|
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: 693.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 17 GESPFDLLLIDAQIVDMATGEIRPADVGIVGEMIASVHPRgsREDAHEVRSMAGGYLSPGLMDTHVHLESSHLPPERYAE 96
Cdd:COG1001 1 GREPADLVIKNGRLVNVFTGEILEGDIAIAGGRIAGVGDY--IGEATEVIDAAGRYLVPGFIDGHVHIESSMVTPAEFAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 97 IVLTQGTTAVFWDPHELANVLGVAGVRYAVDASRHLPLQVMVAAPSSVPSTPGLEMSGADFAGAEMETMLGWPEVRGVAE 176
Cdd:COG1001 79 AVLPHGTTTVIADPHEIANVLGLEGVRYMLEAAEGLPLDIFVMLPSCVPATPGLETAGAVLGAEDLAELLDHPRVIGLGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 177 VMDMHGVLHGSERMQEIVQAGLNSGKLIEGHARGLSGADLQAYLAAGVTSDHELTSADDALEKLRAGLTIEIR-GSHPYL 255
Cdd:COG1001 159 VMNFPGVLNGDPRMLAKIAAALAAGKVIDGHAPGLSGKDLNAYAAAGIRSDHECTTAEEALEKLRRGMYVMIReGSAAKD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 256 LPDIVAALKtlPHLSSQITVCTDDVPPDILLEKGGIIALLNLLIEHGLPAVDALRFATLNAAIRLQRHDLGLIAAGRRAD 335
Cdd:COG1001 239 LPALLPAVT--ELNSRRCALCTDDRHPDDLLEEGHIDHVVRRAIELGLDPVTAIQMATLNAAEHFGLKDLGAIAPGRRAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 336 LVVFDSLEKLVAREVYVGGKLLARAGNLLTPIAPAAGVTPPRDTLQIAPLRADDFILRVQGIrhGIAR-LRHIRGARFTQ 414
Cdd:COG1001 317 IVLLDDLEDFKVEKVYADGKLVAEDGKLLVDLPKYPYPPWARNTVKLRPLTAEDFAIPAPGG--VKVRvIGVIPGQIITE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 415 WGEVEVQVRDGKVQLPA--GFSLIWVKHRHGRhQATPQIALLEGWGELRGAIATSYSHDSHNLVVLGRDANDMALAANQL 492
Cdd:COG1001 395 HLEAELPVEDGEVVPDPerDILKIAVVERHGG-TGNIGLGFVKGFGLKRGAIASTVAHDSHNLIVVGTNDEDMALAANRL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 493 IASGGGMALAQQGEILAHVAMPIAGMLSDLPAAELARQFRELRDLSSQV-ADWEPPYRvfkAIEGTCLACNAGPHLTDLG 571
Cdd:COG1001 474 IEIGGGIVVVKDGKVLAELPLPIAGLMSDEPAEEVAEKLEALRAAARELgCTLEEPFM---TLSFLALPVIPELKLTDRG 550
|
....*....
gi 1031822267 572 LTDGGSRQI 580
Cdd:COG1001 551 LVDVTTFEF 559
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
69-574 |
4.60e-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: 415.85 E-value: 4.60e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 69 AGGYLSPGLMDTHVHLESSHLPPERYAEIVLTQGTTAVFWDPHELANVLGVAGVRYAVDASRHLPLQVMVAAPSSVPSTP 148
Cdd:cd01295 3 EGKYIVPGFIDAHLHIESSMLTPSEFAKAVLPHGTTTVIADPHEIANVAGVDGIEFMLEDAKKTPLDIFWMLPSCVPATP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 149 GlEMSGADFAGAEMETMLGWPEVRGVAEVMDMHGVLHGSERMQEIVQAGLNSGKLIEGHARGLSGADLQAYLAAGVTSDH 228
Cdd:cd01295 83 F-ETSGAELTAEDIKELLEHPEVVGLGEVMDFPGVIEGDDEMLAKIQAAKKAGKPVDGHAPGLSGEELNAYMAAGISTDH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 229 ELTSADDALEKLRAGLTIEIRGSHPylLPDIVAALKTLPH-LSSQITVCTDDVPPDILLEKGGIIALLNLLIEHGLPAVD 307
Cdd:cd01295 162 EAMTGEEALEKLRLGMYVMLREGSI--AKNLEALLPAITEkNFRRFMFCTDDVHPDDLLSEGHLDYIVRRAIEAGIPPED 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 308 ALRFATLNAAIRLQRHDLGLIAAGRRADLVVFDSLEKLVAREVYVGGkllaragnlltpiapaagvtpprdtlqiaplra 387
Cdd:cd01295 240 AIQMATINPAECYGLHDLGAIAPGRIADIVILDDLENFNITTVLAKG--------------------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 388 ddfilrvqgirhgiarlrhirgarftqwgevevqvrdgkvqlpagfslIWVKHRHGRHQATPqIALLEGWGELRGAIATS 467
Cdd:cd01295 287 ------------------------------------------------IAVVERHGKTGNIG-VGFVKGFGLKEGAIASS 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 468 YSHDSHNLVVLGRDANDMALAANQLIASGGGMALAQQGEILAHVAMPIAGMLSDLPAAELARQFRELRDLSSQVADW-EP 546
Cdd:cd01295 318 VAHDSHNIIVIGTNDEDMALAVNRLKEIGGGIVVVKNGKVLAELPLPIAGLMSDEPAEEVAEELKKLREALRELGYAlDD 397
|
490 500 510
....*....|....*....|....*....|
gi 1031822267 547 PYRVFKAIEGTCLacnagPHL--TDLGLTD 574
Cdd:cd01295 398 PFMTLSFLSLPVI-----PELkiTDKGLFD 422
|
|
| ade |
TIGR01178 |
adenine deaminase; The family described by this model includes an experimentally characterized ... |
22-582 |
6.27e-118 |
|
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: 361.40 E-value: 6.27e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 22 DLLLIDAQIVDMATGEIRPADVGIVGEMIASVhprgSREDAHEVRSMAGGYLSPGLMDTHVHLESSHLPPERYAEIVLTQ 101
Cdd:TIGR01178 1 DIVIKNAKIIDVYNGEIIPGDIAIANGHIAGV----GKYNGVKVIDALGEYAVPGFIDAHIHIESSMLTPSEFAKLVLPH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 102 GTTAVFWDPHELANVLGVAGVRYAVDASRHLPLQVMVAAPSSVPSTPgLEMSGADFAGAEMETMLGWPEVRGVAEVMDMH 181
Cdd:TIGR01178 77 GVTTVVSDPHEIANVNGEDGINFMLNNAKKTPLNFYFMLPSCVPALQ-FETSGAVLTAEDIDELMELDEVLGLAEVMDYP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 182 GVLHGSERMQEIVQAGLNSGKLIEGHARGLSGADLQAYLAAGVTSDHELTSADDALEKLRAGLTIEIR-GShpyllpdiv 260
Cdd:TIGR01178 156 GVINADIEMLNKINSARKRNKVIDGHCPGLSGKLLNKYISAGISNDHESTSIEEAREKLRLGMKLMIReGS--------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 261 aALKTLPHL--------SSQITVCTDDVPPDILLEKGGIIALLNLLIEHGLPAVDALRFATLNAAIRLQRHDLGLIAAGR 332
Cdd:TIGR01178 227 -AAKNLEALhplineknCRSLMLCTDDRHVNDILNEGHINHIVRRAIEHGVDPFDALQMASINPAEHFGIDVGGLIAPGD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 333 RADLVVFDSLEKLVAREVYVGGKLLARAGNLLTPIAPAAGVTPPRDTLQI-APLRADDFILRVQGiRHGIARLRHIRGAR 411
Cdd:TIGR01178 306 PADFVILKDLRNFKVNKTYVKGKLLDLNEVFNDEISRIPLINEIPINVKArSPKSISDFGIQFKT-GNRIRVIKVISNQL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 412 FTQWGEVEVQvRDGKVQLPAGFSLIWVKHRHGRHQAtPQIALLEGWGELRGAIATSYSHDSHNLVVLGRDANDMALAANQ 491
Cdd:TIGR01178 385 ITHKTSNSVA-EEFGSDIEEDILKIAVIERHKDNGK-IGKGLIKGFGLKEGAIASTVAHDSHNIIAVGSNDEDLALAVNK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 492 LIASGGGMALAQQGEILAHVAMPIAGMLSDLPAAELARQFRELRDLSSQVAdwepPYRVFKAIEGTCLACNAGPHL--TD 569
Cdd:TIGR01178 463 LIQIGGGLCAAKNGEVTIILPLPIAGLMSDDSAERVAEQIIALNDKCRNVG----GSRDNPFLTLSFLSLPVIPHLkiTD 538
|
570
....*....|...
gi 1031822267 570 LGLTDGGSRQIVD 582
Cdd:TIGR01178 539 KGLFDVESFCFVD 551
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
15-535 |
5.00e-94 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 300.21 E-value: 5.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 15 ARGESPFDLLLIDAQIVDMATGEIRPADVGIVGEMIASVHPRGSREDAHEVRSMAGGYLSPGLMDTHVHLESSHLPPERY 94
Cdd:PRK10027 24 SRGDAVADYIIDNVSILDLINGGEISGPIVIKGRYIAGVGAEYADAPALQRIDARGATAVPGFIDAHLHIESSMMTPVTF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 95 AEIVLTQGTTAVFWDPHELANVLGVAGVRYAVDASRHLPLQVMVAAPSSVPSTPGLEMSGADFAGAEMETMLGWPEVRGV 174
Cdd:PRK10027 104 ETATLPRGLTTVICDPHEIVNVMGEAGFAWFARCAEQARQNQYLQVSSCVPALEGCDVNGASFTLEQMLAWRDHPQVTGL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 175 AEVMDMHGVLHGSERMQEIVQA--GLNsgklIEGHARGLSGADLQAYLAAGVTSDHELTSADDALEKLRAGLTIEIR-GS 251
Cdd:PRK10027 184 AEMMDYPGVISGQNALLDKLDAfrHLT----LDGHCPGLGGKELNAYIAAGIENCHESYQLEEGRRKLQLGMSLMIReGS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 252 hpyllpdIVAALKTLPHL-----SSQITVCTDDVPPDILLEKGGIIALLNLLIE-HGLPAVDALRFATLNAAIRLQRHDL 325
Cdd:PRK10027 260 -------AARNLNALAPLinefnSPQCMLCTDDRNPWEIAHEGHIDALIRRLIEqHNVPLHVAYRVASWSTARHFGLNHL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 326 GLIAAGRRADLVVFDSLEKLVAREVYVGGKLLARAGNLLTPIAPAAGVTPP-RDTLQIAPLRADDFILRV-QGIRHGIAR 403
Cdd:PRK10027 333 GLLAPGKQADIVLLSDARKVTVQQVLVKGEPIDAQTLQAEESARLAQSAPPyGNTIARQPVSASDFALQFtPGKRYRVID 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 404 LRH---IRGARFTQWgevevqvrDGKVQLPAGFSLIWVKHRHGrHQATPQIALLEGWGELRGAIATSYSHDSHNLVVLGR 480
Cdd:PRK10027 413 VIHnelITHSRSSVY--------SENGFDRDDVCFIAVLERYG-QRLAPACGLLGGFGLNEGALAATVSHDSHNIVVIGR 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1031822267 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 |
8.48e-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: 8.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 412 FTQWGEVEVQVRDGKVQ--LPAGFSLIWVKHRHGRHQaTPQIALLEGWGELRGAIATSYSHDSHNLVVLGRDANDMALAA 489
Cdd:pfam13382 2 ITKELEVELPVKDGVVVpdPERDILKIAVVERHGGTG-NIGVGFVKGFGLKRGAIASSVAHDSHNIIVVGTNDEDMALAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 490 NQLIASGGGMALAQQGEILAHVAMPIAGMLSDLPAAELARQFRELRDLSSQ--VADWEPpyrvFKAIEGTCLACNAGPHL 567
Cdd:pfam13382 81 NRLIEMGGGIVVVKDGKVLAELPLPIAGLMSDLPAEEVAEKLEELNAALRElgCELDDP----FMTLSFLALPVIPELKI 156
|
170
....*....|..
gi 1031822267 568 TDLGLTDGGSRQ 579
Cdd:pfam13382 157 TDKGLVDVKKFK 168
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
22-360 |
6.71e-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: 6.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 22 DLLLIDAQIVDMATGE-IRPADVGIVGEMIASVHPRGSRE--DAHEVRSMAGGYLSPGLMDTHVHLessHLPPERYAEIV 98
Cdd:COG1228 9 TLLITNATLVDGTGGGvIENGTVLVEDGKIAAVGPAADLAvpAGAEVIDATGKTVLPGLIDAHTHL---GLGGGRAVEFE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 99 LTQGTTAVFWDPHELANVL----------------GVAGVRYAVDASRhlplQVMVAAPSSVPSTPGLEMSGADFAGAEM 162
Cdd:COG1228 86 AGGGITPTVDLVNPADKRLrralaagvttvrdlpgGPLGLRDAIIAGE----SKLLPGPRVLAAGPALSLTGGAHARGPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 163 ETMLGWPEV--RGV--AEVMDMHGVLHGS-ERMQEIVQAGLNSGKLIEGHARGLSGADLQayLAAGVTS-DHELTSADDA 236
Cdd:COG1228 162 EARAALRELlaEGAdyIKVFAEGGAPDFSlEELRAILEAAHALGLPVAAHAHQADDIRLA--VEAGVDSiEHGTYLDDEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 237 LEKLRA-GLTieirgshpYLLPDIVAALKTLPHLSSQITVCTDDV------PPDILLEKGGIIAL--------------- 294
Cdd:COG1228 240 ADLLAEaGTV--------VLVPTLSLFLALLEGAAAPVAAKARKVreaalaNARRLHDAGVPVALgtdagvgvppgrslh 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1031822267 295 --LNLLIEHGLPAVDALRFATLNAAIRLQR-HDLGLIAAGRRADLVVFD--SLEKLVARE----VYVGGKLLARA 360
Cdd:COG1228 312 reLALAVEAGLTPEEALRAATINAAKALGLdDDVGSLEPGKLADLVLLDgdPLEDIAYLEdvraVMKDGRVVDRS 386
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
72-357 |
4.46e-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: 82.93 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 72 YLSPGLMDTHVHLESSHLP----PERYAEIVLTQGTTAVFWDPHELANVLGVAGVRYAV---DASRHLPLQVMVAAPSSV 144
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRgipvPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEallEAAEELPLGLRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 145 PSTPGlemSGADFAG------AEMETMLGWPEVRGVAEVMDmHGVLH-GSERMQEIVQAGLNSGKLIEGHArgLSGADLQ 217
Cdd:pfam01979 81 LDTDG---ELEGRKAlreklkAGAEFIKGMADGVVFVGLAP-HGAPTfSDDELKAALEEAKKYGLPVAIHA--LETKGEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 218 AYLAAGVTSDHELTSADDALEKLRAGLTIEIRGSHPYLLPDI---------------------------VAALKTLPHLS 270
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLSPTeanllaehlkgagvahcpfsnsklrsgRIALRKALEDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 271 SQITVCTDDVP----PDILLEkGGIIALLNLLIEHGLPAVDALRFATLNAAIRLQR-HDLGLIAAGRRADLVVFD--SLE 343
Cdd:pfam01979 235 VKVGLGTDGAGsgnsLNMLEE-LRLALELQFDPEGGLSPLEALRMATINPAKALGLdDKVGSIEVGKDADLVVVDldPLA 313
|
330 340
....*....|....*....|.
gi 1031822267 344 KLVARE-------VYVGGKLL 357
Cdd:pfam01979 314 AFFGLKpdgnvkkVIVKGKIV 334
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
22-106 |
4.86e-09 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 58.64 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 22 DLLLIDAQIVDMATGEIRPADVGIVGEMIASVHPRGSREDAHEVRSMAGGYLSPGLMDTHVH----LESSHLPPEryaEI 97
Cdd:COG3964 1 DLLIKGGRVIDPANGIDGVMDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTHvfpgGTDYGVDPD---GV 77
|
....*....
gi 1031822267 98 VLTQGTTAV 106
Cdd:COG3964 78 GVRSGVTTV 86
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
50-340 |
4.73e-08 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 55.82 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 50 IASVHPRGSREDAHEVRSMAG--------GYLSPGLMDTHVHLESshlpperyaeivltQGTTAVFWDPHElanvlGVAG 121
Cdd:PRK06151 127 IASLFYRQWAETYAEFAAAAEaagrlglrVYLGPAYRSGGSVLEA--------------DGSLEVVFDEAR-----GLAG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 122 VRYAVD-----ASRHLPLQVMVAAPSSVPS-TPGLEMSGADFAGAemetmLGWPeVR-----GVAEVMDMHgVLHGSERM 190
Cdd:PRK06151 188 LEEAIAfikrvDGAHNGLVRGMLAPDRIETcTVDLLRRTAAAARE-----LGCP-VRlhcaqGVLEVETVR-RLHGTTPL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 191 QEIVQAGLNSGKLIEGHARGLSG---------ADLQAYLAAGVTSDH-ELTSAddaleklRAGltieirgshpyllpDIV 260
Cdd:PRK06151 261 EWLADVGLLGPRLLIPHATYISGsprlnysggDDLALLAEHGVSIVHcPLVSA-------RHG--------------SAL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 261 AALKTLPHLSSQITVCTDDVPPDILLekGGIIAL-LNLLIEHGLPAV---DALRFATLNAAIRLQRHDLGLIAAGRRADL 336
Cdd:PRK06151 320 NSFDRYREAGINLALGTDTFPPDMVM--NMRVGLiLGRVVEGDLDAAsaaDLFDAATLGGARALGRDDLGRLAPGAKADI 397
|
....
gi 1031822267 337 VVFD 340
Cdd:PRK06151 398 VVFD 401
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
293-355 |
7.62e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 54.72 E-value: 7.62e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031822267 293 ALLNLLIEHGLPAVDALRFATLNAAIRLQRHD-LGLIAAGRRADLVVFDslEKLVAREVYVGGK 355
Cdd:COG1820 312 AVRNLVEWTGLPLEEAVRMASLNPARALGLDDrKGSIAPGKDADLVVLD--DDLNVRATWVGGE 373
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
22-84 |
3.58e-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: 53.06 E-value: 3.58e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031822267 22 DLLLIDAQIVdmATGEIRPADVGIVGEMIASVHPRGSREDAHEVRSMAGGYLSPGLMDTHVHL 84
Cdd:cd01315 1 DLVIKNGRVV--TPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHI 61
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
23-83 |
5.62e-07 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 52.16 E-value: 5.62e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031822267 23 LLLIDAQIVDMATGEIRPADVGIVGEMIASVHPRGSREDAHEVRSMAGGYLSPGLMDTHVH 83
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
24-85 |
9.20e-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: 51.63 E-value: 9.20e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1031822267 24 LLIDAQIVDmaTGEIRPADVGIVGEMIASVHPRGSREDAHEVRSMAGGYLSPGLMDTHVHLE 85
Cdd:COG0044 1 LIKNGRVVD--PGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLR 60
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
23-107 |
1.33e-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: 47.57 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 23 LLLIDAQIVDMatGEIRPADVGIVGEMIASVHPRGSREDAHEVRSMAGGYLSPGLMDTHVH----LESSHLPPERYAEIV 98
Cdd:cd00854 1 LIIKNARILTP--GGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHggggADFMDGTAEALKTIA 78
|
90
....*....|..
gi 1031822267 99 ---LTQGTTAVF 107
Cdd:cd00854 79 ealAKHGTTSFL 90
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
22-361 |
1.79e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 47.23 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 22 DLLLIDAQIVDMAtgeirPADVGIVGEMIASVHPRGSREDAHEVRSMAGGYLSPGLMDTHVHLESSHL------------ 89
Cdd:PRK05985 3 DLLFRNVRPAGGA-----AVDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWgdpwypnepgps 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 90 ----------------PP-----ERYAEIVLTQGTTA----VFWDP-HELANVLGVAGVRyavDASRHLPLQVMVAAPSS 143
Cdd:PRK05985 78 lrerianerrrraasgHPaaeraLALARAAAAAGTTAmrshVDVDPdAGLRHLEAVLAAR---ETLRGLIDIQIVAFPQS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 144 -VPSTPGLE--MSGADFAGAEM------ETMLGWPE-----VRGVAEvmdMHGV-----LH-----GSERMQEIVQ---- 195
Cdd:PRK05985 155 gVLSRPGTAelLDAALRAGADVvggldpAGIDGDPEgqldiVFGLAE---RHGVgidihLHepgelGAFQLERIAArtra 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 196 AGLnSGKLIEGHARGLsgadlqaylaaGVTSDHELTSADDALEKLRAGLTIEIRGSHPYlLPdiVAALKtlphlSSQITV 275
Cdd:PRK05985 232 LGM-QGRVAVSHAFCL-----------GDLPEREVDRLAERLAEAGVAIMTNAPGSVPV-PP--VAALR-----AAGVTV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 276 CT--DDV-----P---PDiLLEKGGIIAL-LNLLIEHGLPAvdALRFATLNAAIRLQRHDLGLiAAGRRADLVVFDSL-- 342
Cdd:PRK05985 292 FGgnDGIrdtwwPygnGD-MLERAMLIGYrSGFRTDDELAA--ALDCVTHGGARALGLEDYGL-AVGARADFVLVDAEtv 367
|
410 420
....*....|....*....|....
gi 1031822267 343 -EKLVA----REVYVGGKLLARAG 361
Cdd:PRK05985 368 aEAVVAvpvrRLVVRGGRIVARDG 391
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
22-359 |
1.81e-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: 47.51 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 22 DLLLIDAQIVDM--ATGEIRPADVGIVGEMIASVHPRGS---REDAHEVRSMAGGYLSPGLMDTHVHLESSHL------- 89
Cdd:COG0402 1 DLLIRGAWVLTMdpAGGVLEDGAVLVEDGRIAAVGPGAElpaRYPAAEVIDAGGKLVLPGLVNTHTHLPQTLLrgladdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 90 -----------PPER--------------YAEIVLTqGTTAVF-------WDPHELANVLGVAGVR-------------- 123
Cdd:COG0402 81 plldwleeyiwPLEArldpedvyagallaLAEMLRS-GTTTVAdfyyvhpESADALAEAAAEAGIRavlgrglmdrgfpd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 124 -YAVDASRHL---------------PLQVMVAAPSSVPSTPGLEMSGAdfagAEMETMLGWP------EVRG-VAEVMDM 180
Cdd:COG0402 160 gLREDADEGLadserlierwhgaadGRIRVALAPHAPYTVSPELLRAA----AALARELGLPlhthlaETRDeVEWVLEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 181 HGVlHGSERMQEIvqaGLNSGKLIEGHARGLSGADLQAYLAAGVTSDH----ELTSAD---DALEKLRAGLTI----EIR 249
Cdd:COG0402 236 YGK-RPVEYLDEL---GLLGPRTLLAHCVHLTDEEIALLAETGASVAHcptsNLKLGSgiaPVPRLLAAGVRVglgtDGA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 250 GSHPYLlpDIVAALKTLphlssqitvctddvppdillekgGIIALLNLLIEHGLPAVDALRFATLNAAIRLQR-HDLGLI 328
Cdd:COG0402 312 ASNNSL--DMFEEMRLA-----------------------ALLQRLRGGDPTALSAREALEMATLGGARALGLdDEIGSL 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1031822267 329 AAGRRADLVVFDS-----------LEKLV-------AREVYVGGKLLAR 359
Cdd:COG0402 367 EPGKRADLVVLDLdaphlaplhdpLSALVyaadgrdVRTVWVAGRVVVR 415
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
22-340 |
3.15e-05 |
|
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: 46.52 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 22 DLLLIDAQIVDMATGEIRPADVGIVGEMIASVHPrGSREDAHEVRSMAGGYLSPGLMDTHVH-----LESSHLPPEryae 96
Cdd:cd01297 1 DLVIRNGTVVDGTGAPPFTADVGIRDGRIAAIGP-ILSTSAREVIDAAGLVVAPGFIDVHTHydgqvFWDPDLRPS---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 97 ivLTQGTTAVfwdphelanVLGVAGVRYAVDASRhlplqvMVAAPSSVPSTPGLEMSGADFAGAEMETMLGWPEVRGVA- 175
Cdd:cd01297 76 --SRQGVTTV---------VLGNCGVSPAPANPD------DLARLIMLMEGLVALGEGLPWGWATFAEYLDALEARPPAv 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 176 -------------EVMDMHGVLHGSE---RMQEIVQAGLNSGKLieGHARGLS-----GADLQAYLA--------AGVTS 226
Cdd:cd01297 139 nvaalvghaalrrAVMGLDAREATEEelaKMRELLREALEAGAL--GISTGLAyaprlYAGTAELVAlarvaaryGGVYQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 227 DH---ELTSADDALEKL-----RAGLTIEI----------RGSHPYLLPDIVAALK-------------------TLPHL 269
Cdd:cd01297 217 THvryEGDSILEALDELlrlgrETGRPVHIshlksagapnWGKIDRLLALIEAARAeglqvtadvypygagseddVRRIM 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1031822267 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 ... |
302-354 |
5.05e-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: 46.03 E-value: 5.05e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1031822267 302 GLPAVDALRFATLNAAIRLQ-RHDLGLIAAGRRADLVVFDslEKLVAREVYVGG 354
Cdd:cd00854 323 GCPLEEAVRMASLNPAKLLGlDDRKGSLKPGKDADLVVLD--DDLNVKATWING 374
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
21-84 |
6.58e-05 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 45.85 E-value: 6.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031822267 21 FDLLLIDAQIVdmATGEIRPADVGIVGEMIASVHPrGSREDAHEVRSMAGGYLSPGLMDTHVHL 84
Cdd:PRK06189 3 YDLIIRGGKVV--TPEGVYRADIGIKNGKIAEIAP-EISSPAREIIDADGLYVFPGMIDVHVHF 63
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
300-361 |
6.65e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 45.55 E-value: 6.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031822267 300 EHGLPAVDALRFATLNAAIRLQRHDLGLIAAGRRADLVVFDSLEKL-VAREVYVGGKLLARAG 361
Cdd:PRK15446 321 DGGLDLPQAVALVTANPARAAGLDDRGEIAPGKRADLVRVRRAGGLpVVRAVWRGGRRVFLAG 383
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
303-340 |
6.72e-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: 6.72e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1031822267 303 LPAVDALRFATLNAAIRLQRHDLGLIAAGRRADLVVFD 340
Cdd:cd01298 332 LPAEEALEMATIGGAKALGLDEIGSLEVGKKADLILID 369
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
24-83 |
7.77e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 45.09 E-value: 7.77e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 24 LLIDAQIVDmATGEIRPADVGIVGEMIASVHPRGsrEDAHEVRSMAGGYLSPGLMDTHVH 83
Cdd:COG1820 1 AITNARIFT-GDGVLEDGALLIEDGRIAAIGPGA--EPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
193-341 |
8.17e-05 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 45.33 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 193 IVQAGLNSGKLIEGHARGLS---GADLQAYLAAgVTSDHELTSADDALEKLRAGLTIEIrgshpyLLPDIVAALK-TLPh 268
Cdd:cd01296 198 ILEAAKEAGLPVKIHADELSnigGAELAAELGA-LSADHLEHTSDEGIAALAEAGTVAV------LLPGTAFSLReTYP- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 269 lssqitvctddvPPDILLEKGGIIAL---LN---------LLIEH------GLPAVDALRFATLNAAIRLQR-HDLGLIA 329
Cdd:cd01296 270 ------------PARKLIDAGVPVALgtdFNpgssptssmPLVMHlacrlmRMTPEEALTAATINAAAALGLgETVGSLE 337
|
170
....*....|..
gi 1031822267 330 AGRRADLVVFDS 341
Cdd:cd01296 338 VGKQADLVILDA 349
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
68-340 |
8.61e-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: 44.98 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 68 MAGGYLSPGLMDTHVHL--------ESSHLPPE-------RYAEIVLTQGTTAVFwdphelaNVLGV--AGVRYAVDASr 130
Cdd:cd01299 6 LGGKTLMPGLIDAHTHLgsdpgdlpLDLALPVEyrtiratRQARAALRAGFTTVR-------DAGGAdyGLLRDAIDAG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 131 hlplqvMVAAPSSVPSTPGLEMSG--ADFAGAEMETMLGW--------PEVR-GVAEVM--------------------D 179
Cdd:cd01299 78 ------LIPGPRVFASGRALSQTGghGDPRGLSGLFPAGGlaavvdgvEEVRaAVREQLrrgadqikimatggvlspgdP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 180 MHGVLHGSERMQEIVQAGLNSGKLIEGHARGLSGAdLQAyLAAGVTS-DH-ELTSADDALEKLRAGLtieirgshpYLLP 257
Cdd:cd01299 152 PPDTQFSEEELRAIVDEAHKAGLYVAAHAYGAEAI-RRA-IRAGVDTiEHgFLIDDETIELMKEKGI---------FLVP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 258 DIvAALKTLPHLSSQITVCTDDVPPDILLEKGGIIAL-----------------------------LNLLIEHGLPAVDA 308
Cdd:cd01299 221 TL-ATYEALAAEGAAPGLPADSAEKVALVLEAGRDALrrahkagvkiafgtdagfpvpphgwnareLELLVKAGGTPAEA 299
|
330 340 350
....*....|....*....|....*....|...
gi 1031822267 309 LRFATLNAAIRLQR-HDLGLIAAGRRADLVVFD 340
Cdd:cd01299 300 LRAATANAAELLGLsDELGVIEAGKLADLLVVD 332
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
79-317 |
1.91e-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: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 79 DTHVHLESSHLPPERYAEIVLT----------------------QGTTAVFWDPHELANVLGVAGVRYAVDASRHLPLQV 136
Cdd:cd01292 3 DTHVHLDGSALRGTRLNLELKEaeelspedlyedtlraleallaGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAGIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 137 MVAAPSSVPSTPGLEMSGADFAGAEMETMLGWPeVRGVAEVMDMHGVLHGSERMQEIVQAGLNSGKLIEGHARGLSGA-- 214
Cdd:cd01292 83 VVLGLGIPGVPAAVDEDAEALLLELLRRGLELG-AVGLKLAGPYTATGLSDESLRRVLEEARKLGLPVVIHAGELPDPtr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 215 ---DLQAYLAAG--VTSDHELTSADDALEKLR-AGLTIEIRGSHPYLLPDIVAALKTLPHL---SSQITVCTDDVPPDIL 285
Cdd:cd01292 162 aleDLVALLRLGgrVVIGHVSHLDPELLELLKeAGVSLEVCPLSNYLLGRDGEGAEALRRLlelGIRVTLGTDGPPHPLG 241
|
250 260 270
....*....|....*....|....*....|..
gi 1031822267 286 LEKGGIIALLNLLIEHGLPAVDALRFATLNAA 317
Cdd:cd01292 242 TDLLALLRLLLKVLRLGLSLEEALRLATINPA 273
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
23-83 |
2.62e-04 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 43.71 E-value: 2.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1031822267 23 LLLIDAQIVDmaTGEIRPADVGIVGEMIASVHPRGSREDAHEVRSMAGGYLSPGLMDTHVH 83
Cdd:PRK09236 4 ILIKNARIVN--EGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVH 62
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
303-365 |
4.24e-04 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 42.92 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 303 LPAVDALRFATLNAAIRLQRHDLGLIAAGRRADLVVF-----------DSLEKLV------AREVYVGGKLLARAGNLLT 365
Cdd:PRK08203 351 MTAREALEWATLGGARVLGRDDIGSLAPGKLADLALFdldelrfagahDPVAALVlcgpprADRVMVGGRWVVRDGQLTT 430
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
303-365 |
7.59e-04 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 42.21 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 303 LPAVDALRFATLNAAIRLQR-HDLGLIAAGRRADLV-----------VFDSLEKLV-------AREVYVGGKLLARAGNL 363
Cdd:PRK09045 340 LPAHTALRMATLNGARALGLdDEIGSLEPGKQADLVavdlsgletqpVYDPVSQLVyaagreqVSHVWVAGKQLLDDREL 419
|
..
gi 1031822267 364 LT 365
Cdd:PRK09045 420 TT 421
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
23-105 |
1.52e-03 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 41.33 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 23 LLLIDAQIVDMAtGEIRPADVGIVGEMIASVHPRGSREDAHEVrSMAGGYLSPGLMDTHVHLEsshLPPERYAEIVLTqG 102
Cdd:PRK09357 3 ILIKNGRVIDPK-GLDEVADVLIDDGKIAAIGENIEAEGAEVI-DATGLVVAPGLVDLHVHLR---EPGQEDKETIET-G 76
|
...
gi 1031822267 103 TTA 105
Cdd:PRK09357 77 SRA 79
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
36-105 |
1.93e-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: 40.89 E-value: 1.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 36 GEIRPADVGIVGEMIASVHPRGSREDAhEVRSMAGGYLSPGLMDTHVHLESshlPPERYAEIVLTqGTTA 105
Cdd:TIGR00857 1 GKETEVDILVEGGRIKKIGKLRIPPDA-EVIDAKGLLVLPGFIDLHVHLRD---PGEEYKEDIES-GSKA 65
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
22-84 |
2.03e-03 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 40.75 E-value: 2.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1031822267 22 DLLLIDAQIVDM-ATGEIRPADVGIVGEMIASVHPRGSREDAHEVRSMAGGYLSPGLMDTHVHL 84
Cdd:PRK07228 2 TILIKNAGIVTMnAKREIVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHL 65
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
22-84 |
2.08e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 40.89 E-value: 2.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031822267 22 DLLLIDAQIVDMATGEIRPADVGIVGEMIASVhPRGSREDAHEVRSMAGGYLSPGLMDTHVHL 84
Cdd:PRK06038 3 DIIIKNAYVLTMDAGDLKKGSVVIEDGTITEV-SESTPGDADTVIDAKGSVVMPGLVNTHTHA 64
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
34-89 |
2.17e-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: 40.69 E-value: 2.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1031822267 34 ATGEIRPADVGIVGEMIASVHPRGSREDAHEVRSMAGGYLSPGLMDTHVHLESSHL 89
Cdd:cd01293 8 ADGGTALVDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLDKTFT 63
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
285-356 |
2.21e-03 |
|
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: 40.76 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 285 LLEKGGI------------IALLNLL----IEHGLPAVDALRFATLNAAIRLQRHD-LGLIAAGRRADLVVFD----SLE 343
Cdd:cd01309 266 LLKKGGVafaissdhpvlnIRNLNLEaakaVKYGLSYEEALKAITINPAKILGIEDrVGSLEPGKDADLVVWNgdplEPT 345
|
90
....*....|...
gi 1031822267 344 KLVAReVYVGGKL 356
Cdd:cd01309 346 SKPEQ-VYIDGRL 357
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
21-87 |
2.60e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 40.39 E-value: 2.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1031822267 21 FDLLLIDAQIVDMATGeirpADVGIVGEMIASVHPrGSREDAHEVRSMAGGYLSPGLMDTHVHLESS 87
Cdd:PRK07572 2 FDLIVRNANLPDGRTG----IDIGIAGGRIAAVEP-GLQAEAAEEIDAAGRLVSPPFVDPHFHMDAT 63
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
24-84 |
3.13e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 40.37 E-value: 3.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1031822267 24 LLIDAQIVDM--ATGEIRPADVGIVGEMIASVHPRGSREDAhEVRSMAGGYLSPGLMDTHVHL 84
Cdd:PRK08204 5 LIRGGTVLTMdpAIGDLPRGDILIEGDRIAAVAPSIEAPDA-EVVDARGMIVMPGLVDTHRHT 66
|
|
| 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 1031822267 21 FDLLLIDAQIVDmATGEIRpADVGIVGEMIASV-HPRGSRE-DAHevrsmaGGYLSPGLMDTHVHLE 85
Cdd:PRK08323 1 MSTLIKNGTVVT-ADDTYK-ADVLIEDGKIAAIgANLGDEViDAT------GKYVMPGGIDPHTHME 59
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
230-344 |
5.82e-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: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1031822267 230 LTSADDAlEKLRAGL---TIeirgshpyllpDIVAALKTlPHLSSQITVCTDDVPPdillekgGIIAL-------LNLLI 299
Cdd:cd01317 241 LRSEEDR-EALIEALkdgTI-----------DAIASDHA-PHTDEEKDLPFAEAPP-------GIIGLetalpllWTLLV 300
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1031822267 300 EHG-LPAVDALRFATLNAAiRLQRHDLGLIAAGRRADLVVFDSLEK 344
Cdd:cd01317 301 KGGlLTLPDLIRALSTNPA-KILGLPPGRLEVGAPADLVLFDPDAE 345
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
300-355 |
8.96e-03 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 39.01 E-value: 8.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1031822267 300 EHGLPAVDALRFATLNAAIRL-QRHDLGLIAAGRRADLVVFD---------SLEKLVAREVYVGGK 355
Cdd:COG1574 464 EERLTVEEALRAYTIGAAYAAfEEDEKGSLEPGKLADFVVLDrdpltvppeEIKDIKVLLTVVGGR 529
|
|
| |
