|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
12-514 |
0e+00 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 674.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 12 IVLIASAANVYADSYDVVIQGGHVIDPETGLSDVRNIGINKGTIEAITKDSITGKTIIDANDHIVSPGFIDLHHHGQNIA 91
Cdd:PRK09061 5 AVLSLLLMPASMAPYDLVIRNGRVVDPETGLDAVRDVGIKGGKIAAVGTAAIEGDRTIDATGLVVAPGFIDLHAHGQSVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 92 GYRMQAQQGVTTALELESGILPIGDWYKGQAEKNLPINYGASAAWTFARIATFTDSEPQANLQYFQSMQGLDNWKQKIAT 171
Cdd:PRK09061 85 AYRMQAFDGVTTALELEAGVLPVARWYAEQAGEGRPLNYGASVGWTPARIAVLTGPQAEGTIADFGKALGDPRWQERAAT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 172 PEQLEKIMAYVEQGLDEGAIGIGINAGYAPGYGQKEYYALSKLAAERDVATYTHVRYASMMEPGSSFEAIQELIANSALT 251
Cdd:PRK09061 165 PAELAEILELLEQGLDEGALGIGIGAGYAPGTGHKEYLELARLAARAGVPTYTHVRYLSNVDPRSSVDAYQELIAAAAET 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 252 GAKMHINHINSTSLRDIDATLELFDEATENGFHVTAGAYPWGAASTVVGAAMFsGPEWKERLGYQEESIQM---GTERLN 328
Cdd:PRK09061 245 GAHMHICHVNSTSLRDIDRCLALVEKAQAQGLDVTTEAYPYGAGSTVVGAAFF-DPGWLERMGLGYGSLQWvetGERLLT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 329 NEELLKAQKEQPGSIINWHFLDEAVPSELSALDKSIIHPNVLIESDSMPWMLiEDGKVsyYEGDEWPIPSEAFAHPRSSG 408
Cdd:PRK09061 324 REELAKLRANDPGGLVLIHFLDEDNPRDRALLDRSVLFPGAAIASDAMPWTW-SDGTV--YEGDAWPLPEDAVSHPRSAG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 409 TFTKILGTYVRERGLLSMEEAIRKMSYMPATVLDGFVPQMEKKGRIQVGMDADIVIFDPKTVANKATYQVPAAISTGVDT 488
Cdd:PRK09061 401 TFARFLREYVRERKALSLLEAIRKCTLMPAQILEDSVPAMRRKGRLQAGADADIVVFDPETITDRATFEDPNRPSEGVRH 480
|
490 500
....*....|....*....|....*.
gi 914653889 489 VLVNGQFVVQDGELVTSAAPGQAIRR 514
Cdd:PRK09061 481 VLVNGVPVVSNGELVRDARPGRPVRR 506
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
27-509 |
1.80e-106 |
|
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: 324.25 E-value: 1.80e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 27 DVVIQGGHVIDPETGLSDVRNIGINKGTIEAITKDSIT-GKTIIDANDHIVSPGFIDLHHHGQNIA----GYRMQAQQGV 101
Cdd:cd01297 1 DLVIRNGTVVDGTGAPPFTADVGIRDGRIAAIGPILSTsAREVIDAAGLVVAPGFIDVHTHYDGQVfwdpDLRPSSRQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 102 TTALELESGILPIGDWYKGQAEK----------NLPINYGASAAWTFARIATFTDSEPQANLQYFQSMQGLDNWKQ--KI 169
Cdd:cd01297 81 TTVVLGNCGVSPAPANPDDLARLimlmeglvalGEGLPWGWATFAEYLDALEARPPAVNVAALVGHAALRRAVMGLdaRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 170 ATPEQLEKIMAYVEQGLDEGAIGIGINAGYAP--GYGQKEYYALSKLAAERDVATYTHVRYasmmEPGSSFEAIQELIAN 247
Cdd:cd01297 161 ATEEELAKMRELLREALEAGALGISTGLAYAPrlYAGTAELVALARVAARYGGVYQTHVRY----EGDSILEALDELLRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 248 SALTGAKMHINHINSTS---LRDIDATLELFDEATENGFHVTAGAYPWGAAStvvgaamfsgpewkerlgyqeesiqmgt 324
Cdd:cd01297 237 GRETGRPVHISHLKSAGapnWGKIDRLLALIEAARAEGLQVTADVYPYGAGS---------------------------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 325 erlnneellkaqkeqpgsiinwhfldeavpselsaldksiihpnvliESDSMPWMlieDGKVSYYEGDEWPIPseaFAHP 404
Cdd:cd01297 289 -----------------------------------------------EDDVRRIM---AHPVVMGGSDGGALG---KPHP 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 405 RSSGTFTKILGTYVRERGLLSMEEAIRKMSYMPATVLdgfvpQMEKKGRIQVGMDADIVIFDPKTVANKATYQVPAAIST 484
Cdd:cd01297 316 RSYGDFTRVLGHYVRERKLLSLEEAVRKMTGLPARVF-----GLADRGRIAPGYRADIVVFDPDTLADRATFTRPNQPAE 390
|
490 500
....*....|....*....|....*
gi 914653889 485 GVDTVLVNGQFVVQDGeLVTSAAPG 509
Cdd:cd01297 391 GIEAVLVNGVPVVRDG-AFTGARPG 414
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
25-514 |
3.72e-85 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 272.82 E-value: 3.72e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 25 SYDVVIQGGHVIDPeTGLSDVR-NIGINKGTIEAI-TKDSITGKTIIDANDHIVSPGFIDLHHH--GQNIAGYRMQA--Q 98
Cdd:COG3653 1 MFDLLIRGGTVVDG-TGAPPFRaDVAIKGGRIVAVgDLAAAEAARVIDATGLVVAPGFIDIHTHydLQLLWDPRLEPslR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 99 QGVTTAL--ELESGILPIG----DWYKGQAEKNLPINYGASAAW-TFAR-------------IATFTdsePQANLQYfQS 158
Cdd:COG3653 80 QGVTTVVmgNCGVSFAPVRpedrDRLIDLMEGVEGIPEGLDWDWeSFGEyldalerrglgvnVASLV---GHGTLRA-YV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 159 MqGLDNwkqKIATPEQLEKIMAYVEQGLDEGAIGIGINAGYAPGY--GQKEYYALSKLAAERDvATY-THVRYasmmEPG 235
Cdd:COG3653 156 M-GLDD---RPPTPEELARMRALLREAMEAGALGLSTGLIYVPGTyaSTDELVALAKVVAEYG-GVYqSHMRD----EGD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 236 SSFEAIQELIANSALTGAKMHINHINSTSLRD---IDATLELFDEATENGFHVTAGAYPWGAASTVVGAAMfsgPEWKER 312
Cdd:COG3653 227 GLLEAVDELIRIGREAGVPVHISHLKAAGKPNwgkADEVLALIEAARAEGLDVTADVYPYPAGSTGLGALL---PPWAAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 313 LGYQEEsiqmgTERLNNEEL---LKAQKEQPGS-----IINWHFLDEAVPSELSAL-DKSI--------IHP-NVLIEsd 374
Cdd:COG3653 304 GGLDER-----LARLRDPATrarIRAEIEEGLPdnllgRGGWDNILISDSPPNEPLvGKSLaeiaaergVDPaDAALD-- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 375 smpWMLIEDGKVS--YYEGDEWPI---------------PSEAFAHPRSSGTFTKILGTYVRERGLLSMEEAIRKMSYMP 437
Cdd:COG3653 377 ---LLLEEDGRVLivYFIMSEEDVrellrhpwvmigsdgGLGGKAHPRAYGTFPRVLGHYVRERGVLSLEEAVRKLTSLP 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914653889 438 ATVLdgfvpQMEKKGRIQVGMDADIVIFDPKTVANKATYQVPAAISTGVDTVLVNGQFVVQDGElVTSAAPGQAIRR 514
Cdd:COG3653 454 ADRL-----GLKDRGLLRPGYRADLVVFDPATLADRATFDLPAQRADGIRAVIVNGVVVVEDGK-PTGARPGRVLRG 524
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
29-514 |
1.20e-22 |
|
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: 100.55 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 29 VIQGGHVIDPETglSDVRNIGINKGTIEAITKD--SITGKTIIDANDHIVSPGFIDLHHH----GQ----NIA-GYRMQA 97
Cdd:COG0044 1 LIKNGRVVDPGG--LERADVLIEDGRIAAIGPDlaAPEAAEVIDATGLLVLPGLIDLHVHlrepGLehkeDIEtGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 98 QQGVTTALEL--------ESGILpigDWYKGQAEKNLPINYGASAAWTFARIATFTDSEPQANLQY--FQSMQGLDNwKQ 167
Cdd:COG0044 79 AGGVTTVVDMpntnpvtdTPEAL---EFKLARAEEKALVDVGPHGALTKGLGENLAELGALAEAGAvaFKVFMGSDD-GN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 168 KIATPEQLEKIMAYVEqglDEGAIgIGINAgyapgygqkEYYALSK--LAAERDVATYTHVRYASMM-EpgssFEAIQEL 244
Cdd:COG0044 155 PVLDDGLLRRALEYAA---EFGAL-VAVHA---------EDPDLIRggVMNEGKTSPRLGLKGRPAEaE----EEAVARD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 245 IANSALTGAKMHINHInSTSlrdidATLELFDEATENGFHVTAGA---YPWgaastvvgaamfsgpewkerlgyqeesiq 321
Cdd:COG0044 218 IALAEETGARLHIVHV-STA-----EAVELIREAKARGLPVTAEVcphHLT----------------------------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 322 mgterLNNEEL------------LKAQKEQpgsiinwhfldEAVpseLSALDKSIIHpnvLIESDSMPWMLieDGKvsyy 389
Cdd:COG0044 263 -----LTDEDLerygtnfkvnppLRTEEDR-----------EAL---WEGLADGTID---VIATDHAPHTL--EEK---- 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 390 EGDEWPIPS------EAFAhprssgtftkILGTYVRERGLLSMEEAIRKMSYMPATVLdgfvpQMEKKGRIQVGMDADIV 463
Cdd:COG0044 315 ELPFAEAPNgipgleTALP----------LLLTELVHKGRLSLERLVELLSTNPARIF-----GLPRKGRIAVGADADLV 379
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914653889 464 IFDPktvanKATYQVPAAIS--------------TG-VDTVLVNGQFVVQDGELVTSAApGQAIRR 514
Cdd:COG0044 380 LFDP-----DAEWTVTAEDLhskskntpfegrelTGrVVATIVRGRVVYEDGEVVGEPR-GRFLRR 439
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
27-104 |
9.83e-17 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 81.75 E-value: 9.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 27 DVVIQGGHVIDPETGLSDVRNIGINKGTIEAITKD--SITGKTIIDANDHIVSPGFIDLH-HHGQNIAGYRMQA-----Q 98
Cdd:COG3964 1 DLLIKGGRVIDPANGIDGVMDIAIKDGKIAAVAKDidAAEAKKVIDASGLYVTPGLIDLHtHVFPGGTDYGVDPdgvgvR 80
|
....*.
gi 914653889 99 QGVTTA 104
Cdd:COG3964 81 SGVTTV 86
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
28-103 |
9.79e-13 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 69.49 E-value: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 28 VVIQGGHVIDPETGLSDVRNIGINKGTIEAITKDsITG---KTIIDANDHIVSPGFIDLHHH---GQNIAGY---RMQAQ 98
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGVIDIAIEDGKIAAVAGD-IDGsqaKKVIDLSGLYVSPGWIDLHVHvypGSTPYGDepdEVGVR 79
|
....*
gi 914653889 99 QGVTT 103
Cdd:PRK09237 80 SGVTT 84
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
68-497 |
4.56e-12 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 67.94 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 68 IIDANDHIVSPGFIDLHHH----GQNIAGYRMQAQQgVTTALELESGILPIGDWYKG---------------------QA 122
Cdd:pfam07969 2 VIDAKGRLVLPGFVDPHTHldggGLNLRELRLPDVL-PNAVVKGQAGRTPKGRWLVGegwdeaqfaetrfpyaladldEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 123 EKNLPINYGA---------SAAWTFARIATFTDSEPQANLQYFQSMQGLD-------NWKQKIATPEQLEkimAYVEQGL 186
Cdd:pfam07969 81 APDGPVLLRAlhthaavanSAALDLAGITKATEDPPGGEIARDANGEGLTgllregaYALPPLLAREAEA---AAVAAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 187 DE-GAIGI-GINAGYAPGYGQKEYYALSKLAAERDVATYTHVRYASMMEPGSS---FEAIQ-----ELIANSALTGAKMH 256
Cdd:pfam07969 158 AAlPGFGItSVDGGGGNVHSLDDYEPLRELTAAEKLKELLDAPERLGLPHSIYelrIGAMKlfadgVLGSRTAALTEPYF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 257 INHINSTSLRDIDATLELFDEATENGFHVTAGAYPWGAASTVVGAAMFSGPEW----KERLGYQEeSIQMGTERLNnEEL 332
Cdd:pfam07969 238 DAPGTGWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAVAEKLgnqgRVRIEHAQ-GVVPYTYSQI-ERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 333 LKAQKEQPGSIINWHFLDEAVPSELSALDKSIIHPNVLIESDSMPWMLIEDGKVSYYegDEWPIPSEAFAHprssgtFTK 412
Cdd:pfam07969 316 AALGGAAGVQPVFDPLWGDWLQDRLGAERARGLTPVKELLNAGVKVALGSDAPVGPF--DPWPRIGAAVMR------QTA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 413 ILGTYVRERGLLSMEEAIRKMSYMPATVLDgfvpQMEKKGRIQVGMDADIVIFDpktvANKATYQVPAAISTGVDTVLVN 492
Cdd:pfam07969 388 GGGEVLGPDEELSLEEALALYTSGPAKALG----LEDRKGTLGVGKDADLVVLD----DDPLTVDPPAIADIRVRLTVVD 459
|
....*
gi 914653889 493 GQFVV 497
Cdd:pfam07969 460 GRVVY 464
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
27-513 |
1.14e-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: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 27 DVVIQGGHVIDPEtGLSDVrNIGINKGTIEAITKD--SITGKTIIDANDHIVSPGFIDLHHH----GQN-----IAGYRM 95
Cdd:cd01315 1 DLVIKNGRVVTPD-GVREA-DIAVKGGKIAAIGPDiaNTEAEEVIDAGGLVVMPGLIDTHVHinepGRTewegfETGTKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 96 QAQQGVTTALELESGILP------IGDWYKGQAEKNLPINYGAsaaWTFARIATFTDSEPQAN-----LQYFQSMQGLDN 164
Cdd:cd01315 79 AAAGGITTIIDMPLNSIPptttveNLEAKLEAAQGKLHVDVGF---WGGLVPGNLDQLRPLDEagvvgFKCFLCPSGVDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 165 WKQkiATPEQLEKIMAYVEqglDEGAIgIGINAGYAPGygQKEYYALSKLAAERDVATYTHVRYASMMEpgssfEAIQEL 244
Cdd:cd01315 156 FPA--VDDEQLEEAMKELA---KTGSV-LAVHAENPEI--TEALQEQAKAKGKRDYRDYLASRPVFTEV-----EAIQRI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 245 IANSALTGAKMHINHINSTSlrdidaTLELFDEATENGFHVTA---GAYPWGAASTVVGAamfsGPEWK----ERlgyqe 317
Cdd:cd01315 223 LLLAKETGCRLHIVHLSSAE------AVPLIREARAEGVDVTVetcPHYLTFTAEDVPDG----GTEFKcappIR----- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 318 esiqmgtERLNNEELLkaQKEQPGSIinwhfldEAVPSELS---ALDKSIIHPNVLiesdsmpwmliedgkvsyyegDEW 394
Cdd:cd01315 288 -------DAANQEQLW--EALENGDI-------DMVVSDHSpctPELKLLGKGDFF---------------------KAW 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 395 P-IpseafahprSSGTFT-KILGTYVRERGLLSMEEAIRKMSYMPATV--LDGfvpqmeKKGRIQVGMDADIVIFDPK-- 468
Cdd:cd01315 331 GgI---------SGLQLGlPVMLTEAVNKRGLSLEDIARLMCENPAKLfgLSH------QKGRIAVGYDADFVVWDPEee 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 914653889 469 -TV-------ANKATYQVPAAISTGVDTVLVNGQFVVQDGELVTsAAPGQAIR 513
Cdd:cd01315 396 fTVdaedlyyKNKISPYVGRTLKGRVHATILRGTVVYQDGEVVG-EPLGQLLL 447
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
46-499 |
1.56e-10 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 62.85 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 46 RNIGINKGTIEAITKDSIT-GKTIIDANDHIVSPGFIDLHHH----GQNIA-----GYRMQAQQGVTTALELESGILPIG 115
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPpDAEVIDAKGLLVLPGFIDLHVHlrdpGEEYKediesGSKAAAHGGFTTVADMPNTKPPID 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 116 D-----WYKGQAEKNLPINYgasaAWTFAriatFTDSEPQANLQYFQSMQgldnwkqkiatpeqlekiMAyveqgldeGA 190
Cdd:TIGR00857 86 TpetleWKLQRLKKVSLVDV----HLYGG----VTQGNQGKELTEAYELK------------------EA--------GA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 191 IGIGINAGYAPGYGQKEYYALSKLAAERDVATYTH-----VRYASMMEPGSSF--------------EAIQELIANSALT 251
Cdd:TIGR00857 132 VGRMFTDDGSEVQDILSMRRALEYAAIAGVPIALHaedpdLIYGGVMHEGPSAaqlglparppeaeeVAVARLLELAKHA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 252 GAKMHINHInSTSLrdidaTLELFDEATENGFHVTAGAYPwgaastvvgAAMFsgpewkerlgyqeesiqmgterLNNEE 331
Cdd:TIGR00857 212 GCPVHICHI-STKE-----SLELIVKAKSQGIKITAEVTP---------HHLL----------------------LSEED 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 332 LlkaqkeqPGSIINWHF---LDEavPSELSALDKSIIHPNV-LIESDSMP------WMLIEDGKvSYYEGDEWPIPSeaf 401
Cdd:TIGR00857 255 V-------ARLDGNGKVnppLRE--KEDRLALIEGLKDGIIdIIATDHAPhtleekTKEFAAAP-PGIPGLETALPL--- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 402 ahprssgtftkILGTYVreRGLLSMEEAIRKMSYMPATVLdgfvpQMEKKGRIQVGMDADIVIFDPKTVA--NKATYQVP 479
Cdd:TIGR00857 322 -----------LLQLLV--KGLISLKDLIRMLSINPARIF-----GLPDKGTLEEGNPADITVFDLKKEWtiNAETFYSK 383
|
490 500
....*....|....*....|....*...
gi 914653889 480 AAIS--------TGVDTVLVNGQFVVQD 499
Cdd:TIGR00857 384 AKNTpfegmslkGKPIATILRGKVVYED 411
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
29-105 |
1.78e-10 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 62.81 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 29 VIQGGHVIDPETGLSDVRnIGINKGTIEAITKDSITGKTIIDANDHIVSPGFIDLHHHG--------------QNIAgyR 94
Cdd:COG1820 1 AITNARIFTGDGVLEDGA-LLIEDGRIAAIGPGAEPDAEVIDLGGGYLAPGFIDLHVHGgggvdfmdgtpealRTIA--R 77
|
90
....*....|.
gi 914653889 95 MQAQQGVTTAL 105
Cdd:COG1820 78 AHARHGTTSFL 88
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
421-516 |
3.37e-10 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 62.11 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 421 RGLLSMEEAIRKMSYMPATVLdGFVPQmekKGRIQVGMDADIVIFDP---KTVANKATYQvpaAIS---------TG-VD 487
Cdd:PRK08323 353 TGRITLNRFVELTSTNPAKIF-GLYPR---KGTIAVGADADIVIWDPnatKTISASTLHS---NVDynpyegfevTGwPV 425
|
90 100
....*....|....*....|....*....
gi 914653889 488 TVLVNGQFVVQDGELVTSAAPGQAIRRDT 516
Cdd:PRK08323 426 TTLSRGEVVVEDGEFRGKAGHGRFLKRKP 454
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
28-499 |
1.14e-09 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 60.21 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 28 VVIQGGHVIDPEtGLSDVRNIGINKGTIEAITKD-SITGKTIIDANDHIVSPGFIDLHHH----GQ----NIA-GYRMQA 97
Cdd:PRK09357 3 ILIKNGRVIDPK-GLDEVADVLIDDGKIAAIGENiEAEGAEVIDATGLVVAPGLVDLHVHlrepGQedkeTIEtGSRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 98 QQGVTT-----------------ALELESG-------ILPIGDWYKGQAEKNLPiNYGASAAwtfARIATFTDsepqaNL 153
Cdd:PRK09357 82 AGGFTTvvampntkpvidtpevvEYVLDRAkeaglvdVLPVGAITKGLAGEELT-EFGALKE---AGVVAFSD-----DG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 154 QYFQSMQGLDNWKQKIATpeqLEKIMAYVEQ--GLDEGAigiGINAGyapgygqkeyyalsKLAAERDVATYTHVRyasm 231
Cdd:PRK09357 153 IPVQDARLMRRALEYAKA---LDLLIAQHCEdpSLTEGG---VMNEG--------------EVSARLGLPGIPAVA---- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 232 mepgssfEAIQelIANSAL----TGAKMHINHInSTSlrdidATLELFDEATENGFHVTAGAYPwgaastvvgaamfsgp 307
Cdd:PRK09357 209 -------EEVM--IARDVLlaeaTGARVHICHV-STA-----GSVELIRWAKALGIKVTAEVTP---------------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 308 ewkerlgyqeesiqmgterlnneellkaqkeqpgsiinWHFL--DEAVPSelsalDKSIIHPN----------VLIESds 375
Cdd:PRK09357 258 --------------------------------------HHLLltDEDLLT-----YDPNYKVNpplrteedreALIEG-- 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 376 mpwmlIEDGKVSYYEGDEWPIPSEAFAHPrssgtFTK----ILG---------TYVRERGLLSMEEAIRKMSYMPATVLd 442
Cdd:PRK09357 293 -----LKDGTIDAIATDHAPHAREEKECE-----FEAapfgITGletalsllyTTLVKTGLLDLEQLLEKMTINPARIL- 361
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914653889 443 GFvpqmeKKGRIQVGMDADIVIFDPK---TV-----ANKAT------YQVPAAistgVDTVLVNGQFVVQD 499
Cdd:PRK09357 362 GL-----PAGPLAEGEPADLVIFDPEaewTVdgedfASKGKntpfigMKLKGK----VVYTIVDGKIVYQD 423
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
26-86 |
3.68e-09 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 58.62 E-value: 3.68e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914653889 26 YDVVIQGGHVIDPETGLSDVRNIGINKGTIEAITKDSITG-KTIIDANDHIVSPGFIDLHHH 86
Cdd:PRK12394 3 NDILITNGHIIDPARNINEINNLRIINDIIVDADKYPVASeTRIIHADGCIVTPGLIDYHAH 64
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
413-509 |
4.05e-08 |
|
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: 55.69 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 413 ILGTYVRERGLLSMEEAIRKMSYMPATVLdGFVPQmekKGRIQVGMDADIVIFDP---KTVANKATYQ-VPAAISTGVD- 487
Cdd:cd01314 345 LLWSEGVAKGRITLEKFVELTSTNPAKIF-GLYPR---KGTIAVGSDADLVIWDPnaeKTISADTHHHnVDYNIFEGMKv 420
|
90 100
....*....|....*....|....*..
gi 914653889 488 -----TVLVNGQFVVQDGELVTSAAPG 509
Cdd:cd01314 421 kgwpvVTISRGKVVVEDGELVGEKGSG 447
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
29-503 |
4.48e-08 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 55.09 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 29 VIQGGHVIDPE-TGLSDVRnigINKGTIEAItKDSITGK-----TIIDANDHIVSPGFIDLHHH---GQNIAGYRMQAQQ 99
Cdd:cd01308 3 LIKNAEVYAPEyLGKKDIL---IAGGKILAI-EDQLNLPgyenvTVVDLHGKILVPGFIDQHVHiigGGGEGGPSTRTPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 100 ---------GVTTALELesgilpIGdwykgqaeknlpinygasaawtfariatfTDSEPQanlqyfqSMQGLdnwkqkIA 170
Cdd:cd01308 79 vtlsdlttaGVTTVVGC------LG-----------------------------TDGISR-------SMEDL------LA 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 171 TPEQLEK--IMAYVEQG------------------LDEGAIGIGINAGYAPGYGQKEYYALSKLAAERDV-------ATY 223
Cdd:cd01308 111 KARALEEegITCFVYTGsyevptrtitgsirkdllLIDKVIGVGEIAISDHRSSQPTVEELARIAAEARVggllggkAGI 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 224 THVRyasMMEPGSSFEAIQELIANSALTGAKMHINHINSTSlrdidatlELFDEATEngfHVTAGaypwgaastvvgaam 303
Cdd:cd01308 191 VHIH---LGDGKRALSPIFELIEETEIPITQFLPTHINRTA--------PLFEQGVE---FAKMG--------------- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 304 fsgpewkerlgyqeesiqmGTERLNNEELLKAQKE---QPGSIINwHFLDEAVPSElsaldksiihpNVLIESDSmpwml 380
Cdd:cd01308 242 -------------------GTIDLTSSIDPQFRKEgevRPSEALK-RLLEQGVPLE-----------RITFSSDG----- 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 381 ieDGKVSYYegDEwpipseafahprsSGTFTKI-------LGTYVRE---RGLLSMEEAIRKMSYMPATVLdgfvpQMEK 450
Cdd:cd01308 286 --NGSLPKF--DE-------------NGNLVGLgvgsvdtLLREVREavkCGDIPLEVALRVITSNVARIL-----KLRK 343
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 914653889 451 KGRIQVGMDADIVIFDPKtvankatyqvpaaisTGVDTVLVNGQFVVQDGELV 503
Cdd:cd01308 344 KGEIQPGFDADLVILDKD---------------LDINSVIAKGQIMVRNGKLL 381
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
25-113 |
7.42e-08 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 54.86 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 25 SYDVVIQGGHVIdPETGlSDVRNIGINKGTIEAITKDSITGKTIIDANDHIVSPGFIDLHHH-----GQNIAGY----RM 95
Cdd:PRK08044 2 SFDLIIKNGTVI-LENE-ARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHisepgRSHWEGYetgtRA 79
|
90
....*....|....*...
gi 914653889 96 QAQQGVTTALELESGILP 113
Cdd:PRK08044 80 AAKGGITTMIEMPLNQLP 97
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
26-516 |
1.67e-07 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 53.55 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 26 YDVVIQGGHVIDP-ETGLSDvrnIGINKGTIEAITKDSITGKTIIDANDHIVSPGFIDLHHHGQNIAGyrmqaqQGVTTA 104
Cdd:PRK13404 4 FDLVIRGGTVVTAtDTFQAD---IGIRGGRIAALGEGLGPGAREIDATGRLVLPGGVDSHCHIDQPSG------DGIMMA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 105 LELESG-----------ILPIGDWYKGQ------------AEKNLPINYGasaawtFARIatFTDSEPQANLQYFQSM-- 159
Cdd:PRK13404 75 DDFYTGtvsaafggtttVIPFAAQHRGQslreavedyhrrAAGKAVIDYA------FHLI--VADPTEEVLTEELPALia 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 160 QGLDNWK-------QKIATPEQLEKIMAYVEQGL-------DEGAIGIGINAGYAPGYGQKEYYALSK-LAAERdvatyt 224
Cdd:PRK13404 147 QGYTSFKvfmtyddLKLDDRQILDVLAVARRHGAmvmvhaeNHDMIAWLTKRLLAAGLTAPKYHAISRpMLAER------ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 225 hvryasmmepgssfEAIQELIANSALTGAKMHINHInSTSlrdidATLELFDEATENGFHVTAGAYPwgaastvvgaamf 304
Cdd:PRK13404 221 --------------EATHRAIALAELVDVPILIVHV-SGR-----EAAEQIRRARGRGLKIFAETCP------------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 305 sgpewkerlgyqeESIQMGTERLNNEELLKAQ---KEQPGSIINWHFLDEAVpsELSALDksiihpnvLIESDSMPWMLI 381
Cdd:PRK13404 268 -------------QYLFLTAEDLDRPGMEGAKyicSPPPRDKANQEAIWNGL--ADGTFE--------VFSSDHAPFRFD 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 382 E-DGKVSyyEGDEWPIPSEAFAHPrssGTFTK--ILGTYVRERGLLSMEEAIRKMSYMPATVLdGFVPqmeKKGRIQVGM 458
Cdd:PRK13404 325 DtDGKLA--AGANPSFKAIANGIP---GIETRlpLLFSEGVVKGRISLNRFVALTSTNPAKLY-GLYP---RKGAIAIGA 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 914653889 459 DADIVIFDP---KTVANK-----ATYQVPAAIS-TG-VDTVLVNGQFVVQDGELVTSAAPGQAIRRDT 516
Cdd:PRK13404 396 DADIAIWDPdreVTITNAdlhhaADYTPYEGMRvTGwPVTVLSRGRVVVEDGELVAERGSGQFLARSL 463
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
424-503 |
1.97e-07 |
|
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: 53.36 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 424 LSMEEAIRKMSYMPATVLDgfvpqMEKKGRIQVGMDADIVIFDPKTVANKATYQVPAAI-----STGVDTVLVNGQFVVQ 498
Cdd:cd01298 332 LPAEEALEMATIGGAKALG-----LDEIGSLEVGKKADLILIDLDGPHLLPVHDPISHLvysanGGDVDTVIVNGRVVME 406
|
....*
gi 914653889 499 DGELV 503
Cdd:cd01298 407 DGELL 411
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
27-86 |
2.59e-07 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 53.18 E-value: 2.59e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 27 DVVIQGGHVIDPETGLSDVRNIGINKGTIEAITKDSITGKTIIDANDHIVSPGFIDLHHH 86
Cdd:COG1001 6 DLVIKNGRLVNVFTGEILEGDIAIAGGRIAGVGDYIGEATEVIDAAGRYLVPGFIDGHVH 65
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
25-514 |
4.45e-07 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 52.40 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 25 SYDVVIQGGHVIDPETglsdVR--NIGINKGTIEAITKD-SITGKTIIDANDHIVSPGFIDLH-H-------HGQNIA-G 92
Cdd:PRK06189 2 MYDLIIRGGKVVTPEG----VYraDIGIKNGKIAEIAPEiSSPAREIIDADGLYVFPGMIDVHvHfnepgrtHWEGFAtG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 93 YRMQAQQGVTTALElesgiLPIgdwykgqaeKNLPINYGASAAWTFARIATftdsepQANLQYFQSMQGLdnwkqkiaTP 172
Cdd:PRK06189 78 SAALAAGGCTTYFD-----MPL---------NSIPPTVTREALDAKAELAR------QKSAVDFALWGGL--------VP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 173 EQLEKIMAYVEQGLdegaigIGINAGYA-PGY-------------GQKEYYALSK---LAAERDVATY-----------T 224
Cdd:PRK06189 130 GNLEHLRELAEAGV------IGFKAFMSnSGTdefrssddltlyeGMKEIAALGKilaLHAESDALTRhlttqarqqgkT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 225 HVR-YASMMEPGSSFEAIQELIANSALTGAKMHINHINSTslrdidATLELFDEATENGFHVTAGAYPwgaastvvGAAM 303
Cdd:PRK06189 204 DVRdYLESRPVVAELEAVQRALLYAQETGCPLHFVHISSG------KAVALIAEAKKRGVDVSVETCP--------HYLL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 304 FSGPEWkERLGYQEESIQMGTERLNNEELLKAQKEqpGSIinwhfldeavpsELSALDKSIIHPNvLIESDSM--PWMLI 381
Cdd:PRK06189 270 FTEEDF-ERIGAVAKCAPPLRSRSQKEELWRGLLA--GEI------------DMISSDHSPCPPE-LKEGDDFflVWGGI 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 382 EDGKvsyyegdewpipseafahprssGTFTKILGTYVRERGlLSMEEAIRKMSYMPATVLDgfvpqMEKKGRIQVGMDAD 461
Cdd:PRK06189 334 SGGQ----------------------STLLVMLTEGYIERG-IPLETIARLLATNPAKRFG-----LPQKGRLEVGADAD 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914653889 462 IVIFD---PKTVANKATYQV-PAAISTG------VDTVLVNGQFVVQDGElVTSAAPGQAIRR 514
Cdd:PRK06189 386 FVLVDldeTYTLTKEDLFYRhKQSPYEGrtfpgrVVATYLRGQCVYQDGE-VFPPPRGQLLRP 447
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
27-86 |
4.72e-07 |
|
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: 52.14 E-value: 4.72e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914653889 27 DVVIQGGHVIDPETGLSDVRN--IGINKGTIEAITKDS-----ITGKTIIDANDHIVSPGFIDLHHH 86
Cdd:COG0402 1 DLLIRGAWVLTMDPAGGVLEDgaVLVEDGRIAAVGPGAelparYPAAEVIDAGGKLVLPGLVNTHTH 67
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
416-469 |
5.02e-07 |
|
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: 51.85 E-value: 5.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 914653889 416 TYVRERGLLSMEEAIRKMSYMPATVLdGFVPqmekkGRIQVGMDADIVIFDPKT 469
Cdd:cd01317 297 TLLVKGGLLTLPDLIRALSTNPAKIL-GLPP-----GRLEVGAPADLVLFDPDA 344
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
28-87 |
1.34e-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: 50.66 E-value: 1.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914653889 28 VVIQGGHVIDPEtGLSDVRnIGINKGTIEAITK--DSITGKTIIDANDHIVSPGFIDLHHHG 87
Cdd:cd00854 1 LIIKNARILTPG-GLEDGA-VLVEDGKIVAIGPedELEEADEIIDLKGQYLVPGFIDIHIHG 60
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
378-468 |
2.37e-06 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 49.70 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 378 WMLIEDGKVSYYEGDEWPIPSEafaHPRSSGTFTK-------------ILGTYVRERGLlSMEEAIRKMSYMPATVLdGF 444
Cdd:cd01302 212 WEGVKNGKIDTIASDHAPHSKE---EKESGKDIWKappgfpgletrlpILLTEGVKRGL-SLETLVEILSENPARIF-GL 286
|
90 100
....*....|....*....|....
gi 914653889 445 VPqmekKGRIQVGMDADIVIFDPK 468
Cdd:cd01302 287 YP----KGTIAVGYDADLVIVDPK 306
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
378-468 |
4.00e-06 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 48.87 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 378 WMLIEDGKVSYYEGDEWP-IPSEAFAHPRS--SG-----TFTKILGTYVReRGLLSMEEAIRKMSYMPATVLDgfvpqME 449
Cdd:cd01318 234 LQALADGRIDVIASDHAPhTLEEKRKGYPAapSGipgveTALPLMLTLVN-KGILSLSRVVRLTSHNPARIFG-----IK 307
|
90
....*....|....*....
gi 914653889 450 KKGRIQVGMDADIVIFDPK 468
Cdd:cd01318 308 NKGRIAEGYDADLTVVDLK 326
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
46-470 |
6.76e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 48.49 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 46 RNIGINKGTIEAITKD--SITGKTIIDANDHIVSPGFIDLHHH----GQN-----IAGYRMQAQQGVTTALELESGILPI 114
Cdd:PRK02382 20 RDVRIDGGKITAVGKDldGSSSEEVIDARGMLLLPGGIDVHVHfrepGYThketwYTGSRSAAAGGVTTVVDQPNTDPPT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 115 --GDWYKGQAE----KNL---PINYGASAAWtfariatftdsEPQANLqyfqsmqgldnWKqkiatpeqlEKIMAYVEQG 185
Cdd:PRK02382 100 vdGESFDEKAElaarKSIvdfGINGGVTGNW-----------DPLESL-----------WE---------RGVFALGEIF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 186 LDEGAIGIGINA-------GYAPGYG--------QKEYYALSKLAAERDVATYTHVRYASmmePGSSFEAIQELIANSAL 250
Cdd:PRK02382 149 MADSTGGMGIDEelfeealAEAARLGvlatvhaeDEDLFDELAKLLKGDADADAWSAYRP---AAAEAAAVERALEVASE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 251 TGAKMHINHInstslrdidATLELFDEATENGFhvTAGAYPwgaastvvgAAMF-SGPEWkERLGY---------QEESI 320
Cdd:PRK02382 226 TGARIHIAHI---------STPEGVDAARREGI--TCEVTP---------HHLFlSRRDW-ERLGTfgkmnpplrSEKRR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 321 QMGTERLNNeellkaqkeqpGSIinwhfldeavpselsalDksiihpnvLIESDSMPWMLIEDgkvsyyEGDEWPIPS-- 398
Cdd:PRK02382 285 EALWERLND-----------GTI-----------------D--------VVASDHAPHTREEK------DADIWDAPSgv 322
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914653889 399 ---EafahprssgTFTKILGTYVReRGLLSMEEAIRKMSYMPATVLDgfvpqMEKKGRIQVGMDADIVIFDPKTV 470
Cdd:PRK02382 323 pgvE---------TMLPLLLAAVR-KNRLPLERVRDVTAANPARIFG-----LDGKGRIAEGYDADLVLVDPDAA 382
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
29-92 |
7.79e-06 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 48.65 E-value: 7.79e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914653889 29 VIQGGHVIDPETGLS-DVRNIGINKGTIEAITKDSITGKTIiDANDHIVSPGFIDLHHHgqnIAG 92
Cdd:COG1229 4 IIKNGRVYDPANGIDgEVMDIAIKDGKIVEEPSDPKDAKVI-DASGKVVMAGGVDIHTH---IAG 64
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
452-499 |
1.56e-05 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 47.13 E-value: 1.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 914653889 452 GRIQVGMDADIVIFDPKTVANKATYQVPAAI-----STGVDTVLVNGQFVVQD 499
Cdd:COG0402 364 GSLEPGKRADLVVLDLDAPHLAPLHDPLSALvyaadGRDVRTVWVAGRVVVRD 416
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
27-86 |
2.52e-05 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 46.49 E-value: 2.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914653889 27 DVVIQGGHVIDPETG--LSDVrNIGINKGTIEAITKDSIT----GKTIIDANDHIVSPGFIDLHHH 86
Cdd:COG1228 9 TLLITNATLVDGTGGgvIENG-TVLVEDGKIAAVGPAADLavpaGAEVIDATGKTVLPGLIDAHTH 73
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
30-503 |
4.59e-05 |
|
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: 45.87 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 30 IQGGHVIDPETGLSD-VRNIGINKGTIEAITKDSITGKTIiDANDHIVSPGFIDLHHH---GQNIAGYRMQAQqgvttal 105
Cdd:cd01304 1 IKNGTVYDPLNGINGeKMDIFIRDGKIVESSSGAKPAKVI-DASGKVVMAGGVDMHSHiagGKVNVGRILRPE------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 106 ELESGILPIGDWYKGQAEKNLPinygaSAAWT---FARIATFTDSEP--------QANLQyFQSMQGLD---------NW 165
Cdd:cd01304 73 DHRRDPVPKGALRRAGVGFSVP-----STLATgyrYAEMGYTTAFEAampplnarHTHEE-MADTPILDkgaypllgnNW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 166 K--QKIATPEqLEKIMAYVEQGLdEGAIGIGI---NAG--YAPGYGQ-----------------KEYYALSKLAAERDVA 221
Cdd:cd01304 147 FvlEYLRDGD-MEKLAAYVAWTL-KASKGYGIkvvNPGgtEAWGWGQnvlslddpvpyfditprEILKGLAEANEELGLP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 222 TYTHVRYASMMEPGS------SFEAIQELIANSALTgaKMHINHI--NS---TSLRDIDATLELFDEATENGFHVT--AG 288
Cdd:cd01304 225 HSIHVHCNNLGVPGNyettleTMKAAEGVKPDPRRQ--VLHLTHVqfHSyggTSWRDFESGAERIADYVNANDHVTidVG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 289 AYPWGAASTVVGAAMFsgpewkerlgyQEESIQMGTERLNNEEL----------LKAQKEQPGSIINWhfldeAVPSELS 358
Cdd:cd01304 303 QVIFGETTTMTGDGPM-----------QFDLHGLTGLKWVNCDIeletgsgvvpFIYSPKNPVNALQW-----AIGLELF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 359 AL----DKSII---HPN--VLIE-SDSMPWMLiedgkvSYYEGDEWPIPSEAFAHPRSSgtftkiLGTYVRErglLSMEE 428
Cdd:cd01304 367 LLiddpWKVILttdHPNggPFTRyPRIIAWLM------SKKFRAEEIATLHKWAQDRSA------LPGIDRE---YSLYE 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914653889 429 AIRKMSYMPATVLDgfvpqMEKKGRIQVGMDADIVIF--DPKTVANKATYQVPAAISTGvDTVLVNGQFVVQDGELV 503
Cdd:cd01304 432 IAIMTRAGPAKLLG-----LSDKGHLGVGADADIAIYddDPDQVDPSDYEKVEKAFSRA-AYVLKDGEIVVKDGEVV 502
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
28-83 |
4.72e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 45.82 E-value: 4.72e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 914653889 28 VVIQGGHVIDPETGLSDVRNIGINKGTIEAITK--DSITGKTIIDANDHIVSPGFIDL 83
Cdd:PRK07627 3 IHIKGGRLIDPAAGTDRQADLYVAAGKIAAIGQapAGFNADKTIDASGLIVCPGLVDL 60
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
452-504 |
4.89e-05 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 45.61 E-value: 4.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 914653889 452 GRIQVGMDADIVIFDPKTVANKATYQVPAAISTG----VDTVLVNGQFVVQDGELVT 504
Cdd:PRK08203 374 GSLAPGKLADLALFDLDELRFAGAHDPVAALVLCgpprADRVMVGGRWVVRDGQLTT 430
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
421-513 |
4.91e-05 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 45.63 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 421 RGLLSMEEAIRKMSYMPATVLdgfvpQMEKKGRIQVGMDADIVIFDPKTvankaTYQVPA---------------AISTG 485
Cdd:PRK09236 345 EGKLSLEKVVEKTSHAPAILF-----DIKERGFIREGYWADLVLVDLNS-----PWTVTKenilykcgwspfegrTFRSR 414
|
90 100
....*....|....*....|....*...
gi 914653889 486 VDTVLVNGQFVVQDGELVTSAApGQAIR 513
Cdd:PRK09236 415 VATTFVNGQLVYHNGQLVESCR-GQRLE 441
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
30-169 |
1.10e-04 |
|
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: 44.55 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 30 IQGGHVIDPETGLSDvrnIGINKGTIEAITK--DSITGKTIIDANDHIVSPGFIDLHHH----------GQNIAGYRMQA 97
Cdd:cd01293 2 LRNARLADGGTALVD---IAIEDGRIAAIGPalAVPPDAEEVDAKGRLVLPAFVDPHIHldktftggrwPNNSGGTLLEA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914653889 98 QQGVTTALELESgilpiGDWYKGQAEK--NLPINYGASAawtfarIATFTDSEPQANLQYFQSMQGL-DNWKQKI 169
Cdd:cd01293 79 IIAWEERKLLLT-----AEDVKERAERalELAIAHGTTA------IRTHVDVDPAAGLKALEALLELrEEWADLI 142
|
|
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
32-186 |
1.11e-04 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 44.62 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 32 GGHVIDPETGLSDVRnigINKGTIEAITKDSI---TGKTIIDANDHIVSPGFIDLHHH-GQNIAGYRMQA---QQGVTTA 104
Cdd:PRK06846 21 NGVIVQTETALCTLE---IQDGKIVAIRPNKQvpdATLPTYDANGLLMLPAFREMHIHlDKTYYGGPWKAcrpAKTIQDR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 105 LELESGILPIGDWYKGQ-AEK--NLPINYGAsaawTFARiaTFTDSEPQANLQYFQSMQ-GLDNWKQKIATpeqleKIMA 180
Cdd:PRK06846 98 IELEQKELPELLPTTQErAEKliELLQSKGA----THIR--SHCNIDPVIGLKNLENLQaALERYKDGFTY-----EIVA 166
|
....*.
gi 914653889 181 YVEQGL 186
Cdd:PRK06846 167 FPQHGL 172
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
75-496 |
1.26e-04 |
|
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: 44.03 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 75 IVSPGFIDLHHHGQ--NIAGYRMQAQQ-------GVTTAleLESGILPIGDWYKG---------QAEKNLPINYGASAAW 136
Cdd:pfam01979 1 IVLPGLIDAHVHLEmgLLRGIPVPPEFayealrlGITTM--LKSGTTTVLDMGATtstgieallEAAEELPLGLRFLGPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 137 TFariaTFTDSEPqanlqyfqsmQGLDNWKQKIATPEQLEKIMAyveqgldEGAIGIGINAGYAPGYGQKEYYALSKLAA 216
Cdd:pfam01979 79 CS----LDTDGEL----------EGRKALREKLKAGAEFIKGMA-------DGVVFVGLAPHGAPTFSDDELKAALEEAK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 217 ERDVatythvryasmmepgssfeaiqeliansaltgaKMHInHINSTSLrDIDATLELFDEATENGFHVTAGAYPwgaas 296
Cdd:pfam01979 138 KYGL---------------------------------PVAI-HALETKG-EVEDAIAAFGGGIEHGTHLEVAESG----- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 297 tvvgaamfsgpewkerlgyqeesiqmgteRLNNEELLKAQKeqpgsiiNWHFLD-EAVPSELSALDKSIIH---PNVLIE 372
Cdd:pfam01979 178 -----------------------------GLLDIIKLILAH-------GVHLSPtEANLLAEHLKGAGVAHcpfSNSKLR 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 373 SDSMP-WMLIEDGKVSYYEGDEwpipseafahpRSSGTFTKILG-------TYVRERGLLSMEEAIRKMSYMPATVLdGF 444
Cdd:pfam01979 222 SGRIAlRKALEDGVKVGLGTDG-----------AGSGNSLNMLEelrlaleLQFDPEGGLSPLEALRMATINPAKAL-GL 289
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 914653889 445 vpqMEKKGRIQVGMDADIVIFDPKTVANKATYQVPAAistgVDTVLVNGQFV 496
Cdd:pfam01979 290 ---DDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGN----VKKVIVKGKIV 334
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
421-512 |
1.75e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 43.90 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 421 RGLLSMEEAIRKMSYMPATVLDgfVPqmeKKGRIQVGMDADIVIFD---PKTVANKaTYQVPAAIS-------TG-VDTV 489
Cdd:PRK07575 339 RGKCTVAQVVRWMSTAVARAYG--IP---NKGRIAPGYDADLVLVDlntYRPVRRE-ELLTKCGWSpfegwnlTGwPVTT 412
|
90 100
....*....|....*....|...
gi 914653889 490 LVNGQFVVQDGELVTSAApGQAI 512
Cdd:PRK07575 413 IVGGQIVFDRGQVNTEVR-GQAL 434
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
448-515 |
2.70e-04 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 43.45 E-value: 2.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914653889 448 MEKK-GRIQVGMDADIVIFD-------PKTVANKATYQVPAAISTGVDTVLVNGQFVVQDGELVTSAAPgqAIRRD 515
Cdd:PRK07228 356 FEDEiGSLEEGKKADLAILDldglhatPSHGVDVLSHLVYAAHGSDVETTMVDGKIVMEDGELTTIDAD--AVRRE 429
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
422-513 |
3.94e-04 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 42.98 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 422 GLLSMEEAIRKMSYMPATVLDgfvpqMEKKGRIQVGMDADIVIFDPK---TVANK--ATyqvPAAIS-------TG--VD 487
Cdd:PRK09060 342 GRLSLERFVDLTSAGPARIFG-----IAGKGRIAVGYDADFTIVDLKrreTITNEwiAS---RCGWTpydgkevTGwpVG 413
|
90 100
....*....|....*....|....*.
gi 914653889 488 TVlVNGQFVVQDGELVTSAApGQAIR 513
Cdd:PRK09060 414 TI-VRGQRVMWDGELVGPPT-GEPVR 437
|
|
| PLN02795 |
PLN02795 |
allantoinase |
218-469 |
4.22e-04 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 42.84 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 218 RDVATYTHVRYASMMEpgssfEAIQELIANSALT-------GAKMHINHinstsLRDIDATLELFDEATENGFHVTAGAY 290
Cdd:PLN02795 249 RSYSTYLKSRPPSWEQ-----EAIRQLLEVAKDTrpggvaeGAHVHIVH-----LSDAESSLELIKEAKAKGDSVTVETC 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 291 PwgaastvvgaamfsgpewkERLGYQEESIQMGTERL----------NNEELLKAQKEqpGSIinwhfldEAVPSElsal 360
Cdd:PLN02795 319 P-------------------HYLAFSAEEIPDGDTRYkcappirdaaNRELLWKALLD--GDI-------DMLSSD---- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 361 dksiiHpnvlieSDSMPWM-LIEDGKVSyyegDEWP-IPSEAFAHPrssgtftkILGTYVRERGLlSMEEAIRKMSYMPA 438
Cdd:PLN02795 367 -----H------SPSPPDLkLLEEGNFL----RAWGgISSLQFVLP--------ATWTAGRAYGL-TLEQLARWWSERPA 422
|
250 260 270
....*....|....*....|....*....|.
gi 914653889 439 TvLDGfvpqMEKKGRIQVGMDADIVIFDPKT 469
Cdd:PLN02795 423 K-LAG----LDSKGAIAPGKDADIVVWDPEA 448
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
418-468 |
6.28e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 42.18 E-value: 6.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 914653889 418 VRERGLLSMEEAIRKMSYMPATVLDGFvpqmEKKGRIQVGMDADIVIFDPK 468
Cdd:cd00854 318 MVKWGGCPLEEAVRMASLNPAKLLGLD----DRKGSLKPGKDADLVVLDDD 364
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
47-103 |
6.78e-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: 41.93 E-value: 6.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914653889 47 NIGINKGTIEAITKDSIT--GKTIIDANDHIVSPGFIDLHHH---GQNIAGYR---MQAQQGVTT 103
Cdd:cd01307 1 DVAIENGKIAAVGAALAApaATQIVDAGGCYVSPGWIDLHVHvyqGGTRYGDRpdmIGVKSGVTT 65
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
28-86 |
7.49e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 41.90 E-value: 7.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914653889 28 VVIQGGHVIDPETGLSDVRNIGINKGTIEAITK---DSITGKTIIDANDHIVSPGFIDLHHH 86
Cdd:PRK07369 4 ELLQQVRVLDPVSNTDRIADVLIEDGKIQAIEPhidPIPPDTQIIDASGLILGPGLVDLYSH 65
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
27-86 |
1.10e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 41.54 E-value: 1.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914653889 27 DVVIQGGHVIDPETGLSdvrnIGINKGTIEAITKdSITGK--TIIDANDHIVSPGFIDLHHH 86
Cdd:PRK07572 3 DLIVRNANLPDGRTGID----IGIAGGRIAAVEP-GLQAEaaEEIDAAGRLVSPPFVDPHFH 59
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
416-469 |
1.26e-03 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 41.23 E-value: 1.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 914653889 416 TYVRERGLLSMEEAIRKMSYMPATVLDgfvpqmEKKGRIQVGMDADIVIFDPKT 469
Cdd:PRK08417 307 TYLVKEGIITWSELSRFTSYNPAQFLG------LNSGEIEVGKEADLVLFDPNE 354
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
23-86 |
1.26e-03 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 41.44 E-value: 1.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914653889 23 ADSYDVVIQGGHVIDPetGLSDVRNIGINKGTIEAITK-DSITGKTIIDANDHIVSPGFIDLHHH 86
Cdd:PRK09060 2 TQTFDLILKGGTVVNP--DGEGRADIGIRDGRIAAIGDlSGASAGEVIDCRGLHVLPGVIDSQVH 64
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
28-86 |
1.61e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 41.14 E-value: 1.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914653889 28 VVIQGGHVI--DPETGLSDVRNIGINKGTIEAItKDSI--TGKTIIDANDHIVSPGFIDLHHH 86
Cdd:PRK08204 4 TLIRGGTVLtmDPAIGDLPRGDILIEGDRIAAV-APSIeaPDAEVVDARGMIVMPGLVDTHRH 65
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
27-86 |
1.87e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 40.89 E-value: 1.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914653889 27 DVVIQGGHVIDPETGlsDVRN--IGINKGTIEAITKDSIT-GKTIIDANDHIVSPGFIDLHHH 86
Cdd:PRK06038 3 DIIIKNAYVLTMDAG--DLKKgsVVIEDGTITEVSESTPGdADTVIDAKGSVVMPGLVNTHTH 63
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
430-504 |
2.53e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 40.12 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914653889 430 IRKMSYMPATVLDGF-VPQME----------KKGRIQVGMDADIVIFDPKT-----VANKATYQVPAAISTGVDTVLVNG 493
Cdd:PRK06038 317 LHKVNTMDPTALPARqVLEMAtvngakalgiNTGMLKEGYLADIIIVDMNKphltpVRDVPSHLVYSASGSDVDTTIVDG 396
|
90
....*....|.
gi 914653889 494 QFVVQDGELVT 504
Cdd:PRK06038 397 RILMEDYKVLC 407
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
47-86 |
4.68e-03 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 39.66 E-value: 4.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 914653889 47 NIGINKGTIEAI-TKDSITGKTIIDANDHIVSPGFIDLHHH 86
Cdd:PRK12393 27 DIRIRDGRIAAIgALTPLPGERVIDATDCVVYPGWVNTHHH 67
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
48-86 |
5.09e-03 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 39.16 E-value: 5.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 914653889 48 IGINKGTIEAIT------KDSITGKTIIDANDHIVSPGFIDLHHH 86
Cdd:cd01296 1 IAIRDGRIAAVGpaaslpAPGPAAAEEIDAGGRAVTPGLVDCHTH 45
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
424-469 |
5.30e-03 |
|
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: 39.23 E-value: 5.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 914653889 424 LSMEEAIRKMSYMPATVLdgfvpQMEKKGRIQVGMDADIVIFDPKT 469
Cdd:cd01307 277 MPLEEVIEAVTANPARML-----GLAEIGTLAVGYDADLTVFDLKD 317
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
424-496 |
6.89e-03 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 39.01 E-value: 6.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914653889 424 LSMEEAIRKMSYMPATVLdgfvpQMEK-KGRIQVGMDADIVIF--DPKTVAnkatyqvPAAI-STGVDTVLVNGQFV 496
Cdd:COG1574 467 LTVEEALRAYTIGAAYAA-----FEEDeKGSLEPGKLADFVVLdrDPLTVP-------PEEIkDIKVLLTVVGGRVV 531
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
47-86 |
7.51e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 38.60 E-value: 7.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 914653889 47 NIGINKGTIEAITKDSITGKTIIDANDHIVSPGFIDLHHH 86
Cdd:PRK04250 16 GIGIENGRISKISLRDLKGKEVIKVKGGIILPGLIDVHVH 55
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
28-86 |
8.34e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 38.63 E-value: 8.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914653889 28 VVIQGGHVIDPETgLSDVR-NIGINKGTIEAITKD-SITGKTIIDANDHIVSPGFIDLHHH 86
Cdd:PRK08393 3 ILIKNGYVIYGEN-LKVIRaDVLIEGNKIVEVKRNiNKPADTVIDASGSVVSPGFINAHTH 62
|
|
| |
