|
Name |
Accession |
Description |
Interval |
E-value |
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
3-476 |
6.72e-180 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 514.34 E-value: 6.72e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 3 YDYVFKNATVIDGSGKSEFVSDIAVKDEWIIKISKNISEDAEKIIDCSGLILSPGFIDVHTHDDLIVIDKPEYIEKTSQG 82
Cdd:COG3653 2 FDLLIRGGTVVDGTGAPPFRADVAIKGGRIVAVGDLAAAEAARVIDATGLVVAPGFIDIHTHYDLQLLWDPRLEPSLRQG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 83 VTTIIVGNCGISAACATlKDEVPDPINLLG------ELSEFQFADLASYKQKINNVKPTVNVATLIGHTTLRNNCVTDLL 156
Cdd:COG3653 82 VTTVVMGNCGVSFAPVR-PEDRDRLIDLMEgvegipEGLDWDWESFGEYLDALERRGLGVNVASLVGHGTLRAYVMGLDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 157 KPATPDNIAHMKQVLACALDEGALGLSTGLSYGNAINSSTEEICELAELLAEHQGIYTTHMRTEYDGIIDAMHEAFHIGR 236
Cdd:COG3653 161 RPPTPEELARMRALLREAMEAGALGLSTGLIYVPGTYASTDELVALAKVVAEYGGVYQSHMRDEGDGLLEAVDELIRIGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 237 HAKVPVQISHHKCAGAKNWGRTKETLALIEKYQVM-QDINCDCYPYRAGSSNLDIT------------------------ 291
Cdd:COG3653 241 EAGVPVHISHLKAAGKPNWGKADEVLALIEAARAEgLDVTADVYPYPAGSTGLGALlppwaaagglderlarlrdpatra 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 292 QVTEDYD---------------ILVTWSTPFPEVAGKTLKEIAAMWSSDIFQVAEKIV-----PAGAIYFQMHEDDVRRV 351
Cdd:COG3653 321 RIRAEIEeglpdnllgrggwdnILISDSPPNEPLVGKSLAEIAAERGVDPADAALDLLleedgRVLIVYFIMSEEDVREL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 352 LQHPSSMVGSDGLPRDPnPHPRLWGTFPRVISHYSRDEQLFPMTTAIYKMTGMSAQRFSLKDRGLIQENYFADIVVFDPE 431
Cdd:COG3653 401 LRHPWVMIGSDGGLGGK-AHPRAYGTFPRVLGHYVRERGVLSLEEAVRKLTSLPADRLGLKDRGLLRPGYRADLVVFDPA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1949839140 432 KINETATFQDPKQKADGIEYVFVNGVLTYTKKEMTGNRAGKFLER 476
Cdd:COG3653 480 TLADRATFDLPAQRADGIRAVIVNGVVVVEDGKPTGARPGRVLRG 524
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
4-472 |
2.65e-157 |
|
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: 452.52 E-value: 2.65e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 4 DYVFKNATVIDGSGKSEFVSDIAVKDEWIIKISKNISEDAEKIIDCSGLILSPGFIDVHTHDDLIVIDKPEYIEKTSQGV 83
Cdd:cd01297 1 DLVIRNGTVVDGTGAPPFTADVGIRDGRIAAIGPILSTSAREVIDAAGLVVAPGFIDVHTHYDGQVFWDPDLRPSSRQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 84 TTIIVGNCGISAACATLKDEVPDPINL-----LGELSEFQFADLASYKQKINNVKPTVNVATLIGHTTLRNNCVTDLLKP 158
Cdd:cd01297 81 TTVVLGNCGVSPAPANPDDLARLIMLMeglvaLGEGLPWGWATFAEYLDALEARPPAVNVAALVGHAALRRAVMGLDARE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 159 ATPDNIAHMKQVLACALDEGALGLSTGLSYGNAINSSTEEICELAELLAEHQGIYTTHMRTEYDGIIDAMHEAFHIGRHA 238
Cdd:cd01297 161 ATEEELAKMRELLREALEAGALGISTGLAYAPRLYAGTAELVALARVAARYGGVYQTHVRYEGDSILEALDELLRLGRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 239 KVPVQISHHKCAGAKNWGRTKETLALIEKYQV-MQDINCDCYPYRAGSsnlditqvtedydilvtwstpfpevagktlke 317
Cdd:cd01297 241 GRPVHISHLKSAGAPNWGKIDRLLALIEAARAeGLQVTADVYPYGAGS-------------------------------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 318 iaamwssdifqvaekivpagaiyfqmhEDDVRRVLQHPSSMVGSDGLPrDPNPHPRLWGTFPRVISHYSRDEQLFPMTTA 397
Cdd:cd01297 289 ---------------------------EDDVRRIMAHPVVMGGSDGGA-LGKPHPRSYGDFTRVLGHYVRERKLLSLEEA 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949839140 398 IYKMTGMSAQRFSLKDRGLIQENYFADIVVFDPEKINETATFQDPKQKADGIEYVFVNGVLTYTKKEMTGNRAGK 472
Cdd:cd01297 341 VRKMTGLPARVFGLADRGRIAPGYRADIVVFDPDTLADRATFTRPNQPAEGIEAVLVNGVPVVRDGAFTGARPGR 415
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
3-458 |
2.01e-50 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 179.12 E-value: 2.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 3 YDYVFKNATVIDGSGKSEFVSDIAVKDEWIIKISKNiSEDAEKIIDCSGLILSPGFIDVHTHddliVIDKPEYIEKTSQG 82
Cdd:PRK09061 19 YDLVIRNGRVVDPETGLDAVRDVGIKGGKIAAVGTA-AIEGDRTIDATGLVVAPGFIDLHAH----GQSVAAYRMQAFDG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 83 VTTII---VGNCGISAACATlKDEVPDPINLlGELSEFQFADLAsykqkinnVKPTVNVATLI---GHTTLRNNCVTDll 156
Cdd:PRK09061 94 VTTALeleAGVLPVARWYAE-QAGEGRPLNY-GASVGWTPARIA--------VLTGPQAEGTIadfGKALGDPRWQER-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 157 kPATPDNIAHMKQVLACALDEGALGLSTGLSYgnAINSSTEEICELAELLAEHQGIYTTHMR--------TEYDGIIDAM 228
Cdd:PRK09061 162 -AATPAELAEILELLEQGLDEGALGIGIGAGY--APGTGHKEYLELARLAARAGVPTYTHVRylsnvdprSSVDAYQELI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 229 HEAFHIGRHakvpVQISHHKCAGAKNWGRTketLALIEKYQVM-QDINCDCYPYRAGSSnlDITQVTEDYDILVTWSTPF 307
Cdd:PRK09061 239 AAAAETGAH----MHICHVNSTSLRDIDRC---LALVEKAQAQgLDVTTEAYPYGAGST--VVGAAFFDPGWLERMGLGY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 308 PEV----AGKTL---KEIAAMWSSDifqvaekivPAGAIYFQM-------HEDDVRRVLQHPSSMVGSDG---------- 363
Cdd:PRK09061 310 GSLqwveTGERLltrEELAKLRAND---------PGGLVLIHFldednprDRALLDRSVLFPGAAIASDAmpwtwsdgtv 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 364 -------LPRDPNPHPRLWGTFPRVISHYSRDEQLFPMTTAIYKMTGMSAQRF-----SLKDRGLIQENYFADIVVFDPE 431
Cdd:PRK09061 381 yegdawpLPEDAVSHPRSAGTFARFLREYVRERKALSLLEAIRKCTLMPAQILedsvpAMRRKGRLQAGADADIVVFDPE 460
|
490 500
....*....|....*....|....*..
gi 1949839140 432 KINETATFQDPKQKADGIEYVFVNGVL 458
Cdd:PRK09061 461 TITDRATFEDPNRPSEGVRHVLVNGVP 487
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
45-460 |
5.07e-28 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 116.09 E-value: 5.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 45 KIIDCSGLILSPGFIDVHTHDD-----LIVIDKPEYIektsqgVTTIIVGNCGISaacatlkdevPDPINLLGE-LSEFQ 118
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLDggglnLRELRLPDVL------PNAVVKGQAGRT----------PKGRWLVGEgWDEAQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 119 FAD--LASYKQKINNVKP--TVNVATLIGHTTLRNNCVTDLLKPATPDNIAHMKQVLACALDEGALGLSTGLSYGNAINS 194
Cdd:pfam07969 65 FAEtrFPYALADLDEVAPdgPVLLRALHTHAAVANSAALDLAGITKATEDPPGGEIARDANGEGLTGLLREGAYALPPLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 195 STEEICELAELLAEHQ---GIYT-------THMRTEYDGIIDAMHEAFHIG----------RHAKVPVQISHHKCAGAKN 254
Cdd:pfam07969 145 AREAEAAAVAAALAALpgfGITSvdggggnVHSLDDYEPLRELTAAEKLKElldaperlglPHSIYELRIGAMKLFADGV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 255 WGR--------------------TKETLA-LIEKyqvMQDINCDCYPYRAGSSNLD-----ITQVTEDY-------DILV 301
Cdd:pfam07969 225 LGSrtaaltepyfdapgtgwpdfEDEALAeLVAA---ARERGLDVAIHAIGDATIDtaldaFEAVAEKLgnqgrvrIEHA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 302 TWSTPFPEvagKTLKEIAAM-WSSDIFQVAekiVPAGAIYFQM--------HEDDVRRVLQHPSSMV-GSDGLPRDPNPH 371
Cdd:pfam07969 302 QGVVPYTY---SQIERVAALgGAAGVQPVF---DPLWGDWLQDrlgaerarGLTPVKELLNAGVKVAlGSDAPVGPFDPW 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 372 PRLWGTFPR---VISHYSRDEQLFPMTTAIYKMTGMSAQRFSLKDR-GLIQENYFADIVVFDPEKInetaTFQDPKQKAD 447
Cdd:pfam07969 376 PRIGAAVMRqtaGGGEVLGPDEELSLEEALALYTSGPAKALGLEDRkGTLGVGKDADLVVLDDDPL----TVDPPAIADI 451
|
490
....*....|...
gi 1949839140 448 GIEYVFVNGVLTY 460
Cdd:pfam07969 452 RVRLTVVDGRVVY 464
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
6-476 |
1.48e-20 |
|
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: 93.62 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 6 VFKNATVIDGSGksEFVSDIAVKDEWIIKISKNISE-DAEKIIDCSGLILSPGFIDVHTHddlivIDKPEYIEK----T- 79
Cdd:COG0044 1 LIKNGRVVDPGG--LERADVLIEDGRIAAIGPDLAApEAAEVIDATGLLVLPGLIDLHVH-----LREPGLEHKedieTg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 80 SQ-----GVTTIIvgncgisaacatlkdevpDPINLLGELSEfqfADLASYKQKINNVKPTVNVATLIGhttlrnncvtd 154
Cdd:COG0044 74 TRaaaagGVTTVV------------------DMPNTNPVTDT---PEALEFKLARAEEKALVDVGPHGA----------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 155 llkpATPDNIAHMKQVLACAlDEGALGLSTGLSY-GNAINSSTEEI-----------------CE---LAELLAEHQGIY 213
Cdd:COG0044 122 ----LTKGLGENLAELGALA-EAGAVAFKVFMGSdDGNPVLDDGLLrraleyaaefgalvavhAEdpdLIRGGVMNEGKT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 214 TT--HMRT-----EYDGIidamHEAFHIGRHAKVP---VQIShhkcagaknwgrTKETLALIEKYQvmqdincdcypyRA 283
Cdd:COG0044 197 SPrlGLKGrpaeaEEEAV----ARDIALAEETGARlhiVHVS------------TAEAVELIREAK------------AR 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 284 GssnLDIT-QVT-----------EDYDILVTWSTPFpevagKTLKEIAAMWSSdifqVAEkivpaGAIyfqmheddvrrv 351
Cdd:COG0044 249 G---LPVTaEVCphhltltdedlERYGTNFKVNPPL-----RTEEDREALWEG----LAD-----GTI------------ 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 352 lqhpsSMVGSDGLPRDP----NPHPRLWG-------TFPRVISHYSRDEQLfPMTTAIYKMTGMSAQRFSLKDRGLIQEN 420
Cdd:COG0044 300 -----DVIATDHAPHTLeekeLPFAEAPNgipgletALPLLLTELVHKGRL-SLERLVELLSTNPARIFGLPRKGRIAVG 373
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949839140 421 YFADIVVFDPEKiNETATFQDPKQKAD-----G------IEYVFVNGVLTYTKKEMTGNRAGKFLER 476
Cdd:COG0044 374 ADADLVLFDPDA-EWTVTAEDLHSKSKntpfeGreltgrVVATIVRGRVVYEDGEVVGEPRGRFLRR 439
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
5-64 |
9.13e-16 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 79.08 E-value: 9.13e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 5 YVFKNATVIDGSGKSEfVSDIAVKDEWIIKISKNISEDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:PRK09357 3 ILIKNGRVIDPKGLDE-VADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVH 61
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
4-92 |
4.88e-15 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 76.36 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 4 DYVFKNATVIDGSGKSEFVSDIAVKDEWIIKISKNISE-DAEKIIDCSGLILSPGFIDVHTH-----------DDLIVId 71
Cdd:COG3964 1 DLLIKGGRVIDPANGIDGVMDIAIKDGKIAAVAKDIDAaEAKKVIDASGLYVTPGLIDLHTHvfpggtdygvdPDGVGV- 79
|
90 100
....*....|....*....|..
gi 1949839140 72 kpeyiektSQGVTTII-VGNCG 92
Cdd:COG3964 80 --------RSGVTTVVdAGSAG 93
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
8-92 |
9.02e-13 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 69.49 E-value: 9.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 8 KNATVIDGSGKSEFVSDIAVKDEWIIKISKNISE-DAEKIIDCSGLILSPGFIDVHTHddlIVIDKPEY-IEKTS----Q 81
Cdd:PRK09237 4 RGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDGsQAKKVIDLSGLYVSPGWIDLHVH---VYPGSTPYgDEPDEvgvrS 80
|
90
....*....|..
gi 1949839140 82 GVTTII-VGNCG 92
Cdd:PRK09237 81 GVTTVVdAGSAG 92
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
1-64 |
5.30e-10 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 61.41 E-value: 5.30e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949839140 1 MKYDYVFKNATVIDGSGksEFVSDIAVKDEWIIKISKNISEdAEKIIDCSGLILSPGFIDVHTH 64
Cdd:PRK08044 1 MSFDLIIKNGTVILENE--ARVVDIAVKGGKIAAIGQDLGD-AKEVMDASGLVVSPGMVDAHTH 61
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
4-87 |
8.16e-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: 60.77 E-value: 8.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 4 DYVFKNATVIDGSGksEFVSDIAVKDEWIIKISKNIS-EDAEKIIDCSGLILSPGFIDVHTHddlivIDKP-----EYIE 77
Cdd:cd01315 1 DLVIKNGRVVTPDG--VREADIAVKGGKIAAIGPDIAnTEAEEVIDAGGLVVMPGLIDTHVH-----INEPgrtewEGFE 73
|
90
....*....|....*
gi 1949839140 78 KTSQ-----GVTTII 87
Cdd:cd01315 74 TGTKaaaagGITTII 88
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
4-64 |
8.55e-10 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 60.36 E-value: 8.55e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949839140 4 DYVFKNATVIDGSGKSEFV-SDIAVKDEWIIKISKNIS---EDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:COG1228 9 TLLITNATLVDGTGGGVIEnGTVLVEDGKIAAVGPAADlavPAGAEVIDATGKTVLPGLIDAHTH 73
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
4-87 |
1.13e-09 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 60.50 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 4 DYVFKNATVID-GSGkSEFVSDIAVKDEWIIKISKNISEdAEKIIDCSGLILSPGFIDVHTHddlivID----KPEYIEK 78
Cdd:COG1001 6 DLVIKNGRLVNvFTG-EILEGDIAIAGGRIAGVGDYIGE-ATEVIDAAGRYLVPGFIDGHVH-----IEssmvTPAEFAR 78
|
90
....*....|.
gi 1949839140 79 TS--QGVTTII 87
Cdd:COG1001 79 AVlpHGTTTVI 89
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
6-64 |
1.46e-09 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 59.92 E-value: 1.46e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 6 VFKNATVIDGSGKSEfvSDIAVKDEWIIKISKNISEDAE-KIIDCSGLILSPGFIDVHTH 64
Cdd:cd01314 2 IIKNGTIVTADGSFK--ADILIEDGKIVAIGPNLEAPGGvEVIDATGKYVLPGGIDPHTH 59
|
|
| ade |
TIGR01178 |
adenine deaminase; The family described by this model includes an experimentally characterized ... |
4-64 |
1.97e-09 |
|
adenine deaminase; The family described by this model includes an experimentally characterized adenine deaminase of Bacillus subtilis. It also include a member from Methanobacterium thermoautotrophicum, in which adenine deaminase activity has been detected. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
Pssm-ID: 130246 [Multi-domain] Cd Length: 552 Bit Score: 59.79 E-value: 1.97e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949839140 4 DYVFKNATVIDGSGKSEFVSDIAVKDEWIIKISKNiseDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:TIGR01178 1 DIVIKNAKIIDVYNGEIIPGDIAIANGHIAGVGKY---NGVKVIDALGEYAVPGFIDAHIH 58
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1-64 |
3.17e-09 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 58.78 E-value: 3.17e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949839140 1 MKYDYVFKNATVI--DGSGksefVSDIAVKDEWIIKISKNISEDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:PRK09060 3 QTFDLILKGGTVVnpDGEG----RADIGIRDGRIAAIGDLSGASAGEVIDCRGLHVLPGVIDSQVH 64
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
3-67 |
3.50e-09 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 58.64 E-value: 3.50e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949839140 3 YDYVFKNATVIDGSGksEFVSDIAVKDEWIIKISKNiseDAEKIIDCSGLILSPGFIDVHTHDDL 67
Cdd:PRK08323 1 MSTLIKNGTVVTADD--TYKADVLIEDGKIAAIGAN---LGDEVIDATGKYVMPGGIDPHTHMEM 60
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
1-64 |
3.64e-09 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 58.23 E-value: 3.64e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949839140 1 MKYDYVFKNATVIDGSGKSEFVSDIAVKDEWIIKISKNISEDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:PRK12394 1 MKNDILITNGHIIDPARNINEINNLRIINDIIVDADKYPVASETRIIHADGCIVTPGLIDYHAH 64
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1-64 |
3.87e-09 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 58.56 E-value: 3.87e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949839140 1 MKYDYVFKNATVIDGSGKSEfvSDIAVKDEWIIKISKNISEDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:PRK06189 1 MMYDLIIRGGKVVTPEGVYR--ADIGIKNGKIAEIAPEISSPAREIIDADGLYVFPGMIDVHVH 62
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
24-432 |
8.60e-09 |
|
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: 57.45 E-value: 8.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 24 DIAVKDEWIIKISKNISEDAEKIIDCSGLILSPGFIDVHTH-DDLividKPEYIEKTSQGVTTIIVGncGISAAcATLKD 102
Cdd:TIGR00857 7 DILVEGGRIKKIGKLRIPPDAEVIDAKGLLVLPGFIDLHVHlRDP----GEEYKEDIESGSKAAAHG--GFTTV-ADMPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 103 EVPDPINllgelsefqfADLASYKQKINNVKPTVNVATLIGhttlrnncVTDLLKPATPDNIAHMKQVLACAL------- 175
Cdd:TIGR00857 80 TKPPIDT----------PETLEWKLQRLKKVSLVDVHLYGG--------VTQGNQGKELTEAYELKEAGAVGRmftddgs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 176 -DEGALGLSTGLSYGNAINSSTEEICELAELLAEHQGIYTTHMRTEYDGIIDAMHEAFHI------GRHAKVPVQISHHK 248
Cdd:TIGR00857 142 eVQDILSMRRALEYAAIAGVPIALHAEDPDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVarllelAKHAGCPVHICHIS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 249 cagaknwgrTKETLALIEKY-QVMQDINCDCYPYRAGSSNLDItqvtEDYDILVTWSTPFPEVagktlKEIAAMWSSdif 327
Cdd:TIGR00857 222 ---------TKESLELIVKAkSQGIKITAEVTPHHLLLSEEDV----ARLDGNGKVNPPLREK-----EDRLALIEG--- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 328 qVAEKIVPAGAIYFQMH--EDDVRRVLQHPSsmvgsdGLPRDPNPHPRLWGTFprvishysrDEQLFPMTTAIYKMTGMS 405
Cdd:TIGR00857 281 -LKDGIIDIIATDHAPHtlEEKTKEFAAAPP------GIPGLETALPLLLQLL---------VKGLISLKDLIRMLSINP 344
|
410 420
....*....|....*....|....*..
gi 1949839140 406 AQRFSLKDRGLIQENYFADIVVFDPEK 432
Cdd:TIGR00857 345 ARIFGLPDKGTLEEGNPADITVFDLKK 371
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
6-64 |
1.10e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 57.03 E-value: 1.10e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949839140 6 VFKNATVIDGSGkseFVSD--IAVKDEWIIKISKNISEDAEkIIDCSGLILSPGFIDVHTH 64
Cdd:COG1820 1 AITNARIFTGDG---VLEDgaLLIEDGRIAAIGPGAEPDAE-VIDLGGGYLAPGFIDLHVH 57
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
4-110 |
3.93e-08 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 55.48 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 4 DYVFKNATVID---GSGKSefvsDIAVKDEWIIKISK--------NISED-----AEKIIDCSGLILSPGFIDVHTHddl 67
Cdd:PRK13308 69 DFVLCNVTVIDpvlGIVKG----DIGIRDGRIVGIGKagnpdimdGVDPRlvvgpGTDVRPAEGLIATPGAIDVHVH--- 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1949839140 68 ivIDKPEYIEKT-SQGVTTIIVGNCGISAACATlkdevPDPINL 110
Cdd:PRK13308 142 --FDSAQLVDHAlASGITTMLGGGLGPTVGIDS-----GGPFNT 178
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
6-70 |
2.17e-07 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 52.88 E-value: 2.17e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949839140 6 VFKNATVIDGSGKSEFVSDIAVKDEWIIKISKNISEDAEKIIDCSGLILSPGFIDVHTHDDLIVI 70
Cdd:PRK08393 4 LIKNGYVIYGENLKVIRADVLIEGNKIVEVKRNINKPADTVIDASGSVVSPGFINAHTHSPMVLL 68
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
5-64 |
2.22e-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: 52.97 E-value: 2.22e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949839140 5 YVFKNATVIDGSGksEFVSDIAVKDEWIIKISKNISEDA-EKIIDCSGLILSPGFIDVHTH 64
Cdd:cd00854 1 LIIKNARILTPGG--LEDGAVLVEDGKIVAIGPEDELEEaDEIIDLKGQYLVPGFIDIHIH 59
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
4-64 |
3.13e-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: 52.52 E-value: 3.13e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949839140 4 DYVFKNATVIDGSGKSEFVSD--IAVKDEWIIKISKNIS----EDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:COG0402 1 DLLIRGAWVLTMDPAGGVLEDgaVLVEDGRIAAVGPGAElparYPAAEVIDAGGKLVLPGLVNTHTH 67
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
389-475 |
4.07e-07 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 52.18 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 389 EQLFPMTTAIYKMTGMSAQRFSLKDRGLIQENYFADIVVFDPEKinetaTFQDPKQKA---------DG------IEYVF 453
Cdd:PRK09236 345 EGKLSLEKVVEKTSHAPAILFDIKERGFIREGYWADLVLVDLNS-----PWTVTKENIlykcgwspfEGrtfrsrVATTF 419
|
90 100
....*....|....*....|..
gi 1949839140 454 VNGVLTYTKKEMTGNRAGKFLE 475
Cdd:PRK09236 420 VNGQLVYHNGQLVESCRGQRLE 441
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
6-87 |
4.13e-07 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 51.96 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 6 VFKNATVIDGSGKSEFVSDIAVKDEWIIKISKNI-----SEDAEkIIDCSGLILSPGFIDVHTHddlivIDKP-----EY 75
Cdd:PRK09059 6 LLANARIIDPSRGLDEIGTVLIEDGVIVAAGKGAgnqgaPEGAE-IVDCAGKAVAPGLVDARVF-----VGEPgaehrET 79
|
90
....*....|....*..
gi 1949839140 76 IEKTSQ-----GVTTII 87
Cdd:PRK09059 80 IASASRaaaagGVTSII 96
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
8-64 |
7.51e-07 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 51.41 E-value: 7.51e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1949839140 8 KNATVIDgSGKsEFVSDIAVKDEWIIKISKNIS-EDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:PRK09236 7 KNARIVN-EGK-IFEGDVLIENGRIAKIASSISaKSADTVIDAAGRYLLPGMIDDQVH 62
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
4-66 |
7.61e-07 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 51.17 E-value: 7.61e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949839140 4 DYVFKNATVIDGSGKSefvsDIAVKDEWIIKISKNISEDAEKIIDCSGLILSPGFIDVHTHDD 66
Cdd:PRK07572 3 DLIVRNANLPDGRTGI----DIGIAGGRIAAVEPGLQAEAAEEIDAAGRLVSPPFVDPHFHMD 61
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
1-73 |
1.18e-06 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 50.85 E-value: 1.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949839140 1 MKYDYVFKNATVIDGSGKseFVSDIAVKDEWIIKISKNISEdAEKIIDCSGLILSPGFIDVHTHddlivIDKP 73
Cdd:PRK13404 2 MAFDLVIRGGTVVTATDT--FQADIGIRGGRIAALGEGLGP-GAREIDATGRLVLPGGVDSHCH-----IDQP 66
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
7-87 |
2.00e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 50.04 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 7 FKNATVIDG---SGKSEFVSDIAVKDEWIIKISKNIS-EDAEKIIDCSGLILSPGFIDVHTHddlivIDKPEYIEKT--- 79
Cdd:PRK02382 1 MRDALLKDGrvyYNNSLQPRDVRIDGGKITAVGKDLDgSSSEEVIDARGMLLLPGGIDVHVH-----FREPGYTHKEtwy 75
|
90
....*....|....*
gi 1949839140 80 --SQ-----GVTTII 87
Cdd:PRK02382 76 tgSRsaaagGVTTVV 90
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
4-64 |
2.53e-06 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 49.80 E-value: 2.53e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949839140 4 DYVFKNATVIDGSGKSEFVSDIAVKDEWIIK------ISKNISEDAEkIIDCSGLILSPGFIDVHTH 64
Cdd:COG1574 9 DLLLTNGRIYTMDPAQPVAEAVAVRDGRIVAvgsdaeVRALAGPATE-VIDLGGKTVLPGFIDAHVH 74
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
5-64 |
5.90e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 48.46 E-value: 5.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949839140 5 YVFKNATVIDGSGKSEFV--SDIAVKDEWIIKISKNISEDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:PRK08204 4 TLIRGGTVLTMDPAIGDLprGDILIEGDRIAAVAPSIEAPDAEVVDARGMIVMPGLVDTHRH 65
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
24-92 |
8.47e-06 |
|
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: 47.71 E-value: 8.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949839140 24 DIAVKDEWIIKISKNI-SEDAEKIIDCSGLILSPGFIDVHTH----DDLIVIDKPEYIEKTsqGVTTII-VGNCG 92
Cdd:cd01307 1 DVAIENGKIAAVGAALaAPAATQIVDAGGCYVSPGWIDLHVHvyqgGTRYGDRPDMIGVKS--GVTTVVdAGSAG 73
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
8-64 |
2.47e-05 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 46.43 E-value: 2.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949839140 8 KNATVIDGSGKSEFV-SDIAVKDEWIIKISKNI---SEDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:cd01298 4 RNGTIVTTDPRRVLEdGDVLVEDGRIVAVGPALplpAYPADEVIDAKGKVVMPGLVNTHTH 64
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
25-64 |
4.17e-05 |
|
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: 45.71 E-value: 4.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1949839140 25 IAVKDEWIIKIS-----KNISEDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:cd01296 1 IAIRDGRIAAVGpaaslPAPGPAAAEEIDAGGRAVTPGLVDCHTH 45
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
4-92 |
4.23e-05 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 45.94 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 4 DYVFKNATVIDGSG--KSefvsDIAVKDEWIIKISK----NISEDAEKIIDCS-------GLILSPGFIDVHTHddLIVi 70
Cdd:PRK13207 68 DTVITNALILDHWGivKA----DIGIKDGRIVAIGKagnpDIQDGVDIIIGPGteviageGLIVTAGGIDTHIH--FIC- 140
|
90 100
....*....|....*....|...
gi 1949839140 71 dkPEYIEKT-SQGVTTIIVGNCG 92
Cdd:PRK13207 141 --PQQIEEAlASGVTTMIGGGTG 161
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
25-212 |
4.67e-05 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 45.46 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 25 IAVKDEWIIKISKNIseDAEKIIDCSGLILSPGFID--VHTHDDLIVIDKPEYIEKTSQ--GVTTIIvgncgisaacatL 100
Cdd:PRK08417 1 IRIKDGKITEIGSDL--KGEEILDAKGKTLLPALVDlnVSLKNDSLSSKNLKSLENECLkgGVGSIV------------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 101 KDEVPDPINLLGELSEFQFADLASYKQK---INNVKPT---VNVATLIGH--------TTLRNNCVTDLLkpatpdNIAH 166
Cdd:PRK08417 67 YPDSTPAIDNEIALELINSAQRELPMQIfpsIRALDEDgklSNIATLLKKgakalelsSDLDANLLKVIA------QYAK 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1949839140 167 MKQV---LAC---------ALDEGALGLSTGLSYGNAInSSTEEICELAElLAEHQGI 212
Cdd:PRK08417 141 MLDVpifCRCedssfddsgVMNDGELSFELGLPGIPSI-AETKEVAKMKE-LAKFYKN 196
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
4-64 |
9.61e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 44.74 E-value: 9.61e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949839140 4 DYVFKNATVIDGSGKSEFVSDIAVKDEWIIKISKNISEDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:PRK06038 3 DIIIKNAYVLTMDAGDLKKGSVVIEDGTITEVSESTPGDADTVIDAKGSVVMPGLVNTHTH 63
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
8-64 |
1.79e-04 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 43.94 E-value: 1.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1949839140 8 KNATVID-GSGKSEFVSDIAVKDEWIIKISKNISEDaeKIIDCSGLILSPGFIDVHTH 64
Cdd:cd01304 2 KNGTVYDpLNGINGEKMDIFIRDGKIVESSSGAKPA--KVIDASGKVVMAGGVDMHSH 57
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
7-72 |
2.43e-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: 43.39 E-value: 2.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949839140 7 FKNATVIDGSGKSEfvsDIAVKDEWIIKISKNIS-EDAEKIIDCSGLILSPGFIDVHTHddlivIDK 72
Cdd:cd01293 2 LRNARLADGGTALV---DIAIEDGRIAAIGPALAvPPDAEEVDAKGRLVLPAFVDPHIH-----LDK 60
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
4-67 |
2.71e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 43.24 E-value: 2.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949839140 4 DYVFKNATVIDGSGksEFVSDIAVKDEWIIKISKNISeDAEKIIDCSGLILSPGFIDVHThDDL 67
Cdd:PRK15446 3 EMILSNARLVLPDE--VVDGSLLIEDGRIAAIDPGAS-ALPGAIDAEGDYLLPGLVDLHT-DNL 62
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
32-64 |
3.04e-04 |
|
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: 43.07 E-value: 3.04e-04
10 20 30
....*....|....*....|....*....|....*
gi 1949839140 32 IIKISKNIS--EDAEkIIDCSGLILSPGFIDVHTH 64
Cdd:cd01309 4 IVAVGAEITtpADAE-VIDAKGKHVTPGLIDAHSH 37
|
|
| PLN02303 |
PLN02303 |
urease |
4-99 |
3.95e-04 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 43.20 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 4 DYVFKNATVIDGSGKseFVSDIAVKDEWIIKISKNISEDA-------------EKIIDCSGLILSPGFIDVHTHddlivi 70
Cdd:PLN02303 335 DTVITNAVIIDYTGI--YKADIGIKDGLIVGIGKAGNPDVmdgvtsnmivgvnTEVIAGEGMIVTAGGIDCHVH------ 406
|
90 100 110
....*....|....*....|....*....|....*.
gi 1949839140 71 dkpeYI------EKTSQGVTTIIVGNCG-ISAACAT 99
Cdd:PLN02303 407 ----FIcpqlatEAIASGITTLVGGGTGpAHGTCAT 438
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
4-99 |
5.11e-04 |
|
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: 42.70 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 4 DYVFKNATVIDGSGKseFVSDIAVKDEWIIKISK--------NISED-----AEKIIDCSGLILSPGFIDVHTHddLIVi 70
Cdd:cd00375 66 DLVITNALIIDYTGI--YKADIGIKDGRIVAIGKagnpdimdGVTPNmivgpSTEVIAGEGKIVTAGGIDTHVH--FIC- 140
|
90 100 110
....*....|....*....|....*....|.
gi 1949839140 71 dkPEYIEKT-SQGVTTIIVGNCGISA-ACAT 99
Cdd:cd00375 141 --PQQIEEAlASGITTMIGGGTGPAAgTKAT 169
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
406-466 |
6.51e-04 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 42.01 E-value: 6.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949839140 406 AQRFSLKDRGLIQENYFADIVVF-DPEKINetatfqdpkqkadgIEYVFVNGVLTYTKKEMT 466
Cdd:COG1001 298 AEHFGLKDLGAIAPGRRADIVLLdDLEDFK--------------VEKVYADGKLVAEDGKLL 345
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
43-64 |
6.89e-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: 41.84 E-value: 6.89e-04
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
8-64 |
6.95e-04 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 41.79 E-value: 6.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1949839140 8 KNATVIDGSGKSEFVSDIAVKDEWIIKISKNISEDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:PRK06380 6 KNAWIVTQNEKREILQGNVYIEGNKIVYVGDVNEEADYIIDATGKVVMPGLINTHAH 62
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
384-466 |
8.76e-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: 41.42 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 384 HYSRDEQLFPMTTAIYKMTGMSAQRFSLKDRGLIQENYFADIVVFDPEKINETATFQDPKQ-----KADGIEYVFVNGVL 458
Cdd:cd01298 324 LAHGDPTALPAEEALEMATIGGAKALGLDEIGSLEVGKKADLILIDLDGPHLLPVHDPISHlvysaNGGDVDTVIVNGRV 403
|
....*...
gi 1949839140 459 TYTKKEMT 466
Cdd:cd01298 404 VMEDGELL 411
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
31-64 |
8.80e-04 |
|
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273512 [Multi-domain] Cd Length: 377 Bit Score: 41.63 E-value: 8.80e-04
10 20 30
....*....|....*....|....*....|....
gi 1949839140 31 WIIKISKNISEDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:TIGR01224 15 WIGQLAALPGEEATEIIDCGGGLVTPGLVDPHTH 48
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
8-71 |
9.95e-04 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 41.52 E-value: 9.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949839140 8 KNATVIDGSGKSEFV-SDIAVKDEWIIKISKNIS-EDAEKIIDCSGLILSPGFIDVHTH----------DDLIVID 71
Cdd:PRK07228 6 KNAGIVTMNAKREIVdGDVLIEDDRIAAVGDRLDlEDYDDHIDATGKVVIPGLIQGHIHlcqtlfrgiaDDLELLD 81
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
4-66 |
1.10e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 41.07 E-value: 1.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949839140 4 DYVFKNATVIDGSGKsefvsDIAVKDEWIIKISKNIS-EDAEKIIDCSGLILSPGFIDVHTHDD 66
Cdd:PRK05985 3 DLLFRNVRPAGGAAV-----DILIRDGRIAAIGPALAaPPGAEVEDGGGALALPGLVDGHIHLD 61
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
24-64 |
1.33e-03 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 40.84 E-value: 1.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1949839140 24 DIAVKDEWIIKISKNISED---AEKIIDCSGLILSPGFIDVHTH 64
Cdd:cd01308 19 DILIAGGKILAIEDQLNLPgyeNVTVVDLHGKILVPGFIDQHVH 62
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
6-64 |
2.54e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 39.97 E-value: 2.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949839140 6 VFKNATVIDGSGKSEFVSDIAVKDEWIIKISK---NISEDAEkIIDCSGLILSPGFIDVHTH 64
Cdd:PRK07369 5 LLQQVRVLDPVSNTDRIADVLIEDGKIQAIEPhidPIPPDTQ-IIDASGLILGPGLVDLYSH 65
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
4-87 |
2.69e-03 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 40.20 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 4 DYVFKNATVIDGSGKSEFVSDIAVKDEWIIKISKNIS-EDAEKIIDCSGLILSPGFIDVHTHDDLIVIDKPEYiEKTS-- 80
Cdd:PRK10027 31 DYIIDNVSILDLINGGEISGPIVIKGRYIAGVGAEYAdAPALQRIDARGATAVPGFIDAHLHIESSMMTPVTF-ETATlp 109
|
....*..
gi 1949839140 81 QGVTTII 87
Cdd:PRK10027 110 RGLTTVI 116
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
24-64 |
3.76e-03 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 39.60 E-value: 3.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1949839140 24 DIAVKDEWIIKIS-----KNISEDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:cd01300 1 AVAVRDGRIVAVGsdaeaKALKGPATEVIDLKGKTVLPGFIDSHSH 46
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
4-92 |
6.47e-03 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 39.11 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949839140 4 DYVFKNATVIDGSGKseFVSDIAVKDEWIIKISKNISED-------------AEKIIDCSGLILSPGFIDVHTHddliVI 70
Cdd:PRK13985 66 DLIITNALIIDYTGI--YKADIGIKDGKIAGIGKGGNKDmqdgvknnlsvgpATEALAGEGLIVTAGGIDTHIH----FI 139
|
90 100
....*....|....*....|..
gi 1949839140 71 DKPEYIEKTSQGVTTIIVGNCG 92
Cdd:PRK13985 140 SPQQIPTAFASGVTTMIGGGTG 161
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
8-64 |
7.96e-03 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 38.67 E-value: 7.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1949839140 8 KNATVIDGSgkSEFVSDIAVKDEWIIKISKNIS-EDAEKIIDCSGLILSPGFIDVHTH 64
Cdd:PLN02942 10 KGGTVVNAH--HQELADVYVEDGIIVAVAPNLKvPDDVRVIDATGKFVMPGGIDPHTH 65
|
|
| |
