|
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: 603.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 1 MIINNVKLVLDDDVVHGSLEVQDGRILAFAESQSRLPQALDGEGGWLLPGLIELHTDNLDKFFTPRPKVDWPAHSAMSSH 80
Cdd:PRK15446 4 MILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGAIDAEGDYLLPGLVDLHTDNLEKHLAPRPGVDWPADAALAAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 81 DAMMVASGITTVLDAVAIGDVRDGGDRLENLE-KMVNAVEETQKRGLNRAEHRLHLRCELPHHTTLPLFEKLIDRESVSM 159
Cdd:PRK15446 84 DAQLAAAGITTVFDALSVGDEEDGGLRSRDLArKLIDAIEEARARGLLRADHRLHLRCELTNPDALELFEALLAHPRVDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 160 VSLMDHSPGQRQYADRSKYRDYYQGKYHLTHDEMDRFEAEQMALAATWSQPNRQTIAAMCRARRIALASHDDATEAHVAE 239
Cdd:PRK15446 164 VSLMDHTPGQRQFRDLEKYREYYAGKYGLSDEEFDAFVEERIALSARYAPPNRRAIAALARARGIPLASHDDDTPEHVAE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 240 SHQLGSVIAEFPTTLAAAQASRQHGMHVLMGAPNIVRGGSHSGNVAAHLLANHGLLDILSSDYYPASLLDAAFRIADAED 319
Cdd:PRK15446 244 AHALGVAIAEFPTTLEAARAARALGMSVLMGAPNVVRGGSHSGNVSALDLAAAGLLDILSSDYYPASLLDAAFRLADDGG 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 490311675 320 naFTLAQAIRLVSKHPAQALGLDDRGVIAEGKRADLVLAHRRGEHVHIDHVWRQGRRVF 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: 576.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 1 MIINNVKLVLDDDVVHGSLEVQDGRILAFAESQSRLPQALDGEGGWLLPGLIELHTDNLDKFFTPRPKVDWPAHSAMSSH 80
Cdd:COG3454 5 LVITNARIVLPDEVIDGSVVIEDGRIAAIDEGASAAPGAIDAEGDYLLPGLVDLHTDNLERHIEPRPGVRWPLDAALLAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 81 DAMMVASGITTVLDAVAIGDVRDGGDRLENLEKMVNAVEETQKRGLNRAEHRLHLRCELPHHTTLPLFEKLIDRESVSMV 160
Cdd:COG3454 85 DAQLAAAGITTVFDALSVGDEPDGGRRLENARALADAIAALRAAGLLRADHRLHLRCEVTSPDALELLEELLDDPRVDLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 161 SLMDHSPGQRQYADRSKYRDYYQGKYHLTHDEMDRFEAEQMALAATWSQPNRQTIAAMCRARRIALASHDDATEAHVAES 240
Cdd:COG3454 165 SLMDHTPGQRQFRDLEKYRAYYAGKYGLSDEEFDALVARRRALRARYAAANRAALVALARARGIPLASHDDDTAEHVAES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 241 HQLGSVIAEFPTTLAAAQASRQHGMHVLMGAPNIVRGGSHSGNVAAHLLANHGLLDILSSDYYPASLLDAAFRIadAEDN 320
Cdd:COG3454 245 AALGVAIAEFPTTLEAARAARAAGLAVLMGAPNVVRGGSHSGNVSAAELAEAGLLDILSSDYVPASLLAAAFRL--AEDG 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 490311675 321 AFTLAQAIRLVSKHPAQALGLDDRGVIAEGKRADLVLAHRRGEHVHIDHVWRQGRRVF 378
Cdd:COG3454 323 GLDLPEAVALVTSNPARALGLDDRGEIAPGKRADLVRVRRLDGVPVVRAVWVAGRRVY 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: 546.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 2 IINNVKLVLDDDVVHGSLEVQDGRILAFAESQSRLPQALDGEGGWLLPGLIELHTDNLDKFFTPRPKVDWPAHSAMSSHD 81
Cdd:TIGR02318 1 VLSNARLVLEDEVVEGSVVIEDGAIADIGEGPVALAEAIDGEGDLLLPGLIDLHTDNLERHMSPRPGVDWPIDAAIVEHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 82 AMMVASGITTVLDAVAIGDVRDGGDRLENLEKMVNAVEETQKRGLNRAEHRLHLRCELPHHTTLPLFEKLIDRESVSMVS 161
Cdd:TIGR02318 81 KQLAAAGITTVFDALALGDTESGGRRPDNLRRMIDAISEARDRGLLRADHRLHLRCELPNEEVLPELEELIDDPRVDLIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 162 LMDHSPGQRQYADRSKYRDYYQGKYHLTHDEMDRFEAEQMALAATWSQPNRQTIAAMCRARRIALASHDDATEAHVAESH 241
Cdd:TIGR02318 161 LMDHTPGQRQFRDLEKYREYYRGKRGLSDDEFDEIVEERIARRAEYGLANRSEIAALARARGIPLASHDDDTPEHVAEAH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 242 QLGSVIAEFPTTLAAAQASRQHGMHVLMGAPNIVRGGSHSGNVAAHLLANHGLLDILSSDYYPASLLDAAFRIADAEDNa 321
Cdd:TIGR02318 241 DLGVTISEFPTTLEAAKEARSLGMQILMGAPNIVRGGSHSGNLSARELAHEGLLDVLASDYVPASLLLAAFQLADDVEG- 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490311675 322 FTLAQAIRLVSKHPAQALGLDDRGVIAEGKRADLVLAHRRGEHVHIDHVWRQGRRVF 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 |
1.04e-164 |
|
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: 463.68 E-value: 1.04e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 48 LPGLIELHTDNLDKFFTPRPKVDWPAHSAMSSHDAMMVASGITTVLDAVAIGDVRDGGDRLENLEKMVNAVEETQKRGLN 127
Cdd:cd01306 1 LPGLIDLHTDNLEKHVMPRPGVDWPMDIALAAHDRQLAAAGITTVFDALSFGDEEGGRRRLRNLRKLIDAIRELHARGVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 128 RAEHRLHLRCELPHHTTLPLFEKLIDRESVSMVSLMDHSPGQRQYADRSKYRDYYQGKYHLTHDEMDRFEAEQMALAATW 207
Cdd:cd01306 81 RADHRLHLRCELADPAVLPELESLMADPRVHLVSLMDHTPGQRQFRDLEKYREYYAKKYGLSDEEVEEAILERKARAAAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 208 SQPNRQTIAAMCRARRIALASHDDATEAHVAESHQLGSVIAEFPTTLAAAQASRQHGMHVLMGAPNIVRGGSHSGNVAAH 287
Cdd:cd01306 161 APANRSELAALARARGIPLASHDDDTPEHVAEAHELGVVISEFPTTLEAAKAARELGLQTLMGAPNVVRGGSHSGNVSAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 288 LLANHGLLDILSSDYYPASLLDAAFRIADaeDNAFTLAQAIRLVSKHPAQALGLDDRGVIAEGKRADLVLAHRRGEHVHI 367
Cdd:cd01306 241 ELAAHGLLDILSSDYVPASLLHAAFRLAD--LGGWSLPEAVALVSANPARAVGLTDRGSIAPGKRADLILVDDMDGVPVV 318
|
....*..
gi 490311675 368 DHVWRQG 374
Cdd:cd01306 319 RTVWRGG 325
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-378 |
4.98e-15 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 75.77 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 1 MIINNVKLVLDDD---VVHGSLEVQDGRILAF-AESQSRLPQA---LDGEGGWLLPGLIELHT------DNLDKFFTPRP 67
Cdd:COG1228 10 LLITNATLVDGTGggvIENGTVLVEDGKIAAVgPAADLAVPAGaevIDATGKTVLPGLIDAHThlglggGRAVEFEAGGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 68 KVDWPAHSAMSSHDA-MMVASGITTVLDAvaigdvrdGGDRLENLEkmvnAVEETQKRGLN-----RAEHrlHLRCELPH 141
Cdd:COG1228 90 ITPTVDLVNPADKRLrRALAAGVTTVRDL--------PGGPLGLRD----AIIAGESKLLPgprvlAAGP--ALSLTGGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 142 HTTLPlfeklidRESVSMVslmdhspgQRQYADRSKYRDYY--QGKYHLTHDEM------------------DRFEAEQM 201
Cdd:COG1228 156 HARGP-------EEARAAL--------RELLAEGADYIKVFaeGGAPDFSLEELraileaahalglpvaahaHQADDIRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 202 ALAA--------TWSqpNRQTIAAMCRARRIAL---ASHDDAtEAHVAESHQLGSVIAEFPTTLAAAQASRQHGMHVLMG 270
Cdd:COG1228 221 AVEAgvdsiehgTYL--DDEVADLLAEAGTVVLvptLSLFLA-LLEGAAAPVAAKARKVREAALANARRLHDAGVPVALG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 271 apnivrggSHSGNVAAHLLANHGLLDILssdyypaslldAAFRiadaednaFTLAQAIRLVSKHPAQALGLDDR-GVIAE 349
Cdd:COG1228 298 --------TDAGVGVPPGRSLHRELALA-----------VEAG--------LTPEEALRAATINAAKALGLDDDvGSLEP 350
|
410 420 430
....*....|....*....|....*....|....*
gi 490311675 350 GKRADLV------LAHRRgEHVHIDHVWRQGRRVF 378
Cdd:COG1228 351 GKLADLVlldgdpLEDIA-YLEDVRAVMKDGRVVD 384
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
216-378 |
5.90e-12 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 66.79 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 216 AAMCRARRIALASHDDATEAHVAESHqlGSVIAEFPTTLAAAQASRQ--HGMHVLMGAPNIVRGGSHSGNVAAH------ 287
Cdd:pfam07969 275 TIDTALDAFEAVAEKLGNQGRVRIEH--AQGVVPYTYSQIERVAALGgaAGVQPVFDPLWGDWLQDRLGAERARgltpvk 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 288 LLANHGLLDILSSDYyPASLLDAAFRIADA-------------EDNAFTLAQAIRLVSKHPAQALGLDDR-GVIAEGKRA 353
Cdd:pfam07969 353 ELLNAGVKVALGSDA-PVGPFDPWPRIGAAvmrqtagggevlgPDEELSLEEALALYTSGPAKALGLEDRkGTLGVGKDA 431
|
170 180 190
....*....|....*....|....*....|...
gi 490311675 354 DLVLAHRRGEHVH--------IDHVWRQGRRVF 378
Cdd:pfam07969 432 DLVVLDDDPLTVDppaiadirVRLTVVDGRVVY 464
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
252-377 |
6.77e-12 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 66.66 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 252 TTLAAAQASRQHGMHVLMgapnivRGGSHSGNVAAhLLAnhGLLDILSS-------DYYPASLL-----DAAFRIA---- 315
Cdd:COG1001 213 TTAEEALEKLRRGMYVMI------REGSAAKDLPA-LLP--AVTELNSRrcalctdDRHPDDLLeeghiDHVVRRAielg 283
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490311675 316 -DAEDnaftlaqAIRLVSKHPAQALGLDDRGVIAEGKRADLVLAhRRGEHVHIDHVWRQGRRV 377
Cdd:COG1001 284 lDPVT-------AIQMATLNAAEHFGLKDLGAIAPGRRADIVLL-DDLEDFKVEKVYADGKLV 338
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
308-375 |
4.17e-09 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 57.42 E-value: 4.17e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490311675 308 LDAAFRIAdAEDNAFTLAQAIRLVSKHPAQALGLDDR-GVIAEGKRADLVLAHrrgEHVHIDHVWRQGR 375
Cdd:COG1820 309 MDDAVRNL-VEWTGLPLEEAVRMASLNPARALGLDDRkGSIAPGKDADLVVLD---DDLNVRATWVGGE 373
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
318-357 |
1.10e-08 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 56.72 E-value: 1.10e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 490311675 318 EDNAFTLAQAIRLVSKHPAQALGLDDRGVIAEGKRADLVL 357
Cdd:COG3653 436 ERGVLSLEEAVRKLTSLPADRLGLKDRGLLRPGYRADLVV 475
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
1-374 |
2.17e-08 |
|
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: 55.28 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 1 MIINNVKLVLDDDVVHGSLEVQDGRILAFAESQSRLP--QALDGEGGWLLPGLIELHTDNLDKFFTPrpkvDWPAHSA-- 76
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEadEIIDLKGQYLVPGFIDIHIHGGGGADFM----DGTAEALkt 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 77 MSSHdamMVASGITTVLDAVAIGDVrdggdrlENLEKMVNAVEETQKRGLNRAEHRLHL--------RC-----ELPHHT 143
Cdd:cd00854 77 IAEA---LAKHGTTSFLPTTVTAPP-------EEIAKALAAIAEAIAEGQGAEILGIHLegpfispeKKgahppEYLRAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 144 TLPLFEKLID--RESVSMVSLMDHSPGQRQYADRSKYR-----------DYYQGK-------YHLTH--DEMDRFEAEQM 201
Cdd:cd00854 147 DPEELKKWLEaaGGLIKLVTLAPELDGALELIRYLVERgiivsighsdaTYEQAVaafeagaTHVTHlfNAMSPLHHREP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 202 ALAAtwsqpnrqtiaamcrarriALASHDDATeahvAEshqlgsVIAEF----PTTLAAAQASRQH-------------- 263
Cdd:cd00854 227 GVVG-------------------AALSDDDVY----AE------LIADGihvhPAAVRLAYRAKGAdkivlvtdamaaag 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 264 ---GMHVLMGAPNIVRGGshsgnvAAHL----LAnhglldilSSDyypaSLLDAAFRIAdAEDNAFTLAQAIRLVSKHPA 336
Cdd:cd00854 278 lpdGEYELGGQTVTVKDG------VARLadgtLA--------GST----LTMDQAVRNM-VKWGGCPLEEAVRMASLNPA 338
|
410 420 430
....*....|....*....|....*....|....*....
gi 490311675 337 QALGLDDR-GVIAEGKRADLVLAHrrgEHVHIDHVWRQG 374
Cdd:cd00854 339 KLLGLDDRkGSLKPGKDADLVVLD---DDLNVKATWING 374
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
46-357 |
3.55e-08 |
|
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: 54.43 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 46 WLLPGLIELHTDnldkfFTPRPKVDWPAHSAMSSHDAM-----MVASGITTVLDAVAIGDvrdggdrlENLEKMVNAVEE 120
Cdd:pfam01979 1 IVLPGLIDAHVH-----LEMGLLRGIPVPPEFAYEALRlgittMLKSGTTTVLDMGATTS--------TGIEALLEAAEE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 121 tQKRGLNRAEHRLHLRCELPHHTTLPLFEKLIDR--------ESVSMVSLMDHSPgqrqyadrskyrdyyqgkYHLTHDE 192
Cdd:pfam01979 68 -LPLGLRFLGPGCSLDTDGELEGRKALREKLKAGaefikgmaDGVVFVGLAPHGA------------------PTFSDDE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 193 MDRfeaeqmalaatwsqpnrqtIAAMCRARRIALASHDDATEAHVAESHQLGSVIAEFPTTLAAAQAS---------RQH 263
Cdd:pfam01979 129 LKA-------------------ALEEAKKYGLPVAIHALETKGEVEDAIAAFGGGIEHGTHLEVAESGglldiikliLAH 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 264 GMHVLMGAPNIVR---------------GGSHSGNVAAHLLANHGLLDILSSDYYPA--------SLLDAAFRIADAEDN 320
Cdd:pfam01979 190 GVHLSPTEANLLAehlkgagvahcpfsnSKLRSGRIALRKALEDGVKVGLGTDGAGSgnslnmleELRLALELQFDPEGG 269
|
330 340 350
....*....|....*....|....*....|....*...
gi 490311675 321 aFTLAQAIRLVSKHPAQALGLDDR-GVIAEGKRADLVL 357
Cdd:pfam01979 270 -LSPLEALRMATINPAKALGLDDKvGSIEVGKDADLVV 306
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
1-357 |
7.10e-08 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 53.75 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 1 MIINNVKLVLDDD---VVHGSLEVQDGRILAFAESQSRLP----QALDGEGGWLLPGLIELHT-------------DNLD 60
Cdd:cd01298 1 ILIRNGTIVTTDPrrvLEDGDVLVEDGRIVAVGPALPLPAypadEVIDAKGKVVMPGLVNTHThlamtllrgladdLPLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 61 KFFTprpKVDWPAHSAMSSHD---------AMMVASGITTVLDA------VAIGDVRDGGDR----LENLEKMVNAVEET 121
Cdd:cd01298 81 EWLK---DLIWPLERLLTEEDvylgallalAEMIRSGTTTFADMyffypdAVAEAAEELGIRavlgRGIMDLGTEDVEET 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 122 QkRGLNRAEhRLHLRCELPHHttlPLFEklidresvsmVSLMDHSPgqrQYADRSKYR------DYYQGKYHL----THD 191
Cdd:cd01298 158 E-EALAEAE-RLIREWHGAAD---GRIR----------VALAPHAP---YTCSDELLRevaelaREYGVPLHIhlaeTED 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 192 EMDRFEAEQMALAATWSQP----NRQTIAAMC---RARRIALASHDDATEAHVAESHQ-LGSVIAEFPTTLAAaqasrqh 263
Cdd:cd01298 220 EVEESLEKYGKRPVEYLEElgllGPDVVLAHCvwlTDEEIELLAETGTGVAHNPASNMkLASGIAPVPEMLEA------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 264 GMHVLMGApnivrGGSHSGNVaahllanhglLDILsSDYYPASLLDaafRIADAEDNAFTLAQAIRLVSKHPAQALGLDD 343
Cdd:cd01298 293 GVNVGLGT-----DGAASNNN----------LDMF-EEMRLAALLQ---KLAHGDPTALPAEEALEMATIGGAKALGLDE 353
|
410
....*....|....
gi 490311675 344 RGVIAEGKRADLVL 357
Cdd:cd01298 354 IGSLEVGKKADLIL 367
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
16-377 |
1.45e-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: 52.91 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 16 HGSLEVQDGRILA---FAESQSRLPQA--LDGEGGWLLPGLIELHT-----------DNLDkFFTPRPKVDWPAHSAMSS 79
Cdd:COG0402 21 DGAVLVEDGRIAAvgpGAELPARYPAAevIDAGGKLVLPGLVNTHThlpqtllrglaDDLP-LLDWLEEYIWPLEARLDP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 80 HD---------AMMVASGITTVLDAVAIGDvrdggdrlenlEKMVNAVEETQKRGLnRA-------EHRLHLRCELPHHT 143
Cdd:COG0402 100 EDvyagallalAEMLRSGTTTVADFYYVHP-----------ESADALAEAAAEAGI-RAvlgrglmDRGFPDGLREDADE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 144 TLPLFEKLIDR---ESVSMVSLM--DHSP---------GQRQYADRskyrdyYQGKYHL----THDEMDRFEAEQ----M 201
Cdd:COG0402 168 GLADSERLIERwhgAADGRIRVAlaPHAPytvspellrAAAALARE------LGLPLHThlaeTRDEVEWVLELYgkrpV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 202 ALAATWSQPNRQTIAAMC---RARRIALASHDDATEAHVAESH-QLGSVIAEFPTTLAAaqasrqhGMHVLMGapniVRG 277
Cdd:COG0402 242 EYLDELGLLGPRTLLAHCvhlTDEEIALLAETGASVAHCPTSNlKLGSGIAPVPRLLAA-------GVRVGLG----TDG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 278 GshSGNVAAHLLANhglldilssdyypasLLDAAF--RIADAEDNAFTLAQAIRLVSKHPAQALGLDDR-GVIAEGKRAD 354
Cdd:COG0402 311 A--ASNNSLDMFEE---------------MRLAALlqRLRGGDPTALSAREALEMATLGGARALGLDDEiGSLEPGKRAD 373
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 490311675 355 LVLAHRRGEHV-----------------HIDHVWRQGRRV 377
Cdd:COG0402 374 LVVLDLDAPHLaplhdplsalvyaadgrDVRTVWVAGRVV 413
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
321-378 |
1.83e-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: 52.68 E-value: 1.83e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 321 AFTLAQAIRLVSKHPAQALGLDDRGVIAEGKRADLVL-----AHRRGEHVH-------IDHVWRQGRRVF 378
Cdd:cd01297 334 LLSLEEAVRKMTGLPARVFGLADRGRIAPGYRADIVVfdpdtLADRATFTRpnqpaegIEAVLVNGVPVV 403
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
23-378 |
4.27e-07 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 51.16 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 23 DGRILAFAEsQSRLP---QALDGEGGWLLPGLIELHTD-NLDKFFTPRPKVD------------------WPAHSAMSsh 80
Cdd:cd01309 1 DGKIVAVGA-EITTPadaEVIDAKGKHVTPGLIDAHSHlGLDEEGGVRETSDaneetdpvtphvraidgiNPDDEAFK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 81 daMMVASGITTVL----DAVAIG--------DVRDGGDRLENLE---KMvnAVEETQKRGLNRAEHRLHLRCElphhTTL 145
Cdd:cd01309 78 --RARAGGVTTVQvlpgSANLIGgqgvviktDGGTIEDMFIKAPaglKM--ALGENPKRVYGGKGKEPATRMG----VAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 146 PLFEKLIDresvsmvslmdhspgQRQYAdrSKYRDYYQGKyhlthDEMDRFEAEQMALAATWsqpnRQTIAAMCRARRIA 225
Cdd:cd01309 150 LLRDAFIK---------------AQEYG--RKYDLGKNAK-----KDPPERDLKLEALLPVL----KGEIPVRIHAHRAD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 226 --LASHDDATE-------AHVAESHQLGSVIAEfpttlaaaqasrqHGMHVLMGAPNIVRGGSHSGN----VAAHLLANH 292
Cdd:cd01309 204 diLTAIRIAKEfgikitiEHGAEGYKLADELAK-------------HGIPVIYGPTLTLPKKVEEVNdaidTNAYLLKKG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 293 GLLDILSSDYYPASLLDAAFRIADAEDNAFTLAQAIRLVSKHPAQALGLDDR-GVIAEGKRADLVLAHrrGEHVH----I 367
Cdd:cd01309 271 GVAFAISSDHPVLNIRNLNLEAAKAVKYGLSYEEALKAITINPAKILGIEDRvGSLEPGKDADLVVWN--GDPLEptskP 348
|
410
....*....|.
gi 490311675 368 DHVWRQGRRVF 378
Cdd:cd01309 349 EQVYIDGRLVY 359
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
291-357 |
1.32e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 50.04 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 291 NHGLLDILSSDYYPASLLDAAFRIADA------------------EDNAFTLAQAIRLVSKHPAQALGLDDRGVIAEGKR 352
Cdd:PRK02382 292 NDGTIDVVASDHAPHTREEKDADIWDApsgvpgvetmlplllaavRKNRLPLERVRDVTAANPARIFGLDGKGRIAEGYD 371
|
....*
gi 490311675 353 ADLVL 357
Cdd:PRK02382 372 ADLVL 376
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
291-357 |
1.37e-06 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 49.64 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 291 NHGLLDILSSDYYPASLLDAAFRIADA------------------EDNAFTLAQAIRLVSKHPAQALGLDDRGVIAEGKR 352
Cdd:cd01318 238 ADGRIDVIASDHAPHTLEEKRKGYPAApsgipgvetalplmltlvNKGILSLSRVVRLTSHNPARIFGIKNKGRIAEGYD 317
|
....*
gi 490311675 353 ADLVL 357
Cdd:cd01318 318 ADLTV 322
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
254-368 |
1.93e-06 |
|
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: 49.25 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 254 LAAAQASRQHGMHVLMGapnivRGGSH-SGNVAAHLLANHGLLDILSSD-YYPASLLDAAFRIADAEDN----AFTLAQA 327
Cdd:cd01307 208 LPLVRRARERGVIFDVG-----HGTASfSFRVARAAIAAGLLPDTISSDiHGRNRTNGPVYALATTLSKllalGMPLEEV 282
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 490311675 328 IRLVSKHPAQALGLDDRGVIAEGKRADL-VLAHRRGEHVHID 368
Cdd:cd01307 283 IEAVTANPARMLGLAEIGTLAVGYDADLtVFDLKDGRVELVD 324
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
252-357 |
2.20e-06 |
|
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: 49.14 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 252 TTLAAAQASRQHGMHVLMgapnivRGGSHSGNVAAHLLANHGLL---------DILSSDYYPASLLDAAFRIAdaEDNAF 322
Cdd:cd01295 164 MTGEEALEKLRLGMYVML------REGSIAKNLEALLPAITEKNfrrfmfctdDVHPDDLLSEGHLDYIVRRA--IEAGI 235
|
90 100 110
....*....|....*....|....*....|....*
gi 490311675 323 TLAQAIRLVSKHPAQALGLDDRGVIAEGKRADLVL 357
Cdd:cd01295 236 PPEDAIQMATINPAECYGLHDLGAIAPGRIADIVI 270
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
322-357 |
3.26e-06 |
|
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: 48.93 E-value: 3.26e-06
10 20 30
....*....|....*....|....*....|....*.
gi 490311675 322 FTLAQAIRLVSKHPAQALGLDDRGVIAEGKRADLVL 357
Cdd:COG0044 345 LSLERLVELLSTNPARIFGLPRKGRIAVGADADLVL 380
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
2-56 |
3.71e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 48.56 E-value: 3.71e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 490311675 2 IINNVKLVLDDDVVH-GSLEVQDGRILAFAESQSRLPQALDGEGGWLLPGLIELHT 56
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPGAEPDAEVIDLGGGYLAPGFIDLHV 56
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1-357 |
1.51e-05 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 46.62 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 1 MIINNVKLVLDDDVVHGSLEVQDGRILAFAES-QSRLPQALDGEGGWLLPGLIELHTDnldkfFTPRPKVDWpahSAMSS 79
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEiSSPAREIIDADGLYVFPGMIDVHVH-----FNEPGRTHW---EGFAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 80 HDAMMVASGITTVLDAvaigdvrdggdRLENLEKMVNAVEETQKRGLNRAEHRLHLRC---ELPHHttLPLFEKLIDRES 156
Cdd:PRK06189 77 GSAALAAGGCTTYFDM-----------PLNSIPPTVTREALDAKAELARQKSAVDFALwggLVPGN--LEHLRELAEAGV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 157 VSMVSLMDHSPGQ--RQYADRSKYRDYYQ----GKYHLTHDEMDRFEAeqmALAATWSQPNRQTIAAMCRAR-------- 222
Cdd:PRK06189 144 IGFKAFMSNSGTDefRSSDDLTLYEGMKEiaalGKILALHAESDALTR---HLTTQARQQGKTDVRDYLESRpvvaelea 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 223 --RIALASHDDATEAHVAeshQLGSVIAefpttLAAAQASRQHGMHV----------------------LMGAPNiVRGG 278
Cdd:PRK06189 221 vqRALLYAQETGCPLHFV---HISSGKA-----VALIAEAKKRGVDVsvetcphyllfteedferigavAKCAPP-LRSR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 279 SHSGNVAAHLLAnhGLLDILSSDYYPA--------SLLDAAFRIADAEdnaFTLA---------------QAIRLVSKHP 335
Cdd:PRK06189 292 SQKEELWRGLLA--GEIDMISSDHSPCppelkegdDFFLVWGGISGGQ---STLLvmltegyiergipleTIARLLATNP 366
|
410 420
....*....|....*....|..
gi 490311675 336 AQALGLDDRGVIAEGKRADLVL 357
Cdd:PRK06189 367 AKRFGLPQKGRLEVGADADFVL 388
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
293-358 |
5.73e-05 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 44.69 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 293 GLLDILSSDYYPASLL-------DAAFRIaDAEDNAF-------------TLAQAIRLVSKHPAQALGLdDRGVIAEGKR 352
Cdd:PRK08417 267 GKIDFLTSLHSAKSNSkkdlafdEAAFGI-DSICEYFslcytylvkegiiTWSELSRFTSYNPAQFLGL-NSGEIEVGKE 344
|
....*.
gi 490311675 353 ADLVLA 358
Cdd:PRK08417 345 ADLVLF 350
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
277-368 |
1.02e-04 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 44.07 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 277 GGSHSGNVAAHLLANHGLLDILSSDYYPASLLD-AAFRIADAEDNAF----TLAQAIRLVSKHPAQALGLDDRGVIAEGK 351
Cdd:PRK09237 246 TASFSFKVAEAAIAAGILPDTISTDIYCRNRINgPVYSLATVMSKFLalgmPLEEVIAAVTKNAADALRLPELGRLQVGS 325
|
90
....*....|....*...
gi 490311675 352 RADL-VLAHRRGEHVHID 368
Cdd:PRK09237 326 DADLtLFTLKDGPFTLTD 343
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
286-374 |
1.08e-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: 43.79 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 286 AHLLANHGLLDILSSDY----YPASLLDAAFRIAdAEDNAFTLAQAIRLVSKHPAQALGL-DDRGVIAEGKRADLV---- 356
Cdd:cd01296 271 ARKLIDAGVPVALGTDFnpgsSPTSSMPLVMHLA-CRLMRMTPEEALTAATINAAAALGLgETVGSLEVGKQADLVilda 349
|
90 100
....*....|....*....|...
gi 490311675 357 -----LAHRRGEHvHIDHVWRQG 374
Cdd:cd01296 350 psyehLAYRFGVN-LVEYVIKNG 371
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
293-357 |
1.60e-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: 43.38 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 293 GLLDILSSDYYP-------ASLLDAAFRIADAEdNAF-------------TLAQAIRLVSKHPAQALGLDDrGVIAEGKR 352
Cdd:cd01317 257 GTIDAIASDHAPhtdeekdLPFAEAPPGIIGLE-TALpllwtllvkggllTLPDLIRALSTNPAKILGLPP-GRLEVGAP 334
|
....*
gi 490311675 353 ADLVL 357
Cdd:cd01317 335 ADLVL 339
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
1-357 |
1.71e-04 |
|
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: 43.43 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 1 MIINNVKLVLDDDVVHGSLEVQDGRILAFAESQSRLP--QALDGEGGWLLPGLIELHTDNLDKFFTprpkvDWPAHSAMS 78
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEaeEVIDAGGLVVMPGLIDTHVHINEPGRT-----EWEGFETGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 79 shdAMMVASGITTVLDAV--AIGDVRDGgdrlENLEKMVNAVEETQK------RGL---NRAE-HRLH------LRC--- 137
Cdd:cd01315 77 ---KAAAAGGITTIIDMPlnSIPPTTTV----ENLEAKLEAAQGKLHvdvgfwGGLvpgNLDQlRPLDeagvvgFKCflc 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 138 -----ELPHHTTLPLFE---KLIDRESVSMV-----SLMDHSPGQRQYADRSKYRDYYQGKYHLTHDemdrfEAEQMALa 204
Cdd:cd01315 150 psgvdEFPAVDDEQLEEamkELAKTGSVLAVhaenpEITEALQEQAKAKGKRDYRDYLASRPVFTEV-----EAIQRIL- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 205 atwsqpnRQTIAAMCRArRIALASHDDATEAhVAESHQLG-SVIAEfpT-----TLAAAQASRqhGMHVLMGAPNIvRGG 278
Cdd:cd01315 224 -------LLAKETGCRL-HIVHLSSAEAVPL-IREARAEGvDVTVE--TcphylTFTAEDVPD--GGTEFKCAPPI-RDA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 279 SHSGNVAAHLLAnhGLLDILSSDYYPASLLDAAFRIAD----------------------AEDNAFTLAQAIRLVSKHPA 336
Cdd:cd01315 290 ANQEQLWEALEN--GDIDMVVSDHSPCTPELKLLGKGDffkawggisglqlglpvmlteaVNKRGLSLEDIARLMCENPA 367
|
410 420
....*....|....*....|..
gi 490311675 337 QALGLDDR-GVIAEGKRADLVL 357
Cdd:cd01315 368 KLFGLSHQkGRIAVGYDADFVV 389
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
88-357 |
2.01e-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: 43.07 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 88 GITTVLDAVAigdvrDGGDRLENLEKMVNAVEETqkrglnraehrLHLR-CELPHHTTLPLFEKLIDRE--------SVS 158
Cdd:cd01300 196 GVTTVHDAGG-----GAADDIEAYRRLAAAGELT-----------LRVRvALYVSPLAEDLLEELGARKngagddrlRLG 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 159 MVSL-MDHSPGQRQYADRSKYRDYYQGKYHLTHDEmDRFEAE---------QMALAATWSQPNRQTIAAMCRAR------ 222
Cdd:cd01300 260 GVKLfADGSLGSRTAALSEPYLDSPGTGGLLLISP-EELEELvraadeaglQVAIHAIGDRAVDTVLDALEAALkdnpra 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 223 ----RIALASHddATEAHVAESHQLGsVIAEFpttlaaaqasrQHGM-HVLMGAPNIVRGGSH--SGNVAAHLLANHGLL 295
Cdd:cd01300 339 dhrhRIEHAQL--VSPDDIPRFAKLG-VIASV-----------QPNHlYSDGDAAEDRRLGEEraKRSYPFRSLLDAGVP 404
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490311675 296 DILSSDYyPASLLD-------AAFRIADA------EDNAFTLAQAIRLVSKHPAQALGLDD-RGVIAEGKRADLVL 357
Cdd:cd01300 405 VALGSDA-PVAPPDpllgiwaAVTRKTPGggvlgnPEERLSLEEALRAYTIGAAYAIGEEDeKGSLEPGKLADFVV 479
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
322-375 |
2.11e-04 |
|
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: 43.15 E-value: 2.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 490311675 322 FTLAQAIRLVSKHPAQALGLDDRGVIAEGKRADLVLAHRRgehVHIDHVWRQGR 375
Cdd:cd01308 322 IPLEVALRVITSNVARILKLRKKGEIQPGFDADLVILDKD---LDINSVIAKGQ 372
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
289-357 |
3.66e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 42.48 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 289 LANHGLLDILSSDYyPASLLD-------AAFRIAD-----AEDNAFTLAQAIRLVSKHPAQALGLDDR-GVIAEGKRADL 355
Cdd:COG1574 423 LLDAGAPLAFGSDA-PVEPLDpllgiyaAVTRRTPsgrglGPEERLTVEEALRAYTIGAAYAAFEEDEkGSLEPGKLADF 501
|
..
gi 490311675 356 VL 357
Cdd:COG1574 502 VV 503
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
2-52 |
4.40e-04 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 42.16 E-value: 4.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 490311675 2 IINNVKLVLDDDVVHGSLEVQDGRILAFAESQSRLP--QALDGEGGWLLPGLI 52
Cdd:PRK09236 5 LIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSadTVIDAAGRYLLPGMI 57
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
324-357 |
1.03e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 40.74 E-value: 1.03e-03
10 20 30
....*....|....*....|....*....|....
gi 490311675 324 LAQAIRLVSKHPAQALGLDDRGVIAEGKRADLVL 357
Cdd:PRK07583 362 YDDWPAAVTTTPADIMGLPDLGRIAVGAPADLVL 395
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
38-107 |
1.15e-03 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 40.74 E-value: 1.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490311675 38 QALDGEGGWLLPGLIELHTdNLDKFFTPRPKVDWPAHSAMS----SHDAMMVASGITTVLDA--VAIGDVRDGGDR 107
Cdd:cd01299 2 QVIDLGGKTLMPGLIDAHT-HLGSDPGDLPLDLALPVEYRTiratRQARAALRAGFTTVRDAggADYGLLRDAIDA 76
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
309-357 |
1.19e-03 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 40.35 E-value: 1.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311675 309 DAAFRIADAEDNA----------FTLAQAIRLVSKHPAQALGLDDR-GVIAEGKRADLVL 357
Cdd:cd01299 271 DAGFPVPPHGWNArelellvkagGTPAEALRAATANAAELLGLSDElGVIEAGKLADLLV 330
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
318-357 |
1.37e-03 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 40.56 E-value: 1.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 490311675 318 EDNAFTLAQAIRLVSKHPAQALGLDDrGVIAEGKRADLVL 357
Cdd:PRK09357 340 KTGLLDLEQLLEKMTINPARILGLPA-GPLAEGEPADLVI 378
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
7-55 |
2.45e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 39.75 E-value: 2.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 490311675 7 KLVLDDDVVHGSLEVQDGRILAFAESQSRLPQALDGEGGWLLPGLIELH 55
Cdd:PRK04250 5 KFLLKGRIVEGGIGIENGRISKISLRDLKGKEVIKVKGGIILPGLIDVH 53
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
324-357 |
2.80e-03 |
|
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: 39.30 E-value: 2.80e-03
10 20 30
....*....|....*....|....*....|....
gi 490311675 324 LAQAIRLVSKHPAQALGLDDRGVIAEGKRADLVL 357
Cdd:cd01302 269 LETLVEILSENPARIFGLYPKGTIAVGYDADLVI 302
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
21-95 |
5.04e-03 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 38.68 E-value: 5.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490311675 21 VQDGRILAFAE--SQSRLPQALDGEGGWLLPGLIELHTDNldkFFTPRPKVDWPahsamsshDAMMVASGITTVLDA 95
Cdd:PRK09237 23 IEDGKIAAVAGdiDGSQAKKVIDLSGLYVSPGWIDLHVHV---YPGSTPYGDEP--------DEVGVRSGVTTVVDA 88
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
306-357 |
7.50e-03 |
|
Metallo-dependent hydrolases, subgroup D 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: 238637 [Multi-domain] Cd Length: 381 Bit Score: 38.20 E-value: 7.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 490311675 306 SLLD---AAFRIADAEDNAFTLAQAIRLVSKHPAQALGLDDrGVIAEGKRADLVL 357
Cdd:cd01312 297 SLLDelrALLDLHPEEDLLELASELLLMATLGGARALGLNN-GEIEAGKRADFAV 350
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
2-75 |
9.22e-03 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 38.00 E-value: 9.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490311675 2 IINNVKLVLDDDVVHgSLEVQDGRILAFAESQSRLP--QALDGEGGWLLPGLIELHTdNLDKFFTPRPkvdWPAHS 75
Cdd:cd01293 1 LLRNARLADGGTALV-DIAIEDGRIAAIGPALAVPPdaEEVDAKGRLVLPAFVDPHI-HLDKTFTGGR---WPNNS 71
|
|
| |
