|
Name |
Accession |
Description |
Interval |
E-value |
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
11-548 |
0e+00 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 646.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 11 NAKILDVFNQRFEDTELWIDNGSIYFRGKSKDlTAKNNFNAEGNYIVPGLIDAHLHIESSLLAPSELAKLELRHGVTSIF 90
Cdd:COG1001 11 NGRLVNVFTGEILEGDIAIAGGRIAGVGDYIG-EATEVIDAAGRYLVPGFIDGHVHIESSMVTPAEFARAVLPHGTTTVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 91 ADPHEIGSVSGVSGLFYMIQEARNTPLHIHYMLPSSVPAT-NFEHAGAVLHADALKPFYGFPEINGLAEVMDFPAVANGD 169
Cdd:COG1001 90 ADPHEIANVLGLEGVRYMLEAAEGLPLDIFVMLPSCVPATpGLETAGAVLGAEDLAELLDHPRVIGLGEVMNFPGVLNGD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 170 PDMLEKIRDAQAAGHHADGHGAGLTREQLAVYRAVGIDTDHESTSGKEALERIQAGMKVFIREGTVERDEKSILPVVRKN 249
Cdd:COG1001 170 PRMLAKIAAALAAGKVIDGHAPGLSGKDLNAYAAAGIRSDHECTTAEEALEKLRRGMYVMIREGSAAKDLPALLPAVTEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 250 NQSYFSFCTDDKSAIDIQKEGSVDNNVRLAISKGIPAERAFTMASYNAAVAQHVKNVGALTDGFIADLVIISNLDNFVTE 329
Cdd:COG1001 250 NSRRCALCTDDRHPDDLLEEGHIDHVVRRAIELGLDPVTAIQMATLNAAEHFGLKDLGAIAPGRRADIVLLDDLEDFKVE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 330 KVMTEGNWVD---KLESKVTTFTSPA-----VN-AELSLNDLKLPLKS-DKAHVINIQPEHITTKHTIESVNRdQQGNFV 399
Cdd:COG1001 330 KVYADGKLVAedgKLLVDLPKYPYPPwarntVKlRPLTAEDFAIPAPGgVKVRVIGVIPGQIITEHLEAELPV-EDGEVV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 400 AD--QDYAKIIVAERYHNLGH-GLGIIHGFNMQEGAIGSTIAHDSHNMIIAGVDDKPMIIAYDRLKRMGGGMILVDKNGF 476
Cdd:COG1001 409 PDpeRDILKIAVVERHGGTGNiGLGFVKGFGLKRGAIASTVAHDSHNLIVVGTNDEDMALAANRLIEIGGGIVVVKDGKV 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488906998 477 TRELPLEIAGLMSDKPYQEVIAKQKSLKGAFAKIskGIDF-DPFLTLSFMALPVIPSLKITDQGLFDFDQFKF 548
Cdd:COG1001 489 LAELPLPIAGLMSDEPAEEVAEKLEALRAAAREL--GCTLeEPFMTLSFLALPVIPELKLTDRGLVDVTTFEF 559
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
50-542 |
0e+00 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 535.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 50 NAEGNYIVPGLIDAHLHIESSLLAPSELAKLELRHGVTSIFADPHEIGSVSGVSGLFYMIQEARNTPLHIHYMLPSSVPA 129
Cdd:cd01295 1 DAEGKYIVPGFIDAHLHIESSMLTPSEFAKAVLPHGTTTVIADPHEIANVAGVDGIEFMLEDAKKTPLDIFWMLPSCVPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 130 TNFEHAGAVLHADALKPFYGFPEINGLAEVMDFPAVANGDPDMLEKIRDAQAAGHHADGHGAGLTREQLAVYRAVGIDTD 209
Cdd:cd01295 81 TPFETSGAELTAEDIKELLEHPEVVGLGEVMDFPGVIEGDDEMLAKIQAAKKAGKPVDGHAPGLSGEELNAYMAAGISTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 210 HESTSGKEALERIQAGMKVFIREGTVERDEKSILPVVRKNNQSYFSFCTDDKSAIDIQKEGSVDNNVRLAISKGIPAERA 289
Cdd:cd01295 161 HEAMTGEEALEKLRLGMYVMLREGSIAKNLEALLPAITEKNFRRFMFCTDDVHPDDLLSEGHLDYIVRRAIEAGIPPEDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 290 FTMASYNAAVAQHVKNVGALTDGFIADLVIISNLDNFVTEKVMTEGnwvdkleskvttftspavnaelslndlklplksd 369
Cdd:cd01295 241 IQMATINPAECYGLHDLGAIAPGRIADIVILDDLENFNITTVLAKG---------------------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 370 kahviniqpehittkhtiesvnrdqqgnfvadqdyakIIVAERYHNLGH-GLGIIHGFNMQEGAIGSTIAHDSHNMIIAG 448
Cdd:cd01295 287 -------------------------------------IAVVERHGKTGNiGVGFVKGFGLKEGAIASSVAHDSHNIIVIG 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 449 VDDKPMIIAYDRLKRMGGGMILVDKNGFTRELPLEIAGLMSDKPYQEVIAKQKSLKGAFAKISkGIDFDPFLTLSFMALP 528
Cdd:cd01295 330 TNDEDMALAVNRLKEIGGGIVVVKNGKVLAELPLPIAGLMSDEPAEEVAEELKKLREALRELG-YALDDPFMTLSFLSLP 408
|
490
....*....|....
gi 488906998 529 VIPSLKITDQGLFD 542
Cdd:cd01295 409 VIPELKITDKGLFD 422
|
|
| ade |
TIGR01178 |
adenine deaminase; The family described by this model includes an experimentally characterized ... |
9-551 |
2.31e-162 |
|
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: 473.49 E-value: 2.31e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 9 IFNAKILDVFNQRFEDTELWIDNGSIYFRGKSKDLtakNNFNAEGNYIVPGLIDAHLHIESSLLAPSELAKLELRHGVTS 88
Cdd:TIGR01178 4 IKNAKIIDVYNGEIIPGDIAIANGHIAGVGKYNGV---KVIDALGEYAVPGFIDAHIHIESSMLTPSEFAKLVLPHGVTT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 89 IFADPHEIGSVSGVSGLFYMIQEARNTPLHIHYMLPSSVPATNFEHAGAVLHADALKPFYGFPEINGLAEVMDFPAVANG 168
Cdd:TIGR01178 81 VVSDPHEIANVNGEDGINFMLNNAKKTPLNFYFMLPSCVPALQFETSGAVLTAEDIDELMELDEVLGLAEVMDYPGVINA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 169 DPDMLEKIRDAQAAGHHADGHGAGLTREQLAVYRAVGIDTDHESTSGKEALERIQAGMKVFIREGTVERDEKSILPVVRK 248
Cdd:TIGR01178 161 DIEMLNKINSARKRNKVIDGHCPGLSGKLLNKYISAGISNDHESTSIEEAREKLRLGMKLMIREGSAAKNLEALHPLINE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 249 NNQSYFSFCTDDKSAIDIQKEGSVDNNVRLAISKGIPAERAFTMASYNAAVAQHVKNVGALTDGFIADLVIISNLDNFVT 328
Cdd:TIGR01178 241 KNCRSLMLCTDDRHVNDILNEGHINHIVRRAIEHGVDPFDALQMASINPAEHFGIDVGGLIAPGDPADFVILKDLRNFKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 329 EKVMTEGNWVDKLE---SKVTTFTSPAVN-------AELSLNDLKLPLKS-DKAHVINIQPEHITTKHTIESVNRDQQgn 397
Cdd:TIGR01178 321 NKTYVKGKLLDLNEvfnDEISRIPLINEIpinvkarSPKSISDFGIQFKTgNRIRVIKVISNQLITHKTSNSVAEEFG-- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 398 FVADQDYAKIIVAERYHNLGH-GLGIIHGFNMQEGAIGSTIAHDSHNMIIAGVDDKPMIIAYDRLKRMGGGMILVDKNGF 476
Cdd:TIGR01178 399 SDIEEDILKIAVIERHKDNGKiGKGLIKGFGLKEGAIASTVAHDSHNIIAVGSNDEDLALAVNKLIQIGGGLCAAKNGEV 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488906998 477 TRELPLEIAGLMSDKPYQEVIAKQKSLKGAFAKISkGIDFDPFLTLSFMALPVIPSLKITDQGLFDFDQFKFIDI 551
Cdd:TIGR01178 479 TIILPLPIAGLMSDDSAERVAEQIIALNDKCRNVG-GSRDNPFLTLSFLSLPVIPHLKITDKGLFDVESFCFVDL 552
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
7-551 |
1.25e-113 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 349.51 E-value: 1.25e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 7 LHIFNAKILDVFNQRFEDTELWIDNGSIYFRGKSKDLT-AKNNFNAEGNYIVPGLIDAHLHIESSLLAPSELAKLELRHG 85
Cdd:PRK10027 32 YIIDNVSILDLINGGEISGPIVIKGRYIAGVGAEYADApALQRIDARGATAVPGFIDAHLHIESSMMTPVTFETATLPRG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 86 VTSIFADPHEIGSVSGVSGLFYMIQEARNTPLHIHYMLPSSVPA-TNFEHAGAVLHADALKPFYGFPEINGLAEVMDFPA 164
Cdd:PRK10027 112 LTTVICDPHEIVNVMGEAGFAWFARCAEQARQNQYLQVSSCVPAlEGCDVNGASFTLEQMLAWRDHPQVTGLAEMMDYPG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 165 VANGDPDMLEKIrdaQAAGH-HADGHGAGLTREQLAVYRAVGIDTDHESTSGKEALERIQAGMKVFIREGTVERDEKSIL 243
Cdd:PRK10027 192 VISGQNALLDKL---DAFRHlTLDGHCPGLGGKELNAYIAAGIENCHESYQLEEGRRKLQLGMSLMIREGSAARNLNALA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 244 PVVRKNNQSYFSFCTDDKSAIDIQKEGSVDNNVRLAISK-GIPAERAFTMASYNAAVAQHVKNVGALTDGFIADLVIISN 322
Cdd:PRK10027 269 PLINEFNSPQCMLCTDDRNPWEIAHEGHIDALIRRLIEQhNVPLHVAYRVASWSTARHFGLNHLGLLAPGKQADIVLLSD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 323 LDNFVTEKVMTEGNWVD------KLESKVTTFTSPAVN----AELSLNDLKLPLKSDKAH-VINIQPEHITTKHtiESVN 391
Cdd:PRK10027 349 ARKVTVQQVLVKGEPIDaqtlqaEESARLAQSAPPYGNtiarQPVSASDFALQFTPGKRYrVIDVIHNELITHS--RSSV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 392 RDQQGnfVADQDYAKIIVAERY-HNLGHGLGIIHGFNMQEGAIGSTIAHDSHNMIIAGVDDKPMIIAYDRLKRMGGGMIL 470
Cdd:PRK10027 427 YSENG--FDRDDVCFIAVLERYgQRLAPACGLLGGFGLNEGALAATVSHDSHNIVVIGRSAEEMALAVNQVIQDGGGLCV 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 471 VDKNGFTRELPLEIAGLMSDKPYQEVIAKQKSLKGAFAKISKGIDfDPFLTLSFMALPVIPSLKITDQGLFDFDQFKFID 550
Cdd:PRK10027 505 VRNGQVQSHLPLPIAGLMSTDTAQSLAEQIDALKAAARECGPLPD-EPFIQMAFLSLPVIPALKLTSQGLFDGEKFAFTT 583
|
.
gi 488906998 551 I 551
Cdd:PRK10027 584 L 584
|
|
| Adenine_deam_C |
pfam13382 |
Adenine deaminase C-terminal domain; This family represents a C-terminal region of the adenine ... |
381-547 |
8.25e-66 |
|
Adenine deaminase C-terminal domain; This family represents a C-terminal region of the adenine deaminase enzyme.
Pssm-ID: 463864 [Multi-domain] Cd Length: 168 Bit Score: 211.15 E-value: 8.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 381 ITTKHTIESVNRDQqGNFVAD--QDYAKIIVAERYHNLGH-GLGIIHGFNMQEGAIGSTIAHDSHNMIIAGVDDKPMIIA 457
Cdd:pfam13382 1 LITKELEVELPVKD-GVVVPDpeRDILKIAVVERHGGTGNiGVGFVKGFGLKRGAIASSVAHDSHNIIVVGTNDEDMALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 458 YDRLKRMGGGMILVDKNGFTRELPLEIAGLMSDKPYQEVIAKQKSLKGAFAKIskGIDF-DPFLTLSFMALPVIPSLKIT 536
Cdd:pfam13382 80 VNRLIEMGGGIVVVKDGKVLAELPLPIAGLMSDLPAEEVAEKLEELNAALREL--GCELdDPFMTLSFLALPVIPELKIT 157
|
170
....*....|.
gi 488906998 537 DQGLFDFDQFK 547
Cdd:pfam13382 158 DKGLVDVKKFK 168
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
11-548 |
0e+00 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 646.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 11 NAKILDVFNQRFEDTELWIDNGSIYFRGKSKDlTAKNNFNAEGNYIVPGLIDAHLHIESSLLAPSELAKLELRHGVTSIF 90
Cdd:COG1001 11 NGRLVNVFTGEILEGDIAIAGGRIAGVGDYIG-EATEVIDAAGRYLVPGFIDGHVHIESSMVTPAEFARAVLPHGTTTVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 91 ADPHEIGSVSGVSGLFYMIQEARNTPLHIHYMLPSSVPAT-NFEHAGAVLHADALKPFYGFPEINGLAEVMDFPAVANGD 169
Cdd:COG1001 90 ADPHEIANVLGLEGVRYMLEAAEGLPLDIFVMLPSCVPATpGLETAGAVLGAEDLAELLDHPRVIGLGEVMNFPGVLNGD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 170 PDMLEKIRDAQAAGHHADGHGAGLTREQLAVYRAVGIDTDHESTSGKEALERIQAGMKVFIREGTVERDEKSILPVVRKN 249
Cdd:COG1001 170 PRMLAKIAAALAAGKVIDGHAPGLSGKDLNAYAAAGIRSDHECTTAEEALEKLRRGMYVMIREGSAAKDLPALLPAVTEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 250 NQSYFSFCTDDKSAIDIQKEGSVDNNVRLAISKGIPAERAFTMASYNAAVAQHVKNVGALTDGFIADLVIISNLDNFVTE 329
Cdd:COG1001 250 NSRRCALCTDDRHPDDLLEEGHIDHVVRRAIELGLDPVTAIQMATLNAAEHFGLKDLGAIAPGRRADIVLLDDLEDFKVE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 330 KVMTEGNWVD---KLESKVTTFTSPA-----VN-AELSLNDLKLPLKS-DKAHVINIQPEHITTKHTIESVNRdQQGNFV 399
Cdd:COG1001 330 KVYADGKLVAedgKLLVDLPKYPYPPwarntVKlRPLTAEDFAIPAPGgVKVRVIGVIPGQIITEHLEAELPV-EDGEVV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 400 AD--QDYAKIIVAERYHNLGH-GLGIIHGFNMQEGAIGSTIAHDSHNMIIAGVDDKPMIIAYDRLKRMGGGMILVDKNGF 476
Cdd:COG1001 409 PDpeRDILKIAVVERHGGTGNiGLGFVKGFGLKRGAIASTVAHDSHNLIVVGTNDEDMALAANRLIEIGGGIVVVKDGKV 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488906998 477 TRELPLEIAGLMSDKPYQEVIAKQKSLKGAFAKIskGIDF-DPFLTLSFMALPVIPSLKITDQGLFDFDQFKF 548
Cdd:COG1001 489 LAELPLPIAGLMSDEPAEEVAEKLEALRAAAREL--GCTLeEPFMTLSFLALPVIPELKLTDRGLVDVTTFEF 559
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
50-542 |
0e+00 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 535.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 50 NAEGNYIVPGLIDAHLHIESSLLAPSELAKLELRHGVTSIFADPHEIGSVSGVSGLFYMIQEARNTPLHIHYMLPSSVPA 129
Cdd:cd01295 1 DAEGKYIVPGFIDAHLHIESSMLTPSEFAKAVLPHGTTTVIADPHEIANVAGVDGIEFMLEDAKKTPLDIFWMLPSCVPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 130 TNFEHAGAVLHADALKPFYGFPEINGLAEVMDFPAVANGDPDMLEKIRDAQAAGHHADGHGAGLTREQLAVYRAVGIDTD 209
Cdd:cd01295 81 TPFETSGAELTAEDIKELLEHPEVVGLGEVMDFPGVIEGDDEMLAKIQAAKKAGKPVDGHAPGLSGEELNAYMAAGISTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 210 HESTSGKEALERIQAGMKVFIREGTVERDEKSILPVVRKNNQSYFSFCTDDKSAIDIQKEGSVDNNVRLAISKGIPAERA 289
Cdd:cd01295 161 HEAMTGEEALEKLRLGMYVMLREGSIAKNLEALLPAITEKNFRRFMFCTDDVHPDDLLSEGHLDYIVRRAIEAGIPPEDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 290 FTMASYNAAVAQHVKNVGALTDGFIADLVIISNLDNFVTEKVMTEGnwvdkleskvttftspavnaelslndlklplksd 369
Cdd:cd01295 241 IQMATINPAECYGLHDLGAIAPGRIADIVILDDLENFNITTVLAKG---------------------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 370 kahviniqpehittkhtiesvnrdqqgnfvadqdyakIIVAERYHNLGH-GLGIIHGFNMQEGAIGSTIAHDSHNMIIAG 448
Cdd:cd01295 287 -------------------------------------IAVVERHGKTGNiGVGFVKGFGLKEGAIASSVAHDSHNIIVIG 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 449 VDDKPMIIAYDRLKRMGGGMILVDKNGFTRELPLEIAGLMSDKPYQEVIAKQKSLKGAFAKISkGIDFDPFLTLSFMALP 528
Cdd:cd01295 330 TNDEDMALAVNRLKEIGGGIVVVKNGKVLAELPLPIAGLMSDEPAEEVAEELKKLREALRELG-YALDDPFMTLSFLSLP 408
|
490
....*....|....
gi 488906998 529 VIPSLKITDQGLFD 542
Cdd:cd01295 409 VIPELKITDKGLFD 422
|
|
| ade |
TIGR01178 |
adenine deaminase; The family described by this model includes an experimentally characterized ... |
9-551 |
2.31e-162 |
|
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: 473.49 E-value: 2.31e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 9 IFNAKILDVFNQRFEDTELWIDNGSIYFRGKSKDLtakNNFNAEGNYIVPGLIDAHLHIESSLLAPSELAKLELRHGVTS 88
Cdd:TIGR01178 4 IKNAKIIDVYNGEIIPGDIAIANGHIAGVGKYNGV---KVIDALGEYAVPGFIDAHIHIESSMLTPSEFAKLVLPHGVTT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 89 IFADPHEIGSVSGVSGLFYMIQEARNTPLHIHYMLPSSVPATNFEHAGAVLHADALKPFYGFPEINGLAEVMDFPAVANG 168
Cdd:TIGR01178 81 VVSDPHEIANVNGEDGINFMLNNAKKTPLNFYFMLPSCVPALQFETSGAVLTAEDIDELMELDEVLGLAEVMDYPGVINA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 169 DPDMLEKIRDAQAAGHHADGHGAGLTREQLAVYRAVGIDTDHESTSGKEALERIQAGMKVFIREGTVERDEKSILPVVRK 248
Cdd:TIGR01178 161 DIEMLNKINSARKRNKVIDGHCPGLSGKLLNKYISAGISNDHESTSIEEAREKLRLGMKLMIREGSAAKNLEALHPLINE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 249 NNQSYFSFCTDDKSAIDIQKEGSVDNNVRLAISKGIPAERAFTMASYNAAVAQHVKNVGALTDGFIADLVIISNLDNFVT 328
Cdd:TIGR01178 241 KNCRSLMLCTDDRHVNDILNEGHINHIVRRAIEHGVDPFDALQMASINPAEHFGIDVGGLIAPGDPADFVILKDLRNFKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 329 EKVMTEGNWVDKLE---SKVTTFTSPAVN-------AELSLNDLKLPLKS-DKAHVINIQPEHITTKHTIESVNRDQQgn 397
Cdd:TIGR01178 321 NKTYVKGKLLDLNEvfnDEISRIPLINEIpinvkarSPKSISDFGIQFKTgNRIRVIKVISNQLITHKTSNSVAEEFG-- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 398 FVADQDYAKIIVAERYHNLGH-GLGIIHGFNMQEGAIGSTIAHDSHNMIIAGVDDKPMIIAYDRLKRMGGGMILVDKNGF 476
Cdd:TIGR01178 399 SDIEEDILKIAVIERHKDNGKiGKGLIKGFGLKEGAIASTVAHDSHNIIAVGSNDEDLALAVNKLIQIGGGLCAAKNGEV 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488906998 477 TRELPLEIAGLMSDKPYQEVIAKQKSLKGAFAKISkGIDFDPFLTLSFMALPVIPSLKITDQGLFDFDQFKFIDI 551
Cdd:TIGR01178 479 TIILPLPIAGLMSDDSAERVAEQIIALNDKCRNVG-GSRDNPFLTLSFLSLPVIPHLKITDKGLFDVESFCFVDL 552
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
7-551 |
1.25e-113 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 349.51 E-value: 1.25e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 7 LHIFNAKILDVFNQRFEDTELWIDNGSIYFRGKSKDLT-AKNNFNAEGNYIVPGLIDAHLHIESSLLAPSELAKLELRHG 85
Cdd:PRK10027 32 YIIDNVSILDLINGGEISGPIVIKGRYIAGVGAEYADApALQRIDARGATAVPGFIDAHLHIESSMMTPVTFETATLPRG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 86 VTSIFADPHEIGSVSGVSGLFYMIQEARNTPLHIHYMLPSSVPA-TNFEHAGAVLHADALKPFYGFPEINGLAEVMDFPA 164
Cdd:PRK10027 112 LTTVICDPHEIVNVMGEAGFAWFARCAEQARQNQYLQVSSCVPAlEGCDVNGASFTLEQMLAWRDHPQVTGLAEMMDYPG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 165 VANGDPDMLEKIrdaQAAGH-HADGHGAGLTREQLAVYRAVGIDTDHESTSGKEALERIQAGMKVFIREGTVERDEKSIL 243
Cdd:PRK10027 192 VISGQNALLDKL---DAFRHlTLDGHCPGLGGKELNAYIAAGIENCHESYQLEEGRRKLQLGMSLMIREGSAARNLNALA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 244 PVVRKNNQSYFSFCTDDKSAIDIQKEGSVDNNVRLAISK-GIPAERAFTMASYNAAVAQHVKNVGALTDGFIADLVIISN 322
Cdd:PRK10027 269 PLINEFNSPQCMLCTDDRNPWEIAHEGHIDALIRRLIEQhNVPLHVAYRVASWSTARHFGLNHLGLLAPGKQADIVLLSD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 323 LDNFVTEKVMTEGNWVD------KLESKVTTFTSPAVN----AELSLNDLKLPLKSDKAH-VINIQPEHITTKHtiESVN 391
Cdd:PRK10027 349 ARKVTVQQVLVKGEPIDaqtlqaEESARLAQSAPPYGNtiarQPVSASDFALQFTPGKRYrVIDVIHNELITHS--RSSV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 392 RDQQGnfVADQDYAKIIVAERY-HNLGHGLGIIHGFNMQEGAIGSTIAHDSHNMIIAGVDDKPMIIAYDRLKRMGGGMIL 470
Cdd:PRK10027 427 YSENG--FDRDDVCFIAVLERYgQRLAPACGLLGGFGLNEGALAATVSHDSHNIVVIGRSAEEMALAVNQVIQDGGGLCV 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 471 VDKNGFTRELPLEIAGLMSDKPYQEVIAKQKSLKGAFAKISKGIDfDPFLTLSFMALPVIPSLKITDQGLFDFDQFKFID 550
Cdd:PRK10027 505 VRNGQVQSHLPLPIAGLMSTDTAQSLAEQIDALKAAARECGPLPD-EPFIQMAFLSLPVIPALKLTSQGLFDGEKFAFTT 583
|
.
gi 488906998 551 I 551
Cdd:PRK10027 584 L 584
|
|
| Adenine_deam_C |
pfam13382 |
Adenine deaminase C-terminal domain; This family represents a C-terminal region of the adenine ... |
381-547 |
8.25e-66 |
|
Adenine deaminase C-terminal domain; This family represents a C-terminal region of the adenine deaminase enzyme.
Pssm-ID: 463864 [Multi-domain] Cd Length: 168 Bit Score: 211.15 E-value: 8.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 381 ITTKHTIESVNRDQqGNFVAD--QDYAKIIVAERYHNLGH-GLGIIHGFNMQEGAIGSTIAHDSHNMIIAGVDDKPMIIA 457
Cdd:pfam13382 1 LITKELEVELPVKD-GVVVPDpeRDILKIAVVERHGGTGNiGVGFVKGFGLKRGAIASSVAHDSHNIIVVGTNDEDMALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 458 YDRLKRMGGGMILVDKNGFTRELPLEIAGLMSDKPYQEVIAKQKSLKGAFAKIskGIDF-DPFLTLSFMALPVIPSLKIT 536
Cdd:pfam13382 80 VNRLIEMGGGIVVVKDGKVLAELPLPIAGLMSDLPAEEVAEKLEELNAALREL--GCELdDPFMTLSFLALPVIPELKIT 157
|
170
....*....|.
gi 488906998 537 DQGLFDFDQFK 547
Cdd:pfam13382 158 DKGLVDVKKFK 168
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
55-338 |
4.54e-20 |
|
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: 91.41 E-value: 4.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 55 YIVPGLIDAHLHIESSLL----APSELAKLELRHGVTSIFADPHEIGSVSGVSGLFY---MIQEARNTPLHIHYMLPSSV 127
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGieaLLEAAEELPLGLRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 128 PATNFEHAGAVLHADALKPFYGFPEING----LAEVMDFPAVANGDPDMLEKIRDAQAAGHHADGHGAGLTREQLAVYRA 203
Cdd:pfam01979 81 LDTDGELEGRKALREKLKAGAEFIKGMAdgvvFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKGEVEDAIAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 204 VGIDTDHES-----------------------TSGKEALERIQAGMKVFIR-----EGTVERDEKSILPVVrkNNQSYFS 255
Cdd:pfam01979 161 FGGGIEHGThlevaesgglldiiklilahgvhLSPTEANLLAEHLKGAGVAhcpfsNSKLRSGRIALRKAL--EDGVKVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 256 FCTDDKSAIDiqkEGSVDNNVRLAISK------GIPAERAFTMASYNAAVAQHV-KNVGALTDGFIADLVIIS------- 321
Cdd:pfam01979 239 LGTDGAGSGN---SLNMLEELRLALELqfdpegGLSPLEALRMATINPAKALGLdDKVGSIEVGKDADLVVVDldplaaf 315
|
330
....*....|....*....
gi 488906998 322 --NLDNFVTEKVMTEGNWV 338
Cdd:pfam01979 316 fgLKPDGNVKKVIVKGKIV 334
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
9-340 |
1.13e-10 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 63.44 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 9 IFNAKILDVFNQR-FEDTELWIDNGSIYFRGKSKDLTAKNN---FNAEGNYIVPGLIDAHLHI----------------- 67
Cdd:COG1228 12 ITNATLVDGTGGGvIENGTVLVEDGKIAAVGPAADLAVPAGaevIDATGKTVLPGLIDAHTHLglgggravefeagggit 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 68 -ESSLLAP-SELAKLELRHGVTSIfADPHeiGSVSG-----VSGLFYMIQEAR----NTPLHIHYMLPSSVPATNFEHAG 136
Cdd:COG1228 92 pTVDLVNPaDKRLRRALAAGVTTV-RDLP--GGPLGlrdaiIAGESKLLPGPRvlaaGPALSLTGGAHARGPEEARAALR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 137 AVL--HADALKpfygfpeinglaeVMDFPAVANGDPDMLEKIRD-AQAAGHHADGHGAGLTREQLAVyrAVGIDT-DHES 212
Cdd:COG1228 169 ELLaeGADYIK-------------VFAEGGAPDFSLEELRAILEaAHALGLPVAAHAHQADDIRLAV--EAGVDSiEHGT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 213 TSGKEALERIQAGMKVFI------REGTVERDEKSILPVVRKNNQSY-------------FSFCTDdkSAIDIQKEGSVD 273
Cdd:COG1228 234 YLDDEVADLLAEAGTVVLvptlslFLALLEGAAAPVAAKARKVREAAlanarrlhdagvpVALGTD--AGVGVPPGRSLH 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488906998 274 NNVRLAISKGIPAERAFTMASYNAAVAQHV-KNVGALTDGFIADLVI--------ISNLDNfvTEKVMTEGNWVDK 340
Cdd:COG1228 312 RELALAVEAGLTPEEALRAATINAAKALGLdDDVGSLEPGKLADLVLldgdpledIAYLED--VRAVMKDGRVVDR 385
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
60-300 |
6.91e-06 |
|
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: 48.10 E-value: 6.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 60 LIDAHLHIESSLL----------------------APSELAKLELRHGVTSIFADPHEIGSVSGVSGLFYMIQEARNTPL 117
Cdd:cd01292 1 FIDTHVHLDGSALrgtrlnlelkeaeelspedlyeDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 118 HIHYMLP--SSVPATNFEHAGAVLHADALKPFygFPEINGLAEVMDFPAVANGDPDMLEKIRDAQAAGHHADGHGAGLTR 195
Cdd:cd01292 81 IRVVLGLgiPGVPAAVDEDAEALLLELLRRGL--ELGAVGLKLAGPYTATGLSDESLRRVLEEARKLGLPVVIHAGELPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 196 EQLAVYRAVGIDTD-------HESTSGKEALERI-QAGMKVFIREGTVERDEKS---ILPVVR-KNNQSYFSFCTDDKSA 263
Cdd:cd01292 159 PTRALEDLVALLRLggrvvigHVSHLDPELLELLkEAGVSLEVCPLSNYLLGRDgegAEALRRlLELGIRVTLGTDGPPH 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 488906998 264 IDIQKEGSVDNNVRLAISKGIPAERAFTMASYNAAVA 300
Cdd:cd01292 239 PLGTDLLALLRLLLKVLRLGLSLEEALRLATINPARA 275
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
9-336 |
1.50e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 47.40 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 9 IFNAKILDVfNQRFEDTELWIDNGSIYFRGKSKDLTAKNnFNAEGNYIVPGLIDAHLH-------IESSLLAPSELAKLE 81
Cdd:COG1820 2 ITNARIFTG-DGVLEDGALLIEDGRIAAIGPGAEPDAEV-IDLGGGYLAPGFIDLHVHggggvdfMDGTPEALRTIARAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 82 LRHGVTSIFA----DPHE--IGSVSGVSGlfYMIQEARNTPLHIH----YMlpssvpatNFEHAGAvlH-ADALKPfygf 150
Cdd:COG1820 80 ARHGTTSFLPttitAPPEdlLRALAAIAE--AIEQGGGAGILGIHlegpFL--------SPEKKGA--HpPEYIRP---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 151 PEINGLAEVMDFPA-------VA---NGDPDMLEKIRDAQ---AAGH-HAD-------------------------GH-- 189
Cdd:COG1820 144 PDPEELDRLLEAAGgliklvtLApelPGALEFIRYLVEAGvvvSLGHtDATyeqaraafeagathvthlfnamsplHHre 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 190 ----GAGLTREQL-----------------AVYRAVGID-----TDheSTSGkealeriqAGMKvfirEGTVERDEksiL 243
Cdd:COG1820 224 pgvvGAALDDDDVyaeliadgihvhpaavrLALRAKGPDrlilvTD--AMAA--------AGLP----DGEYELGG---L 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 244 PVVRKNNQsyfsfCTDDKSAIdiqkEGSV---DNNVRLAISK-GIPAERAFTMASYNAAVAQHV-KNVGALTDGFIADLV 318
Cdd:COG1820 287 EVTVKDGV-----ARLADGTL----AGSTltmDDAVRNLVEWtGLPLEEAVRMASLNPARALGLdDRKGSIAPGKDADLV 357
|
410
....*....|....*...
gi 488906998 319 IISnlDNFVTEKVMTEGN 336
Cdd:COG1820 358 VLD--DDLNVRATWVGGE 373
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
9-120 |
8.15e-05 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 45.19 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 9 IFNAKILDVFNqRFEDTELWIDNGSIYFRGKSKDLTAKNNFNAEGNYIVPGLIDAHLH-----------IESSLLApsel 77
Cdd:PRK09357 5 IKNGRVIDPKG-LDEVADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVHlrepgqedketIETGSRA---- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 488906998 78 AkleLRHGVTSIFADPHEIGSVSGVSGLFYMIQEARNTPL-HIH 120
Cdd:PRK09357 80 A---AAGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLvDVL 120
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
7-66 |
2.30e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 43.87 E-value: 2.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488906998 7 LHIFNAKILdvFNQRFEDTELWIDNGSI-----YFRGKSKDLTaknnFNAEGNYIVPGLIDAHLH 66
Cdd:PRK02382 4 ALLKDGRVY--YNNSLQPRDVRIDGGKItavgkDLDGSSSEEV----IDARGMLLLPGGIDVHVH 62
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
7-73 |
3.05e-04 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 43.28 E-value: 3.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488906998 7 LHIFNAKILDVFNQR--FEDTELWIDNGSIYFRGKSKDLTAKNN----FNAEGNYIVPGLIDAHLHIESSLLA 73
Cdd:COG0402 2 LLIRGAWVLTMDPAGgvLEDGAVLVEDGRIAAVGPGAELPARYPaaevIDAGGKLVLPGLVNTHTHLPQTLLR 74
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
9-95 |
3.13e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 43.34 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 9 IFNAKILDvfNQRFEDTELWIDNGSIYFRGKSKDLTAKNN-FNAEGNYIVPGLIDAHLH-------IESSLLAPSELAKL 80
Cdd:cd00854 3 IKNARILT--PGGLEDGAVLVEDGKIVAIGPEDELEEADEiIDLKGQYLVPGFIDIHIHggggadfMDGTAEALKTIAEA 80
|
90
....*....|....*....
gi 488906998 81 ELRHGVTSIFA----DPHE 95
Cdd:cd00854 81 LAKHGTTSFLPttvtAPPE 99
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
7-89 |
6.42e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 42.48 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 7 LHIFNAKILDVFNQRFEDTELWIDNGSIYFRGKSKDLTAKNN-----FNAEGNYIVPGLIDAHLHIESSLLApseLAKLE 81
Cdd:COG1574 10 LLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGpatevIDLGGKTVLPGFIDAHVHLLGGGLA---LLGVD 86
|
....*...
gi 488906998 82 LRhGVTSI 89
Cdd:COG1574 87 LS-GARSL 93
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
9-102 |
2.12e-03 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 40.60 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 9 IFNAKILDVFNQRFEDTELWIDNGSIYFRGKSKDLT-AKNNFNAEGNYIVPGLIDAHLHIessllapselaklelRHGVT 87
Cdd:PRK09237 3 LRGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDGSqAKKVIDLSGLYVSPGWIDLHVHV---------------YPGST 67
|
90
....*....|....*
gi 488906998 88 SIFADPHEIGSVSGV 102
Cdd:PRK09237 68 PYGDEPDEVGVRSGV 82
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
25-104 |
2.37e-03 |
|
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: 40.66 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 25 TELWIDNGSIYFRGKskDLTAKNN---FNAEGNYIVPGLIDAHLHIESSLLapselaklelrhGVTSifADPHEIGSVSG 101
Cdd:cd01314 17 ADILIEDGKIVAIGP--NLEAPGGvevIDATGKYVLPGGIDPHTHLELPFM------------GTVT--ADDFESGTRAA 80
|
...
gi 488906998 102 VSG 104
Cdd:cd01314 81 AAG 83
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
51-90 |
3.75e-03 |
|
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: 39.58 E-value: 3.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 488906998 51 AEGNYIVPGLIDAHLH----------------IESSLLAPSELAKLeLRHGVTSIF 90
Cdd:cd01299 6 LGGKTLMPGLIDAHTHlgsdpgdlpldlalpvEYRTIRATRQARAA-LRAGFTTVR 60
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
284-326 |
6.12e-03 |
|
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: 39.11 E-value: 6.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488906998 284 IPAERAFTMASYNAAVAQHVKNVGALTDGFIADLVIIsNLDNF 326
Cdd:cd01298 332 LPAEEALEMATIGGAKALGLDEIGSLEVGKKADLILI-DLDGP 373
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
9-67 |
8.45e-03 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 38.59 E-value: 8.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488906998 9 IFNAKILDVFNQRFEDTELWIDNGSIYFRGKSKDLTAKNNFNAEGNYIVPGLIDAHLHI 67
Cdd:PRK12394 7 ITNGHIIDPARNINEINNLRIINDIIVDADKYPVASETRIIHADGCIVTPGLIDYHAHV 65
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
17-149 |
9.83e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 38.60 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488906998 17 VFNQRFEDTELWIDNGSIYfRGKSKDLTAKNNFNAEGNYIVPGLIDAHLH-----------IESSLLAPselakleLRHG 85
Cdd:PRK04250 7 LLKGRIVEGGIGIENGRIS-KISLRDLKGKEVIKVKGGIILPGLIDVHVHlrdfeesyketIESGTKAA-------LHGG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488906998 86 VTSIFADPHEIGSVSGVSGLFYMIQEARNTPlHIHYMLpSSVPATNFEHAGAVLhADALKPFYG 149
Cdd:PRK04250 79 ITLVFDMPNTKPPIMDEKTYEKRMRIAEKKS-YADYAL-NFLIAGNCEKAEEIK-ADFYKIFMG 139
|
|
| |
