|
Name |
Accession |
Description |
Interval |
E-value |
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
17-580 |
0e+00 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 693.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 17 GESPFDLLLIDAQIVDMATGEIRAADVGIVGEMIASVHPRgsREDAHEVRSLAGGYLSPGLMDTHVHLESSHLPPERYAE 96
Cdd:COG1001 1 GREPADLVIKNGRLVNVFTGEILEGDIAIAGGRIAGVGDY--IGEATEVIDAAGRYLVPGFIDGHVHIESSMVTPAEFAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 97 IVLTQGTTAVFWDPHELANVLGVAGVRYAVDASRHLPLQVMVAAPSSVPSTPGLEMSGADFAGAEMETMLGWPEVRGVAE 176
Cdd:COG1001 79 AVLPHGTTTVIADPHEIANVLGLEGVRYMLEAAEGLPLDIFVMLPSCVPATPGLETAGAVLGAEDLAELLDHPRVIGLGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 177 VMDMHGVLHGSERMQEIVQAGLNSGKLIEGHARGLSGADLQAYLAAGVTSDHELTSADDALEKLRAGLTIEIR-GSHPYL 255
Cdd:COG1001 159 VMNFPGVLNGDPRMLAKIAAALAAGKVIDGHAPGLSGKDLNAYAAAGIRSDHECTTAEEALEKLRRGMYVMIReGSAAKD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 256 LPDIVAALKtlPHLSSQITVCTDDVPPDILLEKGGIIALLNLLIEHGLPAVDALRFATLNAAIRLQRHDLGLIAAGRRAD 335
Cdd:COG1001 239 LPALLPAVT--ELNSRRCALCTDDRHPDDLLEEGHIDHVVRRAIELGLDPVTAIQMATLNAAEHFGLKDLGAIAPGRRAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 336 LVVFDSLEKLVAREVYIGGKLLARAGNLLTPIAPAAGVTPPRDTLQIAPLRADDFILRVQGIrhGIAR-LRHIRGARFTQ 414
Cdd:COG1001 317 IVLLDDLEDFKVEKVYADGKLVAEDGKLLVDLPKYPYPPWARNTVKLRPLTAEDFAIPAPGG--VKVRvIGVIPGQIITE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 415 WGEVEVQVRDGKVQLPA--GFSLIWVKHRHGRhQATPQIALLEGWGELRGAIATSYSHDSHNLVVLGRDANDMALAANQL 492
Cdd:COG1001 395 HLEAELPVEDGEVVPDPerDILKIAVVERHGG-TGNIGLGFVKGFGLKRGAIASTVAHDSHNLIVVGTNDEDMALAANRL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 493 IASGGGMALAQQGEILAHVAMPIAGMLSDLPAAELARQFRELRDLSSQV-ADWEPPYRvfkAIEGTCLACNAGPHLTDLG 571
Cdd:COG1001 474 IEIGGGIVVVKDGKVLAELPLPIAGLMSDEPAEEVAEKLEALRAAARELgCTLEEPFM---TLSFLALPVIPELKLTDRG 550
|
....*....
gi 1790602168 572 LTDGGSRQI 580
Cdd:COG1001 551 LVDVTTFEF 559
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
68-574 |
2.83e-141 |
|
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: 416.62 E-value: 2.83e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 68 LAGGYLSPGLMDTHVHLESSHLPPERYAEIVLTQGTTAVFWDPHELANVLGVAGVRYAVDASRHLPLQVMVAAPSSVPST 147
Cdd:cd01295 2 AEGKYIVPGFIDAHLHIESSMLTPSEFAKAVLPHGTTTVIADPHEIANVAGVDGIEFMLEDAKKTPLDIFWMLPSCVPAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 148 PGlEMSGADFAGAEMETMLGWPEVRGVAEVMDMHGVLHGSERMQEIVQAGLNSGKLIEGHARGLSGADLQAYLAAGVTSD 227
Cdd:cd01295 82 PF-ETSGAELTAEDIKELLEHPEVVGLGEVMDFPGVIEGDDEMLAKIQAAKKAGKPVDGHAPGLSGEELNAYMAAGISTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 228 HELTSADDALEKLRAGLTIEIRGSHPylLPDIVAALKTLPH-LSSQITVCTDDVPPDILLEKGGIIALLNLLIEHGLPAV 306
Cdd:cd01295 161 HEAMTGEEALEKLRLGMYVMLREGSI--AKNLEALLPAITEkNFRRFMFCTDDVHPDDLLSEGHLDYIVRRAIEAGIPPE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 307 DALRFATLNAAIRLQRHDLGLIAAGRRADLVVFDSLEKLVAREVYIGGkllaragnlltpiapaagvtpprdtlqiaplr 386
Cdd:cd01295 239 DAIQMATINPAECYGLHDLGAIAPGRIADIVILDDLENFNITTVLAKG-------------------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 387 addfilrvqgirhgiarlrhirgarftqwgevevqvrdgkvqlpagfslIWVKHRHGRHQATPqIALLEGWGELRGAIAT 466
Cdd:cd01295 287 -------------------------------------------------IAVVERHGKTGNIG-VGFVKGFGLKEGAIAS 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 467 SYSHDSHNLVVLGRDANDMALAANQLIASGGGMALAQQGEILAHVAMPIAGMLSDLPAAELARQFRELRDLSSQVADW-E 545
Cdd:cd01295 317 SVAHDSHNIIVIGTNDEDMALAVNRLKEIGGGIVVVKNGKVLAELPLPIAGLMSDEPAEEVAEELKKLREALRELGYAlD 396
|
490 500 510
....*....|....*....|....*....|.
gi 1790602168 546 PPYRVFKAIEGTCLacnagPHL--TDLGLTD 574
Cdd:cd01295 397 DPFMTLSFLSLPVI-----PELkiTDKGLFD 422
|
|
| ade |
TIGR01178 |
adenine deaminase; The family described by this model includes an experimentally characterized ... |
22-582 |
2.45e-117 |
|
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: 359.86 E-value: 2.45e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 22 DLLLIDAQIVDMATGEIRAADVGIVGEMIASVhprgSREDAHEVRSLAGGYLSPGLMDTHVHLESSHLPPERYAEIVLTQ 101
Cdd:TIGR01178 1 DIVIKNAKIIDVYNGEIIPGDIAIANGHIAGV----GKYNGVKVIDALGEYAVPGFIDAHIHIESSMLTPSEFAKLVLPH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 102 GTTAVFWDPHELANVLGVAGVRYAVDASRHLPLQVMVAAPSSVPSTPgLEMSGADFAGAEMETMLGWPEVRGVAEVMDMH 181
Cdd:TIGR01178 77 GVTTVVSDPHEIANVNGEDGINFMLNNAKKTPLNFYFMLPSCVPALQ-FETSGAVLTAEDIDELMELDEVLGLAEVMDYP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 182 GVLHGSERMQEIVQAGLNSGKLIEGHARGLSGADLQAYLAAGVTSDHELTSADDALEKLRAGLTIEIR-GShpyllpdiv 260
Cdd:TIGR01178 156 GVINADIEMLNKINSARKRNKVIDGHCPGLSGKLLNKYISAGISNDHESTSIEEAREKLRLGMKLMIReGS--------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 261 aALKTLPHL--------SSQITVCTDDVPPDILLEKGGIIALLNLLIEHGLPAVDALRFATLNAAIRLQRHDLGLIAAGR 332
Cdd:TIGR01178 227 -AAKNLEALhplineknCRSLMLCTDDRHVNDILNEGHINHIVRRAIEHGVDPFDALQMASINPAEHFGIDVGGLIAPGD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 333 RADLVVFDSLEKLVAREVYIGGKLLARAGNLLTPIAPAAGVTPPRDTLQI-APLRADDFILRVQGiRHGIARLRHIRGAR 411
Cdd:TIGR01178 306 PADFVILKDLRNFKVNKTYVKGKLLDLNEVFNDEISRIPLINEIPINVKArSPKSISDFGIQFKT-GNRIRVIKVISNQL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 412 FTQWGEVEVQvRDGKVQLPAGFSLIWVKHRHGRHQAtPQIALLEGWGELRGAIATSYSHDSHNLVVLGRDANDMALAANQ 491
Cdd:TIGR01178 385 ITHKTSNSVA-EEFGSDIEEDILKIAVIERHKDNGK-IGKGLIKGFGLKEGAIASTVAHDSHNIIAVGSNDEDLALAVNK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 492 LIASGGGMALAQQGEILAHVAMPIAGMLSDLPAAELARQFRELRDLSSQVAdwepPYRVFKAIEGTCLACNAGPHL--TD 569
Cdd:TIGR01178 463 LIQIGGGLCAAKNGEVTIILPLPIAGLMSDDSAERVAEQIIALNDKCRNVG----GSRDNPFLTLSFLSLPVIPHLkiTD 538
|
570
....*....|...
gi 1790602168 570 LGLTDGGSRQIVD 582
Cdd:TIGR01178 539 KGLFDVESFCFVD 551
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
15-535 |
5.60e-93 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 297.51 E-value: 5.60e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 15 ARGESPFDLLLIDAQIVDMATGEIRAADVGIVGEMIASVHPRGSREDAHEVRSLAGGYLSPGLMDTHVHLESSHLPPERY 94
Cdd:PRK10027 24 SRGDAVADYIIDNVSILDLINGGEISGPIVIKGRYIAGVGAEYADAPALQRIDARGATAVPGFIDAHLHIESSMMTPVTF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 95 AEIVLTQGTTAVFWDPHELANVLGVAGVRYAVDASRHLPLQVMVAAPSSVPSTPGLEMSGADFAGAEMETMLGWPEVRGV 174
Cdd:PRK10027 104 ETATLPRGLTTVICDPHEIVNVMGEAGFAWFARCAEQARQNQYLQVSSCVPALEGCDVNGASFTLEQMLAWRDHPQVTGL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 175 AEVMDMHGVLHGSERMQEIVQA--GLNsgklIEGHARGLSGADLQAYLAAGVTSDHELTSADDALEKLRAGLTIEIR-GS 251
Cdd:PRK10027 184 AEMMDYPGVISGQNALLDKLDAfrHLT----LDGHCPGLGGKELNAYIAAGIENCHESYQLEEGRRKLQLGMSLMIReGS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 252 hpyllpdIVAALKTLPHL-----SSQITVCTDDVPPDILLEKGGIIALLNLLIE-HGLPAVDALRFATLNAAIRLQRHDL 325
Cdd:PRK10027 260 -------AARNLNALAPLinefnSPQCMLCTDDRNPWEIAHEGHIDALIRRLIEqHNVPLHVAYRVASWSTARHFGLNHL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 326 GLIAAGRRADLVVFDSLEKLVAREVYIGGKLLARAGNLLTPIAPAAGVTPP-RDTLQIAPLRADDFILRV-QGIRHGIAR 403
Cdd:PRK10027 333 GLLAPGKQADIVLLSDARKVTVQQVLVKGEPIDAQTLQAEESARLAQSAPPyGNTIARQPVSASDFALQFtPGKRYRVID 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 404 LRH---IRGARFTQWgevevqvrDGKVQLPAGFSLIWVKHRHGrHQATPQIALLEGWGELRGAIATSYSHDSHNLVVLGR 480
Cdd:PRK10027 413 VIHnelITHSRSSVY--------SENGFDRDDVCFIAVLERYG-QRLAPACGLLGGFGLNEGALAATVSHDSHNIVVIGR 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1790602168 481 DANDMALAANQLIASGGGMALAQQGEILAHVAMPIAGMLSDLPAAELARQFRELR 535
Cdd:PRK10027 484 SAEEMALAVNQVIQDGGGLCVVRNGQVQSHLPLPIAGLMSTDTAQSLAEQIDALK 538
|
|
| Adenine_deam_C |
pfam13382 |
Adenine deaminase C-terminal domain; This family represents a C-terminal region of the adenine ... |
412-579 |
9.11e-48 |
|
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: 164.54 E-value: 9.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 412 FTQWGEVEVQVRDGKVQ--LPAGFSLIWVKHRHGRHQaTPQIALLEGWGELRGAIATSYSHDSHNLVVLGRDANDMALAA 489
Cdd:pfam13382 2 ITKELEVELPVKDGVVVpdPERDILKIAVVERHGGTG-NIGVGFVKGFGLKRGAIASSVAHDSHNIIVVGTNDEDMALAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 490 NQLIASGGGMALAQQGEILAHVAMPIAGMLSDLPAAELARQFRELRDLSSQ--VADWEPpyrvFKAIEGTCLACNAGPHL 567
Cdd:pfam13382 81 NRLIEMGGGIVVVKDGKVLAELPLPIAGLMSDLPAEEVAEKLEELNAALRElgCELDDP----FMTLSFLALPVIPELKI 156
|
170
....*....|..
gi 1790602168 568 TDLGLTDGGSRQ 579
Cdd:pfam13382 157 TDKGLVDVKKFK 168
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
22-360 |
5.41e-26 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 110.05 E-value: 5.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 22 DLLLIDAQIVDMATGEIRA-ADVGIVGEMIASVHPRGSRE--DAHEVRSLAGGYLSPGLMDTHVHLessHLPPERYAEIV 98
Cdd:COG1228 9 TLLITNATLVDGTGGGVIEnGTVLVEDGKIAAVGPAADLAvpAGAEVIDATGKTVLPGLIDAHTHL---GLGGGRAVEFE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 99 LTQGTTAVFWDPHELANVL----------------GVAGVRYAVDASRhlplQVMVAAPSSVPSTPGLEMSGADFAGAEM 162
Cdd:COG1228 86 AGGGITPTVDLVNPADKRLrralaagvttvrdlpgGPLGLRDAIIAGE----SKLLPGPRVLAAGPALSLTGGAHARGPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 163 ETMLGWPEV--RGV--AEVMDMHGVLHGS-ERMQEIVQAGLNSGKLIEGHARGLSGADLQayLAAGVTS-DHELTSADDA 236
Cdd:COG1228 162 EARAALRELlaEGAdyIKVFAEGGAPDFSlEELRAILEAAHALGLPVAAHAHQADDIRLA--VEAGVDSiEHGTYLDDEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 237 LEKLRA-GLTieirgshpYLLPDIVAALKTLPHLSSQITVCTDDV------PPDILLEKGGIIAL--------------- 294
Cdd:COG1228 240 ADLLAEaGTV--------VLVPTLSLFLALLEGAAAPVAAKARKVreaalaNARRLHDAGVPVALgtdagvgvppgrslh 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1790602168 295 --LNLLIEHGLPAVDALRFATLNAAIRLQR-HDLGLIAAGRRADLVVFD--SLEKLVARE----VYIGGKLLARA 360
Cdd:COG1228 312 reLALAVEAGLTPEEALRAATINAAKALGLdDDVGSLEPGKLADLVLLDgdPLEDIAYLEdvraVMKDGRVVDRS 386
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
72-357 |
5.17e-17 |
|
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: 82.55 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 72 YLSPGLMDTHVHLESSHLP----PERYAEIVLTQGTTAVFWDPHELANVLGVAGVRYAV---DASRHLPLQVMVAAPSSV 144
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRgipvPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEallEAAEELPLGLRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 145 PSTPGlemSGADFAG------AEMETMLGWPEVRGVAEVMDmHGVLH-GSERMQEIVQAGLNSGKLIEGHArgLSGADLQ 217
Cdd:pfam01979 81 LDTDG---ELEGRKAlreklkAGAEFIKGMADGVVFVGLAP-HGAPTfSDDELKAALEEAKKYGLPVAIHA--LETKGEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 218 AYLAAGVTSDHELTSADDALEKLRAGLTIEIRGSHPYLLPDI---------------------------VAALKTLPHLS 270
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLSPTeanllaehlkgagvahcpfsnsklrsgRIALRKALEDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 271 SQITVCTDDVP----PDILLEkGGIIALLNLLIEHGLPAVDALRFATLNAAIRLQR-HDLGLIAAGRRADLVVFD--SLE 343
Cdd:pfam01979 235 VKVGLGTDGAGsgnsLNMLEE-LRLALELQFDPEGGLSPLEALRMATINPAKALGLdDKVGSIEVGKDADLVVVDldPLA 313
|
330 340
....*....|....*....|.
gi 1790602168 344 KLVARE-------VYIGGKLL 357
Cdd:pfam01979 314 AFFGLKpdgnvkkVIVKGKIV 334
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
22-106 |
4.37e-09 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 58.64 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 22 DLLLIDAQIVDMATGEIRAADVGIVGEMIASVHPRGSREDAHEVRSLAGGYLSPGLMDTHVH----LESSHLPPEryaEI 97
Cdd:COG3964 1 DLLIKGGRVIDPANGIDGVMDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTHvfpgGTDYGVDPD---GV 77
|
....*....
gi 1790602168 98 VLTQGTTAV 106
Cdd:COG3964 78 GVRSGVTTV 86
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
293-355 |
1.02e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 54.33 E-value: 1.02e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1790602168 293 ALLNLLIEHGLPAVDALRFATLNAAIRLQRHD-LGLIAAGRRADLVVFDslEKLVAREVYIGGK 355
Cdd:COG1820 312 AVRNLVEWTGLPLEEAVRMASLNPARALGLDDrKGSIAPGKDADLVVLD--DDLNVRATWVGGE 373
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
71-340 |
1.05e-07 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 54.66 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 71 GYLSPGLMDTHVHLESshlpperyaeivltQGTTAVFWDPHElanvlGVAGVRYAVD-----ASRHLPLQVMVAAPSSVP 145
Cdd:PRK06151 156 VYLGPAYRSGGSVLEA--------------DGSLEVVFDEAR-----GLAGLEEAIAfikrvDGAHNGLVRGMLAPDRIE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 146 S-TPGLEMSGADFAGAemetmLGWPeVR-----GVAEVMDMHgVLHGSERMQEIVQAGLNSGKLIEGHARGLSG------ 213
Cdd:PRK06151 217 TcTVDLLRRTAAAARE-----LGCP-VRlhcaqGVLEVETVR-RLHGTTPLEWLADVGLLGPRLLIPHATYISGsprlny 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 214 ---ADLQAYLAAGVTSDH-ELTSAddaleklRAGltieirgshpyllpDIVAALKTLPHLSSQITVCTDDVPPDILLekG 289
Cdd:PRK06151 290 sggDDLALLAEHGVSIVHcPLVSA-------RHG--------------SALNSFDRYREAGINLALGTDTFPPDMVM--N 346
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1790602168 290 GIIAL-LNLLIEHGLPAV---DALRFATLNAAIRLQRHDLGLIAAGRRADLVVFD 340
Cdd:PRK06151 347 MRVGLiLGRVVEGDLDAAsaaDLFDAATLGGARALGRDDLGRLAPGAKADIVVFD 401
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
24-85 |
6.05e-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: 52.02 E-value: 6.05e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1790602168 24 LLIDAQIVDmaTGEIRAADVGIVGEMIASVHPRGSREDAHEVRSLAGGYLSPGLMDTHVHLE 85
Cdd:COG0044 1 LIKNGRVVD--PGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLR 60
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
23-83 |
7.19e-07 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 51.77 E-value: 7.19e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1790602168 23 LLLIDAQIVDMATGEIRAADVGIVGEMIASVHPRGSREDAHEVRSLAGGYLSPGLMDTHVH 83
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
22-84 |
8.42e-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: 51.52 E-value: 8.42e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1790602168 22 DLLLIDAQIVdmATGEIRAADVGIVGEMIASVHPRGSREDAHEVRSLAGGYLSPGLMDTHVHL 84
Cdd:cd01315 1 DLVIKNGRVV--TPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHI 61
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
22-340 |
6.86e-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: 48.83 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 22 DLLLIDAQIVDMATGEIRAADVGIVGEMIASVHPrGSREDAHEVRSLAGGYLSPGLMDTHVH-----LESSHLPPEryae 96
Cdd:cd01297 1 DLVIRNGTVVDGTGAPPFTADVGIRDGRIAAIGP-ILSTSAREVIDAAGLVVAPGFIDVHTHydgqvFWDPDLRPS---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 97 ivLTQGTTAVfwdphelanVLGVAGVRYAVDASRhlplqvMVAAPSSVPSTPGLEMSGADFAGAEMETMLGWPEVRGVA- 175
Cdd:cd01297 76 --SRQGVTTV---------VLGNCGVSPAPANPD------DLARLIMLMEGLVALGEGLPWGWATFAEYLDALEARPPAv 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 176 -------------EVMDMHGVLHGSE---RMQEIVQAGLNSGKLieGHARGLS-----GADLQAYLA--------AGVTS 226
Cdd:cd01297 139 nvaalvghaalrrAVMGLDAREATEEelaKMRELLREALEAGAL--GISTGLAyaprlYAGTAELVAlarvaaryGGVYQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 227 DH---ELTSADDALEKL-----RAGLTIEI----------RGSHPYLLPDIVAALK-------------------TLPHL 269
Cdd:cd01297 217 THvryEGDSILEALDELlrlgrETGRPVHIshlksagapnWGKIDRLLALIEAARAeglqvtadvypygagseddVRRIM 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1790602168 270 SSQIT-VCTDDVPPDIllEKGGIIALLNLLIEH------GLPAVDALRFATLNAAIRLQRHDLGLIAAGRRADLVVFD 340
Cdd:cd01297 297 AHPVVmGGSDGGALGK--PHPRSYGDFTRVLGHyvrerkLLSLEEAVRKMTGLPARVFGLADRGRIAPGYRADIVVFD 372
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
23-107 |
7.87e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 48.34 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 23 LLLIDAQIVDMatGEIRAADVGIVGEMIASVHPRGSREDAHEVRSLAGGYLSPGLMDTHVH----LESSHLPPERYAEIV 98
Cdd:cd00854 1 LIIKNARILTP--GGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHggggADFMDGTAEALKTIA 78
|
90
....*....|..
gi 1790602168 99 ---LTQGTTAVF 107
Cdd:cd00854 79 ealAKHGTTSFL 90
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
22-361 |
1.71e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 47.23 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 22 DLLLIDAQIVDMAtgeirAADVGIVGEMIASVHPRGSREDAHEVRSLAGGYLSPGLMDTHVHLESSHL------------ 89
Cdd:PRK05985 3 DLLFRNVRPAGGA-----AVDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWgdpwypnepgps 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 90 ----------------PP-----ERYAEIVLTQGTTA----VFWDP-HELANVLGVAGVRyavDASRHLPLQVMVAAPSS 143
Cdd:PRK05985 78 lrerianerrrraasgHPaaeraLALARAAAAAGTTAmrshVDVDPdAGLRHLEAVLAAR---ETLRGLIDIQIVAFPQS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 144 -VPSTPGLE--MSGADFAGAEM------ETMLGWPE-----VRGVAEvmdMHGV-----LH-----GSERMQEIVQ---- 195
Cdd:PRK05985 155 gVLSRPGTAelLDAALRAGADVvggldpAGIDGDPEgqldiVFGLAE---RHGVgidihLHepgelGAFQLERIAArtra 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 196 AGLnSGKLIEGHARGLsgadlqaylaaGVTSDHELTSADDALEKLRAGLTIEIRGSHPYlLPdiVAALKtlphlSSQITV 275
Cdd:PRK05985 232 LGM-QGRVAVSHAFCL-----------GDLPEREVDRLAERLAEAGVAIMTNAPGSVPV-PP--VAALR-----AAGVTV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 276 CT--DDV-----P---PDiLLEKGGIIAL-LNLLIEHGLPAvdALRFATLNAAIRLQRHDLGLiAAGRRADLVVFDSL-- 342
Cdd:PRK05985 292 FGgnDGIrdtwwPygnGD-MLERAMLIGYrSGFRTDDELAA--ALDCVTHGGARALGLEDYGL-AVGARADFVLVDAEtv 367
|
410 420
....*....|....*....|....
gi 1790602168 343 -EKLVA----REVYIGGKLLARAG 361
Cdd:PRK05985 368 aEAVVAvpvrRLVVRGGRIVARDG 391
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
22-359 |
2.23e-05 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 47.13 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 22 DLLLIDAQIVDM--ATGEIRAADVGIVGEMIASVHPRGS---REDAHEVRSLAGGYLSPGLMDTHVHLESSHL------- 89
Cdd:COG0402 1 DLLIRGAWVLTMdpAGGVLEDGAVLVEDGRIAAVGPGAElpaRYPAAEVIDAGGKLVLPGLVNTHTHLPQTLLrgladdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 90 -----------PPER--------------YAEIVLTqGTTAVF-------WDPHELANVLGVAGVR-------------- 123
Cdd:COG0402 81 plldwleeyiwPLEArldpedvyagallaLAEMLRS-GTTTVAdfyyvhpESADALAEAAAEAGIRavlgrglmdrgfpd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 124 -YAVDASRHL---------------PLQVMVAAPSSVPSTPGLEMSGAdfagAEMETMLGWP------EVRG-VAEVMDM 180
Cdd:COG0402 160 gLREDADEGLadserlierwhgaadGRIRVALAPHAPYTVSPELLRAA----AALARELGLPlhthlaETRDeVEWVLEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 181 HGVlHGSERMQEIvqaGLNSGKLIEGHARGLSGADLQAYLAAGVTSDH----ELTSAD---DALEKLRAGLTI----EIR 249
Cdd:COG0402 236 YGK-RPVEYLDEL---GLLGPRTLLAHCVHLTDEEIALLAETGASVAHcptsNLKLGSgiaPVPRLLAAGVRVglgtDGA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 250 GSHPYLlpDIVAALKTLphlssqitvctddvppdillekgGIIALLNLLIEHGLPAVDALRFATLNAAIRLQR-HDLGLI 328
Cdd:COG0402 312 ASNNSL--DMFEEMRLA-----------------------ALLQRLRGGDPTALSAREALEMATLGGARALGLdDEIGSL 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1790602168 329 AAGRRADLVVFDS-----------LEKLV-------AREVYIGGKLLAR 359
Cdd:COG0402 367 EPGKRADLVVLDLdaphlaplhdpLSALVyaadgrdVRTVWVAGRVVVR 415
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
302-354 |
3.23e-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: 46.42 E-value: 3.23e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1790602168 302 GLPAVDALRFATLNAAIRLQ-RHDLGLIAAGRRADLVVFDslEKLVAREVYIGG 354
Cdd:cd00854 323 GCPLEEAVRMASLNPAKLLGlDDRKGSLKPGKDADLVVLD--DDLNVKATWING 374
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
68-340 |
5.08e-05 |
|
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: 45.75 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 68 LAGGYLSPGLMDTHVHL--------ESSHLPPE-------RYAEIVLTQGTTAVFwdphelaNVLGV--AGVRYAVDASr 130
Cdd:cd01299 6 LGGKTLMPGLIDAHTHLgsdpgdlpLDLALPVEyrtiratRQARAALRAGFTTVR-------DAGGAdyGLLRDAIDAG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 131 hlplqvMVAAPSSVPSTPGLEMSG--ADFAGAEMETMLGW--------PEVR-GVAEVM--------------------D 179
Cdd:cd01299 78 ------LIPGPRVFASGRALSQTGghGDPRGLSGLFPAGGlaavvdgvEEVRaAVREQLrrgadqikimatggvlspgdP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 180 MHGVLHGSERMQEIVQAGLNSGKLIEGHARGLSGAdLQAyLAAGVTS-DH-ELTSADDALEKLRAGLtieirgshpYLLP 257
Cdd:cd01299 152 PPDTQFSEEELRAIVDEAHKAGLYVAAHAYGAEAI-RRA-IRAGVDTiEHgFLIDDETIELMKEKGI---------FLVP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 258 DIvAALKTLPHLSSQITVCTDDVPPDILLEKGGIIAL-----------------------------LNLLIEHGLPAVDA 308
Cdd:cd01299 221 TL-ATYEALAAEGAAPGLPADSAEKVALVLEAGRDALrrahkagvkiafgtdagfpvpphgwnareLELLVKAGGTPAEA 299
|
330 340 350
....*....|....*....|....*....|...
gi 1790602168 309 LRFATLNAAIRLQR-HDLGLIAAGRRADLVVFD 340
Cdd:cd01299 300 LRAATANAAELLGLsDELGVIEAGKLADLLVVD 332
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
21-84 |
6.53e-05 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 45.85 E-value: 6.53e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1790602168 21 FDLLLIDAQIVdmATGEIRAADVGIVGEMIASVHPrGSREDAHEVRSLAGGYLSPGLMDTHVHL 84
Cdd:PRK06189 3 YDLIIRGGKVV--TPEGVYRADIGIKNGKIAEIAP-EISSPAREIIDADGLYVFPGMIDVHVHF 63
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
303-340 |
6.77e-05 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 45.66 E-value: 6.77e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1790602168 303 LPAVDALRFATLNAAIRLQRHDLGLIAAGRRADLVVFD 340
Cdd:cd01298 332 LPAEEALEMATIGGAKALGLDEIGSLEVGKKADLILID 369
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
193-341 |
9.00e-05 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 44.94 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 193 IVQAGLNSGKLIEGHARGLS---GADLQAYLAAgVTSDHELTSADDALEKLRAGLTIEIrgshpyLLPDIVAALK-TLPh 268
Cdd:cd01296 198 ILEAAKEAGLPVKIHADELSnigGAELAAELGA-LSADHLEHTSDEGIAALAEAGTVAV------LLPGTAFSLReTYP- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 269 lssqitvctddvPPDILLEKGGIIAL---LN---------LLIEH------GLPAVDALRFATLNAAIRLQR-HDLGLIA 329
Cdd:cd01296 270 ------------PARKLIDAGVPVALgtdFNpgssptssmPLVMHlacrlmRMTPEEALTAATINAAAALGLgETVGSLE 337
|
170
....*....|..
gi 1790602168 330 AGRRADLVVFDS 341
Cdd:cd01296 338 VGKQADLVILDA 349
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
24-83 |
9.02e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 45.09 E-value: 9.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 24 LLIDAQIVDmATGEIRAADVGIVGEMIASVHPRGsrEDAHEVRSLAGGYLSPGLMDTHVH 83
Cdd:COG1820 1 AITNARIFT-GDGVLEDGALLIEDGRIAAIGPGA--EPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
79-317 |
2.03e-04 |
|
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: 43.48 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 79 DTHVHLESSHLPPERYAEIVLT----------------------QGTTAVFWDPHELANVLGVAGVRYAVDASRHLPLQV 136
Cdd:cd01292 3 DTHVHLDGSALRGTRLNLELKEaeelspedlyedtlraleallaGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAGIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 137 MVAAPSSVPSTPGLEMSGADFAGAEMETMLGWPeVRGVAEVMDMHGVLHGSERMQEIVQAGLNSGKLIEGHARGLSGA-- 214
Cdd:cd01292 83 VVLGLGIPGVPAAVDEDAEALLLELLRRGLELG-AVGLKLAGPYTATGLSDESLRRVLEEARKLGLPVVIHAGELPDPtr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 215 ---DLQAYLAAG--VTSDHELTSADDALEKLR-AGLTIEIRGSHPYLLPDIVAALKTLPHL---SSQITVCTDDVPPDIL 285
Cdd:cd01292 162 aleDLVALLRLGgrVVIGHVSHLDPELLELLKeAGVSLEVCPLSNYLLGRDGEGAEALRRLlelGIRVTLGTDGPPHPLG 241
|
250 260 270
....*....|....*....|....*....|..
gi 1790602168 286 LEKGGIIALLNLLIEHGLPAVDALRFATLNAA 317
Cdd:cd01292 242 TDLLALLRLLLKVLRLGLSLEEALRLATINPA 273
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
300-361 |
3.41e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 43.24 E-value: 3.41e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1790602168 300 EHGLPAVDALRFATLNAAIRLQRHDLGLIAAGRRADLVVFDSLEKL-VAREVYIGGKLLARAG 361
Cdd:PRK15446 321 DGGLDLPQAVALVTANPARAAGLDDRGEIAPGKRADLVRVRRAGGLpVVRAVWRGGRRVFLAG 383
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
285-356 |
7.40e-04 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 42.30 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 285 LLEKGGI------------IALLNLL----IEHGLPAVDALRFATLNAAIRLQRHD-LGLIAAGRRADLVVFD----SLE 343
Cdd:cd01309 266 LLKKGGVafaissdhpvlnIRNLNLEaakaVKYGLSYEEALKAITINPAKILGIEDrVGSLEPGKDADLVVWNgdplEPT 345
|
90
....*....|...
gi 1790602168 344 KLVAReVYIGGKL 356
Cdd:cd01309 346 SKPEQ-VYIDGRL 357
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
303-365 |
7.92e-04 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 42.15 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 303 LPAVDALRFATLNAAIRLQRHDLGLIAAGRRADLVVF-----------DSLEKLV------AREVYIGGKLLARAGNLLT 365
Cdd:PRK08203 351 MTAREALEWATLGGARVLGRDDIGSLAPGKLADLALFdldelrfagahDPVAALVlcgpprADRVMVGGRWVVRDGQLTT 430
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
36-105 |
1.01e-03 |
|
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: 41.66 E-value: 1.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 36 GEIRAADVGIVGEMIASVHPRGSREDAhEVRSLAGGYLSPGLMDTHVHLESshlPPERYAEIVLTqGTTA 105
Cdd:TIGR00857 1 GKETEVDILVEGGRIKKIGKLRIPPDA-EVIDAKGLLVLPGFIDLHVHLRD---PGEEYKEDIES-GSKA 65
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
34-89 |
1.02e-03 |
|
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: 41.85 E-value: 1.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1790602168 34 ATGEIRAADVGIVGEMIASVHPRGSREDAHEVRSLAGGYLSPGLMDTHVHLESSHL 89
Cdd:cd01293 8 ADGGTALVDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLDKTFT 63
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
23-83 |
1.43e-03 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 41.39 E-value: 1.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1790602168 23 LLLIDAQIVDmaTGEIRAADVGIVGEMIASVHPRGSREDAHEVRSLAGGYLSPGLMDTHVH 83
Cdd:PRK09236 4 ILIKNARIVN--EGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVH 62
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
303-365 |
1.49e-03 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 41.44 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 303 LPAVDALRFATLNAAIRLQR-HDLGLIAAGRRADLV-----------VFDSLEKLV-------AREVYIGGKLLARAGNL 363
Cdd:PRK09045 340 LPAHTALRMATLNGARALGLdDEIGSLEPGKQADLVavdlsgletqpVYDPVSQLVyaagreqVSHVWVAGKQLLDDREL 419
|
..
gi 1790602168 364 LT 365
Cdd:PRK09045 420 TT 421
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
22-84 |
2.17e-03 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 40.75 E-value: 2.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1790602168 22 DLLLIDAQIVDM-ATGEIRAADVGIVGEMIASVHPRGSREDAHEVRSLAGGYLSPGLMDTHVHL 84
Cdd:PRK07228 2 TILIKNAGIVTMnAKREIVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHL 65
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
22-84 |
2.21e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 40.89 E-value: 2.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1790602168 22 DLLLIDAQIVDMATGEIRAADVGIVGEMIASVhPRGSREDAHEVRSLAGGYLSPGLMDTHVHL 84
Cdd:PRK06038 3 DIIIKNAYVLTMDAGDLKKGSVVIEDGTITEV-SESTPGDADTVIDAKGSVVMPGLVNTHTHA 64
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
21-87 |
2.96e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 40.39 E-value: 2.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1790602168 21 FDLLLIDAQIVDMATGeiraADVGIVGEMIASVHPrGSREDAHEVRSLAGGYLSPGLMDTHVHLESS 87
Cdd:PRK07572 2 FDLIVRNANLPDGRTG----IDIGIAGGRIAAVEP-GLQAEAAEEIDAAGRLVSPPFVDPHFHMDAT 63
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
21-85 |
3.40e-03 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 40.16 E-value: 3.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1790602168 21 FDLLLIDAQIVDmATGEIRAaDVGIVGEMIASV-HPRGSRE-DAHevrslaGGYLSPGLMDTHVHLE 85
Cdd:PRK08323 1 MSTLIKNGTVVT-ADDTYKA-DVLIEDGKIAAIgANLGDEViDAT------GKYVMPGGIDPHTHME 59
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
24-84 |
4.43e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 39.99 E-value: 4.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1790602168 24 LLIDAQIVDM--ATGEIRAADVGIVGEMIASVHPRGSREDAhEVRSLAGGYLSPGLMDTHVHL 84
Cdd:PRK08204 5 LIRGGTVLTMdpAIGDLPRGDILIEGDRIAAVAPSIEAPDA-EVVDARGMIVMPGLVDTHRHT 66
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
23-86 |
6.05e-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: 39.51 E-value: 6.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1790602168 23 LLLIDAQIVDmATGEIRAaDVGIVGEMIASVHPRGSREDAHEVRSLAGGYLSPGLMDTHVHLES 86
Cdd:cd01314 1 LIIKNGTIVT-ADGSFKA-DILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLEL 62
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
230-344 |
6.08e-03 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 39.14 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790602168 230 LTSADDAlEKLRAGL---TIeirgshpyllpDIVAALKTlPHLSSQITVCTDDVPPdillekgGIIAL-------LNLLI 299
Cdd:cd01317 241 LRSEEDR-EALIEALkdgTI-----------DAIASDHA-PHTDEEKDLPFAEAPP-------GIIGLetalpllWTLLV 300
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1790602168 300 EHG-LPAVDALRFATLNAAiRLQRHDLGLIAAGRRADLVVFDSLEK 344
Cdd:cd01317 301 KGGlLTLPDLIRALSTNPA-KILGLPPGRLEVGAPADLVLFDPDAE 345
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
18-85 |
6.80e-03 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 39.30 E-value: 6.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1790602168 18 ESPFDLLLIDAQIVdmATGEIRAADVGIVGEMIASVH---PRGSRE-DAhevrslAGGYLSPGLMDTHVHLE 85
Cdd:PRK13404 1 MMAFDLVIRGGTVV--TATDTFQADIGIRGGRIAALGeglGPGAREiDA------TGRLVLPGGVDSHCHID 64
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
20-84 |
8.85e-03 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 38.75 E-value: 8.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1790602168 20 PFDLLLIDAQIVDMAtGEIRAaDVGIVGEMIASVHpRGSREDAHEVRSLAGGYLSPGLMDTHVHL 84
Cdd:PRK09060 4 TFDLILKGGTVVNPD-GEGRA-DIGIRDGRIAAIG-DLSGASAGEVIDCRGLHVLPGVIDSQVHF 65
|
|
| |
