|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
1-378 |
0e+00 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 604.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 1 MIINNVNLVLEDEVVHGSLEVQEGSIYAFAESQSQLPQALDGEDGWLLPGLIELHTDNLDKFFTPRPKVDWPAHSAMSSH 80
Cdd:PRK15446 4 MILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGAIDAEGDYLLPGLVDLHTDNLEKHLAPRPGVDWPADAALAAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 81 DALMVASGITTVLDAVAIGDVRDGGDRLENLE-KMINAIEETQKRGINRAEHRLHLRCELPHHTTLPLFEKLVDREPVTL 159
Cdd:PRK15446 84 DAQLAAAGITTVFDALSVGDEEDGGLRSRDLArKLIDAIEEARARGLLRADHRLHLRCELTNPDALELFEALLAHPRVDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 160 VSLMDHSPGQRQFANREKYREYYQGKYQLTHEQMLRYEEEQIALAATWSHANRRSIAAMCRDRHIALASHDDATAEHVLE 239
Cdd:PRK15446 164 VSLMDHTPGQRQFRDLEKYREYYAGKYGLSDEEFDAFVEERIALSARYAPPNRRAIAALARARGIPLASHDDDTPEHVAE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 240 SHQLGSVIAEFPTTLAAAEASRRHGMNVLMGAPNIVRGGSHSGNVAAHQLAASNLLDILSSDYYPASLLDAAFRIADDHD 319
Cdd:PRK15446 244 AHALGVAIAEFPTTLEAARAARALGMSVLMGAPNVVRGGSHSGNVSALDLAAAGLLDILSSDYYPASLLDAAFRLADDGG 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 695766872 320 naFSLPQAIRLVSKNPAQALGLDDRGVIAEGKRADMVLAHRRGEHVHIDHVWRQGKRVF 378
Cdd:PRK15446 324 --LDLPQAVALVTANPARAAGLDDRGEIAPGKRADLVRVRRAGGLPVVRAVWRGGRRVF 380
|
|
| PhnM |
COG3454 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase PhnM [Inorganic ion transport ... |
1-378 |
0e+00 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase PhnM [Inorganic ion transport and metabolism];
Pssm-ID: 442677 Cd Length: 383 Bit Score: 569.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 1 MIINNVNLVLEDEVVHGSLEVQEGSIYAFAESQSQLPQALDGEDGWLLPGLIELHTDNLDKFFTPRPKVDWPAHSAMSSH 80
Cdd:COG3454 5 LVITNARIVLPDEVIDGSVVIEDGRIAAIDEGASAAPGAIDAEGDYLLPGLVDLHTDNLERHIEPRPGVRWPLDAALLAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 81 DALMVASGITTVLDAVAIGDVRDGGDRLENLEKMINAIEETQKRGINRAEHRLHLRCELPHHTTLPLFEKLVDREPVTLV 160
Cdd:COG3454 85 DAQLAAAGITTVFDALSVGDEPDGGRRLENARALADAIAALRAAGLLRADHRLHLRCEVTSPDALELLEELLDDPRVDLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 161 SLMDHSPGQRQFANREKYREYYQGKYQLTHEQMLRYEEEQIALAATWSHANRRSIAAMCRDRHIALASHDDATAEHVLES 240
Cdd:COG3454 165 SLMDHTPGQRQFRDLEKYRAYYAGKYGLSDEEFDALVARRRALRARYAAANRAALVALARARGIPLASHDDDTAEHVAES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 241 HQLGSVIAEFPTTLAAAEASRRHGMNVLMGAPNIVRGGSHSGNVAAHQLAASNLLDILSSDYYPASLLDAAFRIADDHDn 320
Cdd:COG3454 245 AALGVAIAEFPTTLEAARAARAAGLAVLMGAPNVVRGGSHSGNVSAAELAEAGLLDILSSDYVPASLLAAAFRLAEDGG- 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 695766872 321 aFSLPQAIRLVSKNPAQALGLDDRGVIAEGKRADMVLAHRRGEHVHIDHVWRQGKRVF 378
Cdd:COG3454 324 -LDLPEAVALVTSNPARALGLDDRGEIAPGKRADLVRVRRLDGVPVVRAVWVAGRRVY 380
|
|
| phosphono_phnM |
TIGR02318 |
phosphonate metabolism protein PhnM; This family consists of proteins from in the PhnM family. ... |
2-378 |
0e+00 |
|
phosphonate metabolism protein PhnM; This family consists of proteins from in the PhnM family. PhnM is a a protein associated with phosphonate utilization in a number of bacterial species. In Pseudomonas stutzeri WM88, a protein that is part of a system for the oxidation of phosphites (another form of reduced phosphorous compound) scores between trusted and noise cutoffs. [Energy metabolism, Other]
Pssm-ID: 131371 Cd Length: 376 Bit Score: 551.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 2 IINNVNLVLEDEVVHGSLEVQEGSIYAFAESQSQLPQALDGEDGWLLPGLIELHTDNLDKFFTPRPKVDWPAHSAMSSHD 81
Cdd:TIGR02318 1 VLSNARLVLEDEVVEGSVVIEDGAIADIGEGPVALAEAIDGEGDLLLPGLIDLHTDNLERHMSPRPGVDWPIDAAIVEHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 82 ALMVASGITTVLDAVAIGDVRDGGDRLENLEKMINAIEETQKRGINRAEHRLHLRCELPHHTTLPLFEKLVDREPVTLVS 161
Cdd:TIGR02318 81 KQLAAAGITTVFDALALGDTESGGRRPDNLRRMIDAISEARDRGLLRADHRLHLRCELPNEEVLPELEELIDDPRVDLIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 162 LMDHSPGQRQFANREKYREYYQGKYQLTHEQMLRYEEEQIALAATWSHANRRSIAAMCRDRHIALASHDDATAEHVLESH 241
Cdd:TIGR02318 161 LMDHTPGQRQFRDLEKYREYYRGKRGLSDDEFDEIVEERIARRAEYGLANRSEIAALARARGIPLASHDDDTPEHVAEAH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 242 QLGSVIAEFPTTLAAAEASRRHGMNVLMGAPNIVRGGSHSGNVAAHQLAASNLLDILSSDYYPASLLDAAFRIADDHDNa 321
Cdd:TIGR02318 241 DLGVTISEFPTTLEAAKEARSLGMQILMGAPNIVRGGSHSGNLSARELAHEGLLDVLASDYVPASLLLAAFQLADDVEG- 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 695766872 322 FSLPQAIRLVSKNPAQALGLDDRGVIAEGKRADMVLAHRRGEHVHIDHVWRQGKRVF 378
Cdd:TIGR02318 320 IPLPQAVKMVTKNPARAVGLSDRGSIAPGKRADLVRVHRVDGVPRIRAVWRAGRRVY 376
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
48-374 |
1.19e-169 |
|
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: 476.39 E-value: 1.19e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 48 LPGLIELHTDNLDKFFTPRPKVDWPAHSAMSSHDALMVASGITTVLDAVAIGDVRDGGDRLENLEKMINAIEETQKRGIN 127
Cdd:cd01306 1 LPGLIDLHTDNLEKHVMPRPGVDWPMDIALAAHDRQLAAAGITTVFDALSFGDEEGGRRRLRNLRKLIDAIRELHARGVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 128 RAEHRLHLRCELPHHTTLPLFEKLVDREPVTLVSLMDHSPGQRQFANREKYREYYQGKYQLTHEQMLRYEEEQIALAATW 207
Cdd:cd01306 81 RADHRLHLRCELADPAVLPELESLMADPRVHLVSLMDHTPGQRQFRDLEKYREYYAKKYGLSDEEVEEAILERKARAAAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 208 SHANRRSIAAMCRDRHIALASHDDATAEHVLESHQLGSVIAEFPTTLAAAEASRRHGMNVLMGAPNIVRGGSHSGNVAAH 287
Cdd:cd01306 161 APANRSELAALARARGIPLASHDDDTPEHVAEAHELGVVISEFPTTLEAAKAARELGLQTLMGAPNVVRGGSHSGNVSAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 288 QLAASNLLDILSSDYYPASLLDAAFRIADDHDnaFSLPQAIRLVSKNPAQALGLDDRGVIAEGKRADMVLAHRRGEHVHI 367
Cdd:cd01306 241 ELAAHGLLDILSSDYVPASLLHAAFRLADLGG--WSLPEAVALVSANPARAVGLTDRGSIAPGKRADLILVDDMDGVPVV 318
|
....*..
gi 695766872 368 DHVWRQG 374
Cdd:cd01306 319 RTVWRGG 325
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
252-377 |
1.50e-12 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 68.59 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 252 TTLAAAEASRRHGMNVLMgapnivRGGSHSGNVAAhQLAAsnLLDILSS-------DYYPASLL-----DAAFRIADDHd 319
Cdd:COG1001 213 TTAEEALEKLRRGMYVMI------REGSAAKDLPA-LLPA--VTELNSRrcalctdDRHPDDLLeeghiDHVVRRAIEL- 282
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 695766872 320 nAFSLPQAIRLVSKNPAQALGLDDRGVIAEGKRADMVLAhRRGEHVHIDHVWRQGKRV 377
Cdd:COG1001 283 -GLDPVTAIQMATLNAAEHFGLKDLGAIAPGRRADIVLL-DDLEDFKVEKVYADGKLV 338
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-378 |
2.10e-12 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 67.68 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 1 MIINNVNLV--LEDEVV-HGSLEVQEGSIYAF-AESQSQLPQA---LDGEDGWLLPGLIELHT------DNLDKFFTPRP 67
Cdd:COG1228 10 LLITNATLVdgTGGGVIeNGTVLVEDGKIAAVgPAADLAVPAGaevIDATGKTVLPGLIDAHThlglggGRAVEFEAGGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 68 KVDWPAHSAMSSHDA-LMVASGITTVLDAvaigdvrdGGDRLENLEkminAIEETQKRGIN-----RAEHrlHLRCELPH 141
Cdd:COG1228 90 ITPTVDLVNPADKRLrRALAAGVTTVRDL--------PGGPLGLRD----AIIAGESKLLPgprvlAAGP--ALSLTGGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 142 HTTLP-----LFEKLVdREPVTLVSLMDhSPGQRQFaNREKYREYYQGKyqltHEQMLR-----YEEEQIALAA-----T 206
Cdd:COG1228 156 HARGPeearaALRELL-AEGADYIKVFA-EGGAPDF-SLEELRAILEAA----HALGLPvaahaHQADDIRLAVeagvdS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 207 WSHANRRS---IAAMcRDRHIALASHDDATAEHVLESHQLGSVIAE---FPTTLAAAEASRRHGMNVLMGapnivrggSH 280
Cdd:COG1228 229 IEHGTYLDdevADLL-AEAGTVVLVPTLSLFLALLEGAAAPVAAKArkvREAALANARRLHDAGVPVALG--------TD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 281 SGNVAAHqlAASNLLdilssdyypaslldaAFRIADDHDnaFSLPQAIRLVSKNPAQALGLDDR-GVIAEGKRADMV--- 356
Cdd:COG1228 300 AGVGVPP--GRSLHR---------------ELALAVEAG--LTPEEALRAATINAAKALGLDDDvGSLEPGKLADLVlld 360
|
410 420
....*....|....*....|....*
gi 695766872 357 ---LAHRRgEHVHIDHVWRQGKRVF 378
Cdd:COG1228 361 gdpLEDIA-YLEDVRAVMKDGRVVD 384
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
82-378 |
6.20e-10 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 60.62 E-value: 6.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 82 ALMVASGITTVLDAVAIGDVRDGGDRLENL---EKMINAIEETQKRGINRAEHRLHLRcelphhtTLPLFEklvdrepvt 158
Cdd:pfam07969 158 AALPGFGITSVDGGGGNVHSLDDYEPLRELtaaEKLKELLDAPERLGLPHSIYELRIG-------AMKLFA--------- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 159 lvslmDHSPGQRQFANREKYREYYQGKYQLTHEQMLryeEEQIALA--ATW---SHANRRSiAAMCRDRHIALASHDDAT 233
Cdd:pfam07969 222 -----DGVLGSRTAALTEPYFDAPGTGWPDFEDEAL---AELVAAAreRGLdvaIHAIGDA-TIDTALDAFEAVAEKLGN 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 234 AEHVLESHQLGSVIAEFPTTLAAAEASRRHGMNVLMGAPNIVRGGSHSGNVAAHQLAASNLL------DILSSDYyPASL 307
Cdd:pfam07969 293 QGRVRIEHAQGVVPYTYSQIERVAALGGAAGVQPVFDPLWGDWLQDRLGAERARGLTPVKELlnagvkVALGSDA-PVGP 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 308 LDAAFRI--ADDH-----------DNAFSLPQAIRLVSKNPAQALGLDDR-GVIAEGKRADMVLAHRRGEHVH------- 366
Cdd:pfam07969 372 FDPWPRIgaAVMRqtagggevlgpDEELSLEEALALYTSGPAKALGLEDRkGTLGVGKDADLVVLDDDPLTVDppaiadi 451
|
330
....*....|...
gi 695766872 367 -IDHVWRQGKRVF 378
Cdd:pfam07969 452 rVRLTVVDGRVVY 464
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
308-375 |
6.90e-10 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 60.11 E-value: 6.90e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695766872 308 LDAAFRIADDHDNAfSLPQAIRLVSKNPAQALGLDDR-GVIAEGKRADMVLAHrrgEHVHIDHVWRQGK 375
Cdd:COG1820 309 MDDAVRNLVEWTGL-PLEEAVRMASLNPARALGLDDRkGSIAPGKDADLVVLD---DDLNVRATWVGGE 373
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
1-374 |
1.59e-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: 58.74 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 1 MIINNVNLVLEDEVVHGSLEVQEGSIYAFAESQSQLP--QALDGEDGWLLPGLIELHTDNLDKFFTPrpkvDWPAHSA-- 76
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEadEIIDLKGQYLVPGFIDIHIHGGGGADFM----DGTAEALkt 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 77 MSSHdalMVASGITTVLDAVAIGDVrdggdrlENLEKMINAIEETQKRGINRAEHRLHL--------RC-----ELPHHT 143
Cdd:cd00854 77 IAEA---LAKHGTTSFLPTTVTAPP-------EEIAKALAAIAEAIAEGQGAEILGIHLegpfispeKKgahppEYLRAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 144 TLPLFEKLVD--REPVTLVSLMDHSPGQRQFanrekYREYYQG--KYQLTHeQMLRYEEEQIALAATWSHA----Nrrsi 215
Cdd:cd00854 147 DPEELKKWLEaaGGLIKLVTLAPELDGALEL-----IRYLVERgiIVSIGH-SDATYEQAVAAFEAGATHVthlfN---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 216 aAMC----RDRHI--ALASHDDATAEhvleshqlgsVIAEF----PTTLAAAEASRRH-----------------GMNVL 268
Cdd:cd00854 217 -AMSplhhREPGVvgAALSDDDVYAE----------LIADGihvhPAAVRLAYRAKGAdkivlvtdamaaaglpdGEYEL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 269 MGAPNIVRGGshsgnVAAHQ---LAASNLLdilssdyypaslLDAAFRIADDHDNaFSLPQAIRLVSKNPAQALGLDDR- 344
Cdd:cd00854 286 GGQTVTVKDG-----VARLAdgtLAGSTLT------------MDQAVRNMVKWGG-CPLEEAVRMASLNPAKLLGLDDRk 347
|
410 420 430
....*....|....*....|....*....|
gi 695766872 345 GVIAEGKRADMVLAHrrgEHVHIDHVWRQG 374
Cdd:cd00854 348 GSLKPGKDADLVVLD---DDLNVKATWING 374
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
231-378 |
7.26e-08 |
|
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: 53.85 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 231 DATAEHVLESHQLGSVIAEfpttlaaaeasrrHGMNVLMGAPNIVRGGS---HSGNVAAHQL-AASNLLDILSSD--YYP 304
Cdd:cd01309 218 KITIEHGAEGYKLADELAK-------------HGIPVIYGPTLTLPKKVeevNDAIDTNAYLlKKGGVAFAISSDhpVLN 284
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695766872 305 ASLLDAAFRIAddHDNAFSLPQAIRLVSKNPAQALGLDDR-GVIAEGKRADMVLAHrrGEHVH----IDHVWRQGKRVF 378
Cdd:cd01309 285 IRNLNLEAAKA--VKYGLSYEEALKAITINPAKILGIEDRvGSLEPGKDADLVVWN--GDPLEptskPEQVYIDGRLVY 359
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
321-378 |
8.01e-08 |
|
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: 53.84 E-value: 8.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 321 AFSLPQAIRLVSKNPAQALGLDDRGVIAEGKRADMVL-----AHRRGEHVH-------IDHVWRQGKRVF 378
Cdd:cd01297 334 LLSLEEAVRKMTGLPARVFGLADRGRIAPGYRADIVVfdpdtLADRATFTRpnqpaegIEAVLVNGVPVV 403
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
16-377 |
1.24e-07 |
|
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: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 16 HGSLEVQEGSIYA---FAESQSQLPQA--LDGEDGWLLPGLIELHT-----------DNLDkFFTPRPKVDWPAHSAMSS 79
Cdd:COG0402 21 DGAVLVEDGRIAAvgpGAELPARYPAAevIDAGGKLVLPGLVNTHThlpqtllrglaDDLP-LLDWLEEYIWPLEARLDP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 80 HDAL---------MVASGITTVLDAVAIGDvrdggdrlenlEKMINAIEETQKRGInraehRLHLrceLPHHTTLPLFEK 150
Cdd:COG0402 100 EDVYagallalaeMLRSGTTTVADFYYVHP-----------ESADALAEAAAEAGI-----RAVL---GRGLMDRGFPDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 151 LVDRepvtlvslmdhspGQRQFANREKYREYYQGKyqltHEQMLRYeeeqiALAAtwsHANR-------RSIAAMCRDRH 223
Cdd:COG0402 161 LRED-------------ADEGLADSERLIERWHGA----ADGRIRV-----ALAP---HAPYtvspellRAAAALARELG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 224 IALASH--------DDATAEH------VLESHQL------------------------GSVIAEFPTT-------LAAAE 258
Cdd:COG0402 216 LPLHTHlaetrdevEWVLELYgkrpveYLDELGLlgprtllahcvhltdeeiallaetGASVAHCPTSnlklgsgIAPVP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 259 ASRRHGMNVLMGapniVRGGshsgnvaahqlAASNLLDILssdyypASLLDAAF--RIADDHDNAFSLPQAIRLVSKNPA 336
Cdd:COG0402 296 RLLAAGVRVGLG----TDGA-----------ASNNSLDMF------EEMRLAALlqRLRGGDPTALSAREALEMATLGGA 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695766872 337 QALGLDDR-GVIAEGKRADMVL---------------------AHRRgehvHIDHVWRQGKRV 377
Cdd:COG0402 355 RALGLDDEiGSLEPGKRADLVVldldaphlaplhdplsalvyaADGR----DVRTVWVAGRVV 413
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
320-357 |
2.33e-07 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 52.48 E-value: 2.33e-07
10 20 30
....*....|....*....|....*....|....*...
gi 695766872 320 NAFSLPQAIRLVSKNPAQALGLDDRGVIAEGKRADMVL 357
Cdd:COG3653 438 GVLSLEEAVRKLTSLPADRLGLKDRGLLRPGYRADLVV 475
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
46-357 |
3.99e-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: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 46 WLLPGLIELHTDnldkfFTPRPKVDWPAHSAMSSHDAL-----MVASGITTVLDAvaiGDVRDGGDR--LENLEKMINAI 118
Cdd:pfam01979 1 IVLPGLIDAHVH-----LEMGLLRGIPVPPEFAYEALRlgittMLKSGTTTVLDM---GATTSTGIEalLEAAEELPLGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 119 EETQKRGIN----RAEHRLHLRCELphhttLPLFEKLVDREP-VTLVSLMDHSPgqrqfanrekyreyyqgkYQLTHEQM 193
Cdd:pfam01979 73 RFLGPGCSLdtdgELEGRKALREKL-----KAGAEFIKGMADgVVFVGLAPHGA------------------PTFSDDEL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 194 lryeeeqialaatwshanrRSIAAMCRDRHIALASHDDATAEHVLESHQLGSVIAEFPTTLAAAEASRRHGMNVLMGAPN 273
Cdd:pfam01979 130 -------------------KAALEEAKKYGLPVAIHALETKGEVEDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 274 I------------------------VRGGSHSGNVAAHQLAASNLLDILSSDYYPA--------SLLDAAFRIADDHDNa 321
Cdd:pfam01979 191 VhlspteanllaehlkgagvahcpfSNSKLRSGRIALRKALEDGVKVGLGTDGAGSgnslnmleELRLALELQFDPEGG- 269
|
330 340 350
....*....|....*....|....*....|....*..
gi 695766872 322 FSLPQAIRLVSKNPAQALGLDDR-GVIAEGKRADMVL 357
Cdd:pfam01979 270 LSPLEALRMATINPAKALGLDDKvGSIEVGKDADLVV 306
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
307-357 |
4.79e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 48.11 E-value: 4.79e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 695766872 307 LLDAAfriaddHDNAFSLPQAIRLVSKNPAQALGLDDRGVIAEGKRADMVL 357
Cdd:PRK02382 332 LLAAV------RKNRLPLERVRDVTAANPARIFGLDGKGRIAEGYDADLVL 376
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
1-357 |
1.25e-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: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 1 MIINNVNLVLED---EVVHGSLEVQEGSIYAFAESQSQLP----QALDGEDGWLLPGLIELHT-------------DNLD 60
Cdd:cd01298 1 ILIRNGTIVTTDprrVLEDGDVLVEDGRIVAVGPALPLPAypadEVIDAKGKVVMPGLVNTHThlamtllrgladdLPLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 61 KFFTprpKVDWPAHSAMSSHD---------ALMVASGITTVLDA------VAIGDVRDGGDRLENLEKMI---NAIEETQ 122
Cdd:cd01298 81 EWLK---DLIWPLERLLTEEDvylgallalAEMIRSGTTTFADMyffypdAVAEAAEELGIRAVLGRGIMdlgTEDVEET 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 123 KRGINRAEhRLHLRCELPHHttlPLFEklvdrepvtlVSLMDHSPgqrQFANREKYREYYQ--GKYQL---TH------- 190
Cdd:cd01298 158 EEALAEAE-RLIREWHGAAD---GRIR----------VALAPHAP---YTCSDELLREVAElaREYGVplhIHlaetede 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 191 -EQML-RYEEEQIALAATWSHANRRSIAAMC---RDRHIA-LASHDDATAeHVLESHQ-LGSVIAEFPTTLAAaeasrrh 263
Cdd:cd01298 221 vEESLeKYGKRPVEYLEELGLLGPDVVLAHCvwlTDEEIElLAETGTGVA-HNPASNMkLASGIAPVPEMLEA------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 264 GMNVLMGapniVRGgshsgnvaahqlAASNL-LDILSsDYYPASLLDaafRIADDHDNAFSLPQAIRLVSKNPAQALGLD 342
Cdd:cd01298 293 GVNVGLG----TDG------------AASNNnLDMFE-EMRLAALLQ---KLAHGDPTALPAEEALEMATIGGAKALGLD 352
|
410
....*....|....*
gi 695766872 343 DRGVIAEGKRADMVL 357
Cdd:cd01298 353 EIGSLEVGKKADLIL 367
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
261-357 |
1.56e-05 |
|
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: 46.45 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 261 RRHGMNVLMgapnivRGGSHSGNVAA-----HQLAASNLL----DILSSDYYPASLLDAAFRIAddHDNAFSLPQAIRLV 331
Cdd:cd01295 173 LRLGMYVML------REGSIAKNLEAllpaiTEKNFRRFMfctdDVHPDDLLSEGHLDYIVRRA--IEAGIPPEDAIQMA 244
|
90 100
....*....|....*....|....*.
gi 695766872 332 SKNPAQALGLDDRGVIAEGKRADMVL 357
Cdd:cd01295 245 TINPAECYGLHDLGAIAPGRIADIVI 270
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
277-378 |
1.69e-05 |
|
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: 46.17 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 277 GGSHSGNVAAHQLAASNLLDILSSD-YYPASLLDAAFRIADDHDN----AFSLPQAIRLVSKNPAQALGLDDRGVIAEGK 351
Cdd:cd01307 227 TASFSFRVARAAIAAGLLPDTISSDiHGRNRTNGPVYALATTLSKllalGMPLEEVIEAVTANPARMLGLAEIGTLAVGY 306
|
90 100 110
....*....|....*....|....*....|
gi 695766872 352 RADM-VLAHRRGEHVHIDHV--WRQGKRVF 378
Cdd:cd01307 307 DADLtVFDLKDGRVELVDSEgdTLIAERLL 336
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
322-375 |
1.94e-05 |
|
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: 46.23 E-value: 1.94e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 695766872 322 FSLPQAIRLVSKNPAQALGLDDRGVIAEGKRADMVLAHRRgehVHIDHVWRQGK 375
Cdd:cd01308 322 IPLEVALRVITSNVARILKLRKKGEIQPGFDADLVILDKD---LDINSVIAKGQ 372
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
277-368 |
3.50e-05 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 45.23 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 277 GGSHSGNVAAHQLAASNLLDILSSDYYPASLLDAAFRiadDHDNAFS--------LPQAIRLVSKNPAQALGLDDRGVIA 348
Cdd:PRK09237 246 TASFSFKVAEAAIAAGILPDTISTDIYCRNRINGPVY---SLATVMSkflalgmpLEEVIAAVTKNAADALRLPELGRLQ 322
|
90 100
....*....|....*....|.
gi 695766872 349 EGKRADM-VLAHRRGEHVHID 368
Cdd:PRK09237 323 VGSDADLtLFTLKDGPFTLTD 343
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
322-357 |
7.33e-05 |
|
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: 44.54 E-value: 7.33e-05
10 20 30
....*....|....*....|....*....|....*.
gi 695766872 322 FSLPQAIRLVSKNPAQALGLDDrGVIAEGKRADMVL 357
Cdd:cd01317 305 LTLPDLIRALSTNPAKILGLPP-GRLEVGAPADLVL 339
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
323-374 |
2.54e-04 |
|
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: 42.63 E-value: 2.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695766872 323 SLPQAIRLVSKNPAQALGL-DDRGVIAEGKRADMV---------LAHRRGEHvHIDHVWRQG 374
Cdd:cd01296 311 TPEEALTAATINAAAALGLgETVGSLEVGKQADLVildapsyehLAYRFGVN-LVEYVIKNG 371
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
295-358 |
2.55e-04 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 42.77 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 295 LDILSSDYYPASLL-------DAAFRIaDDHDNAFSL-------------PQAIRLVSKNPAQALGLdDRGVIAEGKRAD 354
Cdd:PRK08417 269 IDFLTSLHSAKSNSkkdlafdEAAFGI-DSICEYFSLcytylvkegiitwSELSRFTSYNPAQFLGL-NSGEIEVGKEAD 346
|
....
gi 695766872 355 MVLA 358
Cdd:PRK08417 347 LVLF 350
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
318-357 |
3.01e-04 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 42.49 E-value: 3.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 695766872 318 HDNAFSLPQAIRLVSKNPAQALGLDDrGVIAEGKRADMVL 357
Cdd:PRK09357 340 KTGLLDLEQLLEKMTINPARILGLPA-GPLAEGEPADLVI 378
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
319-357 |
3.40e-04 |
|
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: 42.30 E-value: 3.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 695766872 319 DNAFSLPQAIRLVSKNPAQALGLDD-RGVIAEGKRADMVL 357
Cdd:cd01300 440 EERLSLEEALRAYTIGAAYAIGEEDeKGSLEPGKLADFVV 479
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
319-357 |
3.82e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 42.48 E-value: 3.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 695766872 319 DNAFSLPQAIRLVSKNPAQALGLDDR-GVIAEGKRADMVL 357
Cdd:COG1574 464 EERLTVEEALRAYTIGAAYAAFEEDEkGSLEPGKLADFVV 503
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
287-357 |
6.84e-04 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 41.51 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 287 HQLAASNLLDILSSD-----YYPASLLD------AAFRIAD-DHdnafSLPQAIRLVSKNPAQALGLDDRGVIAEGKRAD 354
Cdd:PRK07583 317 HELKAAGIPVAVASDncrdpFYAYGDHDmlevfrEAVRILHlDH----PYDDWPAAVTTTPADIMGLPDLGRIAVGAPAD 392
|
...
gi 695766872 355 MVL 357
Cdd:PRK07583 393 LVL 395
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
323-357 |
9.27e-04 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 40.84 E-value: 9.27e-04
10 20 30
....*....|....*....|....*....|....*
gi 695766872 323 SLPQAIRLVSKNPAQALGLDDRGVIAEGKRADMVL 357
Cdd:cd01302 268 SLETLVEILSENPARIFGLYPKGTIAVGYDADLVI 302
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
226-354 |
2.06e-03 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 39.90 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 226 LASHDD-ATAEhVLESHqlgsviaefpTTLAAAEASRRHGMNVLMGAPniVRGGSHSGnvAAHQLAASNLLDILSSDY-- 302
Cdd:PRK09060 244 LADHKDvATVE-VTPHH----------LTLAAPECYERLGTLAQMNPP--IRDARHRD--GLWRGVRQGVVDVLGSDHap 308
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695766872 303 ---------YPAS---------LLDaafrIADDHDNA--FSLPQAIRLVSKNPAQALGLDDRGVIAEGKRAD 354
Cdd:PRK09060 309 htleekakpYPASpsgmtgvqtLVP----IMLDHVNAgrLSLERFVDLTSAGPARIFGIAGKGRIAVGYDAD 376
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
326-357 |
2.22e-03 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 39.58 E-value: 2.22e-03
10 20 30
....*....|....*....|....*....|...
gi 695766872 326 QAIRLVSKNPAQALGLDDR-GVIAEGKRADMVL 357
Cdd:cd01299 298 EALRAATANAAELLGLSDElGVIEAGKLADLLV 330
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
291-357 |
2.93e-03 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 39.47 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 291 ASNLLDILSSDYYPASL--------------------LDAAFRIAddHDNAFSLPQAIRLVSKNPAQALGLDDRGVIAEG 350
Cdd:PRK09236 299 ADDRIDVIATDHAPHTWeekqgpyfqapsglplvqhaLPALLELV--HEGKLSLEKVVEKTSHAPAILFDIKERGFIREG 376
|
....*..
gi 695766872 351 KRADMVL 357
Cdd:PRK09236 377 YWADLVL 383
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
38-117 |
3.62e-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: 38.81 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695766872 38 QALDGEDGWLLPGLIELHTdNLDKFFTPRPKVDWPAHSAMS----SHDALMVASGITTVLDAvaigdvrdGGDRLENLEK 113
Cdd:cd01299 2 QVIDLGGKTLMPGLIDAHT-HLGSDPGDLPLDLALPVEYRTiratRQARAALRAGFTTVRDA--------GGADYGLLRD 72
|
....
gi 695766872 114 MINA 117
Cdd:cd01299 73 AIDA 76
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
290-356 |
4.22e-03 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 39.12 E-value: 4.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695766872 290 AASN-LLDILSsDYYPASLLDAAfrIADDhdnAFSLP--QAIRLVSKNPAQALGLDDR-GVIAEGKRADMV 356
Cdd:PRK09045 311 AASNnDLDLFG-EMRTAALLAKA--VAGD---ATALPahTALRMATLNGARALGLDDEiGSLEPGKQADLV 375
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
318-357 |
6.88e-03 |
|
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: 38.42 E-value: 6.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 695766872 318 HDNAFSLPQAIRLVSKNPAQALGLDDR-GVIAEGKRADMVL 357
Cdd:cd01315 349 NKRGLSLEDIARLMCENPAKLFGLSHQkGRIAVGYDADFVV 389
|
|
| |
