|
Name |
Accession |
Description |
Interval |
E-value |
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
29-366 |
2.74e-169 |
|
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: 476.42 E-value: 2.74e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 29 IAAIKPHIESTQDMTVIDARALHLLPGFIDVHTHLGLYDEGTGWAGNDANETSEVLTPHIRSLDGIHPFDIAFQDAVENG 108
Cdd:cd01309 4 IVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLGLDEEGGVRETSDANEETDPVTPHVRAIDGINPDDEAFKRARAGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 109 VTTAHVMPGSQNIIGGTTCVIKTAGTCIDHMIIQEPAGLKIAFGENPKRVHSNGTKESITRMGIMGLLRESFYEAQHYGN 188
Cdd:cd01309 84 VTTVQVLPGSANLIGGQGVVIKTDGGTIEDMFIKAPAGLKMALGENPKRVYGGKGKEPATRMGVAALLRDAFIKAQEYGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 189 -------------EADFRMLPILKALRREIPVRIHAHRADDILSSLRFAKEFNLDLRIEHCTEGHFIVKELANQNLKISV 255
Cdd:cd01309 164 kydlgknakkdppERDLKLEALLPVLKGEIPVRIHAHRADDILTAIRIAKEFGIKITIEHGAEGYKLADELAKHGIPVIY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 256 GPTLTRRSKIELKNKSWDTYHTLSKHG-IEVSITTDHPYTPIQYLNVCAAIAVREGLDERIALEGVTIIPARNLRLEKRI 334
Cdd:cd01309 244 GPTLTLPKKVEEVNDAIDTNAYLLKKGgVAFAISSDHPVLNIRNLNLEAAKAVKYGLSYEEALKAITINPAKILGIEDRV 323
|
330 340 350
....*....|....*....|....*....|..
gi 1264379975 335 GSIEVGKDADLVLWTHHPFHYLAKPVLTMIEG 366
Cdd:cd01309 324 GSLEPGKDADLVVWNGDPLEPTSKPEQVYIDG 355
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
3-366 |
4.04e-57 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 190.94 E-value: 4.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 3 TLFKQAIVYPITSSKFQ--GDVLVKHNQIAAIKPHIEST--QDMTVIDARALHLLPGFIDVHTHLGLYDEGTGWAGNDAN 78
Cdd:COG1228 10 LLITNATLVDGTGGGVIenGTVLVEDGKIAAVGPAADLAvpAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 79 ETSEVltphirslDGIHPFDIAFQDAVENGVTTAHVMPGS-----QNIIGGTTCVIKTAgtcidhMIIQEPAGLKIAFGE 153
Cdd:COG1228 90 ITPTV--------DLVNPADKRLRRALAAGVTTVRDLPGGplglrDAIIAGESKLLPGP------RVLAAGPALSLTGGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 154 NpkrvhsNGTKESITRMgimglLRESFYE-AQH-----YGNEADFR---MLPIL-KALRREIPVRIHAHRADDILSSLrf 223
Cdd:COG1228 156 H------ARGPEEARAA-----LRELLAEgADYikvfaEGGAPDFSleeLRAILeAAHALGLPVAAHAHQADDIRLAV-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 224 akEFNLDLrIEHCTEGHF-IVKELANQNlKISVGPTLTRRSKI-------------ELKNKSWDTYHTLSKHGIEVSITT 289
Cdd:COG1228 223 --EAGVDS-IEHGTYLDDeVADLLAEAG-TVVLVPTLSLFLALlegaaapvaakarKVREAALANARRLHDAGVPVALGT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 290 DHP--YTPIQYLNVCAAIAVREGLDERIALEGVTIIPARNLRLEKRIGSIEVGKDADLVLWTHHPF---HYLAKPVLTMI 364
Cdd:COG1228 299 DAGvgVPPGRSLHRELALAVEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLediAYLEDVRAVMK 378
|
..
gi 1264379975 365 EG 366
Cdd:COG1228 379 DG 380
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
4-64 |
6.61e-12 |
|
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: 66.27 E-value: 6.61e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1264379975 4 LFKQA-IVYPitSSKFQGDVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTHLG 64
Cdd:COG0044 1 LIKNGrVVDP--GGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLR 60
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
44-366 |
8.63e-12 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 66.02 E-value: 8.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 44 VIDARALHLLPGFIDVHTHL--------GLYDEGT-------GWAG-------------NDANETSEVLTPHIRSLDGI- 94
Cdd:pfam07969 2 VIDAKGRLVLPGFVDPHTHLdggglnlrELRLPDVlpnavvkGQAGrtpkgrwlvgegwDEAQFAETRFPYALADLDEVa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 95 --HPFDIAFQD---AVENGVTTAHVM--PGSQNIIGG-----------------------TTCVIKTAGTCIDHMIIQEP 144
Cdd:pfam07969 82 pdGPVLLRALHthaAVANSAALDLAGitKATEDPPGGeiardangegltgllregayalpPLLAREAEAAAVAAALAALP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 145 A-GLKIAFGENPKrVHSNGTKESITRM---GIMGLLRESFYEAQHYGNEADFRMLPI----------------------- 197
Cdd:pfam07969 162 GfGITSVDGGGGN-VHSLDDYEPLRELtaaEKLKELLDAPERLGLPHSIYELRIGAMklfadgvlgsrtaaltepyfdap 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 198 ---------------LKALR-REIPVRIHAHRADDILSSL-----RFAKEFNLDL-RIEHCTEGHFI----VKELANQNL 251
Cdd:pfam07969 241 gtgwpdfedealaelVAAAReRGLDVAIHAIGDATIDTALdafeaVAEKLGNQGRvRIEHAQGVVPYtysqIERVAALGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 252 KISVGPTLT-------RRSKIELKNKSWDTYHTLSKHGIEVSITTDH------PYTPIQYLN--VCAAIAVREGLDERI- 315
Cdd:pfam07969 321 AAGVQPVFDplwgdwlQDRLGAERARGLTPVKELLNAGVKVALGSDApvgpfdPWPRIGAAVmrQTAGGGEVLGPDEELs 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 316 ---ALEGVTIIPARNLRLEKRIGSIEVGKDADLVLW------THHPFHYLAKPVLTMIEG 366
Cdd:pfam07969 401 leeALALYTSGPAKALGLEDRKGTLGVGKDADLVVLdddpltVDPPAIADIRVRLTVVDG 460
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-63 |
1.39e-10 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 62.14 E-value: 1.39e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1264379975 1 MKTLFKQAIVYPITSSKFQGDVLVKHNQIAAIKPHIESTQDmTVIDARALHLLPGFIDVHTHL 63
Cdd:PRK09357 1 MMILIKNGRVIDPKGLDEVADVLIDDGKIAAIGENIEAEGA-EVIDATGLVVAPGLVDLHVHL 62
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
52-366 |
2.88e-10 |
|
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: 60.98 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 52 LLPGFIDVHTHLGlydegtgwagnDANETSEVLTPHIRsldgihpfdiafQDAVENGVTTAhvmpgsqnIIGGTTCVIKT 131
Cdd:pfam01979 2 VLPGLIDAHVHLE-----------MGLLRGIPVPPEFA------------YEALRLGITTM--------LKSGTTTVLDM 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 132 AGTCIDHMiiqepAGLKIAFGENPKRVHSNGTKESITRMG----IMGLLRESFYEAQHYGNEADFRMLPILK-------- 199
Cdd:pfam01979 51 GATTSTGI-----EALLEAAEELPLGLRFLGPGCSLDTDGelegRKALREKLKAGAEFIKGMADGVVFVGLAphgaptfs 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 200 ----------ALRREIPVRIHAH--RADDILSSLRFAKEFNLDLRIEHCTEGHF--IVKELANQNLKISvgPTLTRRSKI 265
Cdd:pfam01979 126 ddelkaaleeAKKYGLPVAIHALetKGEVEDAIAAFGGGIEHGTHLEVAESGGLldIIKLILAHGVHLS--PTEANLLAE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 266 ELKNKSWDTY----HTLSKH----------GIEVSITTDHPY-----TPIQYLNVCAAIA--VREGLDERIALEGVTIIP 324
Cdd:pfam01979 204 HLKGAGVAHCpfsnSKLRSGrialrkaledGVKVGLGTDGAGsgnslNMLEELRLALELQfdPEGGLSPLEALRMATINP 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1264379975 325 ARNLRLEKRIGSIEVGKDADLVLWTHHP---FHYLAK---PVLTMIEG 366
Cdd:pfam01979 284 AKALGLDDKVGSIEVGKDADLVVVDLDPlaaFFGLKPdgnVKKVIVKG 331
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
15-70 |
3.87e-10 |
|
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: 61.08 E-value: 3.87e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1264379975 15 SSKFQGDVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTHLGLYDEGT 70
Cdd:cd01314 12 DGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGT 67
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
21-112 |
6.17e-10 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 60.18 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 21 DVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTHlgLYDEGTGWagndanetsevltphirsldGIHPFDIA 100
Cdd:COG3964 21 DIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTH--VFPGGTDY--------------------GVDPDGVG 78
|
90
....*....|..
gi 1264379975 101 FqdavENGVTTA 112
Cdd:COG3964 79 V----RSGVTTV 86
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
197-347 |
1.99e-09 |
|
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: 58.86 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 197 ILKALRREIPVRIHAH--RADDIL-----SSLRFAKEFNLDLRIEHC---TEGHfiVKELANQNLKISV--------GPT 258
Cdd:cd01300 301 VRAADEAGLQVAIHAIgdRAVDTVldaleAALKDNPRADHRHRIEHAqlvSPDD--IPRFAKLGVIASVqpnhlysdGDA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 259 LTRRSKIELKNKSWDTYHTLSKHGIEVSITTDHPYTPIQ-YLNVCAAI-------AVREGLDERI----ALEGVTIIPAR 326
Cdd:cd01300 379 AEDRRLGEERAKRSYPFRSLLDAGVPVALGSDAPVAPPDpLLGIWAAVtrktpggGVLGNPEERLsleeALRAYTIGAAY 458
|
170 180
....*....|....*....|.
gi 1264379975 327 NLRLEKRIGSIEVGKDADLVL 347
Cdd:cd01300 459 AIGEEDEKGSLEPGKLADFVV 479
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
275-366 |
2.11e-09 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 59.04 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 275 YHTLSKHGIEVSITTDHPYTPIQ-YLNVCAAIAvRE-------GLDERI----ALEGVTIIPARNLRLEKRIGSIEVGKD 342
Cdd:COG1574 420 FRSLLDAGAPLAFGSDAPVEPLDpLLGIYAAVT-RRtpsgrglGPEERLtveeALRAYTIGAAYAAFEEDEKGSLEPGKL 498
|
90 100 110
....*....|....*....|....*....|
gi 1264379975 343 ADLVLWTHHPF----HYLA--KPVLTMIEG 366
Cdd:COG1574 499 ADFVVLDRDPLtvppEEIKdiKVLLTVVGG 528
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-70 |
3.35e-09 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 57.96 E-value: 3.35e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1264379975 1 MKTLFKQAIVypITSSK-FQGDVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTHL---GLYDEGT 70
Cdd:PRK09236 2 KRILIKNARI--VNEGKiFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFrepGLTHKGD 73
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
281-360 |
3.60e-09 |
|
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: 57.65 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 281 HGIEVSITTDH-PYT-PIQYLNVCAAIAVRE-GLDERIALEGVTIIPARNLRLEKRIGSIEVGKDADLVLW-----THHP 352
Cdd:cd01296 277 AGVPVALGTDFnPGSsPTSSMPLVMHLACRLmRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILdapsyEHLA 356
|
....*...
gi 1264379975 353 FHYLAKPV 360
Cdd:cd01296 357 YRFGVNLV 364
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
19-347 |
7.58e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 56.93 E-value: 7.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 19 QGDVLVKHNQIAAIKPHIEStQDMTVIDARALHLLPGFIDVHTHL---GLYDEGTGWAGNDA-NETSEVLTPHIRSLDGI 94
Cdd:PRK08204 23 RGDILIEGDRIAAVAPSIEA-PDAEVVDARGMIVMPGLVDTHRHTwqsVLRGIGADWTLQTYfREIHGNLGPMFRPEDVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 95 HPFDIAFQDAVENGVTT----AHVMPGSQNiiggttcviktAGTCIDHMiiqEPAGLKIAFGE-NPKR-VHSNGTKESIT 168
Cdd:PRK08204 102 IANLLGALEALDAGVTTlldwSHINNSPEH-----------ADAAIRGL---AEAGIRAVFAHgSPGPsPYWPFDSVPHP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 169 RMGIMGLLRESFYEAQ------------HYGN----EADFRMlpilkALRREIPVRIHA-----HRADDILSSLRFAKEF 227
Cdd:PRK08204 168 REDIRRVKKRYFSSDDglltlglairgpEFSSwevaRADFRL-----ARELGLPISMHQgfgpwGATPRGVEQLHDAGLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 228 NLDLRIEHCTE-GHFIVKELANQNLKISVGPtltrrsKIEL-KNKSWDTYHTLSKHGIEVSITTD-------HPYTPI-- 296
Cdd:PRK08204 243 GPDLNLVHGNDlSDDELKLLADSGGSFSVTP------EIEMmMGHGYPVTGRLLAHGVRPSLGVDvvtstggDMFTQMrf 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1264379975 297 -----------QYLNVCAAIAVREGLDERIALEGVTIIPARNLRLEKRIGSIEVGKDADLVL 347
Cdd:PRK08204 317 alqaerardnaVHLREGGMPPPRLTLTARQVLEWATIEGARALGLEDRIGSLTPGKQADLVL 378
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-62 |
9.16e-09 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 56.61 E-value: 9.16e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1264379975 1 MKTLFKQA-IVYPiTSSKFQGDVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTH 62
Cdd:PRK07575 3 MSLLIRNArILLP-SGELLLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVH 64
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
16-141 |
1.54e-08 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 56.00 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 16 SKFQGDVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTHLGLYDEGTgwagndanETSEVLtphirsldgih 95
Cdd:PLN02942 19 HQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGT--------ETIDDF----------- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1264379975 96 pfdIAFQDAVENGVTTAH---VMPGSQNIIGG-TTCVIKTAGTCID---HMII 141
Cdd:PLN02942 80 ---FSGQAAALAGGTTMHidfVIPVNGNLLAGyEAYEKKAEKSCMDygfHMAI 129
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
18-84 |
2.59e-08 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 55.56 E-value: 2.59e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1264379975 18 FQGDVLVKHNQIAAIKPhIESTQDMTVIDARALHLLPGFIDVHTHlglYDEGTGWAGNDANE-----TSEVL 84
Cdd:COG3653 20 FRADVAIKGGRIVAVGD-LAAAEAARVIDATGLVVAPGFIDIHTH---YDLQLLWDPRLEPSlrqgvTTVVM 87
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1-63 |
6.50e-08 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 54.02 E-value: 6.50e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1264379975 1 MKTLFKQAIVypITSSK-FQGDVLVKHNQIAAIKPHiestQDMTVIDARALHLLPGFIDVHTHL 63
Cdd:PRK08323 1 MSTLIKNGTV--VTADDtYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHM 58
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
20-348 |
9.72e-08 |
|
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: 53.29 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 20 GDVLVKHNQIAAIKPHIE---STQDMTVIDARALHLLPGFIDVHTHL------GLYDEGT--GWAgndanetSEVLTPHI 88
Cdd:COG0402 22 GAVLVEDGRIAAVGPGAElpaRYPAAEVIDAGGKLVLPGLVNTHTHLpqtllrGLADDLPllDWL-------EEYIWPLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 89 RSLDGIHPFDIA---FQDAVENGVTTAHVMPGSQNiiGGTTCVIKTAgtcidhmiiqEPAGLKIAFGenpkRVHSNGTKE 165
Cdd:COG0402 95 ARLDPEDVYAGAllaLAEMLRSGTTTVADFYYVHP--ESADALAEAA----------AEAGIRAVLG----RGLMDRGFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 166 SITRMGIMGLLRESFYEAQHYGNEADFRMLPIL----------------KALRREIPVRIHAH-----------RADDIL 218
Cdd:COG0402 159 DGLREDADEGLADSERLIERWHGAADGRIRVALaphapytvspellraaAALARELGLPLHTHlaetrdevewvLELYGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 219 SSLRFAKEFNL---DLRIEHCTegHF---IVKELANQ----------NLKISVGPTLTRRskielknkswdtyhtLSKHG 282
Cdd:COG0402 239 RPVEYLDELGLlgpRTLLAHCV--HLtdeEIALLAETgasvahcptsNLKLGSGIAPVPR---------------LLAAG 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1264379975 283 IEVSITTD-----HPYTPIQYLNVCAAIA-VREGLDERI----ALEGVTIIPARNLRLEKRIGSIEVGKDADLVLW 348
Cdd:COG0402 302 VRVGLGTDgaasnNSLDMFEEMRLAALLQrLRGGDPTALsareALEMATLGGARALGLDDEIGSLEPGKRADLVVL 377
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
14-63 |
1.64e-07 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 52.77 E-value: 1.64e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1264379975 14 TSSKFQGDVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTHL 63
Cdd:TIGR02033 11 ADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHL 60
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
3-82 |
1.96e-07 |
|
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: 52.58 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 3 TLFKQAIVYPiTSSKFQGDVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTHlglydegtGWAGNDANETSE 82
Cdd:cd00854 1 LIIKNARILT-PGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH--------GGGGADFMDGTA 71
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
18-67 |
2.32e-07 |
|
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: 52.30 E-value: 2.32e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1264379975 18 FQGDVLVKHNQIAAIKPhIESTQDMTVIDARALHLLPGFIDVHTHlglYD 67
Cdd:cd01297 18 FTADVGIRDGRIAAIGP-ILSTSAREVIDAAGLVVAPGFIDVHTH---YD 63
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
56-326 |
3.41e-07 |
|
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: 51.18 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 56 FIDVHTHLGLYDEGTGWAGNDANETSEVLTPHIRSLdgihpFDIAFQDAVENGVTTAHVMPGSQNIIGGTTCVIKTAGTC 135
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEELSPEDLYED-----TLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 136 IDHMIIQEPAGLKIAFGENPK----RVHSNGTKESITRMGIMGLLRESFYEaqHYGNEADFRMLPILKALRREIPVRIHA 211
Cdd:cd01292 76 RASAGIRVVLGLGIPGVPAAVdedaEALLLELLRRGLELGAVGLKLAGPYT--ATGLSDESLRRVLEEARKLGLPVVIHA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 212 H---RADDILSSLRFAKEFNLDLRIEHCTEGH-FIVKELANQNLKISVGPTLTRRskieLKNKSWDTYHT--LSKHGIEV 285
Cdd:cd01292 154 GelpDPTRALEDLVALLRLGGRVVIGHVSHLDpELLELLKEAGVSLEVCPLSNYL----LGRDGEGAEALrrLLELGIRV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1264379975 286 SITTDHPY--TPIQYLNVC--AAIAVREGLDERIALEGVTIIPAR 326
Cdd:cd01292 230 TLGTDGPPhpLGTDLLALLrlLLKVLRLGLSLEEALRLATINPAR 274
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
21-111 |
4.66e-07 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 51.39 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 21 DVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTHlgLYDEGTGWagndanetsevltphirsldGIHPFDIa 100
Cdd:PRK09237 20 DIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVH--VYPGSTPY--------------------GDEPDEV- 76
|
90
....*....|.
gi 1264379975 101 fqdAVENGVTT 111
Cdd:PRK09237 77 ---GVRSGVTT 84
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
20-63 |
4.93e-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: 4.93e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1264379975 20 GDVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTHL 63
Cdd:cd01315 18 ADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHI 61
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
21-347 |
7.06e-07 |
|
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: 50.71 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 21 DVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTHL--GLY-------DEGTGWAGNDANETSEVLTPHI--- 88
Cdd:cd01293 16 DIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLdkTFTggrwpnnSGGTLLEAIIAWEERKLLLTAEdvk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 89 -RSLDGIhpfdiafQDAVENGVTT--AHVMpgsqniiggttcviktagtcidhmiIQEPAGLKI--AFGENPKRVhsngt 163
Cdd:cd01293 96 eRAERAL-------ELAIAHGTTAirTHVD-------------------------VDPAAGLKAleALLELREEW----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 164 KESIT-------RMGIM------GLLRESfyeAQHYG----------NEADF-----RMLPIlkALRREIPVRIHAHRAD 215
Cdd:cd01293 139 ADLIDlqivafpQHGLLstpggeELMREA---LKMGAdvvggippaeIDEDGeesldTLFEL--AQEHGLDIDLHLDETD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 216 DILSS-----LRFAKEFNLDLR--IEHCTE-GHF-------IVKELANQNLKISVGPT----LTRRSKIELKNKSWDTYH 276
Cdd:cd01293 214 DPGSRtleelAEEAERRGMQGRvtCSHATAlGSLpeaevsrLADLLAEAGISVVSLPPinlyLQGREDTTPKRRGVTPVK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 277 TLSKHGIEVSITTDH---PYTPiqY-----LNVCAAIAVREGLDE----RIALEGVTIIPARNLRLEKRIgsIEVGKDAD 344
Cdd:cd01293 294 ELRAAGVNVALGSDNvrdPWYP--FgsgdmLEVANLAAHIAQLGTpedlALALDLITGNAARALGLEDYG--IKVGCPAD 369
|
...
gi 1264379975 345 LVL 347
Cdd:cd01293 370 LVL 372
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
3-347 |
7.87e-07 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 50.47 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 3 TLFKQAIVYpitSSKFQG--DVLVKHNQIAAIKPHIEST--QDMTVIDARALHLLPGFIDVHTHLglydEGTGWAGNDAN 78
Cdd:cd01308 2 TLIKNAEVY---APEYLGkkDILIAGGKILAIEDQLNLPgyENVTVVDLHGKILVPGFIDQHVHI----IGGGGEGGPST 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 79 ETSEVLTPHIRS-----------LDGI--HPFD-IAFQDAVENGVTTAHVMPGSQNIIGGT-TCVIKTAGTCIDHMIiqe 143
Cdd:cd01308 75 RTPEVTLSDLTTagvttvvgclgTDGIsrSMEDlLAKARALEEEGITCFVYTGSYEVPTRTiTGSIRKDLLLIDKVI--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 144 paGLKIAFGENPKRvhSNGTKESITRMG----IMGLL-RESFYEAQHYGNEAdfRML-PILKALRR-EIPVR----IHAH 212
Cdd:cd01308 152 --GVGEIAISDHRS--SQPTVEELARIAaearVGGLLgGKAGIVHIHLGDGK--RALsPIFELIEEtEIPITqflpTHIN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 213 RADDIL-SSLRFAK-----EFNLDLRIEHCTEGHFIVKELANQNLKISVGPtltrrSKIELKNKSWDTYHTLSKHGIEVS 286
Cdd:cd01308 226 RTAPLFeQGVEFAKmggtiDLTSSIDPQFRKEGEVRPSEALKRLLEQGVPL-----ERITFSSDGNGSLPKFDENGNLVG 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1264379975 287 IT---TDHPYTPIQYLNVCAAIAVregldeRIALEGVTIIPARNLRLEKRiGSIEVGKDADLVL 347
Cdd:cd01308 301 LGvgsVDTLLREVREAVKCGDIPL------EVALRVITSNVARILKLRKK-GEIQPGFDADLVI 357
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
20-82 |
1.01e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 50.10 E-value: 1.01e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1264379975 20 GDVLVKHNQIAAIKPhiESTQDMTVIDARALHLLPGFIDVHTHlglydegtGWAGNDANETSE 82
Cdd:COG1820 17 GALLIEDGRIAAIGP--GAEPDAEVIDLGGGYLAPGFIDLHVH--------GGGGVDFMDGTP 69
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
20-62 |
1.05e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 50.42 E-value: 1.05e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1264379975 20 GDVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTH 62
Cdd:PRK02382 20 RDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVH 62
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
21-63 |
1.54e-06 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 49.55 E-value: 1.54e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1264379975 21 DVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTHL 63
Cdd:PRK05985 18 DILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHL 60
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
21-73 |
1.68e-06 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 49.60 E-value: 1.68e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1264379975 21 DVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTHLglyDEGTGWA 73
Cdd:PRK07583 42 DIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTHL---DKGHIWP 91
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
19-63 |
2.41e-06 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 49.31 E-value: 2.41e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1264379975 19 QGDVLVKHNQIAAIKPHIESTQDMtVIDARALHLLPGFIDVHTHL 63
Cdd:PRK06189 20 RADIGIKNGKIAEIAPEISSPARE-IIDADGLYVFPGMIDVHVHF 63
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
42-347 |
3.23e-06 |
|
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: 48.44 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 42 MTVIDARALHLLPGFIDVHTHLGL--YDEGTGWAGNDANETSEVlTPHIRsldgihpfdiafqDAVENGVTTAHVMpGSQ 119
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHLGSdpGDLPLDLALPVEYRTIRA-TRQAR-------------AALRAGFTTVRDA-GGA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 120 NIIggttcVIKTAgtcIDHMIIQEPaglkiafgenpkRVHSNGTKESIT-RMGIMGLLRESFYeAQHYGNEAD------- 191
Cdd:cd01299 66 DYG-----LLRDA---IDAGLIPGP------------RVFASGRALSQTgGHGDPRGLSGLFP-AGGLAAVVDgveevra 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 192 -----FRM--------------------------LPILKAL-----RREIPVRIHAHRADDILSSLRfAkefNLDLrIEH 235
Cdd:cd01299 125 avreqLRRgadqikimatggvlspgdpppdtqfsEEELRAIvdeahKAGLYVAAHAYGAEAIRRAIR-A---GVDT-IEH 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 236 CTE------------GHFIVKELANQNLKISVG------PTLTRRSKIELKnKSWDTYHTLSKHGIEVSITTD--HPYTP 295
Cdd:cd01299 200 GFLiddetielmkekGIFLVPTLATYEALAAEGaapglpADSAEKVALVLE-AGRDALRRAHKAGVKIAFGTDagFPVPP 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1264379975 296 IQYLNVCAAIAVREGLDERIALEGVTIIPARNLRLEKRIGSIEVGKDADLVL 347
Cdd:cd01299 279 HGWNARELELLVKAGGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLV 330
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
299-350 |
3.51e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 48.56 E-value: 3.51e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1264379975 299 LNVCAAIAVRE-GLDERIALEGVTIIPARNLRLEKRIGSIEVGKDADLVLWTH 350
Cdd:COG1820 309 MDDAVRNLVEWtGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDD 361
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
20-352 |
1.45e-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: 46.81 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 20 GDVLVKHNQIAAIKPHIE--STQDMTVIDARALHLLPGFIDVHTHLGLydegT---GWAgnDANETSEVLTPHIRSLDGI 94
Cdd:cd01298 20 GDVLVEDGRIVAVGPALPlpAYPADEVIDAKGKVVMPGLVNTHTHLAM----TllrGLA--DDLPLMEWLKDLIWPLERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 95 HPfdiafQDAVENGVTTAHV-MpgsqnIIGGTTCViktagtcIDHMIIqEPAGLKIAFGENPKRVH------SNGTKESI 167
Cdd:cd01298 94 LT-----EEDVYLGALLALAeM-----IRSGTTTF-------ADMYFF-YPDAVAEAAEELGIRAVlgrgimDLGTEDVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 168 TRMGImglLRES--FYEAQHYGNEADFR--------------MLPILKALRREIPVRIHAHRA---DDILSSLR------ 222
Cdd:cd01298 156 ETEEA---LAEAerLIREWHGAADGRIRvalaphapytcsdeLLREVAELAREYGVPLHIHLAeteDEVEESLEkygkrp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 223 --FAKEFNL---DLRIEHCTegHFIVKELA-------------NQNLKISVGPTLTRRskielknkswdtyhtLSKHGIE 284
Cdd:cd01298 233 veYLEELGLlgpDVVLAHCV--WLTDEEIEllaetgtgvahnpASNMKLASGIAPVPE---------------MLEAGVN 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1264379975 285 VSITTDHPY----------TPIQYLNVCAAIAVREGLDERIALEGVTIIPARNLRLEKrIGSIEVGKDADLVLW-THHP 352
Cdd:cd01298 296 VGLGTDGAAsnnnldmfeeMRLAALLQKLAHGDPTALPAEEALEMATIGGAKALGLDE-IGSLEVGKKADLILIdLDGP 373
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
19-64 |
4.16e-05 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 45.13 E-value: 4.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1264379975 19 QGDVLVKHNQIAAIKpHIESTQDMTVIDARALHLLPGFIDVHTHLG 64
Cdd:TIGR00857 5 EVDILVEGGRIKKIG-KLRIPPDAEVIDAKGLLVLPGFIDLHVHLR 49
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
310-348 |
6.16e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 44.49 E-value: 6.16e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1264379975 310 GLDERIALEGVTIIPARNLRLEKRIGSIEVGKDADLVLW 348
Cdd:cd00854 323 GCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVL 361
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
1-63 |
7.12e-05 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 44.61 E-value: 7.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1264379975 1 MKTLFKQAIVYPITSSK--FQGDVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTHL 63
Cdd:PRK07228 1 MTILIKNAGIVTMNAKReiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHL 65
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
1-64 |
1.18e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 43.82 E-value: 1.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1264379975 1 MKTLFKQAIVY-PITSSKFQGDVLVKHNQIAAIKPHIESTQ-DMTVIDARALHLLPGFIDVHTHLG 64
Cdd:PRK07369 2 SNELLQQVRVLdPVSNTDRIADVLIEDGKIQAIEPHIDPIPpDTQIIDASGLILGPGLVDLYSHSG 67
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
19-63 |
1.47e-04 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 43.76 E-value: 1.47e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1264379975 19 QGDVLVKHNQIAAIKpHIESTQDMTVIDARALHLLPGFIDVHTHL 63
Cdd:PRK09060 22 RADIGIRDGRIAAIG-DLSGASAGEVIDCRGLHVLPGVIDSQVHF 65
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
20-62 |
2.23e-04 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 43.14 E-value: 2.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1264379975 20 GDVLVKHNQIAAIkphieSTQDMT---VIDARALHLLPGFIDVHTH 62
Cdd:PRK09061 39 RDVGIKGGKIAAV-----GTAAIEgdrTIDATGLVVAPGFIDLHAH 79
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
285-347 |
2.47e-04 |
|
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: 42.98 E-value: 2.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1264379975 285 VSITTD--HPYTPIQ--YLNVCAAIAVREGLDERIALEGVTIIPARNLRLEKrIGSIEVGKDADLVL 347
Cdd:cd01295 205 FMFCTDdvHPDDLLSegHLDYIVRRAIEAGIPPEDAIQMATINPAECYGLHD-LGAIAPGRIADIVI 270
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
311-346 |
3.31e-04 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 42.59 E-value: 3.31e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1264379975 311 LDERIALEGVTIIPARNLRLEKRIGSIEVGKDADLV 346
Cdd:PRK09045 340 LPAHTALRMATLNGARALGLDDEIGSLEPGKQADLV 375
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
321-366 |
3.43e-04 |
|
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: 42.70 E-value: 3.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1264379975 321 TIIPARNLRLEKRIGSIEVGKDADLVLWThhPFHYLAKPVLTMIEG 366
Cdd:cd00375 409 TINPAIAHGISHEVGSVEVGKLADLVLWE--PAFFGVKPEMVLKGG 452
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
18-62 |
3.58e-04 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 42.39 E-value: 3.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1264379975 18 FQGDVLVKHNQIAAIKPHIesTQDMTVIDARALHLLPGFIDVHTH 62
Cdd:COG1001 23 LEGDIAIAGGRIAGVGDYI--GEATEVIDAAGRYLVPGFIDGHVH 65
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-347 |
6.20e-04 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 41.41 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 1 MKTLFKQAIVYPITSSK--FQGDVLVKHNQIAAIKpHIESTQDMtVIDARALHLLPGFIDVHTHLGLydegTGWAG-NDA 77
Cdd:PRK06380 1 MSILIKNAWIVTQNEKReiLQGNVYIEGNKIVYVG-DVNEEADY-IIDATGKVVMPGLINTHAHVGM----TASKGlFDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 78 NETSEVLTPHI-----RSLDGIH-PFDIAFQDAVENGVTTAHVMPGSQNIIG------GTTCVIKTAgTCIDHMIIQEPA 145
Cdd:PRK06380 75 VDLEEFLMKTFkydskRTREGIYnSAKLGMYEMINSGITAFVDLYYSEDIIAkaaeelGIRAFLSWA-VLDEEITTQKGD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 146 GLKIAfgENPKRVHSNG--TKESITRMGIMGLLRESFYEAQHYGNEADFRMLPILKALRREI--PVRIHAHRADDILSSL 221
Cdd:PRK06380 154 PLNNA--ENFIREHRNEelVTPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETRKEVydHVKRTGERPVEHLEKI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 222 RFakeFNLDLRIEHCTEGHF-IVKELANQNLKISVGPTltrrSKIELKNKSWDTYHTLSKHGIEVSITTD-----HPYTP 295
Cdd:PRK06380 232 GF---LNSKLIAAHCVWATYhEIKLLSKNGVKVSWNSV----SNFKLGTGGSPPIPEMLDNGINVTIGTDsngsnNSLDM 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1264379975 296 IQYLNVCAAIAVREGLDERIA-----LEGVTIIPARNLRLEKriGSIEVGKDADLVL 347
Cdd:PRK06380 305 FEAMKFSALSVKNERWDASIIkaqeiLDFATINAAKALELNA--GSIEVGKLADLVI 359
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
321-361 |
6.57e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 41.70 E-value: 6.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1264379975 321 TIIPARNLRLEKRIGSIEVGKDADLVLWthHPFHYLAKPVL 361
Cdd:PRK13207 409 TINPAIAHGISHEVGSVEVGKLADLVLW--KPAFFGVKPEL 447
|
|
| PLN02303 |
PLN02303 |
urease |
321-359 |
7.60e-04 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 41.66 E-value: 7.60e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1264379975 321 TIIPARNLRLEKRIGSIEVGKDADLVLWthHPFHYLAKP 359
Cdd:PLN02303 678 TINPAIAHGMSHFVGSVEVGKLADLVLW--KPAFFGAKP 714
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
41-348 |
8.41e-04 |
|
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: 41.07 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 41 DMTVIDARALHLLPGFIDVHTHLGlyDEGTGWAGNDANE---------TSEVLTPHIR-SLDgiHPFDIAFQDAVENGVT 110
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLR--EPGFEYKETLESGakaaaaggfTTVVCMPNTNpVID--NPAVVELLKNRAKDVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 111 TAHVMPgsqniIGGTT-----------CVIKTAGtCI-----DHMIIQ-----------EPAGLKIAF-GENPKRVHSNG 162
Cdd:cd01317 77 IVRVLP-----IGALTkglkgeelteiGELLEAG-AVgfsddGKPIQDaellrraleyaAMLDLPIIVhPEDPSLAGGGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 163 TKESI--TRMGIMGLLRESfyeaqhygnEADfrMLPILKALRREIPVRIHAHRaddiLSS------LRFAKEFNLDLrie 234
Cdd:cd01317 151 MNEGKvaSRLGLPGIPPEA---------ETI--MVARDLELAEATGARVHFQH----LSTarslelIRKAKAKGLPV--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 235 HC--TEGHFIVKE--LANQNLKISVGPTLTRRSKIE-----LKNkswdtyhtlskhGIEVSITTDHpyTPIQY------- 298
Cdd:cd01317 213 TAevTPHHLLLDDeaLESYDTNAKVNPPLRSEEDREalieaLKD------------GTIDAIASDH--APHTDeekdlpf 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1264379975 299 -------------LNVCAAIAVREGLDERIAL-EGVTIIPARNLRLEKriGSIEVGKDADLVLW 348
Cdd:cd01317 279 aeappgiigletaLPLLWTLLVKGGLLTLPDLiRALSTNPAKILGLPP--GRLEVGAPADLVLF 340
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
18-61 |
8.43e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 40.93 E-value: 8.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1264379975 18 FQGDVLVKHNQIAAIKPhiESTQDMTVIDARALHLLPGFIDVHT 61
Cdd:PRK15446 18 VDGSLLIEDGRIAAIDP--GASALPGAIDAEGDYLLPGLVDLHT 59
|
|
| ureC |
PRK13309 |
urease subunit alpha; Reviewed |
320-366 |
9.65e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183966 [Multi-domain] Cd Length: 572 Bit Score: 41.01 E-value: 9.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1264379975 320 VTIIPARNLRLEKRIGSIEVGKDADLVLWthHPFHYLAKPVLTMIEG 366
Cdd:PRK13309 412 ITINPAITQGVSHVIGSVEVGKMADLVLW--EPRFFGAKPKMVIKGG 456
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
321-348 |
9.67e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 41.23 E-value: 9.67e-04
10 20
....*....|....*....|....*...
gi 1264379975 321 TIIPARNLRLEKRIGSIEVGKDADLVLW 348
Cdd:PRK13206 414 TICPAVAHGIDHEIGSVEVGKLADLVLW 441
|
|
| ade |
TIGR01178 |
adenine deaminase; The family described by this model includes an experimentally characterized ... |
9-63 |
1.14e-03 |
|
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: 40.91 E-value: 1.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1264379975 9 IVYPITSSKFQGDVLVKHNQIAAIkphiESTQDMTVIDARALHLLPGFIDVHTHL 63
Cdd:TIGR01178 9 IIDVYNGEIIPGDIAIANGHIAGV----GKYNGVKVIDALGEYAVPGFIDAHIHI 59
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
1-62 |
1.35e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 40.55 E-value: 1.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1264379975 1 MKTLFKQA-IVYPITSSKFQGDVLVKHNQIAAIKPHIESTQDmTVIDARALHLLPGFIDVHTH 62
Cdd:PRK08393 1 MSILIKNGyVIYGENLKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTH 62
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
321-348 |
1.37e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 40.46 E-value: 1.37e-03
10 20
....*....|....*....|....*...
gi 1264379975 321 TIIPARNLRLEKRIGSIEVGKDADLVLW 348
Cdd:PRK13308 410 TINPAITFGIDDHIGSLEPGKLADIVLW 437
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
311-350 |
1.84e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 39.96 E-value: 1.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1264379975 311 LDEriALEGVTIIPARNLRLEKRIGSIEVGKDADLVLWTH 350
Cdd:PRK11170 328 LDE--ALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTR 365
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
14-63 |
1.93e-03 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 40.07 E-value: 1.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1264379975 14 TSSKFQGDVLVKHNQIAAIKPHIESTQDmtVIDARALHLLPGFIDVHTHL 63
Cdd:PRK13404 16 ATDTFQADIGIRGGRIAALGEGLGPGAR--EIDATGRLVLPGGVDSHCHI 63
|
|
| UreC |
COG0804 |
Urease alpha subunit [Amino acid transport and metabolism]; |
321-348 |
2.17e-03 |
|
Urease alpha subunit [Amino acid transport and metabolism];
Pssm-ID: 440567 [Multi-domain] Cd Length: 570 Bit Score: 40.12 E-value: 2.17e-03
10 20
....*....|....*....|....*...
gi 1264379975 321 TIIPARNLRLEKRIGSIEVGKDADLVLW 348
Cdd:COG0804 411 TINPAIAHGISHEVGSVEVGKLADLVLW 438
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
21-349 |
2.83e-03 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 39.23 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 21 DVLVKHNQIAAIKPHIESTQDMTVIDARALHLLPGFIDVHTHlgLYDEGTgwagndanetsevltphirsLDGIHPFDIa 100
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVH--VYQGGT--------------------RYGDRPDMI- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 101 fqdAVENGVTTahVM----PGSQNIIGGTTCVIKTAGTCIDHMIIQEPAGLkIAFGE--NPKRVHSNGTKESITRMG--I 172
Cdd:cd01307 58 ---GVKSGVTT--VVdagsAGADNIDGFRYTVIERSATRVYAFLNISRVGL-VAQDElpDPDNIDEDAVVAAAREYPdvI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 173 MGL-LRESfyeaQHYGNEADFRMLPILKALRRE--IPVRIHAHRA----DDILSSLRFAkefnlDLrIEHCTEGH--FIV 243
Cdd:cd01307 132 VGLkARAS----KSVVGEWGIKPLELAKKIAKEadLPLMVHIGSPppilDEVVPLLRRG-----DV-LTHCFNGKpnGIV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 244 KElaNQNLKISVGPTLTRRSKIELKNK----SWDTYHTLSKHGI-EVSITTDHPYT-----PIQYLNVCAA--IAVREGL 311
Cdd:cd01307 202 DE--EGEVLPLVRRARERGVIFDVGHGtasfSFRVARAAIAAGLlPDTISSDIHGRnrtngPVYALATTLSklLALGMPL 279
|
330 340 350
....*....|....*....|....*....|....*...
gi 1264379975 312 DERIalEGVTIIPARNLRLeKRIGSIEVGKDADLVLWT 349
Cdd:cd01307 280 EEVI--EAVTANPARMLGL-AEIGTLAVGYDADLTVFD 314
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
306-347 |
3.20e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 39.31 E-value: 3.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1264379975 306 AVREGLDERIALEGVTIIPARNLRLeKRIGSIEVGKDADLVL 347
Cdd:COG1001 279 AIELGLDPVTAIQMATLNAAEHFGL-KDLGAIAPGRRADIVL 319
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
9-62 |
3.86e-03 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 38.97 E-value: 3.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1264379975 9 IVYPITSSKFQGDVLVKHNQIAAIKpHIESTQDMTVIDARALHLLPGFIDVHTH 62
Cdd:PRK12394 12 IIDPARNINEINNLRIINDIIVDAD-KYPVASETRIIHADGCIVTPGLIDYHAH 64
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
19-79 |
4.77e-03 |
|
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: 38.55 E-value: 4.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1264379975 19 QGDVLVKHNQIAAIKPHIE--STQDMTVIDARALHLLPGFIDVHTHLglydegtGWAGNDANE 79
Cdd:TIGR01224 3 DAVILIHGGKIVWIGQLAAlpGEEATEIIDCGGGLVTPGLVDPHTHL-------VFAGDRVNE 58
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
20-116 |
5.30e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 38.87 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264379975 20 GDVLVKHNQIAAIKPHIESTQDmTVIDARALHLLPGFIDV-------HTHLGLyDEGTGWAGND-------ANETSEVLT 85
Cdd:PRK06151 24 GEVVFEGDRILFVGHRFDGEVD-RVIDAGNALVGPGFIDLdalsdldTTILGL-DNGPGWAKGRvwsrdyvEAGRREMYT 101
|
90 100 110
....*....|....*....|....*....|....*..
gi 1264379975 86 PHirsldgihpfDIAFQDA------VENGVTTAhvMP 116
Cdd:PRK06151 102 PE----------ELAFQKRyafaqlLRNGITTA--MP 126
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
19-65 |
6.09e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 38.58 E-value: 6.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1264379975 19 QGDVLVKHNQIAAIKPHIESTQDmTVIDARALHLLPGFIDVHTHLGL 65
Cdd:PRK06038 21 KGSVVIEDGTITEVSESTPGDAD-TVIDAKGSVVMPGLVNTHTHAAM 66
|
|
| |
