|
Name |
Accession |
Description |
Interval |
E-value |
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
29-405 |
0e+00 |
|
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: 515.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 29 DGAIAVRDGKIVWIGEHAALPPgLIADETVKFDGGIVTPGFVDCHTHLVFGGNRSGEFEQRLNGVSYADIAAQGGGIIST 108
Cdd:TIGR01224 3 DAVILIHGGKIVWIGQLAALPG-EEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGGGILST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 109 VKATREADEALLLEQALFRLRPLLAEGVTCVEIKSGYGLSPESELKMLRVARKLGELLPVEVKTTCLAAHALPPEYANRA 188
Cdd:TIGR01224 82 VRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPEFQGRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 189 DDYINLVCDTIIPQAAAAGLADAVDAFCEHLAFSPAQVERVFAAAEAAGLPVKLHAEQLSALGGSTLAARHHALSADHLE 268
Cdd:TIGR01224 162 DDYVDGICEELIPQVAEEGLASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAKLGAVSADHLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 269 YATEQDARAMGDAGTVAVLLPGAYYLLREtQCPPVALFRKHHVAMAIASDANPGTSPALSLRLMINMACTLFRLTPEEAL 348
Cdd:TIGR01224 242 HASDAGIKALAEAGTVAVLLPGTTFYLRE-TYPPARQLIDYGVPVALATDLNPGSSPTLSMQLIMSLACRLMKMTPEEAL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 515494776 349 AGVTTHAAKALGLQHSHGTLETGKVADFVHWPLSRPAELAYWLGGQLPCTVIFRGEV 405
Cdd:TIGR01224 321 HAATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPYHYGVNHVHAVIKNGNI 377
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
32-403 |
1.75e-161 |
|
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: 458.65 E-value: 1.75e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 32 IAVRDGKIVWIGEHAALPPGLIA-DETVKFDGGIVTPGFVDCHTHLVFGGNRSGEFEQRLNGVSYADIAAQGGGIISTVK 110
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPAPGPAaAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILSTVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 111 ATREADEALLLEQALFRLRPLLAEGVTCVEIKSGYGLSPESELKMLRVARKLGELLPVEVKTTCLAAHALPPEYANRaDD 190
Cdd:cd01296 81 ATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGR-EE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 191 YINLVCDTIIPQAAAAGLADAVDAFCEHLAFSPAQVERVFAAAEAAGLPVKLHAEQLSALGGSTLAARHHALSADHLEYA 270
Cdd:cd01296 160 YIDLVIEEVLPAVAEENLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSADHLEHT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 271 TEQDARAMGDAGTVAVLLPGAYYLLRETQcPPVALFRKHHVAMAIASDANPGTSPALSLRLMINMACTLFRLTPEEALAG 350
Cdd:cd01296 240 SDEGIAALAEAGTVAVLLPGTAFSLRETY-PPARKLIDAGVPVALGTDFNPGSSPTSSMPLVMHLACRLMRMTPEEALTA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 515494776 351 VTTHAAKALGLQHSHGTLETGKVADFVHWPLSRPAELAYWLGGQLPCTVIFRG 403
Cdd:cd01296 319 ATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNLVEYVIKNG 371
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
10-405 |
6.78e-77 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 243.33 E-value: 6.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 10 LWHGADIVTMRDGKyhTLTDGAIAVRDGKIVWIGEHAAL--PPGliaDETVKFDGGIVTPGFVDCHTHLVFGGNRSGEFE 87
Cdd:COG1228 11 LITNATLVDGTGGG--VIENGTVLVEDGKIAAVGPAADLavPAG---AEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 88 QrlngvsyadiaaqGGGIISTVKATREADEallleqalfRLRPLLAEGVTCVEIKSGYGLS-----PESELKMLRVARKL 162
Cdd:COG1228 86 A-------------GGGITPTVDLVNPADK---------RLRRALAAGVTTVRDLPGGPLGlrdaiIAGESKLLPGPRVL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 163 GELLPVevkTTCLAAHALPPE---------YANRADdYINLVCDTIIPQaaaagladavdafcehlaFSPAQVERVFAAA 233
Cdd:COG1228 144 AAGPAL---SLTGGAHARGPEearaalrelLAEGAD-YIKVFAEGGAPD------------------FSLEELRAILEAA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 234 EAAGLPVKLHAEQLSalgGSTLAARHHALSADHLEYATEQDARAMGDAGTVaVLLPGAYYLL-----------------R 296
Cdd:COG1228 202 HALGLPVAAHAHQAD---DIRLAVEAGVDSIEHGTYLDDEVADLLAEAGTV-VLVPTLSLFLallegaaapvaakarkvR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 297 ETQCPPVALFRKHHVAMAIASDANPGTSPALSLRLMINMACtLFRLTPEEALAGVTTHAAKALGLQHSHGTLETGKVADF 376
Cdd:COG1228 278 EAALANARRLHDAGVPVALGTDAGVGVPPGRSLHRELALAV-EAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADL 356
|
410 420
....*....|....*....|....*....
gi 515494776 377 VHWPLSRPAELAYWlggQLPCTVIFRGEV 405
Cdd:COG1228 357 VLLDGDPLEDIAYL---EDVRAVMKDGRV 382
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
8-406 |
1.45e-35 |
|
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: 134.95 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 8 DSLWHGADIVTMrDGKYHTLTDGAIAVRDGKIVWIGEHAALPPGLIADETVKFDGGIVTPGFVDCHTHLVFGGNRS---- 83
Cdd:COG0402 1 DLLIRGAWVLTM-DPAGGVLEDGAVLVEDGRIAAVGPGAELPARYPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGladd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 84 GEFEQRLNGVSYadiaaqgggiistvKATREADEALLLEQALFRLRPLLAEGVTCV-EIksgYGLSPESELKMLRVARKL 162
Cdd:COG0402 80 LPLLDWLEEYIW--------------PLEARLDPEDVYAGALLALAEMLRSGTTTVaDF---YYVHPESADALAEAAAEA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 163 G---ELLPVevkttcLAAHALPPEYANRADDYINLvCDTIIPQAAAAGLADAVDAFCEHLAF--SPAQVERVFAAAEAAG 237
Cdd:COG0402 143 GiraVLGRG------LMDRGFPDGLREDADEGLAD-SERLIERWHGAADGRIRVALAPHAPYtvSPELLRAAAALARELG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 238 LPVKLH-AEQ-------LSALGGSTLA--ARHHALSAD----HLEYATEQDARAMGDAGTVAVLLPGAYYLLRETqCPPV 303
Cdd:COG0402 216 LPLHTHlAETrdevewvLELYGKRPVEylDELGLLGPRtllaHCVHLTDEEIALLAETGASVAHCPTSNLKLGSG-IAPV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 304 ALFRKHHVAMAIASDaNPGTSPALSLRLMINMACTLFR--------LTPEEALAGVTTHAAKALGLQHSHGTLETGKVAD 375
Cdd:COG0402 295 PRLLAAGVRVGLGTD-GAASNNSLDMFEEMRLAALLQRlrggdptaLSAREALEMATLGGARALGLDDEIGSLEPGKRAD 373
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 515494776 376 FVHWPLSRP---------AELAYWLGGQLPCTVIFRGEVR 406
Cdd:COG0402 374 LVVLDLDAPhlaplhdplSALVYAADGRDVRTVWVAGRVV 413
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
31-377 |
2.77e-19 |
|
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: 89.29 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 31 AIAVRDGKIVWIG-EHAALPPGLIADETVKFDGGIVTPGFVDCHTHLVFGG------NRSG------------------E 85
Cdd:cd01300 1 AVAVRDGRIVAVGsDAEAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGlsllwlDLSGvtskeealariredaaaaP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 86 FEQRLNGVSY------------------------------------------------ADIAAQGGGII---STVKAT-- 112
Cdd:cd01300 81 PGEWILGFGWdesllgegryptraeldavspdrpvlllrrdghsawvnsaalrlagitRDTPDPPGGEIvrdADGEPTgv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 113 -READEALLLEQALFR------------LRPLLAEGVTCVeikSGYGLSPESELKMLRVARKLGEL-LPVEV-----KTT 173
Cdd:cd01300 161 lVEAAAALVLEAVPPPtpeerraalraaARELASLGVTTV---HDAGGGAADDIEAYRRLAAAGELtLRVRValyvsPLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 174 CLAAHALPPEYANRADDYINLVCDTII----PQA---AAAGLADAVDAFCEHLAFSPAQVERVFAAAEAAGLPVKLHA-- 244
Cdd:cd01300 238 EDLLEELGARKNGAGDDRLRLGGVKLFadgsLGSrtaALSEPYLDSPGTGGLLLISPEELEELVRAADEAGLQVAIHAig 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 245 -----------EQLSALGGstlaARHHALSADHLEYATEQDARAMGDAGTVAVLLPG-AYYLL-----------RETQCP 301
Cdd:cd01300 318 dravdtvldalEAALKDNP----RADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNhLYSDGdaaedrrlgeeRAKRSY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 302 PVALFRKHHVAMAIASDANPGT-SPALSLRLMIN--------MACTLFRLTPEEALAGVTTHAAKALGLQHSHGTLETGK 372
Cdd:cd01300 394 PFRSLLDAGVPVALGSDAPVAPpDPLLGIWAAVTrktpgggvLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGK 473
|
....*
gi 515494776 373 VADFV 377
Cdd:cd01300 474 LADFV 478
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
1-394 |
9.89e-19 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 87.93 E-value: 9.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 1 MT-SEIHCDSLWHGADIVTMRDGkyhTLTDGAIAVRDGKIVWIGEHAALPPgLIADETVKFD--GGIVTPGFVDCHTHLV 77
Cdd:COG1574 1 MKlAAAAADLLLTNGRIYTMDPA---QPVAEAVAVRDGRIVAVGSDAEVRA-LAGPATEVIDlgGKTVLPGFIDAHVHLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 78 FGGNRSGEFeqRLNGV-SYADIAA---------------QGGG--------------------------IISTV------ 109
Cdd:COG1574 77 GGGLALLGV--DLSGArSLDELLArlraaaaelppgewiLGRGwdeslwpegrfptradldavspdrpvVLTRVdghaaw 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 110 ---KATREA----------------DEA-----LLLEQALFRLRP--------------------LLAEGVTCVeiksGY 145
Cdd:COG1574 155 vnsAALELAgitadtpdpeggeierDADgeptgVLREAAMDLVRAaippptpeelraalraalreLASLGITSV----HD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 146 GLSPESELKMLRVARKLGELlPVEVkttCLAAHALPPE---------YANRADDYIN-----LVCDTIIPQAAAAGLA-- 209
Cdd:COG1574 231 AGLGPDDLAAYRELAAAGEL-PLRV---VLYLGADDEDleellalglRTGYGDDRLRvggvkLFADGSLGSRTAALLEpy 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 210 DAVDAFCEHLAFSPAQVERVFAAAEAAGLPVKLHA-------------EQLSALGGstLAARHHALSadHLEYATEQDAR 276
Cdd:COG1574 307 ADDPGNRGLLLLDPEELRELVRAADAAGLQVAVHAigdaavdevldayEAARAANG--RRDRRHRIE--HAQLVDPDDLA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 277 AMGDAGTVAVLLPG-AYYLL----------RETQCPPVALFRKHHVAMAIASDAnpgtsPALSLRLMINMACTLFR---- 341
Cdd:COG1574 383 RFAELGVIASMQPThATSDGdwaedrlgpeRAARAYPFRSLLDAGAPLAFGSDA-----PVEPLDPLLGIYAAVTRrtps 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515494776 342 ---------LTPEEALAGVTTHAAKALGLQHSHGTLETGKVADFVHW---PLSRPAE-------LAYWLGGQ 394
Cdd:COG1574 458 grglgpeerLTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLdrdPLTVPPEeikdikvLLTVVGGR 529
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
32-405 |
1.05e-14 |
|
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: 74.98 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 32 IAVRDGKIVWIGEHAALPPGliaDETVKFDGGIVTPGFVDCHTHL--VFGGNRSGEFeqrlngvsyaDIAAQGGGIISTV 109
Cdd:cd01293 17 IAIEDGRIAAIGPALAVPPD---AEEVDAKGRLVLPAFVDPHIHLdkTFTGGRWPNN----------SGGTLLEAIIAWE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 110 KATREADEALLLEQALFRLRPLLAEGVTcvEIKSGYGLSPESELK----MLRVARKLGELLPVEVKttclaahALPPEYA 185
Cdd:cd01293 84 ERKLLLTAEDVKERAERALELAIAHGTT--AIRTHVDVDPAAGLKaleaLLELREEWADLIDLQIV-------AFPQHGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 186 NR-------ADDYINLVCDTI--IPqaaaagladavdaFCEHLAFSPAQVERVFAAAEAAGLPVKLH------------- 243
Cdd:cd01293 155 LStpggeelMREALKMGADVVggIP-------------PAEIDEDGEESLDTLFELAQEHGLDIDLHldetddpgsrtle 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 244 --AEQLSALGGSTLAARHHALSADHL-EYATEQDARAMGDAG-TVAVLLPGAYYLL-RETQCP------PVALFRKHHVA 312
Cdd:cd01293 222 elAEEAERRGMQGRVTCSHATALGSLpEAEVSRLADLLAEAGiSVVSLPPINLYLQgREDTTPkrrgvtPVKELRAAGVN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 313 MAIASDA-----NPGTSPALsLRLMiNMACTLFRLTPEE----ALAGVTTHAAKALGLQhsHGTLETGKVADFVHWPLSR 383
Cdd:cd01293 302 VALGSDNvrdpwYPFGSGDM-LEVA-NLAAHIAQLGTPEdlalALDLITGNAARALGLE--DYGIKVGCPADLVLLDAED 377
|
410 420
....*....|....*....|...
gi 515494776 384 PAElayWLGGQLPCTVIFR-GEV 405
Cdd:cd01293 378 VAE---AVARQPPRRVVIRkGRV 397
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
37-400 |
2.36e-14 |
|
Metallo-dependent hydrolases, subgroup D 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: 238637 [Multi-domain] Cd Length: 381 Bit Score: 74.02 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 37 GKIVWIGEHAALP---PGLIADetvKFDGGIVTPGFVDCHTHLVFGGNRS----GEFEQRLNGV--SYADIAAQ------ 101
Cdd:cd01312 1 DKILEVGDYEKLEkryPGAKHE---FFPNGVLLPGLINAHTHLEFSANVAqftyGRFRAWLLSVinSRDELLKQpweeai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 102 ----------GGGIISTVKATREADEAL---------LLE-------QALFRLRPLLAEGVTCVEIKSG----------- 144
Cdd:cd01312 78 rqgirqmlesGTTSIGAISSDGSLLPALassglrgvfFNEvigsnpsAIDFKGETFLERFKRSKSFESQlfipaisphap 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 145 YGLSPESELKMLRVARKLGELLpvevkTTCLAAHALPPEYANRADDYINlvcdtiipqaaaagladavdAFCEHlaFSPA 224
Cdd:cd01312 158 YSVHPELAQDLIDLAKKLNLPL-----STHFLESKEEREWLEESKGWFK--------------------HFWES--FLKL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 225 QVERVFAAAEAaglpvklHAEQLSALGGSTLAArhhalsadHLEYATEQDARAMGDAGTVAVLLPGAYYLLrETQCPPVA 304
Cdd:cd01312 211 PKPKKLATAID-------FLDMLGGLGTRVSFV--------HCVYANLEEAEILASRGASIALCPRSNRLL-NGGKLDVS 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 305 LFRKHHVAMAIASDanpGTSPALSLRLMINMACTLF-------RLTPEEALAGVTTHAAKALGLqhSHGTLETGKVADFV 377
Cdd:cd01312 275 ELKKAGIPVSLGTD---GLSSNISLSLLDELRALLDlhpeedlLELASELLLMATLGGARALGL--NNGEIEAGKRADFA 349
|
410 420
....*....|....*....|....*....
gi 515494776 378 HWPLSRP-----AELAYWLG-GQLPCTVI 400
Cdd:cd01312 350 VFELPGPgikeqAPLQFILHaKEVRHLFI 378
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
69-358 |
2.47e-14 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 72.75 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 69 FVDCHTHLVFGGNRSGEFEQRLNGVSYADIAAqgggiistvkatreadealLLEQALFRLRPLLAEGVTCVEIKSGYGLS 148
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEELSPED-------------------LYEDTLRALEALLAGGVTTVVDMGSTPPP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 149 PESELKMLRVARKLGELLPVEVkttcLAAHALPPEYANRADDYINLVCDTIIPQAAAAGLADAVDAFCEHLAFSPAQVER 228
Cdd:cd01292 62 TTTKAAIEAVAEAARASAGIRV----VLGLGIPGVPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDESLRR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 229 VFAAAEAAGLPVKLHAEQLSALGGSTLAARH-----HALSADHLEYATEQDARAMGDAG-TVAVLLPGAYYLLR-ETQCP 301
Cdd:cd01292 138 VLEEARKLGLPVVIHAGELPDPTRALEDLVAllrlgGRVVIGHVSHLDPELLELLKEAGvSLEVCPLSNYLLGRdGEGAE 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 515494776 302 PVALFRKHHVAMAIASDANPGTSPALSLRLM-INMACTLFRLTPEEALAGVTTHAAKA 358
Cdd:cd01292 218 ALRRLLELGIRVTLGTDGPPHPLGTDLLALLrLLLKVLRLGLSLEEALRLATINPARA 275
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
13-384 |
1.82e-13 |
|
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: 71.46 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 13 GADIVTMRDGKyhTLTDGAIAVRDGKIVWIGEHAALPPGlIADETVKFDGGIVTPGFVDCHTHLVFGGNRS----GEFEQ 88
Cdd:cd01298 5 NGTIVTTDPRR--VLEDGDVLVEDGRIVAVGPALPLPAY-PADEVIDAKGKVVMPGLVNTHTHLAMTLLRGladdLPLME 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 89 RLNGVSYAdiaaqgggiistvkatreadEALLLEQALFRLRPLLAegvtCVE-IKSG-------YGLSPESELKmlrVAR 160
Cdd:cd01298 82 WLKDLIWP--------------------LERLLTEEDVYLGALLA----LAEmIRSGtttfadmYFFYPDAVAE---AAE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 161 KLGellpvevkttcLAAHA------LPPEYANRADDYINLvCDTIIPQAAAAGLADAVDAFCEHLAF--SPAQVERVFAA 232
Cdd:cd01298 135 ELG-----------IRAVLgrgimdLGTEDVEETEEALAE-AERLIREWHGAADGRIRVALAPHAPYtcSDELLREVAEL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 233 AEAAGLPVKLHA----------------------EQLSALGGSTLAArhhalsadHLEYATEQDARAMGDAGTVAVLLPG 290
Cdd:cd01298 203 AREYGVPLHIHLaetedeveeslekygkrpveylEELGLLGPDVVLA--------HCVWLTDEEIELLAETGTGVAHNPA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 291 AYYLLrETQCPPVALFRKHHVAMAIASDanpGTSPALSLRLM--INMACTLFR--------LTPEEALAGVTTHAAKALG 360
Cdd:cd01298 275 SNMKL-ASGIAPVPEMLEAGVNVGLGTD---GAASNNNLDMFeeMRLAALLQKlahgdptaLPAEEALEMATIGGAKALG 350
|
410 420
....*....|....*....|....
gi 515494776 361 LQHShGTLETGKVADFVHWPLSRP 384
Cdd:cd01298 351 LDEI-GSLEVGKKADLILIDLDGP 373
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
64-405 |
1.03e-12 |
|
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: 68.68 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 64 IVTPGFVDCHTHLVFGGNRSgefeQRLNGVSYADIAAQGggiistvkatreadeallleqalfrLRPLLAEGVTCVeIKS 143
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRG----IPVPPEFAYEALRLG-------------------------ITTMLKSGTTTV-LDM 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 144 GYGLSPESELkMLRVARKLGELLPVEVKTTCLAA---HALPPEYANRADDYINLVCDTiipqaaaaGLADAVDAFCEHLA 220
Cdd:pfam01979 51 GATTSTGIEA-LLEAAEELPLGLRFLGPGCSLDTdgeLEGRKALREKLKAGAEFIKGM--------ADGVVFVGLAPHGA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 221 --FSPAQVERVFAAAEAAGLPVKLHAEQLSALGGSTLAA-RHHALSADHLEYATEQDA----RAMGDAG-----TVAVLL 288
Cdd:pfam01979 122 ptFSDDELKAALEEAKKYGLPVAIHALETKGEVEDAIAAfGGGIEHGTHLEVAESGGLldiiKLILAHGvhlspTEANLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 289 PGAYYLLRETQCP-PVALFRKH----------HVAMAIASDANPGTSPALSLRLMINMACTLFR----LTPEEALAGVTT 353
Cdd:pfam01979 202 AEHLKGAGVAHCPfSNSKLRSGrialrkaledGVKVGLGTDGAGSGNSLNMLEELRLALELQFDpeggLSPLEALRMATI 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 515494776 354 HAAKALGLQHSHGTLETGKVADFVHWPLSRPAELAYWLGGQLPCTVIFRGEV 405
Cdd:pfam01979 282 NPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKKVIVKGKI 333
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
24-377 |
8.10e-12 |
|
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 132012 [Multi-domain] Cd Length: 401 Bit Score: 66.12 E-value: 8.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 24 YHTLTDGAIAVRDGKIVWIGEHAALPPGLIADETVK-FDGGIVTPGFVDCHTHlvfggnrsgeFEQrlngvsYADIAAQG 102
Cdd:TIGR02967 1 LEYFEDGLLVVENGRIVAVGDYAELKETLPAGVEIDdYRGHLIMPGFIDTHIH----------YPQ------TEMIASYG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 103 GGII------STVKATREADEALLLEQALFRLRPLLAEGVT--CVeiksgYG-LSPESELKMLRVARKLGELLPveVKTT 173
Cdd:TIGR02967 65 EQLLewlekyTFPTEARFADPDHAEEVAEFFLDELLRNGTTtaLV-----FAtVHPESVDALFEAALKRGMRMI--AGKV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 174 CLAAHAlPPEYANRADDYI-------------NLVCDTIIPQAAaagladavdafcehLAFSPAQVERVFA-AAEAAGLP 239
Cdd:TIGR02967 138 LMDRNA-PDYLRDTAESSYdeskalierwhgkGRLLYAVTPRFA--------------PTSSPEQLAAAGElAKEYPDVY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 240 VKLH-AEQLSAL----------GGSTLAARHHALSAD-----HLEYATEQDARAMGDAGTVAVLLPGAYYLLrETQCPPV 303
Cdd:TIGR02967 203 VQTHlSENKDEIawvkelfpeaKDYLDVYDHYGLLGRrsvfaHCIHLSDEECQRLAETGAAIAHCPTSNLFL-GSGLFNL 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515494776 304 ALFRKHHVAMAIASDANPGTSPALsLRLMIN--MACTL--FRLTPEEALAGVTTHAAKALGLQHSHGTLETGKVADFV 377
Cdd:TIGR02967 282 KKALEHGVRVGLGTDVGGGTSFSM-LQTLREayKVSQLqgARLSPFEAFYLATLGGARALDLDDRIGNFEPGKEADFV 358
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
221-386 |
2.03e-11 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 65.25 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 221 FSPAQVERVFAAAEAAGLPVKLHAEQ----LSALGGSTLAARHHAL----SADH---LEYATEQDARAMGDAGTVAVLLP 289
Cdd:pfam07969 247 FEDEALAELVAAARERGLDVAIHAIGdatiDTALDAFEAVAEKLGNqgrvRIEHaqgVVPYTYSQIERVAALGGAAGVQP 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 290 GAYYLL-----------RETQCPPVALFRKHHVAMAIASDAN-------PGTSPALSLRLMINMACTLF--RLTPEEALA 349
Cdd:pfam07969 327 VFDPLWgdwlqdrlgaeRARGLTPVKELLNAGVKVALGSDAPvgpfdpwPRIGAAVMRQTAGGGEVLGPdeELSLEEALA 406
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515494776 350 GVTTHAAKALGLQHSHGTLETGKVADFVHW---PLSRPAE 386
Cdd:pfam07969 407 LYTSGPAKALGLEDRKGTLGVGKDADLVVLdddPLTVDPP 446
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
36-382 |
1.49e-09 |
|
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: 59.25 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 36 DGKIVWIGEHAALPPGL-IADETVKFdggiVTPGFVDCHTHL-VFGGnrSGEFEQRLNGVSYADIAAQgggiISTVKATR 113
Cdd:cd01309 1 DGKIVAVGAEITTPADAeVIDAKGKH----VTPGLIDAHSHLgLDEE--GGVRETSDANEETDPVTPH----VRAIDGIN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 114 EADEALllEQALfrlrpllAEGVTCVEIKSGYGLS---------------------PESELKM-LRVARKLGELLPVEVK 171
Cdd:cd01309 71 PDDEAF--KRAR-------AGGVTTVQVLPGSANLiggqgvviktdggtiedmfikAPAGLKMaLGENPKRVYGGKGKEP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 172 TTCLAAHALPPEYANRADDYINLVCDTIIPQAaaagladavdafcEHLAFSPaQVERvFAAAEAAGLPVKLHA----EQL 247
Cdd:cd01309 142 ATRMGVAALLRDAFIKAQEYGRKYDLGKNAKK-------------DPPERDL-KLEA-LLPVLKGEIPVRIHAhradDIL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 248 SALG-----GSTLAARHHA---LSADHLeyaTEQDARAmgdaGTVAVL-LPGAYYLLRETQCPPVALFRKHHVAMAIASD 318
Cdd:cd01309 207 TAIRiakefGIKITIEHGAegyKLADEL---AKHGIPV----IYGPTLtLPKKVEEVNDAIDTNAYLLKKGGVAFAISSD 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515494776 319 anpgtSPALSLR-LMINMA-CTLFRLTPEEALAGVTTHAAKALGLQHSHGTLETGKVADFVHW---PLS 382
Cdd:cd01309 280 -----HPVLNIRnLNLEAAkAVKYGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWngdPLE 343
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
62-377 |
1.91e-09 |
|
Metallo-dependent hydrolases, subgroup A 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: 238624 [Multi-domain] Cd Length: 342 Bit Score: 58.84 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 62 GGIVTPGFVDCHTHLVFGGNRSGEfeqrlngvsyadiAAQGGGIISTVKATREADEAL---------LLEQALFRLRPLL 132
Cdd:cd01299 8 GKTLMPGLIDAHTHLGSDPGDLPL-------------DLALPVEYRTIRATRQARAALragfttvrdAGGADYGLLRDAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 133 AEGVtcVE----IKSGYGLS-PESELKMLRVARKLGELLPVEVKTTCLAAHALPPEYANRADDYINLVCD--TIIPQAAA 205
Cdd:cd01299 75 DAGL--IPgprvFASGRALSqTGGHGDPRGLSGLFPAGGLAAVVDGVEEVRAAVREQLRRGADQIKIMATggVLSPGDPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 206 agladavdafcEHLAFSPAQVERVFAAAEAAGLPVKLHAEQLSALggsTLAARHHALSADHLEYATEQDARAMGDAGTVA 285
Cdd:cd01299 153 -----------PDTQFSEEELRAIVDEAHKAGLYVAAHAYGAEAI---RRAIRAGVDTIEHGFLIDDETIELMKEKGIFL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 286 VLLPGAYYLLRETQCPP--------------------VALFRKHHVAMAIASDA-NPGTSPALSLRLMINMACTLfrLTP 344
Cdd:cd01299 219 VPTLATYEALAAEGAAPglpadsaekvalvleagrdaLRRAHKAGVKIAFGTDAgFPVPPHGWNARELELLVKAG--GTP 296
|
330 340 350
....*....|....*....|....*....|...
gi 515494776 345 EEALAGVTTHAAKALGLQHSHGTLETGKVADFV 377
Cdd:cd01299 297 AEALRAATANAAELLGLSDELGVIEAGKLADLL 329
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
24-377 |
6.65e-09 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 57.51 E-value: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 24 YHTLTDGAIAVRDGKIVWIGEHAALPPGLIAD-ETVKFDGGIVTPGFVDCHTHlvfggnrsgeFEQrlngvsyAD-IAAQ 101
Cdd:PRK09228 26 LRYIEDGLLLVEDGRIVAAGPYAELRAQLPADaEVTDYRGKLILPGFIDTHIH----------YPQ-------TDmIASY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 102 GGGII-----STVKA-TREADEALLLEQALFRLRPLLAEGVTCVEIksgYGLS-PES---------ELKMLRVARKlgel 165
Cdd:PRK09228 89 GEQLLdwlntYTFPEeRRFADPAYAREVAEFFLDELLRNGTTTALV---FGTVhPQSvdalfeaaeARNMRMIAGK---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 166 lpvevktTCLAAHAlpPEYanraddyinlVCDTiiPQAAAAGLADAVDAFceH--------------LAFSPAQVERVFA 231
Cdd:PRK09228 162 -------VLMDRNA--PDG----------LRDT--AESGYDDSKALIERW--HgkgrllyaitprfaPTSTPEQLEAAGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 232 -AAEAAGLPVKLH-AEQLSA-----------------------LGGSTLAArhHALsadHLEyatEQDARAMGDAGTVAV 286
Cdd:PRK09228 219 lAREHPDVWIQTHlSENLDEiawvkelfpeardyldvyeryglLGPRAVFA--HCI---HLE---DRERRRLAETGAAIA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 287 LlpgayyllretqCP-----------PVALFRKHHVAMAIASDANPGTSPALsLRLMiNMA---CTL--FRLTPEEALAG 350
Cdd:PRK09228 291 F------------CPtsnlflgsglfDLKRADAAGVRVGLGTDVGGGTSFSM-LQTM-NEAykvQQLqgYRLSPFQAFYL 356
|
410 420
....*....|....*....|....*..
gi 515494776 351 VTTHAAKALGLQHSHGTLETGKVADFV 377
Cdd:PRK09228 357 ATLGGARALGLDDRIGNLAPGKEADFV 383
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
15-377 |
7.48e-08 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 54.24 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 15 DIVTMrDGKYHTLTDGAIAVRDGKIVWIGEHaalPPGLI--ADETVKFDGGIVTPGFVDCHTHLVFGGNR---------- 82
Cdd:PRK06687 8 NIVTC-DQDFHVYLDGILAVKDSQIVYVGQD---KPAFLeqAEQIIDYQGAWIMPGLVNCHTHSAMTGLRgirddsnlhe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 83 ---------SGEF--------------EQRLNG-VSYADI-AAQGGGIISTVKATREA------------DEALLLEQAL 125
Cdd:PRK06687 84 wlndyiwpaESEFtpdmttnavkealtEMLQSGtTTFNDMyNPNGVDIQQIYQVVKTSkmrcyfsptlfsSETETTAETI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 126 FRLRPLLAEGVT--------CVEIKSGYGLSPESELKMLRVARKLGELLPVEVKTTCLAAHALPPEYANRAddyinlvcd 197
Cdd:PRK06687 164 SRTRSIIDEILKyknpnfkvMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIILKRYGKRP--------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 198 tiipqaaaagladavDAFCEHLAF--SPAqverVFAAAeaaglpVKLHAEQLSALGGSTLAARHHALSADHLeyateqda 275
Cdd:PRK06687 235 ---------------LAFLEELGYldHPS----VFAHG------VELNEREIERLASSQVAIAHNPISNLKL-------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 276 ramgdAGTVAvllpgayyllretqcpPVALFRKHHVAMAIASDA----------NPGTSPALsLRLMINMACTLFrlTPE 345
Cdd:PRK06687 282 -----ASGIA----------------PIIQLQKAGVAVGIATDSvasnnnldmfEEGRTAAL-LQKMKSGDASQF--PIE 337
|
410 420 430
....*....|....*....|....*....|..
gi 515494776 346 EALAGVTTHAAKALGLQHSHGTLETGKVADFV 377
Cdd:PRK06687 338 TALKVLTIEGAKALGMENQIGSLEVGKQADFL 369
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
27-76 |
1.08e-07 |
|
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: 53.56 E-value: 1.08e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 515494776 27 LTDGAIAVRDGKIVWIGEHAALPPgliADETVKFDGGIVTPGFVDCHTHL 76
Cdd:COG0044 13 LERADVLIEDGRIAAIGPDLAAPE---AAEVIDATGLLVLPGLIDLHVHL 59
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
12-76 |
1.66e-07 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 52.93 E-value: 1.66e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515494776 12 HGADIVTMrDGKYHTLTDGAIAVRDGKIVWIGEHAALPPGliADETVKFDGGIVTPGFVDCHTHL 76
Cdd:PRK08203 7 NPLAIVTM-DAARREIADGGLVVEGGRIVEVGPGGALPQP--ADEVFDARGHVVTPGLVNTHHHF 68
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
12-75 |
2.84e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 52.02 E-value: 2.84e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515494776 12 HGADIVTmrdgKYHTLTDGAIAVRDGKIVWIGEHAALppgliADETVKFDGGIVTPGFVDCHTH 75
Cdd:COG1820 3 TNARIFT----GDGVLEDGALLIEDGRIAAIGPGAEP-----DAEVIDLGGGYLAPGFIDLHVH 57
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
32-145 |
5.80e-07 |
|
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: 51.24 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 32 IAVRDGKIVWIGEHAALPpGLIADETVKFDGGIVTPGFVDCHTHLVFGGNRSGeFEQRLNGVSYADIaAQGG-----GII 106
Cdd:cd01308 20 ILIAGGKILAIEDQLNLP-GYENVTVVDLHGKILVPGFIDQHVHIIGGGGEGG-PSTRTPEVTLSDL-TTAGvttvvGCL 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 515494776 107 STVKATREADEalLLEQAlfrlRPLLAEGVTCVEIKSGY 145
Cdd:cd01308 97 GTDGISRSMED--LLAKA----RALEEEGITCFVYTGSY 129
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
30-75 |
7.29e-07 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 51.33 E-value: 7.29e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 515494776 30 GAIAVRDGKIVWIGEHAALPpgliADETVKFDGGIVTPGFVDCHTH 75
Cdd:COG3653 22 ADVAIKGGRIVAVGDLAAAE----AARVIDATGLVVAPGFIDIHTH 63
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
26-405 |
9.09e-07 |
|
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: 50.75 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 26 TLTDGAIAVRDGKIVWIGEHAALPPgliADETVKFDGGIVTPGFVDCHTHLvfggNRSG--EFEqrlnGVSYADIAAQGG 103
Cdd:cd01315 14 GVREADIAVKGGKIAAIGPDIANTE---AEEVIDAGGLVVMPGLIDTHVHI----NEPGrtEWE----GFETGTKAAAAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 104 GIISTV----------------KATREA-------DEAL---LLEQALFRLRPLLAEGVT---CVEIKSGYGLSP---ES 151
Cdd:cd01315 83 GITTIIdmplnsipptttvenlEAKLEAaqgklhvDVGFwggLVPGNLDQLRPLDEAGVVgfkCFLCPSGVDEFPavdDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 152 ELKM-LRVARKLG-------ELLPVEVKTTCLAAHALPPEYAnradDYinlvcdtiipqaaaagladavdafcehLAFSP 223
Cdd:cd01315 163 QLEEaMKELAKTGsvlavhaENPEITEALQEQAKAKGKRDYR----DY---------------------------LASRP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 224 AQ-----VERVFAAAEAAGlpVKLHAEQLSALGGSTLAARHHALSAD-------HLEYATEQDARamgDAGTVAvllpga 291
Cdd:cd01315 212 VFteveaIQRILLLAKETG--CRLHIVHLSSAEAVPLIREARAEGVDvtvetcpHYLTFTAEDVP---DGGTEF------ 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 292 yyllreTQCPPV-----------ALFRKhHVAMaIASDANPGT-------------------SPALSLRLMINMACTLFR 341
Cdd:cd01315 281 ------KCAPPIrdaanqeqlweALENG-DIDM-VVSDHSPCTpelkllgkgdffkawggisGLQLGLPVMLTEAVNKRG 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515494776 342 LTPEEALAGVTTHAAKALGLQHSHGTLETGKVADFVHWPLS-----RPAELAY------WLGGQLPCTV---IFRGEV 405
Cdd:cd01315 353 LSLEDIARLMCENPAKLFGLSHQKGRIAVGYDADFVVWDPEeeftvDAEDLYYknkispYVGRTLKGRVhatILRGTV 430
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
26-377 |
3.14e-06 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 48.78 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 26 TLTDGA---IAVRDGKIVWIGEHAALPPGLiadETVKFDGGIVTPGFVDCHTHL--VFGG-----NRSG-------EFEQ 88
Cdd:PRK05985 10 RPAGGAavdILIRDGRIAAIGPALAAPPGA---EVEDGGGALALPGLVDGHIHLdkTFWGdpwypNEPGpslreriANER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 89 RLNGVSYADIAAQgggiistvkATREADEALLLEQALFRlrpllaegvTCVEIKSGYGLSpeSELKMLRVARKLGELLPV 168
Cdd:PRK05985 87 RRRAASGHPAAER---------ALALARAAAAAGTTAMR---------SHVDVDPDAGLR--HLEAVLAARETLRGLIDI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 169 EVKttclaahALP-------PEYANRADDYINLVCDTIipqaaaagladavdafcehLAFSPA--------QVERVFAAA 233
Cdd:PRK05985 147 QIV-------AFPqsgvlsrPGTAELLDAALRAGADVV-------------------GGLDPAgidgdpegQLDIVFGLA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 234 EAAGLPVKLHAEQLSALGGSTL---AARHHALS-------------ADHLEYATEQDARAMGDAGtVAVLL--PGAyyll 295
Cdd:PRK05985 201 ERHGVGIDIHLHEPGELGAFQLeriAARTRALGmqgrvavshafclGDLPEREVDRLAERLAEAG-VAIMTnaPGS---- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 296 reTQCPPVALFRKHHVAMAIASDA-----NP-GTSPALSLRLMINMACTLFrlTPEE---ALAGVTTHAAKALGLQHsHG 366
Cdd:PRK05985 276 --VPVPPVAALRAAGVTVFGGNDGirdtwWPyGNGDMLERAMLIGYRSGFR--TDDElaaALDCVTHGGARALGLED-YG 350
|
410
....*....|.
gi 515494776 367 tLETGKVADFV 377
Cdd:PRK05985 351 -LAVGARADFV 360
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
32-84 |
3.82e-06 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 48.62 E-value: 3.82e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 515494776 32 IAVRDGKIVWIGEHAALPPgliADETVKFDGGIVTPGFVDCHTHLVFGGNRSG 84
Cdd:COG3964 22 IAIKDGKIAAVAKDIDAAE---AKKVIDASGLYVTPGLIDLHTHVFPGGTDYG 71
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
30-75 |
8.20e-06 |
|
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: 47.68 E-value: 8.20e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 515494776 30 GAIAVRDGKIVWIGEHAALPpgliADETVKFDGGIVTPGFVDCHTH 75
Cdd:cd01297 20 ADVGIRDGRIAAIGPILSTS----AREVIDAAGLVVAPGFIDVHTH 61
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
29-404 |
8.42e-06 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 47.66 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 29 DGAIAVRDGKIVWIGEHAALPPGLIADETVK-FDGGIVTPGFVDCHTHlvfggnrsgeFEQrlngvsYADIAAQGGgiiS 107
Cdd:cd01303 26 DGLIVVVDGNIIAAGAAETLKRAAKPGARVIdSPNQFILPGFIDTHIH----------APQ------YANIGSGLG---E 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 108 TV-----KAT-----READEALLLEQALFRLRPLLAEGVTCVeikSGYG-LSPESELKMLRVARKLGE-----------L 165
Cdd:cd01303 87 PLldwleTYTfpeeaKFADPAYAREVYGRFLDELLRNGTTTA---CYFAtIHPESTEALFEEAAKRGQraiagkvcmdrN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 166 LPVEVKTTCLAAHALPPEYANRADDYINLVCDTIIPQaaaagladavdafcehlaFSPAQVERVFA-----AAEAAGLPV 240
Cdd:cd01303 164 APEYYRDTAESSYRDTKRLIERWHGKSGRVKPAITPR------------------FAPSCSEELLAalgklAKEHPDLHI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 241 KLH-AEQLSA-----------------------LGGSTLAArhHALsadHLEyatEQDARAMGDAGTVAVllpgayyllr 296
Cdd:cd01303 226 QTHiSENLDEiawvkelfpgardyldvydkyglLTEKTVLA--HCV---HLS---EEEFNLLKERGASVA---------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 297 etQCP-----------PVALFRKHHVAMAIASDANPGTSPALsLRLM---------INMACT-LFRLTPEEALAGVTTHA 355
Cdd:cd01303 288 --HCPtsnlflgsglfDVRKLLDAGIKVGLGTDVGGGTSFSM-LDTLrqaykvsrlLGYELGgHAKLSPAEAFYLATLGG 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 515494776 356 AKALGLQHSHGTLETGKVADFVhwpLSRPAelaywlGGQLPCTVIFRGE 404
Cdd:cd01303 365 AEALGLDDKIGNFEVGKEFDAV---VIDPS------ATPLLADRMFRVE 404
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
32-103 |
9.58e-06 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 47.50 E-value: 9.58e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515494776 32 IAVRDGKIVWIGEHAALPpgliADETVKFDGGIVTPGFVDCHTHLvfggnrsgefeqRLNGVSYA-DI------AAQGG 103
Cdd:PRK09357 22 VLIDDGKIAAIGENIEAE----GAEVIDATGLVVAPGLVDLHVHL------------REPGQEDKeTIetgsraAAAGG 84
|
|
| isoAsp_dipep |
TIGR01975 |
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ... |
32-138 |
1.19e-05 |
|
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 131030 Cd Length: 389 Bit Score: 47.09 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 32 IAVRDGKIVWIGEHAALPPGLIADETVK-FDGGIVTPGFVDCHTHLVFGGNRSGeFEQRLNGVSYADIAAQG----GGII 106
Cdd:TIGR01975 20 ILIANDKIIAIADEIPSTKDFVPNCVVVgLEGMIAVPGFIDQHVHIIGGGGEGG-PTTRTPELTLSDITKGGvttvVGLL 98
|
90 100 110
....*....|....*....|....*....|..
gi 515494776 107 STVKATReaDEALLLEQAlfrlRPLLAEGVTC 138
Cdd:TIGR01975 99 GTDGITR--HMESLLAKA----RALEEEGISC 124
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
12-379 |
1.21e-05 |
|
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: 47.21 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 12 HGADIVTMrDGKYhtLTDgaIAVRDGKIVWIGEHAALPPGLiadETVKFDGGIVTPGFVDCHTHL--VFGGNRSGE-FEQ 88
Cdd:cd01314 4 KNGTIVTA-DGSF--KAD--ILIEDGKIVAIGPNLEAPGGV---EVIDATGKYVLPGGIDPHTHLelPFMGTVTADdFES 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 89 rlngvsyADIAAQGGG---II--------STVKAT-----READEALLL------------EQALFRLRPLLAEGVTCVE 140
Cdd:cd01314 76 -------GTRAAAAGGtttIIdfaipnkgQSLLEAvekwrGKADGKSVIdygfhmiitdwtDSVIEELPELVKKGISSFK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 141 I----KSGYGLSPESELKMLRVARKLGELLPV--------EVKTTCLAA--------HAL--PP----EYANRAddyINL 194
Cdd:cd01314 149 VfmayKGLLMVDDEELLDVLKRAKELGALVMVhaengdviAELQKKLLAqgktgpeyHALsrPPeveaEATARA---IRL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 195 VCDTIIPqaaaagladavdAFCEHLAfSPAQVERVfAAAEAAGLPVklHAEqlsalggsTLAArHHALSADHLEY----- 269
Cdd:cd01314 226 AELAGAP------------LYIVHVS-SKEAADEI-ARARKKGLPV--YGE--------TCPQ-YLLLDDSDYWKdwfeg 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 270 ---------ATEQDARAMGDAgtvavLLPGAYYLLRETQCPpvalFRKHHVAMAIAS-DANPGTSPALSLRLMInmactL 339
Cdd:cd01314 281 akyvcspplRPKEDQEALWDG-----LSSGTLQTVGSDHCP----FNFAQKARGKDDfTKIPNGVPGVETRMPL-----L 346
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 515494776 340 F-------RLTPEEALAGVTTHAAKALGLQHSHGTLETGKVADFVHW 379
Cdd:cd01314 347 WsegvakgRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIW 393
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
220-403 |
1.28e-05 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 47.15 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 220 AFSPAQVERVFAAAEAaGLPVKLH-AEQ-------LSALGGS--TLAARHHALSAD----HLEYATEQDARAMGDAGTVA 285
Cdd:PRK09229 212 AVTPDQLAAVLALAAP-DGPVHIHiAEQtkevddcLAWSGARpvEWLLDHAPVDARwclvHATHLTDAETARLARSGAVA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 286 VLlpgayyllretqCP-----------PVALFRKHHVAMAIASDANPGTSPALSLRLM-------------------INM 335
Cdd:PRK09229 291 GL------------CPtteanlgdgifPAVDYLAAGGRFGIGSDSHVSIDLVEELRLLeygqrlrdrrrnvlaaaaqPSV 358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515494776 336 ACTLFrltpEEALAGvtthAAKALGLqhSHGTLETGKVADFVHWPLSRPAeLAYWLGGQLPCTVIFRG 403
Cdd:PRK09229 359 GRRLF----DAALAG----GAQALGR--AIGGLAVGARADLVVLDLDHPA-LAGREGDALLDRWVFAG 415
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
25-75 |
1.45e-05 |
|
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: 46.80 E-value: 1.45e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 515494776 25 HTLTDGAIAVRDGKIVWIGEHAALPPGliaDETVKFDGGIVTPGFVDCHTH 75
Cdd:cd00854 12 GGLEDGAVLVEDGKIVAIGPEDELEEA---DEIIDLKGQYLVPGFIDIHIH 59
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
13-77 |
1.74e-05 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 46.53 E-value: 1.74e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515494776 13 GADIVTMRDGKyhTLTDGAIAVRDGKIVWIGEHAALPPgliADETVKFDGGIVTPGFVDCHTHLV 77
Cdd:PRK07228 7 NAGIVTMNAKR--EIVDGDVLIEDDRIAAVGDRLDLED---YDDHIDATGKVVIPGLIQGHIHLC 66
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
10-76 |
1.89e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 46.53 E-value: 1.89e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515494776 10 LWHGADIVTMrDGKYHTLTDGAIAVRDGKIVWIGEHAALPpgliADETVKFDGGIVTPGFVDCHTHL 76
Cdd:PRK08204 5 LIRGGTVLTM-DPAIGDLPRGDILIEGDRIAAVAPSIEAP----DAEVVDARGMIVMPGLVDTHRHT 66
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
28-376 |
4.52e-05 |
|
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: 45.13 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 28 TDGAIAVRDGKIVWIGEHAalppgLIADETVK-FDGGIVTPGFVDCHTHL-VFGGNRSGEFEQrlnGVSyadiAAQGGGi 105
Cdd:TIGR00857 4 TEVDILVEGGRIKKIGKLR-----IPPDAEVIdAKGLLVLPGFIDLHVHLrDPGEEYKEDIES---GSK----AAAHGG- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 106 ISTVKA---TRE-ADEALLLEQALFRL------RPLLAEGVTCVEIksGYGLSPESELKMLRVARKLGELLPVEVKTTCL 175
Cdd:TIGR00857 71 FTTVADmpnTKPpIDTPETLEWKLQRLkkvslvDVHLYGGVTQGNQ--GKELTEAYELKEAGAVGRMFTDDGSEVQDILS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 176 AAHALppEYANRADDYINLVcdtiipqaaaagladavdafCEHLAF---SPAQVERVFAAAEAAGLPVKLHAEQLSALGg 252
Cdd:TIGR00857 149 MRRAL--EYAAIAGVPIALH--------------------AEDPDLiygGVMHEGPSAAQLGLPARPPEAEEVAVARLL- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 253 stLAARH--------HALSADHLEyaTEQDARAMGDAGTVAVlLPGAYYLLRETQC---------PP-------VALFR- 307
Cdd:TIGR00857 206 --ELAKHagcpvhicHISTKESLE--LIVKAKSQGIKITAEV-TPHHLLLSEEDVArldgngkvnPPlrekedrLALIEg 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 308 -KHHVAMAIASDANPGT------------SPALSLRLMINMACTLF---RLTPEEALAGVTTHAAKALGLQhSHGTLETG 371
Cdd:TIGR00857 281 lKDGIIDIIATDHAPHTleektkefaaapPGIPGLETALPLLLQLLvkgLISLKDLIRMLSINPARIFGLP-DKGTLEEG 359
|
....*
gi 515494776 372 KVADF 376
Cdd:TIGR00857 360 NPADI 364
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
8-83 |
5.73e-05 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 45.16 E-value: 5.73e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515494776 8 DSLWHGADIVTMrDGKYHtltdGAIAVRDGKIVWIGEHAAlppgliaDETVKFDGGIVTPGFVDCHTHLV--FGGNRS 83
Cdd:PRK08323 2 STLIKNGTVVTA-DDTYK----ADVLIEDGKIAAIGANLG-------DEVIDATGKYVMPGGIDPHTHMEmpFGGTVS 67
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
13-93 |
5.81e-05 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 44.96 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 13 GADIVTMRDGKYHTLTDGAIAVrDGKIVWIGEHAAL----PPGLIADetvkFDGGIVTPGFVDCHTHLVFGGNRS----G 84
Cdd:PRK08418 5 GASYIFTCDENFEILEDGAVVF-DDKILEIGDYENLkkkyPNAKIQF----FKNSVLLPAFINPHTHLEFSANKTtldyG 79
|
....*....
gi 515494776 85 EFEQRLNGV 93
Cdd:PRK08418 80 DFIPWLGSV 88
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
21-111 |
6.71e-05 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 44.75 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 21 DGKYHTLTDGAIAVRDGKIVWIGEHaalpPGLIADETVKFDGGIVTPGFVDCHTHLVFGGNRsgefeqrlNGVSyADIAA 100
Cdd:PRK12394 14 DPARNINEINNLRIINDIIVDADKY----PVASETRIIHADGCIVTPGLIDYHAHVFYDGTE--------GGVR-PDMYM 80
|
90
....*....|.
gi 515494776 101 QGGGIISTVKA 111
Cdd:PRK12394 81 PPNGVTTVVDA 91
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
328-379 |
8.61e-05 |
|
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: 44.49 E-value: 8.61e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 515494776 328 SLRLMINMActlfRLTPEEALAGVTTHAAKALGLQHSHGTLETGKVADFVHW 379
Cdd:cd00854 314 AVRNMVKWG----GCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVL 361
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
27-75 |
1.08e-04 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 44.13 E-value: 1.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 515494776 27 LTDGAIAVRDGKIVWIGEHAALPPGLIADETVKFDGGIVTPGFVDCHTH 75
Cdd:PRK09045 26 LEDHAVAIRDGRIVAILPRAEARARYAAAETVELPDHVLIPGLINAHTH 74
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
8-76 |
1.30e-04 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 43.97 E-value: 1.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515494776 8 DSLWHGADIVTMRDGKyhtLTDGAIAVRDGKIVWIGEHAALPpgliADETVKFDGGIVTPGFVDCHTHL 76
Cdd:PRK06038 3 DIIIKNAYVLTMDAGD---LKKGSVVIEDGTITEVSESTPGD----ADTVIDAKGSVVMPGLVNTHTHA 64
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
32-80 |
1.82e-04 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 43.30 E-value: 1.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 515494776 32 IAVRDGKIVWIGehaALPPGLIADETVKFDGGIVTPGFVDCHTHLVFGG 80
Cdd:PRK09237 21 IAIEDGKIAAVA---GDIDGSQAKKVIDLSGLYVSPGWIDLHVHVYPGS 66
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
32-76 |
3.10e-04 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 42.66 E-value: 3.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 515494776 32 IAVRDGKIVWIgehaaLPPGLIADETVKFD--GGIVTPGFVDCHTHL 76
Cdd:PRK07583 43 IEIADGKIAAI-----LPAGGAPDELPAVDlkGRMVWPCFVDMHTHL 84
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
20-76 |
3.13e-04 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 42.62 E-value: 3.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 515494776 20 RDGKYHTLTDGAIAVRDGKIVWIGEHAALPpGLIADETVK-FDGGIVTPGFVDCHTHL 76
Cdd:PRK07203 12 RDPAKPVIEDGAIAIEGNVIVEIGTTDELK-AKYPDAEFIdAKGKLIMPGLINSHNHI 68
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
8-76 |
4.55e-04 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 42.38 E-value: 4.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515494776 8 DSLWHGADIVTMRDgkyhtLTDGAIAVRDGKIVWIGEhaALPPGliaDETVKFDGGIVTPGFVDCHTHL 76
Cdd:PRK13404 5 DLVIRGGTVVTATD-----TFQADIGIRGGRIAALGE--GLGPG---AREIDATGRLVLPGGVDSHCHI 63
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
26-76 |
8.67e-04 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 41.16 E-value: 8.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 515494776 26 TLTDGA----IAVRDGKIVwigehaALPPGLIAD--ETVKFDGGIVTPGFVDCHTHL 76
Cdd:PRK07572 10 NLPDGRtgidIGIAGGRIA------AVEPGLQAEaaEEIDAAGRLVSPPFVDPHFHM 60
|
|
| PLN02795 |
PLN02795 |
allantoinase |
3-163 |
8.72e-04 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 41.30 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 3 SEIHCDSLWHGADIVTMRDGkyhtLTDGAIAVRDGKIVWIGEHAALPPGLIADETVKFDGGIVTPGFVDCHTHLvfggNR 82
Cdd:PLN02795 39 SLLPWPHFVLYSKRVVTPAG----VIPGAVEVEGGRIVSVTKEEEAPKSQKKPHVLDYGNAVVMPGLIDVHVHL----NE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 83 SG--EFEQRLNGVSyadiAAQGGGIISTVKATREADEALLLEQALfRLRPLLAEGVTCVEIKSGYGLSPE-----SELKM 155
Cdd:PLN02795 111 PGrtEWEGFPTGTK----AAAAGGITTLVDMPLNSFPSTTSVETL-ELKIEAAKGKLYVDVGFWGGLVPEnahnaSVLEE 185
|
....*...
gi 515494776 156 LRVARKLG 163
Cdd:PLN02795 186 LLDAGALG 193
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
31-84 |
9.19e-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: 41.16 E-value: 9.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 515494776 31 AIAVRDGKIVWIGehAALPPGLiADETVKFDGGIVTPGFVDCHTHLVFGGNRSG 84
Cdd:cd01307 1 DVAIENGKIAAVG--AALAAPA-ATQIVDAGGCYVSPGWIDLHVHVYQGGTRYG 51
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
14-75 |
9.59e-04 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 41.24 E-value: 9.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515494776 14 ADIVtMRDGKY-----HTLTDGAIAVRDGKIVWIGEhAALPpgliADETVKFDGGIVTPGFVDCHTH 75
Cdd:COG1001 5 ADLV-IKNGRLvnvftGEILEGDIAIAGGRIAGVGD-YIGE----ATEVIDAAGRYLVPGFIDGHVH 65
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
32-76 |
1.49e-03 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 40.46 E-value: 1.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 515494776 32 IAVRDGKIVWIGEHAALPpgliADETVKFDGGIVTPGFVDCHTHL 76
Cdd:PRK06189 23 IGIKNGKIAEIAPEISSP----AREIIDADGLYVFPGMIDVHVHF 63
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
5-76 |
1.93e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 40.46 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 5 IHCDSLWHGADiVTMRDG----KYHTLTDGA---------------------IAVRDGKIVWIGEhAALP-------PGL 52
Cdd:PRK13308 38 VYGDECLFGGG-KTLRDGmgmaPGVTSADGAldfvlcnvtvidpvlgivkgdIGIRDGRIVGIGK-AGNPdimdgvdPRL 115
|
90 100
....*....|....*....|....*..
gi 515494776 53 I---ADETVKFDGGIVTPGFVDCHTHL 76
Cdd:PRK13308 116 VvgpGTDVRPAEGLIATPGAIDVHVHF 142
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
27-76 |
2.02e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 40.14 E-value: 2.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 515494776 27 LTDGAIAVRDGKIVWIGEHAalppgLIADETVKFDGGIVTPGFVDCHTHL 76
Cdd:PRK04250 12 IVEGGIGIENGRISKISLRD-----LKGKEVIKVKGGIILPGLIDVHVHL 56
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
32-110 |
2.22e-03 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 40.22 E-value: 2.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515494776 32 IAVRDGKIVWIGEHAALPPGLIaDETvkfdGGIVTPGFVDCHTHLVFGGNrsGEFEQRLNGVSyadiAAQGGGIISTVK 110
Cdd:PRK08044 23 IAVKGGKIAAIGQDLGDAKEVM-DAS----GLVVSPGMVDAHTHISEPGR--SHWEGYETGTR----AAAKGGITTMIE 90
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
32-75 |
2.34e-03 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 40.18 E-value: 2.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 515494776 32 IAVRDGKIVwigehaALPPGLIADETVKFDGGIVTPGFVDCHTH 75
Cdd:COG1229 24 IAIKDGKIV------EEPSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
24-71 |
3.37e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 39.19 E-value: 3.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 515494776 24 YHTLTDGAIAVRDGKIVWIGEHAALPPGLiadETVKFDGGIVTPGFVD 71
Cdd:PRK11170 13 HEVLDDHAVVIADGLIEAVCPVAELPPGI---EQRDLNGAILSPGFID 57
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
307-377 |
3.54e-03 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 39.18 E-value: 3.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515494776 307 RKHHVAMAIASDanpGTSPALSLRLMINMACTLFRLTPEEALA-------GVTTHAAKALGLqhSHGTLETGKVADFV 377
Cdd:PRK08418 300 KKAGINYSIATD---GLSSNISLSLLDELRAALLTHANMPLLElakilllSATRYGAKALGL--NNGEIKEGKDADLS 372
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
12-74 |
4.65e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 39.01 E-value: 4.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515494776 12 HGADIVTmRDGkyhtLTDGAIAVRDGKIVWIGEHAALPPGLIAdetvkFDGGIVTPGFVDCHT 74
Cdd:PRK15446 7 SNARLVL-PDE----VVDGSLLIEDGRIAAIDPGASALPGAID-----AEGDYLLPGLVDLHT 59
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
32-75 |
5.15e-03 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 38.91 E-value: 5.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 515494776 32 IAVRDGKIVWIGEHAalppgLIADETVKFDGGIVTPGFVDCHTH 75
Cdd:PRK09061 41 VGIKGGKIAAVGTAA-----IEGDRTIDATGLVVAPGFIDLHAH 79
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
346-385 |
5.58e-03 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 38.74 E-value: 5.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 515494776 346 EALAGVTTHAAKALGLQHSHGTLETGKVADFVHWPLSRPA 385
Cdd:PRK09045 344 TALRMATLNGARALGLDDEIGSLEPGKQADLVAVDLSGLE 383
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
12-163 |
9.85e-03 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 38.12 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515494776 12 HGADIVTMRDGKYHTLTDGAIAVRDGKIVWIGEHAALPPGLIADETvkfdGGIVTPGFVDCHTHLvfggnrsgeFEQRLN 91
Cdd:PRK12393 8 NAAAIMTGLPGDAARLGGPDIRIRDGRIAAIGALTPLPGERVIDAT----DCVVYPGWVNTHHHL---------FQSLLK 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515494776 92 GVSyADIAAQGGGIISTVKATREA--DEALLLEQALFRLRPLLAEGV-TCVEIKSGY--GLSPESELKMLRVARKLG 163
Cdd:PRK12393 75 GVP-AGINQSLTAWLAAVPYRFRArfDEDLFRLAARIGLVELLRSGCtTVADHHYLYhpGMPFDTGDILFDEAEALG 150
|
|
| |
