DEYDFQVQLHTDTLNESGFVEDTLAAIGGRTIHMYHTEGAGGGHAPDIIRVVGEPHCLPSSTNPTNPYTVNTFDEHLDMT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 321 MITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGFLDGD-AEYN 399
Cdd:PRK13308 318 MVCHHLNPDVPEDVAFAESRIRAQTIAAEDVLHDIGAISMLGSDSQGMGRIAEVIARTWQLASKMKDQRGPLPEDrGTFA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 400 DNNRIKRYIAKYTINPAITHGISDYVGSIEGGKLADLVMWEPAFFGVKPELIVKGGLINAAVNGDANGSIPTSEPQKYRK 479
Cdd:PRK13308 398 DNARIKRYIAKYTINPAITFGIDDHIGSLEPGKLADIVLWRPAFFGIKPELVIKGGFPAWAAMGDANGSLMTCEPMLQRP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 480 MYGQYGGNLQHTAITFVSKTAFESGIYRSLNLQRMVRPVHGIRNLTKKDMKNNDATPKLDVDPQTYEVFVDGEKVTSEPA 559
Cdd:PRK13308 478 QWGAFGRAKQALSVCFVSPLAIEAGLGERLGLRKRLLPVRGTRTLTKADMLHNDACPDIRVDPQTFEVFVDGELVTCEPA 557
|
570
....*....|.
gi 1093480465 560 TELPLTQRYFL 570
Cdd:PRK13308 558 TELPLAQRYML 568
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
4-571 |
0e+00 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 800.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 4 KMTQSQYTSLYGPTTGDSIRLGDTNLFAQVEHDYTSYGDEVTFGGGKSIRDGMGQNPNvtrDDRYVADLVITNAVIIDYD 83
Cdd:PRK13985 2 KISRKEYVSMYGPTTGDKVRLGDTDLIAEVEHDYTIYGEELKFGGGKTLREGMSQSNN---PSKEELDLIITNALIIDYT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 84 KVVKADIGIKNGYIFAIGQAGNPDIM--DNIDIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQAEVALESGITTHIGG 161
Cdd:PRK13985 79 GIYKADIGIKDGKIAGIGKGGNKDMQdgVKNNLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTAFASGVTTMIGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 162 GTGASEGTKATTVTPGPWHIHRMLEAAEQLPINVGFTGKGQAVNHTALIEQIHAGVIGLKVHEDWGATPSALDHALAVAD 241
Cdd:PRK13985 159 GTGPADGTNATTITPGRRNLKWMLRAAEEYSMNLGFLGKGNSSNDASLADQIEAGAIGFKIHEDWGTTPSAINHALDVAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 242 EFDVQIALHADTLNEAGFMEDTMAAVKGRVLHMYHTEGAGGGHAPDLIKSASYPNILPSSTNPTLPYTQNTVDEHLDMVM 321
Cdd:PRK13985 239 KYDVQVAIHTDTLNEAGCVEDTMAAIAGRTMHTFHTEGAGGGHAPDIIKVAGEHNILPASTNPTIPFTVNTEAEHMDMLM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 322 ITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGFLDGDAEYNDN 401
Cdd:PRK13985 319 VCHHLDKSIKEDVQFADSRIRPQTIAAEDTLHDMGIFSITSSDSQAMGRVGEVITRTWQTADKNKKEFGRLKEEKGDNDN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 402 NRIKRYIAKYTINPAITHGISDYVGSIEGGKLADLVMWEPAFFGVKPELIVKGGLINAAVNGDANGSIPTSEPQKYRKMY 481
Cdd:PRK13985 399 FRIKRYLSKYTINPAIAHGISEYVGSVEVGKVADLVLWSPAFFGVKPNMIIKGGFIALSQMGDANASIPTPQPVYYREMF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 482 GQYGGNLQHTAITFVSKTAFESGIYRSLNLQRMVRPVHGIRNLTKKDMKNNDATPKLDVDPQTYEVFVDGEKVTSEPATE 561
Cdd:PRK13985 479 AHHGKAKYDANITFVSQAAYDKGIKEELGLERQVLPVKNCRNITKKDMQFNDTTAHIEVNPETYHVFVDGKEVTSKPANK 558
|
570
....*....|
gi 1093480465 562 LPLTQRYFLF 571
Cdd:PRK13985 559 VSLAQLFSIF 568
|
|
| ureC |
PRK13309 |
urease subunit alpha; Reviewed |
5-570 |
0e+00 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183966 [Multi-domain] Cd Length: 572 Bit Score: 746.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 5 MTQSQYTSLYGPTTGDSIRLGDTNLFAQVEHDYTSYGDEVTFGGGKSIRDGMGQNPNVTRDDRyVADLVITNAVIIDYDK 84
Cdd:PRK13309 4 ISRQEYAGLFGPTTGDKIRLGDTNLFIEIEKDLRGYGDESVYGGGKSLRDGMGANNNLTRDNG-VLDLVITNVTIVDARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 85 -VVKADIGIKNGYIFAIGQAGNPDIMD--NIDIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQAEVALESGITTHIGG 161
Cdd:PRK13309 83 gVIKADVGIRDGKIVGIGKSGNPSTMDgvTQGMVVGVSTDAISGEHLILTAAGIDTHIHLISPQQAYHALSNGVTTFFGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 162 GTGASEGTKATTVTPGPWHIHRMLEAAEQLPINVGFTGKGQAVNHTALIEQIHAGVIGLKVHEDWGATPSALDHALAVAD 241
Cdd:PRK13309 163 GIGPTDGTNGTTVTPGPWNIRQMLRSIEGLPVNVGILGKGNSYGRGPLLEQAIAGVAGYKVHEDWGATAAALRHALRVAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 242 EFDVQIALHADTLNEAGFMEDTMAAVKGRVLHMYHTEGAGGGHAPDLIKSASYPNILPSSTNPTLPYTQNTVDEHLDMVM 321
Cdd:PRK13309 243 EVDIQVAVHTDSLNECGYVEDTIDAFEGRTIHTFHTEGAGGGHAPDIIKVASQTNVLPSSTNPTLPYGVNSQAELFDMIM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 322 ITHHLNASIPEDIAFADSRIRKETIAAEDVLQDMGVFSMVSSDSQAMGRVGEVITRTWQVAHRMKEQRGFLDGDAEYNDN 401
Cdd:PRK13309 323 VCHNLNPNVPADVAFAESRVRPETIAAENVLHDMGVISMFSSDSQAMGRVGENWLRAIQTADAMKAARGKLPEDAAGNDN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 402 NRIKRYIAKYTINPAITHGISDYVGSIEGGKLADLVMWEPAFFGVKPELIVKGGLINAAVNGDANGSIPTSEPQKYRKMY 481
Cdd:PRK13309 403 FRVLRYVAKITINPAITQGVSHVIGSVEVGKMADLVLWEPRFFGAKPKMVIKGGMINWAAMGDPNASLPTPQPVFYRPMF 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 482 GQYGGNLQHTAITFVSKTAFESGIYRSLNLQRMVRPVHGIRNLTKKDMKNNDATPKLDVDPQTYEVFVDGEKVTSEPATE 561
Cdd:PRK13309 483 GAMGKTLQDTCVTFVSQAALDDGVKEKAGLDRQVIAVKNCRTISKRDLVRNSQTPNIEVDPETFAVKVDGVHATVKPIAT 562
|
....*....
gi 1093480465 562 LPLTQRYFL 570
Cdd:PRK13309 563 ASLNQRYFF 571
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
129-458 |
1.23e-69 |
|
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: 1.23e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 129 IVTAGGIDTHVHF---------INPEQAEVALESGITTHIGGGTGASEGTKATTVTpgpwHIHRMLEAAEQLPINVGFTG 199
Cdd:pfam01979 1 IVLPGLIDAHVHLemgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTST----GIEALLEAAEELPLGLRFLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 200 K-------GQAVNHTALIEQIHAGV------------IGLKVHEDWGATPSALDHALAVADEFDVQIALHAdtLNEAGFM 260
Cdd:pfam01979 77 PgcsldtdGELEGRKALREKLKAGAefikgmadgvvfVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHA--LETKGEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 261 EDTMAAVKGRVLHMYHTEGAGGGHAPDLIKSASYPNILPSSTnptlpyTQNTVDEHLDMVMITHhlnasipedIAFADSR 340
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLSPT------EANLLAEHLKGAGVAH---------CPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 341 IRKETIAAEDVLQDmGVFSMVSSDSQAMGRVGEVITRTwqvAHRMKEQRgfldgdaEYNDNNRIKRYIAKYTINPAITHG 420
Cdd:pfam01979 220 LRSGRIALRKALED-GVKVGLGTDGAGSGNSLNMLEEL---RLALELQF-------DPEGGLSPLEALRMATINPAKALG 288
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1093480465 421 ISDYVGSIEGGKLADLVMWE----PAFFGVKPELIVKGGLIN 458
Cdd:pfam01979 289 LDDKVGSIEVGKDADLVVVDldplAAFFGLKPDGNVKKVIVK 330
|
|
| Urease_alpha |
pfam00449 |
Urease alpha-subunit, N-terminal domain; The N-terminal domain is a composite domain and plays ... |
4-123 |
4.39e-57 |
|
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: 186.93 E-value: 4.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 4 KMTQSQYTSLYGPTTGDSIRLGDTNLFAQVEHDYTSYGDEVTFGGGKSIRDGMGQNPNVTRDDryVADLVITNAVIIDYD 83
Cdd:pfam00449 1 KISREAYADMYGPTTGDRIRLGDTDLFIEVEKDLTVYGDEVKFGGGKVIRDGMGQSQGRTRDD--ALDLVITNALILDYT 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1093480465 84 KVVKADIGIKNGYIFAIGQAGNPDIMDNIDIII--GATTDII 123
Cdd:pfam00449 79 GIVKADIGIKDGRIVGIGKAGNPDTMDGVTPGMviGPSTEVI 120
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
73-262 |
4.01e-18 |
|
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: 87.07 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 73 VITNAVIIDYDKVVKADIGIKNGYIFAIGQAGNPdimdnidiiiGATTDIISAEGKIVTAGGIDTHVHFINP--EQAEva 150
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAA----------PEAAEVIDATGLLVLPGLIDLHVHLREPglEHKE-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 151 lesGITThigggtgaseGTKA------TTV------TPG---PWHIHRMLEAAEQLP-INVGFTG---KGQAVNHTALIE 211
Cdd:COG0044 69 ---DIET----------GTRAaaaggvTTVvdmpntNPVtdtPEALEFKLARAEEKAlVDVGPHGaltKGLGENLAELGA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1093480465 212 QIHAGVIGLKV-----HEDWGATPSALDHALAVADEFDVQIALHA--DTLNEAGFMED 262
Cdd:COG0044 136 LAEAGAVAFKVfmgsdDGNPVLDDGLLRRALEYAAEFGALVAVHAedPDLIRGGVMNE 193
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
71-440 |
1.83e-14 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 75.38 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 71 DLVITNAVIID--YDKVVK-ADIGIKNGYIFAIGQAGnpdimdniDIIIGATTDIISAEGKIVTAGGIDTHVHF------ 141
Cdd:COG1228 9 TLLITNATLVDgtGGGVIEnGTVLVEDGKIAAVGPAA--------DLAVPAGAEVIDATGKTVLPGLIDAHTHLglgggr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 142 ---------INPE---------QAEVALESGITT---HIGGGTGASEGTKATT--VTPGPwhihRMLEAAEQLPINVGFT 198
Cdd:COG1228 81 avefeagggITPTvdlvnpadkRLRRALAAGVTTvrdLPGGPLGLRDAIIAGEskLLPGP----RVLAAGPALSLTGGAH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 199 GKGQAVNHTALIEQIHAGVIGLKVHEDWGA---TPSALDHALAVADEFDVQIALHADTLneagfmEDTMAAVKGRVLHMY 275
Cdd:COG1228 157 ARGPEEARAALRELLAEGADYIKVFAEGGApdfSLEELRAILEAAHALGLPVAAHAHQA------DDIRLAVEAGVDSIE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 276 HTEGAGGGHApDLIKSASypnilPSSTNPTLPYTQNTVDEHldmvmithhlnasiPEDIAFADSRIRKETIAAEDVLQDM 355
Cdd:COG1228 231 HGTYLDDEVA-DLLAEAG-----TVVLVPTLSLFLALLEGA--------------AAPVAAKARKVREAALANARRLHDA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 356 GVFSMVSSDSQAMGRVGEVITRTWQVAHRMkeqrGFLDGDAeyndnnrikryIAKYTINPAITHGISDYVGSIEGGKLAD 435
Cdd:COG1228 291 GVPVALGTDAGVGVPPGRSLHRELALAVEA----GLTPEEA-----------LRAATINAAKALGLDDDVGSLEPGKLAD 355
|
....*
gi 1093480465 436 LVMWE 440
Cdd:COG1228 356 LVLLD 360
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
71-251 |
1.62e-13 |
|
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: 72.71 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 71 DLVITNAVIIDYDKVVKADIGIKNGYIFAIGQAGnpdimdnidiIIGATTDIISAEGKIVTAGGIDTHVHFINPEQAE-- 148
Cdd:cd01315 1 DLVIKNGRVVTPDGVREADIAVKGGKIAAIGPDI----------ANTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEwe 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 149 -------VALESGITTHIGGGTGASEGTkaTTVTpgpwHIHRMLEAAE-QLPINVGFTGKGQAVNHTALIEQIHAGVIGL 220
Cdd:cd01315 71 gfetgtkAAAAGGITTIIDMPLNSIPPT--TTVE----NLEAKLEAAQgKLHVDVGFWGGLVPGNLDQLRPLDEAGVVGF 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 1093480465 221 K-------VHEDWGATPSALDHALAVADEFDVQIALHA 251
Cdd:cd01315 145 KcflcpsgVDEFPAVDDEQLEEAMKELAKTGSVLAVHA 182
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
71-252 |
7.21e-12 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 67.41 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 71 DLVITNAVIIDYDKVVKADIGIKNGYIFAIGQAgnpdimdnidiIIGATTDIISAEGKIVTAGGIDTHVHFINPEQAE-- 148
Cdd:TIGR03178 1 DLIIRGGRVILPNGEREADVGVKGGKIAAIGPD-----------ILGPAAKIIDAGGLVVFPGVVDTHVHINEPGRTEwe 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 149 -------VALESGITTHIGGGTGASEGTkaTTVTpgpwHIHRMLEAA-EQLPINVGFTGKGQAVNHTALIEQIHAGVIGL 220
Cdd:TIGR03178 70 gfetgtrAAAAGGITTYIDMPLNSIPAT--TTRA----SLEAKFEAAkGKLAVDVGFWGGLVPYNLDDLRELDEAGVVGF 143
|
170 180 190
....*....|....*....|....*....|....*....
gi 1093480465 221 K-------VHEDWGATPSALDHALAVADEFDVQIALHAD 252
Cdd:TIGR03178 144 KaflspsgDDEFPHVDDWQLYKGMRELARLGQLLLVHAE 182
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
70-198 |
1.43e-11 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 67.05 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 70 ADLVITNAVIIDydkVV-----KADIGIKNGYIFAIGQAgnpdimdnidiiIGATTDIISAEGKIVTAGGIDTHVHF--- 141
Cdd:COG1001 5 ADLVIKNGRLVN---VFtgeilEGDIAIAGGRIAGVGDY------------IGEATEVIDAAGRYLVPGFIDGHVHIess 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093480465 142 -INPEQ-AEVALESGITT-----H-IGGGTGAsEGTKAttvtpgpwhihrMLEAAEQLPINVGFT 198
Cdd:COG1001 70 mVTPAEfARAVLPHGTTTviadpHeIANVLGL-EGVRY------------MLEAAEGLPLDIFVM 121
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
72-250 |
4.36e-11 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 64.87 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 72 LVITNAVIIDYDKVVKA--DIGIKNGYIFAIGQAGNPdimdnidiiiGATTDIISAEGKIVTAGGIDTHVH--------F 141
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDG----------SQAKKVIDLSGLYVSPGWIDLHVHvypgstpyG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 142 INPEqaEVALESGITTHI-GGGTGAS--EGTKATTVTPGPWHIHRMLeaaeqlpiNVGFTGkGQAVNHTALIEQI----- 213
Cdd:PRK09237 71 DEPD--EVGVRSGVTTVVdAGSAGADnfDDFRKLTIEASKTRVLAFL--------NISRIG-LLAQDELADLEDIdadav 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1093480465 214 ------HAGVI-GLKVHE------DWGATPsaLDHALAVADEFDVQIALH 250
Cdd:PRK09237 140 aeavkrNPDFIvGIKARMsssvvgDNGIEP--LELAKAIAAEANLPLMVH 187
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
72-190 |
2.39e-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: 63.01 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 72 LVITNAVIIDYDKVVKADIGIKNGYIFAIGQagnpdimdniDIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQAEVA- 150
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGP----------NLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTa 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1093480465 151 --LESGITTHIGGGTgasegtkaTTVTP--GPWHIHRMLEAAEQ 190
Cdd:cd01314 71 ddFESGTRAAAAGGT--------TTIIDfaIPNKGQSLLEAVEK 106
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
71-176 |
1.79e-09 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 60.10 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 71 DLVITNAVIIDYDKVVKADIGIKNGYIFAIGQAgnpdimdnidiiIGATTDIISAEGKIVTAGGIDTHVHFINPEQAEVA 150
Cdd:PRK13404 5 DLVIRGGTVVTATDTFQADIGIRGGRIAALGEG------------LGPGAREIDATGRLVLPGGVDSHCHIDQPSGDGIM 72
|
90 100 110
....*....|....*....|....*....|
gi 1093480465 151 L----ESGITTHIGGGTgasegtkaTTVTP 176
Cdd:PRK13404 73 MaddfYTGTVSAAFGGT--------TTVIP 94
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
71-141 |
1.53e-08 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 57.10 E-value: 1.53e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093480465 71 DLVITNAVIIDYDKVVKADIGIKNGYIFAIGQAGNpdimdnidiiigatTDIISAEGKIVTAGGIDTHVHF 141
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGANLG--------------DEVIDATGKYVMPGGIDPHTHM 58
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
71-221 |
1.82e-08 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 57.02 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 71 DLVITNAVIIDYDKVVKADIGIKNGYIFAIGQagnpdimdnidIIIGATTDIISAEGKIVTAGGIDTHVHFINPEQAE-V 149
Cdd:PRK06189 4 DLIIRGGKVVTPEGVYRADIGIKNGKIAEIAP-----------EISSPAREIIDADGLYVFPGMIDVHVHFNEPGRTHwE 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093480465 150 ALESGITTHI-GGGTGASE---GTKATTVTPGpwHIHRMLEAAEQLP-INVGFTGKGQAVNHTALIEQIHAGVIGLK 221
Cdd:PRK06189 73 GFATGSAALAaGGCTTYFDmplNSIPPTVTRE--ALDAKAELARQKSaVDFALWGGLVPGNLEHLRELAEAGVIGFK 147
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
89-250 |
3.48e-08 |
|
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: 55.41 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 89 DIGIKNGYIFAIGQAGNPdimdnidiiiGATTDIISAEGKIVTAGGIDTHVH--------FINPEQaeVALESGITTHI- 159
Cdd:cd01307 1 DVAIENGKIAAVGAALAA----------PAATQIVDAGGCYVSPGWIDLHVHvyqggtryGDRPDM--IGVKSGVTTVVd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 160 GGGTGASEgtkattvTPGPWHiHRMLEAAEQLP--INVGFTGkGQAVNHTALIEQI-----------HAGVI-GLKVHE- 224
Cdd:cd01307 69 AGSAGADN-------IDGFRY-TVIERSATRVYafLNISRVG-LVAQDELPDPDNIdedavvaaareYPDVIvGLKARAs 139
|
170 180 190
....*....|....*....|....*....|.
gi 1093480465 225 -----DWGATPsaLDHALAVADEFDVQIALH 250
Cdd:cd01307 140 ksvvgEWGIKP--LELAKKIAKEADLPLMVH 168
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
72-266 |
1.26e-07 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 54.05 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 72 LVITNAVIID-YDKVVKADIGIKNGYIFAIGQAGNPdimdnidiiigATTDIISAEGKIVTAGGIDTHVHFINP--EQAE 148
Cdd:PRK09357 3 ILIKNGRVIDpKGLDEVADVLIDDGKIAAIGENIEA-----------EGAEVIDATGLVVAPGLVDLHVHLREPgqEDKE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 149 vALESGITTHIGGGTgasegtkaTTV-----------TPGpwHIHRMLEAAEQLP---------INVGFTGKgqavNHTA 208
Cdd:PRK09357 72 -TIETGSRAAAAGGF--------TTVvampntkpvidTPE--VVEYVLDRAKEAGlvdvlpvgaITKGLAGE----ELTE 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093480465 209 LIEQIHAGVI-----GLKVHedwgaTPSALDHALAVADEFDVQIALHA--DTLNEAGFMEDTMAA 266
Cdd:PRK09357 137 FGALKEAGVVafsddGIPVQ-----DARLMRRALEYAKALDLLIAQHCedPSLTEGGVMNEGEVS 196
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
72-191 |
1.84e-07 |
|
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: 53.35 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 72 LVITNAVIIDYDKVVKADIGIKNGYIFAIGQAGNPDimdnidiiigATTDIISAEGKIVTAGGIDTHVHFIN----PEQA 147
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELE----------EADEIIDLKGQYLVPGFIDIHIHGGGgadfMDGT 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1093480465 148 EVALESGITTHigggtgASEGTK---ATTVTPGPWHIHRMLEAAEQL 191
Cdd:cd00854 71 AEALKTIAEAL------AKHGTTsflPTTVTAPPEEIAKALAAIAEA 111
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
71-166 |
3.30e-07 |
|
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: 52.68 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 71 DLVITNAVIID------YdkvvKADIGIKNGYIFAIGQAGNPDimdnidiiiGATTdiISAEGKIVTAGGIDTHVH---- 140
Cdd:cd01297 1 DLVIRNGTVVDgtgappF----TADVGIRDGRIAAIGPILSTS---------AREV--IDAAGLVVAPGFIDVHTHydgq 65
|
90 100
....*....|....*....|....*.
gi 1093480465 141 FINPEQAEVALESGITTHIGGGTGAS 166
Cdd:cd01297 66 VFWDPDLRPSSRQGVTTVVLGNCGVS 91
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
71-176 |
4.77e-07 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 52.23 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 71 DLVITNAVIIDYDKVVKADIGIKNGYIFAIGQAGnpdimdnidiiiGATTD-IISAEGKIVTAGGIDTHVHFINPEQAEV 149
Cdd:PRK09060 6 DLILKGGTVVNPDGEGRADIGIRDGRIAAIGDLS------------GASAGeVIDCRGLHVLPGVIDSQVHFREPGLEHK 73
|
90 100 110
....*....|....*....|....*....|.
gi 1093480465 150 A-LESGITTHIGGG-TGASE--GTKATTVTP 176
Cdd:PRK09060 74 EdLETGSRAAVLGGvTAVFEmpNTNPLTTTA 104
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
389-438 |
5.65e-06 |
|
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: 48.84 E-value: 5.65e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1093480465 389 RGFLDGDAEYNDNNRIKRY--IAKYTINPAITHGISDYVGSIEGGKLADLVM 438
Cdd:cd01300 428 RKTPGGGVLGNPEERLSLEeaLRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
94-439 |
7.29e-06 |
|
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: 48.46 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 94 NGYIFAIGQAgnpdimdnidIIIGATTDIISAEGKIVTAGGIDTHVH------------------------------FIN 143
Cdd:cd01309 1 DGKIVAVGAE----------ITTPADAEVIDAKGKHVTPGLIDAHSHlgldeeggvretsdaneetdpvtphvraidGIN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 144 P--EQAEVALESGITT-HIGGGTGASEGTKATTVTPGPWHIHRMLEAAE-QLPINVG-----FTGKGQAVNHTA------ 208
Cdd:cd01309 71 PddEAFKRARAGGVTTvQVLPGSANLIGGQGVVIKTDGGTIEDMFIKAPaGLKMALGenpkrVYGGKGKEPATRmgvaal 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 209 LIEQIHAGVIGLKVHEDW---GATPSALD---HALAVADEFDVQIALHADTLNEagfMEDTMAAVKGRVLHMYHTEGAGG 282
Cdd:cd01309 151 LRDAFIKAQEYGRKYDLGknaKKDPPERDlklEALLPVLKGEIPVRIHAHRADD---ILTAIRIAKEFGIKITIEHGAEG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 283 GHAPDLIKSASYPNILPsstnPTLpytqntvdehldmvmithhlnaSIPEDIAFADSRIrkeTIAAEdVLQDMGVFSMVS 362
Cdd:cd01309 228 YKLADELAKHGIPVIYG----PTL----------------------TLPKKVEEVNDAI---DTNAY-LLKKGGVAFAIS 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093480465 363 SDSQamgrvgEVITR--TWQVAHRMKEQRgfldgdaeyndnnRIKRYIAKYTINPAITHGISDYVGSIEGGKLADLVMW 439
Cdd:cd01309 278 SDHP------VLNIRnlNLEAAKAVKYGL-------------SYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVW 337
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
71-250 |
8.60e-06 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 48.22 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 71 DLVITNAVIID--YDKVVKADIGIKNGYIFAIGQAGnpdimdnidiIIGATTdIISAEGKIVTAGGIDTHVHF------- 141
Cdd:PRK12394 4 DILITNGHIIDpaRNINEINNLRIINDIIVDADKYP----------VASETR-IIHADGCIVTPGLIDYHAHVfydgteg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 142 -INPEQaeVALESGITTHIGG---GTGASEGTKATTVTPGPWHIHRMLEAAeqlPINVGFTGKGQAVNHT--------AL 209
Cdd:PRK12394 73 gVRPDM--YMPPNGVTTVVDAgsaGTANFDAFYRTVICASKVRIKAFLTVS---PPGQTWSGYQENYDPDnidenkihAL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1093480465 210 IEQIHAGVIGLKVH---EDWGATPS-ALDHALAVADEFDVQIALH 250
Cdd:PRK12394 148 FRQYRNVLQGLKLRvqtEDIAEYGLkPLTETLRIANDLRCPVAVH 192
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
71-157 |
1.17e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 48.11 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 71 DLVITNAVIIDYDKVVKADIGIKNGYIFAIGQAgnpdimdnidiIIGATTD-IISAEGKIVTAGGIDTHVHFINPEQAE- 148
Cdd:PRK02382 3 DALLKDGRVYYNNSLQPRDVRIDGGKITAVGKD-----------LDGSSSEeVIDARGMLLLPGGIDVHVHFREPGYTHk 71
|
90
....*....|....*..
gi 1093480465 149 --------VALESGITT 157
Cdd:PRK02382 72 etwytgsrSAAAGGVTT 88
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
73-191 |
1.25e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 47.79 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 73 VITNAVIIDYDKVVK-ADIGIKNGYIFAIGQAGNPDimdnidiiigatTDIISAEGKIVTAGGIDTHVH------F--IN 143
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPGAEPD------------AEVIDLGGGYLAPGFIDLHVHggggvdFmdGT 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1093480465 144 PEQAEVALEsgitTHigggtgASEGTK---ATTVTPGPWHIHRMLEAAEQL 191
Cdd:COG1820 69 PEALRTIAR----AH------ARHGTTsflPTTITAPPEDLLRALAAIAEA 109
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
70-159 |
3.64e-05 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 46.39 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 70 ADLVITNAVIIDYDKVVKADIGIKNGYIFAIGQagnpdimdnidiIIGATTDIISAEGKIVTAGGIDTHVHFINPEQA-- 147
Cdd:PRK08044 3 FDLIIKNGTVILENEARVVDIAVKGGKIAAIGQ------------DLGDAKEVMDASGLVVSPGMVDAHTHISEPGRShw 70
|
90
....*....|....*....
gi 1093480465 148 -------EVALESGITTHI 159
Cdd:PRK08044 71 egyetgtRAAAKGGITTMI 89
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
135-312 |
6.07e-05 |
|
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: 45.02 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 135 IDTHVHFINP---------EQAEVALESGITTHIGGGTGASEGTKA--TTV---------TPGPWHIHRMLEAAEQLP-I 193
Cdd:cd01292 2 IDTHVHLDGSalrgtrlnlELKEAEELSPEDLYEDTLRALEALLAGgvTTVvdmgstpppTTTKAAIEAVAEAARASAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 194 NVGFTGKGQAVNHT-----------ALIEQIHAGVIGLKVHEDWGAT---PSALDHALAVADEFDVQIALHA-DTLNEAG 258
Cdd:cd01292 82 RVVLGLGIPGVPAAvdedaeallleLLRRGLELGAVGLKLAGPYTATglsDESLRRVLEEARKLGLPVVIHAgELPDPTR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1093480465 259 FMEDTMAAVK-GRVLHMYHtegaGGGHAPDLIKSASYPNILPSSTNPTLPYTQNT 312
Cdd:cd01292 162 ALEDLVALLRlGGRVVIGH----VSHLDPELLELLKEAGVSLEVCPLSNYLLGRD 212
|
|
| PLN02795 |
PLN02795 |
allantoinase |
129-252 |
7.66e-05 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 45.54 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 129 IVTAGGIDTHVHFINPEQAE---------VALESGITTHIGggtgASEGTKATTVTPGpwHIHRMLEAAE-QLPINVGFT 198
Cdd:PLN02795 96 VVMPGLIDVHVHLNEPGRTEwegfptgtkAAAAGGITTLVD----MPLNSFPSTTSVE--TLELKIEAAKgKLYVDVGFW 169
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093480465 199 GK---GQAVNHTALIEQIHAGVIGLKVH------EDWGAT-PSALDHALAVADEFDVQIALHAD 252
Cdd:PLN02795 170 GGlvpENAHNASVLEELLDAGALGLKSFmcpsgiNDFPMTtATHIKAALPVLAKYGRPLLVHAE 233
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
72-157 |
1.11e-04 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 44.86 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 72 LVITNAVIIDYDKVVKADIGIKNGYIFAIGqagnpdimdNIDIIIGATTdIISAEGKIVTAGGIDTHVHFINP---EQAE 148
Cdd:PRK09236 4 ILIKNARIVNEGKIFEGDVLIENGRIAKIA---------SSISAKSADT-VIDAAGRYLLPGMIDDQVHFREPgltHKGD 73
|
90
....*....|....*
gi 1093480465 149 VALES------GITT 157
Cdd:PRK09236 74 IASESraavagGITS 88
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
408-452 |
1.13e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 44.83 E-value: 1.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1093480465 408 IAKYTINPAITHGISDYVGSIEGGKLADLVMWEPAFFGVKPELIV 452
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIA 449
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
71-157 |
1.76e-04 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 44.30 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 71 DLVITNAVIID----YDKVvkADIGIKNGYIFAIGQAgnpdimdnidIIIGATTdiISAEGKIVTAGGIDTHVHFINPEQ 146
Cdd:PRK09061 20 DLVIRNGRVVDpetgLDAV--RDVGIKGGKIAAVGTA----------AIEGDRT--IDATGLVVAPGFIDLHAHGQSVAA 85
|
90
....*....|.
gi 1093480465 147 AEVALESGITT 157
Cdd:PRK09061 86 YRMQAFDGVTT 96
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
72-159 |
2.87e-04 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 43.53 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 72 LVITNAVIIDYDKVVKADIGIKNGYIFAIGQAGNPDimdnidiiigATTDIISAEGKIVTAGGIDTHVHFINPEQAEV-- 149
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPP----------DAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTta 70
|
90
....*....|....*....
gi 1093480465 150 ---------ALESGITTHI 159
Cdd:TIGR02033 71 ddfftgtkaAAAGGTTTII 89
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
72-141 |
3.23e-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: 43.34 E-value: 3.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093480465 72 LVITNAVII---DYDKVVKADIGIKNGYIFAIGQAGNPDIMDNIdiiigattDIISAEGKIVTAGGIDTHVHF 141
Cdd:cd01298 1 ILIRNGTIVttdPRRVLEDGDVLVEDGRIVAVGPALPLPAYPAD--------EVIDAKGKVVMPGLVNTHTHL 65
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
71-251 |
4.63e-04 |
|
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: 42.89 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 71 DLVITNAVIIDYDK----VVKADIGIKNGYIFAIGQAGNPDIMDnidiiigATTDIISAEGKIVTAGGIDTHVHF----- 141
Cdd:COG0402 1 DLLIRGAWVLTMDPaggvLEDGAVLVEDGRIAAVGPGAELPARY-------PAAEVIDAGGKLVLPGLVNTHTHLpqtll 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 142 -----------------------INPEQAEVALESGITTHIGGGTgasegtkaTTV----TPGPWHIHRMLEAAEQLPIN 194
Cdd:COG0402 74 rgladdlplldwleeyiwplearLDPEDVYAGALLALAEMLRSGT--------TTVadfyYVHPESADALAEAAAEAGIR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093480465 195 vGFTGKG---------------QAVNHT-ALIEQIHAG-----VIGLKVHEDWGATPSALDHALAVADEFDVQIALHA 251
Cdd:COG0402 146 -AVLGRGlmdrgfpdglredadEGLADSeRLIERWHGAadgriRVALAPHAPYTVSPELLRAAAALARELGLPLHTHL 222
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
121-269 |
5.80e-04 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 42.22 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 121 DIISAEGKIVTAGGIDTHVHFINP--EQAEvALESGITTHIGGGTgaseGTKATTVTPGPW-----HIHRMLEAAEQLPI 193
Cdd:cd01317 3 EVIDAEGKILAPGLVDLHVHLREPgfEYKE-TLESGAKAAAAGGF----TTVVCMPNTNPVidnpaVVELLKNRAKDVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 194 N---------VGFTGKgQAVNHTALIEqihAGVIGL----KVHEDWgatpSALDHALAVADEFDVQIALHA--DTLNEAG 258
Cdd:cd01317 78 VrvlpigaltKGLKGE-ELTEIGELLE---AGAVGFsddgKPIQDA----ELLRRALEYAAMLDLPIIVHPedPSLAGGG 149
|
170
....*....|..
gi 1093480465 259 FM-EDTMAAVKG 269
Cdd:cd01317 150 VMnEGKVASRLG 161
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
70-142 |
1.27e-03 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 41.71 E-value: 1.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093480465 70 ADLVITNAVII--DYDKVVKADIGIKNGYIFAIGQAgnpdimDNIDIIIGATTDIISAEGKIVTAGGIDTHVHFI 142
Cdd:COG1574 8 ADLLLTNGRIYtmDPAQPVAEAVAVRDGRIVAVGSD------AEVRALAGPATEVIDLGGKTVLPGFIDAHVHLL 76
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
411-451 |
1.50e-03 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 41.32 E-value: 1.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1093480465 411 YTINPAITHGISDYVGSIEGGKLADLVMWEPAFFGVKPELI 451
Cdd:COG1574 476 YTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEI 516
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
84-157 |
1.68e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 40.91 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 84 KVVKADIGIKNGYIFAIGQAGNPDImdnidiiigattDIISAEGKIVTAGGIDTHVHFINPEQAE---------VALESG 154
Cdd:PRK04250 11 RIVEGGIGIENGRISKISLRDLKGK------------EVIKVKGGIILPGLIDVHVHLRDFEESYketiesgtkAALHGG 78
|
...
gi 1093480465 155 ITT 157
Cdd:PRK04250 79 ITL 81
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
90-142 |
2.74e-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: 40.32 E-value: 2.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1093480465 90 IGIKNGYIFAIGQAgnpdimDNIDIIIGATTDIISAEGKIVTAGGIDTHVHFI 142
Cdd:cd01296 1 IAIRDGRIAAVGPA------ASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLV 47
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
53-159 |
6.57e-03 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 39.43 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 53 RDGMGQNPNVTRDDRyVADLVITNAVIIDY--DKVVKADIGIKNGYIFAIGQAgnpdimdnidIIIGATTDIISAEGKIV 130
Cdd:PRK10027 14 RAEYQELLAVSRGDA-VADYIIDNVSILDLinGGEISGPIVIKGRYIAGVGAE----------YADAPALQRIDARGATA 82
|
90 100 110
....*....|....*....|....*....|....
gi 1093480465 131 TAGGIDTHVHFINPEQAEVALES-----GITTHI 159
Cdd:PRK10027 83 VPGFIDAHLHIESSMMTPVTFETatlprGLTTVI 116
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
412-443 |
7.22e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 38.93 E-value: 7.22e-03
10 20 30
....*....|....*....|....*....|..
gi 1093480465 412 TINPAITHGISDYVGSIEGGKLADLVMWEPAF 443
Cdd:COG1820 332 SLNPARALGLDDRKGSIAPGKDADLVVLDDDL 363
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
72-159 |
8.22e-03 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 39.06 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093480465 72 LVITNAVIIDYDKVVKADIGIKNGYIFAIGqagnpdimdnIDIIIGATTDIISAEGKIVTAGGIDTHVH----FINPEQA 147
Cdd:PLN02942 7 ILIKGGTVVNAHHQELADVYVEDGIIVAVA----------PNLKVPDDVRVIDATGKFVMPGGIDPHTHlampFMGTETI 76
|
90
....*....|....*....
gi 1093480465 148 E-------VALESGITTHI 159
Cdd:PLN02942 77 DdffsgqaAALAGGTTMHI 95
|
|
| |
