|
Name |
Accession |
Description |
Interval |
E-value |
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
2-382 |
2.87e-151 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 432.20 E-value: 2.87e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 2 FILIKNGTIYAPQYLGKKSILISENKIIKIGDIDEETLYQlgvDIKVIDAAESLIFPGLIDPHVHLIGGGGEGGFATRTP 81
Cdd:cd01308 1 FTLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYE---NVTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 82 EIQLSEIIKSGITTMVGLLGTDGTTRHMTSLLAKARGLEEEGITTYIYSGNYHVPTPTITSSIKDDVILIDKVIGAGEIA 161
Cdd:cd01308 78 EVTLSDLTTAGVTTVVGCLGTDGISRSMEDLLAKARALEEEGITCFVYTGSYEVPTRTITGSIRKDLLLIDKVIGVGEIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 162 ISDSRSAQPSVHELAKLCAEARIGGLLSKKAGVTHFHVGPGKAYLTLLHQIIDEYEIPPTSIYATHITRSKELVDDAIKL 241
Cdd:cd01308 158 ISDHRSSQPTVEELARIAAEARVGGLLGGKAGIVHIHLGDGKRALSPIFELIEETEIPITQFLPTHINRTAPLFEQGVEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 242 SQKGAYVDITADEQTIKW----------VKYFKENGGRMDHLTISSDGNGSLPKFNEGGELIGFGVASPSTLFEQLKAVV 311
Cdd:cd01308 238 AKMGGTIDLTSSIDPQFRkegevrpseaLKRLLEQGVPLERITFSSDGNGSLPKFDENGNLVGLGVGSVDTLLREVREAV 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518208556 312 KGDELSLEEIVPLLTSNTAAALRLNEKGIIEQHADADLIVINKQtFDLEHVIAKGRLMMRDKKVVVKGTFE 382
Cdd:cd01308 318 KCGDIPLEVALRVITSNVARILKLRKKGEIQPGFDADLVILDKD-LDINSVIAKGQIMVRNGKLLVKGTFE 387
|
|
| isoAsp_dipep |
TIGR01975 |
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ... |
2-382 |
5.99e-137 |
|
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 131030 Cd Length: 389 Bit Score: 396.08 E-value: 5.99e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 2 FILIKNGTIYAPQYLGKKSILISENKIIKIGDidEETLYQLGVDIKVIDAAESLIF-PGLIDPHVHLIGGGGEGGFATRT 80
Cdd:TIGR01975 1 FTLLKGAEVYAPEYIGKKDILIANDKIIAIAD--EIPSTKDFVPNCVVVGLEGMIAvPGFIDQHVHIIGGGGEGGPTTRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 81 PEIQLSEIIKSGITTMVGLLGTDGTTRHMTSLLAKARGLEEEGITTYIYSGNYHVPTPTITSSIKDDVILIDKVIGAGEI 160
Cdd:TIGR01975 79 PELTLSDITKGGVTTVVGLLGTDGITRHMESLLAKARALEEEGISCYMLTGAYHVPSRTITGSVESDLLLIDKVIGVGEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 161 AISDSRSAQPSVHELAKLCAEARIGGLLSKKAGVTHFHVGPGKAYLTLLHQIIDEYEIPPTSIYATHITRSKELVDDAIK 240
Cdd:TIGR01975 159 AISDHRSAQPTVEHLTNMAAEARVGGLLGGKPGIVNFHVGDSKRALQPIYELVENTDVPITQFLPTHINRNVPLFEAGLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 241 LSQKGAYVDITA--DEQTIKW--------VKYFKENGGRMDHLTISSDGNGSLPKFNEGGELIGFGVASPSTLFEQLKAV 310
Cdd:TIGR01975 239 FAKKGGTIDLTSsiDPQFRKEgevapaegIKKALEAGVPLEKVTFSSDGNGSQPFFDENGELTGLGVGSFETLFEEVREA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518208556 311 VKGDELSLEEIVPLLTSNTAAALRLNEKGIIEQHADADLIVINKQtFDLEHVIAKGRLMMRDKKVVVKGTFE 382
Cdd:TIGR01975 319 VKDGDVPLEKALRVITSNVAGVLNLTGKGEISPGNDADLVVLDPD-LRIHSVIARGKLMVKDGKACVKGTFE 389
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
3-372 |
8.94e-13 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 68.83 E-value: 8.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 3 ILIKNGTIY---APQYLGKKSILISENKIIKIGDIDEETLYQlgvDIKVIDAAESLIFPGLIDPHVHLIGGGGEGGFATR 79
Cdd:COG1228 10 LLITNATLVdgtGGGVIENGTVLVEDGKIAAVGPAADLAVPA---GAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 80 TPEI------------QLSEIIKSGITTMVGLLGTDGTTRHMTsllakargleEEGITTYIYSGNYHVPTPTIT------ 141
Cdd:COG1228 87 GGGItptvdlvnpadkRLRRALAAGVTTVRDLPGGPLGLRDAI----------IAGESKLLPGPRVLAAGPALSltggah 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 142 SSIKDDVI-LIDKVIGAGEIAI---SDSRSAQPSVHELAKLCAEARIGGLLSKkagvthFHVGPGKAYLTLL---HQIID 214
Cdd:COG1228 157 ARGPEEARaALRELLAEGADYIkvfAEGGAPDFSLEELRAILEAAHALGLPVA------AHAHQADDIRLAVeagVDSIE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 215 eyeipptsiyatHITRskeLVDDAIKL--SQKGAYVDITADeqTIKWVKYFKENGGRMDHLTISSDGNGSLPKFNEGGEL 292
Cdd:COG1228 231 ------------HGTY---LDDEVADLlaEAGTVVLVPTLS--LFLALLEGAAAPVAAKARKVREAALANARRLHDAGVP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 293 IGFG------VASPSTLFEQLKAVVKGDeLSLEEIVPLLTSNTAAALRL-NEKGIIEQHADADLIVIN-------KQTFD 358
Cdd:COG1228 294 VALGtdagvgVPPGRSLHRELALAVEAG-LTPEEALRAATINAAKALGLdDDVGSLEPGKLADLVLLDgdplediAYLED 372
|
410
....*....|....
gi 518208556 359 LEHVIAKGRLMMRD 372
Cdd:COG1228 373 VRAVMKDGRVVDRS 386
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
4-67 |
1.76e-11 |
|
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: 65.11 E-value: 1.76e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518208556 4 LIKNGTIYAPQYLGKKSILISENKIIKIG-DIDEETlyqlgvDIKVIDAAESLIFPGLIDPHVHL 67
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGpDLAAPE------AAEVIDATGLLVLPGLIDLHVHL 59
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-67 |
2.02e-11 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 64.83 E-value: 2.02e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518208556 1 MFILIKNGTIYAPQYLG-KKSILISENKIIKIGDIDEETlyqlgvDIKVIDAAESLIFPGLIDPHVHL 67
Cdd:PRK09357 1 MMILIKNGRVIDPKGLDeVADVLIDDGKIAAIGENIEAE------GAEVIDATGLVVAPGLVDLHVHL 62
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
3-372 |
9.80e-11 |
|
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: 62.92 E-value: 9.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 3 ILIKNGTIY----APQYLGKKSILISENKIIKIGDIDEetLYQLGVDIKVIDAAESLIFPGLIDPHVHL----------- 67
Cdd:COG0402 2 LLIRGAWVLtmdpAGGVLEDGAVLVEDGRIAAVGPGAE--LPARYPAAEVIDAGGKLVLPGLVNTHTHLpqtllrgladd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 68 ------IGGGGEGGFATRTPE-------IQLSEIIKSGITTMVgllgtDGTTRHMTSLLAKARGLEEEGITTYIYSGNY- 133
Cdd:COG0402 80 lplldwLEEYIWPLEARLDPEdvyagalLALAEMLRSGTTTVA-----DFYYVHPESADALAEAAAEAGIRAVLGRGLMd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 134 -HVPTPTITS---SIKDDVILIDKVIGAGE------IAIsdsRSAqPSVH-ELAKLCAEarigglLSKKAGV---THFHV 199
Cdd:COG0402 155 rGFPDGLREDadeGLADSERLIERWHGAADgrirvaLAP---HAP-YTVSpELLRAAAA------LARELGLplhTHLAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 200 GP----------GKAYLTLLHQI--IDeyeipPTSIYA--THITrskelvDDAIK-LSQKGAYV---------------D 249
Cdd:COG0402 225 TRdevewvlelyGKRPVEYLDELglLG-----PRTLLAhcVHLT------DEEIAlLAETGASVahcptsnlklgsgiaP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 250 ITAdeqtikwvkyFKENGGRmdhLTISSDGNGSLPKFNeggeligfgvaspstLFEQLKAVVK--------GDELSLEEI 321
Cdd:COG0402 294 VPR----------LLAAGVR---VGLGTDGAASNNSLD---------------MFEEMRLAALlqrlrggdPTALSAREA 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518208556 322 VPLLTSNTAAALRLNEK-GIIEQHADADLIVINKQTF-------------------DLEHVIAKGRLMMRD 372
Cdd:COG0402 346 LEMATLGGARALGLDDEiGSLEPGKRADLVVLDLDAPhlaplhdplsalvyaadgrDVRTVWVAGRVVVRD 416
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
3-376 |
1.18e-10 |
|
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: 62.70 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 3 ILIKNGTIY----APQYLGkkSILISENKIIKIGDIDEetlyQLGVdiKVIDAAESLIFPGLIDPHVHliggggEGGFAT 78
Cdd:cd01297 2 LVIRNGTVVdgtgAPPFTA--DVGIRDGRIAAIGPILS----TSAR--EVIDAAGLVVAPGFIDVHTH------YDGQVF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 79 RTPEiqLSEIIKSGITTMVglLGTDGTT-------------RHMTSLLAKARG--------------LEEEG----ITTY 127
Cdd:cd01297 68 WDPD--LRPSSRQGVTTVV--LGNCGVSpapanpddlarliMLMEGLVALGEGlpwgwatfaeyldaLEARPpavnVAAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 128 IYSGN--YHV-------PTPTITSSIKDdviLIDKVIGAGEIAISDSRSAQPSVH----ELAKLCaearigGLLSKKAGV 194
Cdd:cd01297 144 VGHAAlrRAVmgldareATEEELAKMRE---LLREALEAGALGISTGLAYAPRLYagtaELVALA------RVAARYGGV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 195 THFHV-GPGKAYLTLLHQIIDEYEIPPTSIYATHITRSKELVDDAIKL------SQKGAYVDITAD---------EQTIK 258
Cdd:cd01297 215 YQTHVrYEGDSILEALDELLRLGRETGRPVHISHLKSAGAPNWGKIDRllalieAARAEGLQVTADvypygagseDDVRR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 259 WVkyfkenggRMDHLTISSDGnGSLPKFNEGgeLIGfgvASPSTLfeqLKAVVKGDELSLEEIVPLLTSNTAAALRLNEK 338
Cdd:cd01297 295 IM--------AHPVVMGGSDG-GALGKPHPR--SYG---DFTRVL---GHYVRERKLLSLEEAVRKMTGLPARVFGLADR 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 518208556 339 GIIEQHADADLIVINKQTFDL--------------EHVIAKGRLMMRDKKVV 376
Cdd:cd01297 358 GRIAPGYRADIVVFDPDTLADratftrpnqpaegiEAVLVNGVPVVRDGAFT 409
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
3-67 |
3.19e-09 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 58.38 E-value: 3.19e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518208556 3 ILIKNGTIYAPQYLGKKSILISENKIIKIGDIDEETLyqlgvDIKVIDAAESLIFPGLIDPHVHL 67
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPG-----GVEVIDATGKYVLPGGIDPHTHL 60
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
4-367 |
8.36e-09 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 56.65 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 4 LIKNGTIYAPQY-LGKKSILISENKIIKIGDIDEEtlyqlgvDIKVIDAAESLIFPGLIDPHVHliggggeggfatrtpe 82
Cdd:COG1820 1 AITNARIFTGDGvLEDGALLIEDGRIAAIGPGAEP-------DAEVIDLGGGYLAPGFIDLHVH---------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 83 iqlseiiksgittmvGLLG---TDGTTrhmTSLLAKARGLEEEGITTYiysgnyhVPTpTITSSIKDdvilIDKVIGAGE 159
Cdd:COG1820 58 ---------------GGGGvdfMDGTP---EALRTIARAHARHGTTSF-------LPT-TITAPPED----LLRALAAIA 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 160 IAISDSRSAQ--------------------------PSVHELAKLCAEAR------------------IGGLLSK----- 190
Cdd:COG1820 108 EAIEQGGGAGilgihlegpflspekkgahppeyirpPDPEELDRLLEAAGgliklvtlapelpgalefIRYLVEAgvvvs 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 191 ---------------KAGVTHF-----------HVGPG---------KAYLTLlhqIIDEYEIPPTSIYATHitRSKE-- 233
Cdd:COG1820 188 lghtdatyeqaraafEAGATHVthlfnamsplhHREPGvvgaaldddDVYAEL---IADGIHVHPAAVRLAL--RAKGpd 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 234 ---LVDDAIKL--SQKGAYvdiTADEQTIkwvkyFKENGG-RMDhltissdgNGSLpkfneGGeligfgvaSPSTLFEQL 307
Cdd:COG1820 263 rliLVTDAMAAagLPDGEY---ELGGLEV-----TVKDGVaRLA--------DGTL-----AG--------STLTMDDAV 313
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518208556 308 KAVVKGDELSLEEIVPLLTSNTAAALRL-NEKGIIEQHADADLIVINKQtFDLEHVIAKGR 367
Cdd:COG1820 314 RNLVEWTGLPLEEAVRMASLNPARALGLdDRKGSIAPGKDADLVVLDDD-LNVRATWVGGE 373
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
3-366 |
9.06e-09 |
|
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: 56.43 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 3 ILIKNGTIYAPQYLGKKSILISENKIIKIGDIDEETlyqlgVDIKVIDAAESLIFPGLIDPHVHliggggeggfatrtpe 82
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELE-----EADEIIDLKGQYLVPGFIDIHIH---------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 83 iqlseiiksGIttmVGLLGTDGTTRhmtSLLAKARGLEEEGITTYiysgnyhVPTpTITSSIKDdvilIDKVIGAGEIAI 162
Cdd:cd00854 60 ---------GG---GGADFMDGTAE---ALKTIAEALAKHGTTSF-------LPT-TVTAPPEE----IAKALAAIAEAI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 163 SDSRSAQ--------------------------PSVHELAKLCAEARIG-----------------GLLSK--------- 190
Cdd:cd00854 113 AEGQGAEilgihlegpfispekkgahppeylraPDPEELKKWLEAAGGLiklvtlapeldgaleliRYLVErgiivsigh 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 191 ------------KAGVTHF-----------HVGPGKAYLTLLHQ------IIDEYEIPPTSIYATHITRSKE---LVDDA 238
Cdd:cd00854 193 sdatyeqavaafEAGATHVthlfnamsplhHREPGVVGAALSDDdvyaelIADGIHVHPAAVRLAYRAKGADkivLVTDA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 239 I--KLSQKGAYvdiTADEQTIkwvkYFKENGGRMDhltissdgNGSLpkfneggeligfgVASPSTLFEQLKAVVKGDEL 316
Cdd:cd00854 273 MaaAGLPDGEY---ELGGQTV----TVKDGVARLA--------DGTL-------------AGSTLTMDQAVRNMVKWGGC 324
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 518208556 317 SLEEIVPLLTSNTAAALRLN-EKGIIEQHADADLIVINKQtFDLEHVIAKG 366
Cdd:cd00854 325 PLEEAVRMASLNPAKLLGLDdRKGSLKPGKDADLVVLDDD-LNVKATWING 374
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1-67 |
2.18e-08 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 55.56 E-value: 2.18e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518208556 1 MFILIKNGTIYAPQYLGKKSILISENKIIKIGDIDEEtlyqlgvdiKVIDAAESLIFPGLIDPHVHL 67
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKADVLIEDGKIAAIGANLGD---------EVIDATGKYVMPGGIDPHTHM 58
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
3-376 |
2.32e-08 |
|
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: 55.29 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 3 ILIKNGTI---YAPQYLGKKSILISENKIIKIGDIDEETLYQlgvDIKVIDAAESLIFPGLIDPHVHL------------ 67
Cdd:cd01298 1 ILIRNGTIvttDPRRVLEDGDVLVEDGRIVAVGPALPLPAYP---ADEVIDAKGKVVMPGLVNTHTHLamtllrgladdl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 68 ----IGGGGEGGFATRTPE--------IQLSEIIKSGITTMVGLLGtdgttrHMTSLLAKArgLEEEGITTYIYSGNYHV 135
Cdd:cd01298 78 plmeWLKDLIWPLERLLTEedvylgalLALAEMIRSGTTTFADMYF------FYPDAVAEA--AEELGIRAVLGRGIMDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 136 PTPTITS---SIKDDVILIDKVIGAGE----IAISdSRSAQPSVHELAKLCAEarigglLSKKAGV-THFHVGPGKAYlt 207
Cdd:cd01298 150 GTEDVEEteeALAEAERLIREWHGAADgrirVALA-PHAPYTCSDELLREVAE------LAREYGVpLHIHLAETEDE-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 208 lLHQIIDEYEIPPtsiyATHITRSKELVDDAIklsqkGAY-VDITADEqtikwVKYFKENGGRMDHLTISSDGNGS---- 282
Cdd:cd01298 221 -VEESLEKYGKRP----VEYLEELGLLGPDVV-----LAHcVWLTDEE-----IELLAETGTGVAHNPASNMKLASgiap 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 283 LPKFNEGGELIGFGV---ASPSTL--FEQLKA------VVKGDE--LSLEEIVPLLTSNTAAALRLNEKGIIEQHADADL 349
Cdd:cd01298 286 VPEMLEAGVNVGLGTdgaASNNNLdmFEEMRLaallqkLAHGDPtaLPAEEALEMATIGGAKALGLDEIGSLEVGKKADL 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 518208556 350 IVINKQTF-------------------DLEHVIAKGRLMMRDKKVV 376
Cdd:cd01298 366 ILIDLDGPhllpvhdpishlvysanggDVDTVIVNGRVVMEDGELL 411
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
60-332 |
3.78e-08 |
|
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: 54.26 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 60 LIDPHVHLI------------GGGGEGGFATRTPEIQLS---EIIKSGITTMVGLLGTDGTTRHMTSLLAKARGLEE-EG 123
Cdd:cd01292 1 FIDTHVHLDgsalrgtrlnleLKEAEELSPEDLYEDTLRaleALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARAsAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 124 ITTYIY---SGNYHVPTPTITSSIKDDVILIDKVIGAGEIAISDSRSAQPSVHELAKLCAEARIGGLLSkkagvtHFHVG 200
Cdd:cd01292 81 IRVVLGlgiPGVPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDESLRRVLEEARKLGLPV------VIHAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 201 PGKAYLTLLHQIIDEYEIPPTSIyATHITRSKElvDDAIKLSQKGAYVDIT--------ADEQTIKWVKYFKENGgrmDH 272
Cdd:cd01292 155 ELPDPTRALEDLVALLRLGGRVV-IGHVSHLDP--ELLELLKEAGVSLEVCplsnyllgRDGEGAEALRRLLELG---IR 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518208556 273 LTISSDGNGSlpkfneggeligfgvASPSTLFEQLKAVVK--GDELSLEEIVPLLTSNTAAA 332
Cdd:cd01292 229 VTLGTDGPPH---------------PLGTDLLALLRLLLKvlRLGLSLEEALRLATINPARA 275
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-353 |
1.06e-07 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 53.35 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 1 MFILIKNGTIYApQYLGKK----SILISENKIIKIGDIDEETLYqlgvdikVIDAAESLIFPGLIDPHVHLIGGGGEGGF 76
Cdd:PRK06380 1 MSILIKNAWIVT-QNEKREilqgNVYIEGNKIVYVGDVNEEADY-------IIDATGKVVMPGLINTHAHVGMTASKGLF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 77 ----------------ATRTPE-------IQLSEIIKSGITTMVGLLGTDGttrhmtsllAKARGLEEEGITTYIysgNY 133
Cdd:PRK06380 73 ddvdleeflmktfkydSKRTREgiynsakLGMYEMINSGITAFVDLYYSED---------IIAKAAEELGIRAFL---SW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 134 HVPTPTITSSIKDDVILIDKVIGageiAISDSRSAQPSVhelaklcaeariggllskkaGVTHFHVGPGKAYLTLLhQII 213
Cdd:PRK06380 141 AVLDEEITTQKGDPLNNAENFIR----EHRNEELVTPSI--------------------GVQGIYVANDETYLKAK-EIA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 214 DEYEipptSIYATHITRSKELVDDAIK---------LSQKGAYVD--ITAD--EQTIKWVKYFKENGGRMDHLTIS---- 276
Cdd:PRK06380 196 EKYD----TIMHMHLSETRKEVYDHVKrtgerpvehLEKIGFLNSklIAAHcvWATYHEIKLLSKNGVKVSWNSVSnfkl 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 277 -SDGNGSLPKFNEGGELIGFGVASPST-----LFEQLK--AVVKGDE------LSLEEIVPLLTSNTAAALRLNeKGIIE 342
Cdd:PRK06380 272 gTGGSPPIPEMLDNGINVTIGTDSNGSnnsldMFEAMKfsALSVKNErwdasiIKAQEILDFATINAAKALELN-AGSIE 350
|
410
....*....|.
gi 518208556 343 QHADADLIVIN 353
Cdd:PRK06380 351 VGKLADLVILD 361
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
27-369 |
1.54e-07 |
|
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: 52.70 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 27 KIIKIGdidEETlyQLGVDIKVIDAAESLIFPGLIDPHVHLIGGGGEGGFATR---------TPEI-----------QLS 86
Cdd:cd01309 3 KIVAVG---AEI--TTPADAEVIDAKGKHVTPGLIDAHSHLGLDEEGGVRETSdaneetdpvTPHVraidginpddeAFK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 87 EIIKSGITTMVGLLGTDGTTRHMTSLLAKARGLEEE-------GITTY-------IYSGNYHVPTPTITSSIkddvILID 152
Cdd:cd01309 78 RARAGGVTTVQVLPGSANLIGGQGVVIKTDGGTIEDmfikapaGLKMAlgenpkrVYGGKGKEPATRMGVAA----LLRD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 153 KVIGAGE----IAISDSRSAQPSVHELAKLCaearIGGLLSKKAGVtHFHVGPGKAYLTLLhQIIDEYEIPPTsiyATHI 228
Cdd:cd01309 154 AFIKAQEygrkYDLGKNAKKDPPERDLKLEA----LLPVLKGEIPV-RIHAHRADDILTAI-RIAKEFGIKIT---IEHG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 229 TRSKELVDdaiKLSQKGAYVDITAD----------EQTIKWVKYFKENGGRMdhLTISSDGNGSLPKFneggeligfgva 298
Cdd:cd01309 225 AEGYKLAD---ELAKHGIPVIYGPTltlpkkveevNDAIDTNAYLLKKGGVA--FAISSDHPVLNIRN------------ 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518208556 299 spsTLFEQLKAVVKGdeLSLEEIVPLLTSNTAAALRLNEK-GIIEQHADADLIVINKQTFDL----EHVIAKGRLM 369
Cdd:cd01309 288 ---LNLEAAKAVKYG--LSYEEALKAITINPAKILGIEDRvGSLEPGKDADLVVWNGDPLEPtskpEQVYIDGRLV 358
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
55-369 |
3.68e-07 |
|
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: 51.35 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 55 LIFPGLIDPHVHLiggGGEGGFATRTPEIQLSEIIKSGITTMVGllgtDGTT-------RHMTSLLAKARGLEEEGITTY 127
Cdd:pfam01979 1 IVLPGLIDAHVHL---EMGLLRGIPVPPEFAYEALRLGITTMLK----SGTTtvldmgaTTSTGIEALLEAAEELPLGLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 128 IYSGNYHVPTPTITSSIKDDVILIDKVIGA----------GEIAISDSRSAQPSvhELAKLCAEAriggllsKKAGVT-H 196
Cdd:pfam01979 74 FLGPGCSLDTDGELEGRKALREKLKAGAEFikgmadgvvfVGLAPHGAPTFSDD--ELKAALEEA-------KKYGLPvA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 197 FHVGPGKAYLTLLHQIIDEyeippTSIYATHITRSKE--LVDDAIKLSQKGAYVDITADEQTIKwvkyfKENGGRMDHLT 274
Cdd:pfam01979 145 IHALETKGEVEDAIAAFGG-----GIEHGTHLEVAESggLLDIIKLILAHGVHLSPTEANLLAE-----HLKGAGVAHCP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 275 ISSDGNGS----LPKFNEGGELIGFGVASPS-----TLFEQLK-----AVVKGDELSLEEIVPLLTSNTAAALRL-NEKG 339
Cdd:pfam01979 215 FSNSKLRSgriaLRKALEDGVKVGLGTDGAGsgnslNMLEELRlalelQFDPEGGLSPLEALRMATINPAKALGLdDKVG 294
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 518208556 340 IIEQHADADLIVIN----------KQTFDLEHVIAKGRLM 369
Cdd:pfam01979 295 SIEVGKDADLVVVDldplaaffglKPDGNVKKVIVKGKIV 334
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
4-97 |
4.38e-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: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 4 LIKNGTIYAPQYLGKKSILISENKIIKIG-DIDEETLYqlgvdiKVIDAAESLIFPGLIDPHVHLIGGGGEG--GFATRT 80
Cdd:cd01315 3 VIKNGRVVTPDGVREADIAVKGGKIAAIGpDIANTEAE------EVIDAGGLVVMPGLIDTHVHINEPGRTEweGFETGT 76
|
90
....*....|....*..
gi 518208556 81 peiqlSEIIKSGITTMV 97
Cdd:cd01315 77 -----KAAAAGGITTII 88
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
3-68 |
5.30e-07 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 51.34 E-value: 5.30e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518208556 3 ILIKNGTIY--APQYLGKKSILISENKIIKIGDiDEETLYQLGVDIKVIDAAESLIFPGLIDPHVHLI 68
Cdd:COG1574 10 LLLTNGRIYtmDPAQPVAEAVAVRDGRIVAVGS-DAEVRALAGPATEVIDLGGKTVLPGFIDAHVHLL 76
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
1-104 |
7.03e-07 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 50.94 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 1 MF-ILIKNGTIY----APQYLGkkSILISENKIIKIGDIDEETlyqlgvDIKVIDAAESLIFPGLIDPHVHLIGGggegg 75
Cdd:COG3653 1 MFdLLIRGGTVVdgtgAPPFRA--DVAIKGGRIVAVGDLAAAE------AARVIDATGLVVAPGFIDIHTHYDLQ----- 67
|
90 100
....*....|....*....|....*....
gi 518208556 76 fATRTPEiqLSEIIKSGITTMVglLGTDG 104
Cdd:COG3653 68 -LLWDPR--LEPSLRQGVTTVV--MGNCG 91
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
3-353 |
7.64e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 50.81 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 3 ILIKNGTIYAPQYLGKKSILISENKIIKIGDIDEETLYQLgvdikVIDAAESLIFPGLIDPHVHLiggggeggfatRTPE 82
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEE-----VIDARGMLLLPGGIDVHVHF-----------REPG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 83 IQLSEIIKS--------GITTMVGLLGTDGTTRHMTSLLAKARGLEEEGITTYIYSGNyhvPTPTItssIKDDVILIDKV 154
Cdd:PRK02382 68 YTHKETWYTgsrsaaagGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGG---VTGNW---DPLESLWERGV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 155 IGAGEIAISDSrSAQPSVHE--LAKLCAEAriggllsKKAGVT-HFHVGPGKAYLTL--LHQIIDEYEIppTSIYATHIT 229
Cdd:PRK02382 142 FALGEIFMADS-TGGMGIDEelFEEALAEA-------ARLGVLaTVHAEDEDLFDELakLLKGDADADA--WSAYRPAAA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 230 RSKElVDDAIKLSQK-GAYVDItADEQTIKWVKYFKENGGRMD----HLTISSDGNGSLPKF------------------ 286
Cdd:PRK02382 212 EAAA-VERALEVASEtGARIHI-AHISTPEGVDAARREGITCEvtphHLFLSRRDWERLGTFgkmnpplrsekrrealwe 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 287 --NEGGELIgfgVAS---PSTLFEQ---------------------LKAVVKGdELSLEEIVPLLTSNTAAALRLNEKGI 340
Cdd:PRK02382 290 rlNDGTIDV---VASdhaPHTREEKdadiwdapsgvpgvetmlpllLAAVRKN-RLPLERVRDVTAANPARIFGLDGKGR 365
|
410
....*....|...
gi 518208556 341 IEQHADADLIVIN 353
Cdd:PRK02382 366 IAEGYDADLVLVD 378
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
3-97 |
1.11e-06 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 50.17 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 3 ILIKNGTIYAPQ--YLGKKSILISENKIIKIG-DIDEetlyqlGVDIKVIDAAESLIFPGLIDPHVHLiggggeggFATR 79
Cdd:COG3964 2 LLIKGGRVIDPAngIDGVMDIAIKDGKIAAVAkDIDA------AEAKKVIDASGLYVTPGLIDLHTHV--------FPGG 67
|
90 100
....*....|....*....|
gi 518208556 80 TPE-IQLSEI-IKSGITTMV 97
Cdd:COG3964 68 TDYgVDPDGVgVRSGVTTVV 87
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
3-360 |
1.65e-06 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 49.69 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 3 ILIKNGTIYAPQYLGKKSILISENKIIKIGDideetlYQLGVDIKVIDAAESLIFPGLIDPHVHLIGGGGEG--GFATRT 80
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGP------DILGPAAKIIDAGGLVVFPGVVDTHVHINEPGRTEweGFETGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 81 peiqlSEIIKSGITTMVGL-LGTDGTTRHMTSLLAKARGLEEEgitTYIYSGNYHVPTPTitsSIKDdvilIDKVIGAGE 159
Cdd:TIGR03178 76 -----RAAAAGGITTYIDMpLNSIPATTTRASLEAKFEAAKGK---LAVDVGFWGGLVPY---NLDD----LRELDEAGV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 160 IA----ISDSRSAQ-PSVHE--LAKLCAE-ARIGGLLSKKAGVTHFH----------VGPG-KAYL---------TLLHQ 211
Cdd:TIGR03178 141 VGfkafLSPSGDDEfPHVDDwqLYKGMRElARLGQLLLVHAENPAITsalgeeappqGGVGaDAYLasrpvfaevEAIRR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 212 IIDEYEIPPTSIYATHITrSKELVDDAIKLSQKGA---------YVDITADE-------------------QTIKWVKYF 263
Cdd:TIGR03178 221 TLALAKVTGCRVHVVHLS-SAEAVELITEAKQEGLdvtvetcphYLTLTAEEvpdggtlakcappirdlanQEGLWEALL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 264 KengGRMDhlTISSDGNGSLPKFNEGGELIGF--GVAS-PSTLFEQLKAVVKGDELSLEEIVPLLTSNTAAALRLNEKGI 340
Cdd:TIGR03178 300 N---GLID--CVVSDHSPCTPDLKRAGDFFKAwgGIAGlQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGLAQKGR 374
|
410 420
....*....|....*....|.
gi 518208556 341 IEQHADADLIVINK-QTFDLE 360
Cdd:TIGR03178 375 IAPGKDADFVFVDPdESYTLT 395
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
3-66 |
9.84e-06 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 47.06 E-value: 9.84e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518208556 3 ILIKNGTIYAPQY--LGKKSILISENKII---KIGDIDEETlyqlgvdikVIDAAESLIFPGLIDPHVH 66
Cdd:PRK12394 5 ILITNGHIIDPARniNEINNLRIINDIIVdadKYPVASETR---------IIHADGCIVTPGLIDYHAH 64
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
4-67 |
1.07e-05 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 47.22 E-value: 1.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518208556 4 LIKNGTIYAPQYLGKKSILISENKIIKIGDIDEETLYQlgvdikVIDAAESLIFPGLIDPHVHL 67
Cdd:PRK09060 8 ILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAGE------VIDCRGLHVLPGVIDSQVHF 65
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
20-368 |
1.11e-05 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 47.05 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 20 SILISENKIIKIGDideetlYQLGVDIKVIDAAESLIFPGLIDPHVHLiggggeggfatRTPEIQLSEIIKS-------- 91
Cdd:TIGR00857 7 DILVEGGRIKKIGK------LRIPPDAEVIDAKGLLVLPGFIDLHVHL-----------RDPGEEYKEDIESgskaaahg 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 92 GITTMVGLLGTDGTTRHMTSLLAKARGLEEEGITtyiysgNYHvPTPTITSSIKDDVIL----IDKVIGAGEIAISDSRS 167
Cdd:TIGR00857 70 GFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLV------DVH-LYGGVTQGNQGKELTeayeLKEAGAVGRMFTDDGSE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 168 AQPSVHELAKLCAEARIGGLLSKKAgVTHFHVGPGKAYLTLLHQIIDEYEIPPTSiYATHItrsKELVDDAIKLSQKGAY 247
Cdd:TIGR00857 143 VQDILSMRRALEYAAIAGVPIALHA-EDPDLIYGGVMHEGPSAAQLGLPARPPEA-EEVAV---ARLLELAKHAGCPVHI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 248 VDITADEqTIKWVKYFKENGGRM------DHLTISSD---GNGSLPKFN------EGGELIGFGVAS-----------PS 301
Cdd:TIGR00857 218 CHISTKE-SLELIVKAKSQGIKItaevtpHHLLLSEEdvaRLDGNGKVNpplrekEDRLALIEGLKDgiidiiatdhaPH 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 302 TLFEQLK---------------------AVVKGdELSLEEIVPLLTSNTAAALRLNEKGIIEQHADADLIVinkqtFDLE 360
Cdd:TIGR00857 297 TLEEKTKefaaappgipgletalplllqLLVKG-LISLKDLIRMLSINPARIFGLPDKGTLEEGNPADITV-----FDLK 370
|
410
....*....|
gi 518208556 361 H--VIAKGRL 368
Cdd:TIGR00857 371 KewTINAETF 380
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
3-67 |
1.18e-05 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 47.24 E-value: 1.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518208556 3 ILIKNGTIY----APQYLGKKSILISENKIIKIGDIDEetLYQLGVDIKVIDAAESLIFPGLIDPHVHL 67
Cdd:PRK07203 2 LLIGNGTAItrdpAKPVIEDGAIAIEGNVIVEIGTTDE--LKAKYPDAEFIDAKGKLIMPGLINSHNHI 68
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
3-368 |
2.78e-05 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 45.61 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 3 ILIKNGTIYAPQYL--GKKSILISENKIIKIG-DIDEetlyqlGVDIKVIDAAESLIFPGLIDPHVHliggggegGFATR 79
Cdd:PRK09237 1 LLLRGGRVIDPANGidGVIDIAIEDGKIAAVAgDIDG------SQAKKVIDLSGLYVSPGWIDLHVH--------VYPGS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 80 TPE-IQLSEI-IKSGITTMVgllgtD-GTTRHMTslLAKARGLEEEGITTYIYSgnyhvptptitssikddviLIDkVIG 156
Cdd:PRK09237 67 TPYgDEPDEVgVRSGVTTVV-----DaGSAGADN--FDDFRKLTIEASKTRVLA-------------------FLN-ISR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 157 AGEIAI---SDSRSAQPsvhELAKLCAEAR---IGGLlskKAGVTHFHVG-PGKAYLTLLHQIIDEYEIP--------PT 221
Cdd:PRK09237 120 IGLLAQdelADLEDIDA---DAVAEAVKRNpdfIVGI---KARMSSSVVGdNGIEPLELAKAIAAEANLPlmvhignpPP 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 222 SIYA-----------TH---------ITRSKELVDDAIKLSQKGAYVDI----------TAdEQTIKwvKYFKENggrmd 271
Cdd:PRK09237 194 SLEEilellrpgdilTHcfngkpnriLDEDGELRPSVLEALERGVRLDVghgtasfsfkVA-EAAIA--AGILPD----- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 272 hlTISSDGNgslpkfneGGELIGFGVASPSTLFEQLKAVvkGdeLSLEEIVPLLTSNTAAALRLNEKGIIEQHADADLIV 351
Cdd:PRK09237 266 --TISTDIY--------CRNRINGPVYSLATVMSKFLAL--G--MPLEEVIAAVTKNAADALRLPELGRLQVGSDADLTL 331
|
410 420
....*....|....*....|....
gi 518208556 352 IN--KQTFDL-----EHVIAKGRL 368
Cdd:PRK09237 332 FTlkDGPFTLtdsegDSLIGERLL 355
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
15-119 |
2.90e-05 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 45.94 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 15 YLG--KKSILISENKIIKIG-----DIdeetlyQLGVDIKV-----IDAAESLIF-PGLIDPHVHLIggggeggfatrTP 81
Cdd:PRK13207 79 HWGivKADIGIKDGRIVAIGkagnpDI------QDGVDIIIgpgteVIAGEGLIVtAGGIDTHIHFI-----------CP 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 518208556 82 EiQLSEIIKSGITTMVG-----LLGTDGTT-----RHMTSLLAKARGL 119
Cdd:PRK13207 142 Q-QIEEALASGVTTMIGggtgpATGTNATTctpgpWHIHRMLQAADAF 188
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
21-67 |
5.15e-05 |
|
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: 44.93 E-value: 5.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 518208556 21 ILISENKIIKIGDIDEETLyqlgvDIKVIDAAESLIFPGLIDPHVHL 67
Cdd:cd01293 17 IAIEDGRIAAIGPALAVPP-----DAEEVDAKGRLVLPAFVDPHIHL 58
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
21-68 |
8.44e-05 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 44.61 E-value: 8.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 518208556 21 ILISENKIIKIGDiDEETLYQLGVDIKVIDAAESLIFPGLIDPHVHLI 68
Cdd:cd01300 2 VAVRDGRIVAVGS-DAEAKALKGPATEVIDLKGKTVLPGFIDSHSHLL 48
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
3-67 |
1.32e-04 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 43.59 E-value: 1.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518208556 3 ILIKNGTIYAPQY--LGKKSILISENKIIKIGDIDEETlyqlgVDiKVIDAAESLIFPGLIDPHVHL 67
Cdd:PRK06038 4 IIIKNAYVLTMDAgdLKKGSVVIEDGTITEVSESTPGD-----AD-TVIDAKGSVVMPGLVNTHTHA 64
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
1-67 |
1.40e-04 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 43.83 E-value: 1.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 1 MFILIKNGTIY---APQYLGKKSILISENKIIKIGDIDEETLYQlgvdiKVIDAAESLIFPGLIDPHVHL 67
Cdd:PRK07228 1 MTILIKNAGIVtmnAKREIVDGDVLIEDDRIAAVGDRLDLEDYD-----DHIDATGKVVIPGLIQGHIHL 65
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
315-377 |
6.90e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 41.36 E-value: 6.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518208556 315 ELSLEEIVPLLTSNTAAALRL-NEKGIIEQHADADLIVINKQTFDLEH---VIAKGRLMMRDKKVVV 377
Cdd:pfam07969 398 ELSLEEALALYTSGPAKALGLeDRKGTLGVGKDADLVVLDDDPLTVDPpaiADIRVRLTVVDGRVVY 464
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
20-126 |
7.55e-04 |
|
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273512 [Multi-domain] Cd Length: 377 Bit Score: 41.24 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 20 SILISENKIIKIGDIDEETLYQlgvDIKVIDAAESLIFPGLIDPHVHLI-GGGGEGGFATRTPEIQLSEIIKSGittmVG 98
Cdd:TIGR01224 5 VILIHGGKIVWIGQLAALPGEE---ATEIIDCGGGLVTPGLVDPHTHLVfAGDRVNEFEMKLQGASYLEILAQG----GG 77
|
90 100 110
....*....|....*....|....*....|....
gi 518208556 99 LLGTDGTTRHMT--SLLAKAR----GLEEEGITT 126
Cdd:TIGR01224 78 ILSTVRATRAASeeELLKLALfrlkSMLRSGTTT 111
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
1-66 |
1.16e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 40.94 E-value: 1.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518208556 1 MFILIKNG-TIYAPQY-LGKKSILISENKIIKIG-DIDEETlyqlgvdIKVIDAAESLIFPGLIDPHVH 66
Cdd:PRK08393 1 MSILIKNGyVIYGENLkVIRADVLIEGNKIVEVKrNINKPA-------DTVIDASGSVVSPGFINAHTH 62
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
48-103 |
1.34e-03 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 40.35 E-value: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518208556 48 VIDAAESLIFPGLIDPHVHLIGGGGEGGFATRTPEI--------QLSEIIKSGITTMVGLLGTD 103
Cdd:cd01299 3 VIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVEyrtiratrQARAALRAGFTTVRDAGGAD 66
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
3-67 |
1.61e-03 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 40.21 E-value: 1.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518208556 3 ILIKNGTIYAPQYLGKKSILISENKIIKIG-DIDeetlyqLGVDIKVIDAAESLIFPGLIDPHVHL 67
Cdd:PLN02942 7 ILIKGGTVVNAHHQELADVYVEDGIIVAVApNLK------VPDDVRVIDATGKFVMPGGIDPHTHL 66
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
4-98 |
1.70e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 40.46 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 4 LIKNGTIYAPqYLG--KKSILISENKIIKIG---------DIDEETLYQLGVDIKvidAAESLIF-PGLIDPHVHLIggg 71
Cdd:PRK13308 71 VLCNVTVIDP-VLGivKGDIGIRDGRIVGIGkagnpdimdGVDPRLVVGPGTDVR---PAEGLIAtPGAIDVHVHFD--- 143
|
90 100
....*....|....*....|....*..
gi 518208556 72 geggfatrTPEiQLSEIIKSGITTMVG 98
Cdd:PRK13308 144 --------SAQ-LVDHALASGITTMLG 161
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
3-66 |
1.85e-03 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 40.24 E-value: 1.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518208556 3 ILIKN------GTIYapqylgKKSILISENKIIKIG-DIDEETLYQlgvdikVIDAAESLIFPGLIDPHVH 66
Cdd:PRK09236 4 ILIKNarivneGKIF------EGDVLIENGRIAKIAsSISAKSADT------VIDAAGRYLLPGMIDDQVH 62
|
|
| PRK09230 |
PRK09230 |
cytosine deaminase; Provisional |
4-67 |
1.97e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 181713 Cd Length: 426 Bit Score: 40.07 E-value: 1.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518208556 4 LIKNGTIyaPQYLGKKSILISENKIIKIGDIDEETLYQLGVdikvIDAAESLIFPGLIDPHVHL 67
Cdd:PRK09230 7 TIKNARL--PGKEGLWQITIEDGKISAIEPQSEASLEAGEV----LDAEGGLAIPPFIEPHIHL 64
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
21-68 |
2.08e-03 |
|
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: 39.93 E-value: 2.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 518208556 21 ILISENKIIKIGDidEETLYQLGV-DIKVIDAAESLIFPGLIDPHVHLI 68
Cdd:cd01296 1 IAIRDGRIAAVGP--AASLPAPGPaAAEEIDAGGRAVTPGLVDCHTHLV 47
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
5-67 |
2.77e-03 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 39.68 E-value: 2.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518208556 5 IKNGTIYAPQYLGKKSILISENKIIKIGDideetlyQLGVDIKVIDAAESLIFPGLIDPHVHL 67
Cdd:PRK13404 8 IRGGTVVTATDTFQADIGIRGGRIAALGE-------GLGPGAREIDATGRLVLPGGVDSHCHI 63
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
3-66 |
3.32e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 39.31 E-value: 3.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518208556 3 ILIKN--------GTIYapqylgKKSILISENKIIKIGDIDEEtlyqlgvDIKVIDAAESLIFPGLIDPHVH 66
Cdd:COG1001 7 LVIKNgrlvnvftGEIL------EGDIAIAGGRIAGVGDYIGE-------ATEVIDAAGRYLVPGFIDGHVH 65
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
21-66 |
3.39e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 39.40 E-value: 3.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 518208556 21 ILISENKIIKIGDIdEETLYQLGVDIKVIDAAESLIFPGLIDPHVH 66
Cdd:PRK09228 34 LLVEDGRIVAAGPY-AELRAQLPADAEVTDYRGKLILPGFIDTHIH 78
|
|
| PLN02795 |
PLN02795 |
allantoinase |
2-67 |
3.64e-03 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 39.37 E-value: 3.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518208556 2 FILIkNGTIYAPQYLGKKSILISENKIIKIGDIDEETLYQLGVdiKVIDAAESLIFPGLIDPHVHL 67
Cdd:PLN02795 46 FVLY-SKRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKSQKKP--HVLDYGNAVVMPGLIDVHVHL 108
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-66 |
3.85e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 39.27 E-value: 3.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518208556 1 MFILIKNGTIYAPQ---YLGkkSILISENKIIKIGDideeTLYQLGVDiKVIDAAESLIFPGLIDPHVH 66
Cdd:PRK07575 3 MSLLIRNARILLPSgelLLG--DVLVEDGKIVAIAP----EISATAVD-TVIDAEGLTLLPGVIDPQVH 64
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
316-353 |
4.28e-03 |
|
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.
Pssm-ID: 238631 Cd Length: 325 Bit Score: 38.80 E-value: 4.28e-03
10 20 30
....*....|....*....|....*....|....*...
gi 518208556 316 LSLEEIVPLLTSNTAAALRLNEKGIIEQHADADLIVIN 353
Cdd:cd01306 273 WSLPEAVALVSANPARAVGLTDRGSIAPGKRADLILVD 310
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
1-66 |
6.23e-03 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 38.63 E-value: 6.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 1 MFILIKNGTIYAPQYlG----KKSILISENKIIkigdiDEETLyqlGVDIKVIDAAESLIFPGLIDPHVH 66
Cdd:COG1229 1 MELIIKNGRVYDPAN-GidgeVMDIAIKDGKIV-----EEPSD---PKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
21-66 |
6.63e-03 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 38.41 E-value: 6.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 518208556 21 ILISENKIIKIGDIDEETLYQLGVDIKVIDAAESLIFPGLIDPHVH 66
Cdd:cd01303 28 LIVVVDGNIIAAGAAETLKRAAKPGARVIDSPNQFILPGFIDTHIH 73
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
2-67 |
6.85e-03 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 38.30 E-value: 6.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518208556 2 FILIKNGTIYAPQYLGKKSILISENKIIKIGDideetlyQLGVDIKVIDAAESLIFPGLIDPHVHL 67
Cdd:PRK08044 4 DLIIKNGTVILENEARVVDIAVKGGKIAAIGQ-------DLGDAKEVMDASGLVVSPGMVDAHTHI 62
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
15-131 |
7.45e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 38.20 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 15 YLGKKSILISENKIIKIGDIDEETLyqlgvdiKVIDAAE-SLIFPGLIDPHVHL--IGGGGEGGFATRTpeiqlSEIIKS 91
Cdd:PRK00369 10 YLGKEIKEICINFDRRIKEIKSRCK-------PDLDLPQgTLILPGAIDLHVHLrgLKLSYKEDVASGT-----SEAAYG 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 518208556 92 GITTMVGLLGTDGTTRHMTSLLAKARGLEEEGITTY-IYSG 131
Cdd:PRK00369 78 GVTLVADMPNTIPPLNTPEAITEKLAELEYYSRVDYfVYSG 118
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
4-119 |
7.53e-03 |
|
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.
Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 38.46 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518208556 4 LIKNGTIYAPQYLGKKSILISENKIIKIG-----DIdeetlyQLGVDIKVI-------DAAESLIF-PGLIDPHVHLIgg 70
Cdd:cd00375 68 VITNALIIDYTGIYKADIGIKDGRIVAIGkagnpDI------MDGVTPNMIvgpstevIAGEGKIVtAGGIDTHVHFI-- 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 518208556 71 ggeggfatrTPEiQLSEIIKSGITTMVG-----LLGTDGTT-----RHMTSLLAKARGL 119
Cdd:cd00375 140 ---------CPQ-QIEEALASGITTMIGggtgpAAGTKATTctpgpWNIKRMLQAADGL 188
|
|
| |
