|
Name |
Accession |
Description |
Interval |
E-value |
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
77-449 |
1.27e-151 |
|
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: 435.59 E-value: 1.27e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 77 DGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSHLGDYPSPSVQALSDGNEATGPVRAEVWAEHSVWPQDPGFSRAL 156
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLGLDEEGGVRETSDANEETDPVTPHVRAIDGINPDDEAFKRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 157 AnGGVTTLQILPGSANLFGGRGVTLKNvYARTAQGMkFPGAPYSLKMACGENPKRVYGSKGQLPQTRMGNMALDRQTWID 236
Cdd:cd01309 81 A-GGVTTVQVLPGSANLIGGQGVVIKT-DGGTIEDM-FIKAPAGLKMALGENPKRVYGGKGKEPATRMGVAALLRDAFIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 237 ATEYKRKWDAYEKkvqdgtaKSADQPGRNLRNETLMGVLNGEITVQNHCYRADEMAQVIDMAKEFGYKVTAFHHAvEAYK 316
Cdd:cd01309 158 AQEYGRKYDLGKN-------AKKDPPERDLKLEALLPVLKGEIPVRIHAHRADDILTAIRIAKEFGIKITIEHGA-EGYK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 317 IGDLLKANGICAAVWADWYGFKM--EGYDAVNENLPLLQKAGACAMIHSDDPN-GIQRLNQEVAKTLADGRrmgiviPDE 393
Cdd:cd01309 230 LADELAKHGIPVIYGPTLTLPKKveEVNDAIDTNAYLLKKGGVAFAISSDHPVlNIRNLNLEAAKAVKYGL------SYE 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1997926616 394 VAWTWLAINPAKAMGIADRTGSLKPGKMADVVLWNGNPLSVYTRPEKVWIDGALLY 449
Cdd:cd01309 304 EALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLEPTSKPEQVYIDGRLVY 359
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
44-451 |
1.51e-63 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 210.59 E-value: 1.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 44 TYRAYPGVPTLVTNVTVYDGEGGR-IDDGSVLFADGKVVEVGQ--TIAAPAGTTVIDGRGKWVTPGIIDIHSHLGDYPSP 120
Cdd:COG1228 1 KKAPAQAGTLLITNATLVDGTGGGvIENGTVLVEDGKIAAVGPaaDLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 121 SVQAlsdgnEATGPVRAEVwaeHSVWPQDPGFSRALANGgVTTLQILPGSAnlFGGRGVTLKNVYARTAQGMKFPGAPYs 200
Cdd:COG1228 81 AVEF-----EAGGGITPTV---DLVNPADKRLRRALAAG-VTTVRDLPGGP--LGLRDAIIAGESKLLPGPRVLAAGPA- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 201 lkMACgenpkrVYGSKGQLPQTrmgNMALDRQTWIDATEYKRKWDAYEKkvqdgtaksadqpgRNLRNETLMGVLNGE-- 278
Cdd:COG1228 149 --LSL------TGGAHARGPEE---ARAALRELLAEGADYIKVFAEGGA--------------PDFSLEELRAILEAAha 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 279 --ITVQNHCYRADEMAQVIdmakEFGYKVtaFHHAVEAYK-IGDLLKANGiCAAVWADWYGFK--------------MEG 341
Cdd:COG1228 204 lgLPVAAHAHQADDIRLAV----EAGVDS--IEHGTYLDDeVADLLAEAG-TVVLVPTLSLFLallegaaapvaakaRKV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 342 YDAVNENLPLLQKAGACAMIHSDDPNGI---QRLNQEVAKTLADGrrmgivIPDEVAWTWLAINPAKAMGIADRTGSLKP 418
Cdd:COG1228 277 REAALANARRLHDAGVPVALGTDAGVGVppgRSLHRELALAVEAG------LTPEEALRAATINAAKALGLDDDVGSLEP 350
|
410 420 430
....*....|....*....|....*....|....*.
gi 1997926616 419 GKMADVVLWNGNPLSVYT---RPEKVWIDGALLYDA 451
Cdd:COG1228 351 GKLADLVLLDGDPLEDIAyleDVRAVMKDGRVVDRS 386
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
54-164 |
5.40e-16 |
|
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: 79.75 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 54 LVTNVTVYDGEGgrIDDGSVLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSHLGDYpspsvqalsdGNE--- 130
Cdd:COG0044 1 LIKNGRVVDPGG--LERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP----------GLEhke 68
|
90 100 110
....*....|....*....|....*....|....*.
gi 1997926616 131 --ATGpvraevwaehsvwpqdpgfSRALANGGVTTL 164
Cdd:COG0044 69 diETG-------------------TRAAAAGGVTTV 85
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
54-118 |
1.85e-13 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 71.74 E-value: 1.85e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997926616 54 LVTNVTVYDGEGGRIDDGSVLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSH-------LGDYP 118
Cdd:COG3964 3 LIKGGRVIDPANGIDGVMDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTHvfpggtdYGVDP 74
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
53-113 |
3.08e-13 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 71.74 E-value: 3.08e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1997926616 53 TLVTNVTVYDGEGGRIDDGSVLFADGKVVEVGQTIAAPAgTTVIDGRGKWVTPGIIDIHSH 113
Cdd:COG3653 4 LLIRGGTVVDGTGAPPFRADVAIKGGRIVAVGDLAAAEA-ARVIDATGLVVAPGFIDIHTH 63
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
54-120 |
3.86e-12 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 67.57 E-value: 3.86e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1997926616 54 LVTNVTVYD---GEGGRIDdgsVLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSH-------LGDYPSP 120
Cdd:PRK09237 2 LLRGGRVIDpanGIDGVID---IAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVHvypgstpYGDEPDE 75
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
53-114 |
1.62e-11 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 65.99 E-value: 1.62e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997926616 53 TLVTNVTVYDGEGgRIDDGSVLFADGKVVEVGQTIAaPAGTTVIDGRGKWVTPGIIDIHSHL 114
Cdd:PRK09357 3 ILIKNGRVIDPKG-LDEVADVLIDDGKIAAIGENIE-AEGAEVIDATGLVVAPGLVDLHVHL 62
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
54-125 |
2.16e-11 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 65.12 E-value: 2.16e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1997926616 54 LVTNVTVYDGEGgRIDDGSVLFADGKVVEVGQtiAAPAGTTVIDGRGKWVTPGIIDIHSH--LG-DYPSPSVQAL 125
Cdd:COG1820 1 AITNARIFTGDG-VLEDGALLIEDGRIAAIGP--GAEPDAEVIDLGGGYLAPGFIDLHVHggGGvDFMDGTPEAL 72
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
53-113 |
2.37e-11 |
|
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: 65.40 E-value: 2.37e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1997926616 53 TLVTNVTVYDGEGGRIDDGSVLFADGKVVEVGqTIAAPAGTTVIDGRGKWVTPGIIDIHSH 113
Cdd:cd01297 2 LVIRNGTVVDGTGAPPFTADVGIRDGRIAAIG-PILSTSAREVIDAAGLVVAPGFIDVHTH 61
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
53-450 |
2.52e-11 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 65.23 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 53 TLVTNVTV--YDGEGGRIDDGSVLFADGKVVEVGQTIAAPA---GTTVIDGRGKWVTPGIIDIHSHLgdyPSPSVQALSD 127
Cdd:COG0402 2 LLIRGAWVltMDPAGGVLEDGAVLVEDGRIAAVGPGAELPArypAAEVIDAGGKLVLPGLVNTHTHL---PQTLLRGLAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 128 GneatgpVRAEVWAEHSVWPQ----DPGFSRA--------LANGGVTTLQ----ILPGSANLF-------GGRGVTLKNV 184
Cdd:COG0402 79 D------LPLLDWLEEYIWPLearlDPEDVYAgallalaeMLRSGTTTVAdfyyVHPESADALaeaaaeaGIRAVLGRGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 185 YARTaqgmkFPGAPyslkmacgenpkrvygskgqlpqtrmgnmALDRQTWIDATEYKRkwDAYEKKVQDGTaksadQPG- 263
Cdd:COG0402 153 MDRG-----FPDGL-----------------------------REDADEGLADSERLI--ERWHGAADGRI-----RVAl 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 264 --RNLRNETlmgvlngeitvqnhcyrADEMAQVIDMAKEFGykvTAFH-HA------------------VEAY-KIGdLL 321
Cdd:COG0402 192 apHAPYTVS-----------------PELLRAAAALARELG---LPLHtHLaetrdevewvlelygkrpVEYLdELG-LL 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 322 KANGICA-AVWADwygfkmegydavNENLPLLQKAGACAmIH----------------------------SDDPNGIQRL 372
Cdd:COG0402 251 GPRTLLAhCVHLT------------DEEIALLAETGASV-AHcptsnlklgsgiapvprllaagvrvglgTDGAASNNSL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 373 NQ-EVAKTLA----DGRRMGIVIPDEVAWTWLAINPAKAMGIADRTGSLKPGKMADVVLWN---------GNPLS--VYT 436
Cdd:COG0402 318 DMfEEMRLAAllqrLRGGDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDldaphlaplHDPLSalVYA 397
|
490
....*....|....*...
gi 1997926616 437 RP----EKVWIDGALLYD 450
Cdd:COG0402 398 ADgrdvRTVWVAGRVVVR 415
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
53-452 |
7.32e-11 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 64.05 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 53 TLVTNVTVYDGEGGRIDDGSVLFADGKVVEVGQTI----AAPAGTTVIDGRGKWVTPGIIDIHSH------------LGD 116
Cdd:COG1574 10 LLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAevraLAGPATEVIDLGGKTVLPGFIDAHVHllggglallgvdLSG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 117 YPSPS-----VQALSDGNEATGPVRAEVWaEHSVWPqDPGF----------------------------SRALANGGVTt 163
Cdd:COG1574 90 ARSLDellarLRAAAAELPPGEWILGRGW-DESLWP-EGRFptradldavspdrpvvltrvdghaawvnSAALELAGIT- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 164 lqilPGSANLFGGRGVTLKN-----VYARTAQGM---KFPGAPY-----SLK----------------MACGENPKRVY- 213
Cdd:COG1574 167 ----ADTPDPEGGEIERDADgeptgVLREAAMDLvraAIPPPTPeelraALRaalrelaslgitsvhdAGLGPDDLAAYr 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 214 --GSKGQLPQTRMGNMALDRQTWIDATEYKRKWDAYEKKVQDGTAKS-----------------ADQPGRNlrnetlmGV 274
Cdd:COG1574 243 elAAAGELPLRVVLYLGADDEDLEELLALGLRTGYGDDRLRVGGVKLfadgslgsrtaallepyADDPGNR-------GL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 275 LNgeitvqnhcYRADEMAQVIDMAKEFGYKV--------------TAFHHAVEAYKIGDL-----------------LKA 323
Cdd:COG1574 316 LL---------LDPEELRELVRAADAAGLQVavhaigdaavdevlDAYEAARAANGRRDRrhriehaqlvdpddlarFAE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 324 NGICAAV-------WADWY----GFK-MEGYDAVNEnlplLQKAGACAMIHSD----DPN---GIQRLnqeVAKTLADGR 384
Cdd:COG1574 387 LGVIASMqpthatsDGDWAedrlGPErAARAYPFRS----LLDAGAPLAFGSDapvePLDpllGIYAA---VTRRTPSGR 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 385 RMGiviPDEV--------AWTwlaINPAKAMGIADRTGSLKPGKMADVVLWNGNPLSV------YTRPEKVWIDGALLYD 450
Cdd:COG1574 460 GLG---PEERltveealrAYT---IGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVppeeikDIKVLLTVVGGRVVYE 533
|
..
gi 1997926616 451 AN 452
Cdd:COG1574 534 AE 535
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
94-432 |
8.22e-11 |
|
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: 63.08 E-value: 8.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 94 TVIDGRGKWVTPGIIDIHSHLGDYPSPSVQALSDGNEATGpVRAEVWAehsvwpqdpgfsRALANGGVTTLQilpgsaNL 173
Cdd:cd01299 2 QVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVEYRT-IRATRQA------------RAALRAGFTTVR------DA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 174 FGGRGVTLKNvyaRTAQGMkFPGApyslkmacgenpkRVYGSKGQLPQT------RMGNMALDRQTWidATEYKRKWDAy 247
Cdd:cd01299 63 GGADYGLLRD---AIDAGL-IPGP-------------RVFASGRALSQTgghgdpRGLSGLFPAGGL--AAVVDGVEEV- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 248 EKKVQDGTAKSADQ-----PGRNLRNETLMGVLNgeitvqnhcYRADEMAQVIDMAKEFGYKVTAFHHAVEAYKIG---- 318
Cdd:cd01299 123 RAAVREQLRRGADQikimaTGGVLSPGDPPPDTQ---------FSEEELRAIVDEAHKAGLYVAAHAYGAEAIRRAirag 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 319 ---------------DLLKANGI----------------CAAVWADWYGFKM-EGYDAVNENLPLLQKAGAcAMIHSDD- 365
Cdd:cd01299 194 vdtiehgfliddetiELMKEKGIflvptlatyealaaegAAPGLPADSAEKVaLVLEAGRDALRRAHKAGV-KIAFGTDa 272
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1997926616 366 --PNGIQRLNqevAKTLADGRRMGIViPDEV--AWTWlaiNPAKAMGIADRTGSLKPGKMADVVLWNGNPL 432
Cdd:cd01299 273 gfPVPPHGWN---ARELELLVKAGGT-PAEAlrAATA---NAAELLGLSDELGVIEAGKLADLLVVDGDPL 336
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
53-113 |
3.58e-10 |
|
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: 61.44 E-value: 3.58e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1997926616 53 TLVTNVTVYDGEGgrIDDGSVLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSH 113
Cdd:cd00854 1 LIIKNARILTPGG--LEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
53-115 |
8.89e-10 |
|
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: 60.29 E-value: 8.89e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1997926616 53 TLVTNVT-VYDGEGGRIDDGSVLFADGKVVEVGQTIAAPAGT--TVIDGRGKWVTPGIIDIHSHLG 115
Cdd:cd01298 1 ILIRNGTiVTTDPRRVLEDGDVLVEDGRIVAVGPALPLPAYPadEVIDAKGKVVMPGLVNTHTHLA 66
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
65-114 |
2.53e-09 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 59.15 E-value: 2.53e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1997926616 65 GGRI--DDGS----VLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSHL 114
Cdd:cd01314 5 NGTIvtADGSfkadILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHL 60
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
316-449 |
5.27e-09 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 58.31 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 316 KIGDLLKANGICAAVWADWYGFKME--GYDAVNENLP--LLQKAGACAMIHSDDPNG-------IQRLNqevakTLADGR 384
Cdd:pfam07969 314 RVAALGGAAGVQPVFDPLWGDWLQDrlGAERARGLTPvkELLNAGVKVALGSDAPVGpfdpwprIGAAV-----MRQTAG 388
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1997926616 385 RMGIVIPDEV--------AWTwlaINPAKAMGIADRTGSLKPGKMADVVLWNGNPLSV------YTRPEKVWIDGALLY 449
Cdd:pfam07969 389 GGEVLGPDEElsleealaLYT---SGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVdppaiaDIRVRLTVVDGRVVY 464
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
53-164 |
1.20e-08 |
|
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: 56.91 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 53 TLVTNVTVYDGEGGRidDGSVLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSHLGDypspsvqalsdgneat 132
Cdd:cd01315 2 LVIKNGRVVTPDGVR--EADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINE---------------- 63
|
90 100 110
....*....|....*....|....*....|....*
gi 1997926616 133 gPVRAEvWAehsvwpqdpGF---SRALANGGVTTL 164
Cdd:cd01315 64 -PGRTE-WE---------GFetgTKAAAAGGITTI 87
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
102-445 |
1.94e-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: 55.97 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 102 WVTPGIIDIHSHLGDYPSPSVqalsdgneatgpvraevwaehsvwPQDPGFSRALANGGVTTLQilpgsanlfgGRGVTL 181
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGI------------------------PVPPEFAYEALRLGITTML----------KSGTTT 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 182 KNV-YARTAQGMKFpgapysLKMACGENPK--RVYGSKGqlpqtrmgNMALDRQTWIDATEYKRKWDAYEKKVQDGTaks 258
Cdd:pfam01979 47 VLDmGATTSTGIEA------LLEAAEELPLglRFLGPGC--------SLDTDGELEGRKALREKLKAGAEFIKGMAD--- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 259 adqpgrnlrnETLMGVLNGEITVQNHcyrADEMAQVIDMAKEFGYKVTAfhHAVEAYKIGDLLKANGICAAVWadwyGFK 338
Cdd:pfam01979 110 ----------GVVFVGLAPHGAPTFS---DDELKAALEEAKKYGLPVAI--HALETKGEVEDAIAAFGGGIEH----GTH 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 339 MEGYDAVN-----------------ENLPLLQKAGACAMI-HSDDPNGIQRLNQE-VAKTLADGRRMGIV---------- 389
Cdd:pfam01979 171 LEVAESGGlldiiklilahgvhlspTEANLLAEHLKGAGVaHCPFSNSKLRSGRIaLRKALEDGVKVGLGtdgagsgnsl 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 390 -IPDEVAW------------------TWLAINPAKAMGIADRTGSLKPGKMADVVLWNGNPLSVYT------RPEKVWID 444
Cdd:pfam01979 251 nMLEELRLalelqfdpegglsplealRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFglkpdgNVKKVIVK 330
|
.
gi 1997926616 445 G 445
Cdd:pfam01979 331 G 331
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
54-115 |
2.33e-08 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 55.91 E-value: 2.33e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997926616 54 LVTNVTVYDGEGGRIDDGSVLFADGKVVEVGQTIAAPAgTTVIDGRGKWVTPGIIDIHSHLG 115
Cdd:PRK06038 5 IIKNAYVLTMDAGDLKKGSVVIEDGTITEVSESTPGDA-DTVIDAKGSVVMPGLVNTHTHAA 65
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
52-163 |
3.35e-08 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 55.57 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 52 PTLVTNVTVYDGegGRIDDGSVLFADGKVVEVGQTIAAPAGTtvIDGRGKWVTPGIIDIHshlGDY------PSPSVQal 125
Cdd:PRK15446 3 EMILSNARLVLP--DEVVDGSLLIEDGRIAAIDPGASALPGA--IDAEGDYLLPGLVDLH---TDNlekhlaPRPGVD-- 73
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1997926616 126 sdgneatgpvraevwaehsvWPQDPGFS---RALANGGVTT 163
Cdd:PRK15446 74 --------------------WPADAALAahdAQLAAAGITT 94
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
52-114 |
4.89e-08 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 54.94 E-value: 4.89e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1997926616 52 PTLVTNVTVYDGEggRIDdgsVLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSHL 114
Cdd:PRK05985 3 DLLFRNVRPAGGA--AVD---ILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHL 60
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
52-113 |
1.34e-07 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 53.72 E-value: 1.34e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997926616 52 PTLVTNVTVYDgEGgRIDDGSVLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSH 113
Cdd:PRK09236 3 RILIKNARIVN-EG-KIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVH 62
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
52-168 |
1.49e-07 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 53.50 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 52 PTLVTNVTVYDGEGGRIDDGSVLFADGKVVEVGQTIA---APAGTTVIDGRGKWVTPGIIDIHSHLGdypspsvqalsdg 128
Cdd:PRK09059 4 PILLANARIIDPSRGLDEIGTVLIEDGVIVAAGKGAGnqgAPEGAEIVDCAGKAVAPGLVDARVFVG------------- 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1997926616 129 neatgpvraEVWAEH-----SVwpqdpgfSRALANGGVTTLQILP 168
Cdd:PRK09059 71 ---------EPGAEHretiaSA-------SRAAAAGGVTSIIMMP 99
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
73-426 |
1.69e-07 |
|
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: 53.47 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 73 VLFADGKVVEVGQTIAAPA----GTTVIDGRGKWVTPGIIDIHSH------------LGDYPSPS---------VQALSD 127
Cdd:cd01300 2 VAVRDGRIVAVGSDAEAKAlkgpATEVIDLKGKTVLPGFIDSHSHlllgglsllwldLSGVTSKEealariredAAAAPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 128 GN-------------EATGPVRAE---------VWA----EHSVWPQdpgfSRALANGGVTtlqilPGSANLFGGRGVTL 181
Cdd:cd01300 82 GEwilgfgwdesllgEGRYPTRAEldavspdrpVLLlrrdGHSAWVN----SAALRLAGIT-----RDTPDPPGGEIVRD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 182 KN------VYARTAQGMKFPGAPYS-------LKMACGEnpkrvYGSKGqlpQTRMGNMALDRQTWIDAteYKRKWDA-- 246
Cdd:cd01300 153 ADgeptgvLVEAAAALVLEAVPPPTpeerraaLRAAARE-----LASLG---VTTVHDAGGGAADDIEA--YRRLAAAge 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 247 ---------YEKKVQDGTAKSADQPGRNLRNETLM---------GVLNGEITVQNHCYR------------ADEMAQVID 296
Cdd:cd01300 223 ltlrvrvalYVSPLAEDLLEELGARKNGAGDDRLRlggvklfadGSLGSRTAALSEPYLdspgtgglllisPEELEELVR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 297 MAKEFGYKV--------------TAFHHAVEAYKIGDL-----------------LKANGICAAV-------WADWYGFK 338
Cdd:cd01300 303 AADEAGLQVaihaigdravdtvlDALEAALKDNPRADHrhriehaqlvspddiprFAKLGVIASVqpnhlysDGDAAEDR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 339 MEGYDAVNENLPL--LQKAGACAMIHSDDP-------NGIQrlnQEVAKTLADGRRMGivIPDEV--------AWTwlaI 401
Cdd:cd01300 383 RLGEERAKRSYPFrsLLDAGVPVALGSDAPvappdplLGIW---AAVTRKTPGGGVLG--NPEERlsleealrAYT---I 454
|
490 500
....*....|....*....|....*
gi 1997926616 402 NPAKAMGIADRTGSLKPGKMADVVL 426
Cdd:cd01300 455 GAAYAIGEEDEKGSLEPGKLADFVV 479
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
73-119 |
1.77e-07 |
|
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: 53.10 E-value: 1.77e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1997926616 73 VLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSH-------LGDYPS 119
Cdd:cd01307 2 VAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHvyqggtrYGDRPD 55
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
351-441 |
1.85e-07 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 53.56 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 351 LLQKAGACAMIHSDDpNGIQRLNQEVAKT--LAD--GRRMGIVIPDE------------VAWtwLAINPAKAMGIADRTG 414
Cdd:PRK13308 348 VLHDIGAISMLGSDS-QGMGRIAEVIARTwqLASkmKDQRGPLPEDRgtfadnarikryIAK--YTINPAITFGIDDHIG 424
|
90 100
....*....|....*....|....*..
gi 1997926616 415 SLKPGKMADVVLWngNPLSVYTRPEKV 441
Cdd:PRK13308 425 SLEPGKLADIVLW--RPAFFGIKPELV 449
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
77-163 |
1.93e-07 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 53.17 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 77 DGKVVEVGQTIAAPAGTtVIDGRGKWVTPGIIDIHSHLgdypspsvqalsdgNEatgPVRAEvWAehsvwpqdpGF---S 153
Cdd:PRK06189 27 NGKIAEIAPEISSPARE-IIDADGLYVFPGMIDVHVHF--------------NE---PGRTH-WE---------GFatgS 78
|
90
....*....|
gi 1997926616 154 RALANGGVTT 163
Cdd:PRK06189 79 AALAAGGCTT 88
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
58-114 |
2.27e-07 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 52.93 E-value: 2.27e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1997926616 58 VTVyDGEGGRIDDGSVLFADGKVVEVGQTIAAPAGT-TVIDGRGKWVTPGIIDIHSHL 114
Cdd:PRK08203 12 VTM-DAARREIADGGLVVEGGRIVEVGPGGALPQPAdEVFDARGHVVTPGLVNTHHHF 68
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
53-114 |
6.22e-07 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 51.71 E-value: 6.22e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997926616 53 TLVTNVTVYDGEGGRIDDgsVLFADGKVVEVGqtiaAPAGTTVIDGRGKWVTPGIIDIHSHL 114
Cdd:PRK08323 3 TLIKNGTVVTADDTYKAD--VLIEDGKIAAIG----ANLGDEVIDATGKYVMPGGIDPHTHM 58
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
68-114 |
7.02e-07 |
|
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: 51.26 E-value: 7.02e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1997926616 68 IDDGSVLFADGKVVEVGQTIAAPA--GTTVIDGRGKWVTPGIIDIHSHL 114
Cdd:TIGR01224 1 IEDAVILIHGGKIVWIGQLAALPGeeATEIIDCGGGLVTPGLVDPHTHL 49
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
54-154 |
9.69e-07 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 50.95 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 54 LVTNVTVYDGEGGRIDDGSVLFADGKVVEVGQTIAAPAgTTVIDGRGKWVTPGIIDIHSHlgdypSPSV--QALSDGnea 131
Cdd:PRK08393 4 LIKNGYVIYGENLKVIRADVLIEGNKIVEVKRNINKPA-DTVIDASGSVVSPGFINAHTH-----SPMVllRGLADD--- 74
|
90 100
....*....|....*....|...
gi 1997926616 132 tgpVRAEVWAEHSVWPQDPGFSR 154
Cdd:PRK08393 75 ---VPLMEWLQNYIWPRERKLKR 94
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
53-114 |
1.14e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 50.77 E-value: 1.14e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1997926616 53 TLVTNVTV--YDGEGGRIDDGSVLFADGKVVEVGQTIAAPaGTTVIDGRGKWVTPGIIDIHSHL 114
Cdd:PRK08204 4 TLIRGGTVltMDPAIGDLPRGDILIEGDRIAAVAPSIEAP-DAEVVDARGMIVMPGLVDTHRHT 66
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
68-118 |
2.41e-06 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 49.80 E-value: 2.41e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1997926616 68 IDDGSVLFADGKVVEVG--QTIAA--PAGTTVIDGRGKWVTPGIIDIHSHlgdYP 118
Cdd:PRK09228 29 IEDGLLLVEDGRIVAAGpyAELRAqlPADAEVTDYRGKLILPGFIDTHIH---YP 80
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
401-428 |
3.10e-06 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 49.41 E-value: 3.10e-06
10 20
....*....|....*....|....*...
gi 1997926616 401 INPAKAMGIADRTGSLKPGKMADVVLWN 428
Cdd:PRK13207 410 INPAIAHGISHEVGSVEVGKLADLVLWK 437
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
66-168 |
3.60e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 49.29 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 66 GRIDDGSVLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDihshlgdypsPSVQALSDGNE-----ATGpvraevw 140
Cdd:PRK07575 17 GELLLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVID----------PQVHFREPGLEhkedlFTA------- 79
|
90 100
....*....|....*....|....*...
gi 1997926616 141 aehsvwpqdpgfSRALANGGVTTLQILP 168
Cdd:PRK07575 80 ------------SRACAKGGVTSFLEMP 95
|
|
| UreC |
COG0804 |
Urease alpha subunit [Amino acid transport and metabolism]; |
401-452 |
3.62e-06 |
|
Urease alpha subunit [Amino acid transport and metabolism];
Pssm-ID: 440567 [Multi-domain] Cd Length: 570 Bit Score: 49.37 E-value: 3.62e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1997926616 401 INPAKAMGIADRTGSLKPGKMADVVLWngNPLSVYTRPEKV----WIDGALLYDAN 452
Cdd:COG0804 412 INPAIAHGISHEVGSVEVGKLADLVLW--DPAFFGVKPELVikggMIAWAQMGDPN 465
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
54-114 |
4.95e-06 |
|
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: 48.78 E-value: 4.95e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1997926616 54 LVTNVTVYDGEGGRIDdgsVLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSHL 114
Cdd:cd01293 1 LLRNARLADGGTALVD---IAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHL 58
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
401-450 |
5.28e-06 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 48.75 E-value: 5.28e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1997926616 401 INPAKAMGIADRTGSLKPGKMADVVLWN---------GNPLS--VYT----RPEKVWIDGALLYD 450
Cdd:PRK09045 351 LNGARALGLDDEIGSLEPGKQADLVAVDlsgletqpvYDPVSqlVYAagreQVSHVWVAGKQLLD 415
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
391-428 |
5.50e-06 |
|
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: 48.41 E-value: 5.50e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1997926616 391 PDEvAWTWLAINPAKAMGIADRTGSLKPGKMADVVLWN 428
Cdd:cd01296 312 PEE-ALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
70-426 |
6.78e-06 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 48.46 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 70 DGSVLFADGKVVEVGQTIAAPAG--TTVIDGRGKWVTPGIIDIHSHLGDYPSPSVQALSDGNEatgpvraevWAEHSVWP 147
Cdd:PRK06687 21 DGILAVKDSQIVYVGQDKPAFLEqaEQIIDYQGAWIMPGLVNCHTHSAMTGLRGIRDDSNLHE---------WLNDYIWP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 148 QDPGFSRALANGGVT---TLQILPGSA---NLFGGRGVTLKNVYARTAQGmkfpgapyslKMACGENPKrVYGSkgqlpQ 221
Cdd:PRK06687 92 AESEFTPDMTTNAVKealTEMLQSGTTtfnDMYNPNGVDIQQIYQVVKTS----------KMRCYFSPT-LFSS-----E 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 222 TRMGNMALDRQTWIDATEYKRKWDAYEKKVQDGTAKSADqpgRNLRNETLMGVLNGEITVQNHCYRADEMAQVI------ 295
Cdd:PRK06687 156 TETTAETISRTRSIIDEILKYKNPNFKVMVAPHSPYSCS---RDLLEASLEMAKELNIPLHVHVAETKEESGIIlkrygk 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 296 ---DMAKEFGY--KVTAFHHAVE--AYKIGDLlkANGICAAVWADWYGFKM-EGYDAVNEnlplLQKAGACAMIHSDDPN 367
Cdd:PRK06687 233 rplAFLEELGYldHPSVFAHGVElnEREIERL--ASSQVAIAHNPISNLKLaSGIAPIIQ----LQKAGVAVGIATDSVA 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1997926616 368 GIQRLNQ-EVAKTLADGRRM----GIVIPDEVAWTWLAINPAKAMGIADRTGSLKPGKMADVVL 426
Cdd:PRK06687 307 SNNNLDMfEEGRTAALLQKMksgdASQFPIETALKVLTIEGAKALGMENQIGSLEVGKQADFLV 370
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
56-163 |
7.76e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 48.11 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 56 TNVTVYDG---EGGRIDDGSVLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSHLGDypspsvqalsdgneaT 132
Cdd:PRK02382 2 RDALLKDGrvyYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFRE---------------P 66
|
90 100 110
....*....|....*....|....*....|.
gi 1997926616 133 GPVRAEVWAEHsvwpqdpgfSRALANGGVTT 163
Cdd:PRK02382 67 GYTHKETWYTG---------SRSAAAGGVTT 88
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
381-429 |
8.16e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 48.07 E-value: 8.16e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1997926616 381 ADGRRMGIVIPDEV------AWTWLAINPAKAMGIADRTGSLKPGKMADVVLWNG 429
Cdd:PRK08204 327 AVHLREGGMPPPRLtltarqVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDA 381
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
77-114 |
8.63e-06 |
|
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: 47.64 E-value: 8.63e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1997926616 77 DGKVVEVGQTIAAP----AGTTVIDGRGKWVTPGIIDIHSHL 114
Cdd:cd01296 5 DGRIAAVGPAASLPapgpAAAEEIDAGGRAVTPGLVDCHTHL 46
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
53-115 |
9.38e-06 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 47.88 E-value: 9.38e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1997926616 53 TLVTNVTVYD---GEGGRIDDgsVLFADGKVVEvgqTIAAPAGTTVIDGRGKWVTPGIIDIHSHLG 115
Cdd:COG1229 3 LIIKNGRVYDpanGIDGEVMD--IAIKDGKIVE---EPSDPKDAKVIDASGKVVMAGGVDIHTHIA 63
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
351-470 |
1.26e-05 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 47.78 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 351 LLQKAGACAMIHSDdPNGIQRLNQEVAKTLADG----RRMGIVIPDEVAWTWLA--------INPAKAMGIADRTGSLKP 418
Cdd:PRK13206 354 VLHDMGAISMIGSD-SQAMGRIGEVVLRTWQTAhvmkRRRGALPGDGRADNNRArryvakytICPAVAHGIDHEIGSVEV 432
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1997926616 419 GKMADVVLWngNPLSVYTRPEKVWIDGALLY----DAND--PRRRPVsdfeLGQPGEG 470
Cdd:PRK13206 433 GKLADLVLW--EPAFFGVRPHAVLKGGAIAWaamgDANAsiPTPQPV----LPRPMFG 484
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
58-113 |
1.51e-05 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 47.40 E-value: 1.51e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1997926616 58 VTVYDGEggrIDDGSVLFADGKVVEVGQtiAAPAGTTVIDGRGKWVTPGIIDIHSH 113
Cdd:COG1001 15 VNVFTGE---ILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHVH 65
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
95-168 |
2.07e-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: 46.46 E-value: 2.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1997926616 95 VIDGRGKWVTPGIIDIHSHLGDypsPSVQAlsDGNEATGpvraevwaehsvwpqdpgfSRALANGGVTTLQILP 168
Cdd:cd01317 4 VIDAEGKILAPGLVDLHVHLRE---PGFEY--KETLESG-------------------AKAAAAGGFTTVVCMP 53
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
401-452 |
2.14e-05 |
|
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: 46.94 E-value: 2.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1997926616 401 INPAKAMGIADRTGSLKPGKMADVVLWngNPLSVYTRPEKVWIDGALLY----DAN 452
Cdd:cd00375 410 INPAIAHGISHEVGSVEVGKLADLVLW--EPAFFGVKPEMVLKGGFIAYaqmgDPN 463
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
54-113 |
2.54e-05 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 46.29 E-value: 2.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 54 LVTNVTVYDGEGGRIDDGSVLFADGKVVEVGQTIAAPAgTTVIDGRGKWVTPGIIDIHSH 113
Cdd:PRK12394 6 LITNGHIIDPARNINEINNLRIINDIIVDADKYPVASE-TRIIHADGCIVTPGLIDYHAH 64
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
54-114 |
2.75e-05 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 46.17 E-value: 2.75e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1997926616 54 LVTNVTVYDGEGGrIDdgsVLFADGKVVEVGQTIAAPAGtTVIDGRGKWVTPGIIDIHSHL 114
Cdd:PRK07572 5 IVRNANLPDGRTG-ID---IGIAGGRIAAVEPGLQAEAA-EEIDAAGRLVSPPFVDPHFHM 60
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
53-128 |
3.07e-05 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 46.23 E-value: 3.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1997926616 53 TLVTNVTVYDGEGGRIDDGSVLFADGKVVEVGQtiAAPAGTTVIDGRGKWVTPGIIDIHSHLGDYPSPSVQALsDG 128
Cdd:PRK09061 21 LVIRNGRVVDPETGLDAVRDVGIKGGKIAAVGT--AAIEGDRTIDATGLVVAPGFIDLHAHGQSVAAYRMQAF-DG 93
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
53-114 |
3.37e-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: 45.84 E-value: 3.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1997926616 53 TLVTNVTVYDGEG-GRIDdgsVLFADGKVVEVGQTIAAP--AGTTVIDGRGKWVTPGIIDIHSHL 114
Cdd:cd01308 2 TLIKNAEVYAPEYlGKKD---ILIAGGKILAIEDQLNLPgyENVTVVDLHGKILVPGFIDQHVHI 63
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
76-191 |
3.88e-05 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 45.84 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 76 ADGKVVEVGQTIaaPAGTTVIDGRGKWVTPGIIDIHSHLgDYPSPSVQALSDGNEaTGpvraevwaehsvwpqdpgfSRA 155
Cdd:PRK13404 27 RGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHI-DQPSGDGIMMADDFY-TG-------------------TVS 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 1997926616 156 LANGGVTTlqILPGSANlfgGRGVTLKNV---YARTAQG 191
Cdd:PRK13404 84 AAFGGTTT--VIPFAAQ---HRGQSLREAvedYHRRAAG 117
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
53-115 |
5.38e-05 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 45.26 E-value: 5.38e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1997926616 53 TLVTN-VTVYDGEGGRIDDGSVLFADGKVVEVGQtiAAPAGTTVIDGRGKWVTPGIIDIHSHLG 115
Cdd:PRK06380 3 ILIKNaWIVTQNEKREILQGNVYIEGNKIVYVGD--VNEEADYIIDATGKVVMPGLINTHAHVG 64
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
54-128 |
5.74e-05 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 45.47 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 54 LVTNVTVYDGEGGrIDDGSVLFADGKVVEVGQT------------IAAPAGTTVIDGRGKWVTPGIIDIHSHLgDYPSPS 121
Cdd:PRK13308 71 VLCNVTVIDPVLG-IVKGDIGIRDGRIVGIGKAgnpdimdgvdprLVVGPGTDVRPAEGLIATPGAIDVHVHF-DSAQLV 148
|
....*..
gi 1997926616 122 VQALSDG 128
Cdd:PRK13308 149 DHALASG 155
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
73-114 |
5.93e-05 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 45.22 E-value: 5.93e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1997926616 73 VLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSHL 114
Cdd:PLN02942 25 VYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHL 66
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
54-114 |
1.05e-04 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 44.82 E-value: 1.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1997926616 54 LVTNVTVYDGEGGRIDDGSVLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSHL 114
Cdd:PRK10027 33 IIDNVSILDLINGGEISGPIVIKGRYIAGVGAEYADAPALQRIDARGATAVPGFIDAHLHI 93
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
68-157 |
1.70e-04 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 43.89 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 68 IDDGSVLFADGKVVEV--GQTIAAPAGTTVIDGRGKWVTPGIIDIHSHLgdypspsVQALSDGneATGPVRAEVWAEHSV 145
Cdd:PRK15493 20 IENGYIIVENDQIIDVnsGEFASDFEVDEVIDMKGKWVLPGLVNTHTHV-------VMSLLRG--IGDDMLLQPWLETRI 90
|
90
....*....|..
gi 1997926616 146 WPQDPGFSRALA 157
Cdd:PRK15493 91 WPLESQFTPELA 102
|
|
| PLN02303 |
PLN02303 |
urease |
401-459 |
2.64e-04 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 43.58 E-value: 2.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1997926616 401 INPAKAMGIADRTGSLKPGKMADVVLWngNPLSVYTRPEKVWIDGALLY----DAND--PRRRPV 459
Cdd:PLN02303 679 INPAIAHGMSHFVGSVEVGKLADLVLW--KPAFFGAKPEMVIKGGQIAWaqmgDPNAsiPTPEPV 741
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
66-117 |
2.73e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 43.22 E-value: 2.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1997926616 66 GRIDDGSVLFADGKVVEVGQTIAApaGTTVIDGRGKWVTPGIIDIHSHLGDY 117
Cdd:PRK04250 10 GRIVEGGIGIENGRISKISLRDLK--GKEVIKVKGGIILPGLIDVHVHLRDF 59
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
401-443 |
3.02e-04 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 43.06 E-value: 3.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1997926616 401 INPAKAMGIADRTGSLKPGKMADVVLWNGNPLSVYTRPEKVWI 443
Cdd:PRK07228 348 LGGAKAAGFEDEIGSLEEGKKADLAILDLDGLHATPSHGVDVL 390
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
55-115 |
4.42e-04 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 42.79 E-value: 4.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997926616 55 VTNVTVYDGEGGRIDD-GSVLFADGKVVEVgqtIAAPAGTTVIDGRGKWVTPGIIDIHSHLG 115
Cdd:cd01304 1 IKNGTVYDPLNGINGEkMDIFIRDGKIVES---SSGAKPAKVIDASGKVVMAGGVDMHSHIA 59
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
53-114 |
6.01e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 42.09 E-value: 6.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1997926616 53 TLVTNVTVYDGEGgrIDDGSVLFADGKVVEVGQ----------TIAAPAGTTVIDGRGKWVTPGIIDIHSHL 114
Cdd:PRK13207 69 TVITNALILDHWG--IVKADIGIKDGRIVAIGKagnpdiqdgvDIIIGPGTEVIAGEGLIVTAGGIDTHIHF 138
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
53-163 |
6.19e-04 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 42.21 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 53 TLVTNVTVY--DGEGgRIDDGsvlFADGKVVEVGQTIAAPAGTtVIDGRGKWVTPGIIDIHSHLGDYPSPSVQALSDGne 130
Cdd:PRK09060 7 LILKGGTVVnpDGEG-RADIG---IRDGRIAAIGDLSGASAGE-VIDCRGLHVLPGVIDSQVHFREPGLEHKEDLETG-- 79
|
90 100 110
....*....|....*....|....*....|...
gi 1997926616 131 atgpvraevwaehsvwpqdpgfSRALANGGVTT 163
Cdd:PRK09060 80 ----------------------SRAAVLGGVTA 90
|
|
| nagA |
TIGR00221 |
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars] |
54-133 |
7.97e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
Pssm-ID: 272968 Cd Length: 380 Bit Score: 41.74 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 54 LVTNVTVYDGEGgRIDDGSVLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSHLG------DYPSPSVQALSD 127
Cdd:TIGR00221 6 LLKDIAIVTGNE-VIDNGAVGINDGKISTVSTEAELEPEIKEIDLPGNVLTPGFIDIHIHGCggvdtnDASFETLEIMSE 84
|
....*.
gi 1997926616 128 GNEATG 133
Cdd:TIGR00221 85 RLPKSG 90
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
371-452 |
1.01e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 41.32 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 371 RLNQEVAKTLADgrrmgivipdevAWTWLAINPAKAMGIADRtGSLKPGKMADVVL---WNGNPlsvytRPEKVWIDGAL 447
Cdd:PRK15446 317 RLADDGGLDLPQ------------AVALVTANPARAAGLDDR-GEIAPGKRADLVRvrrAGGLP-----VVRAVWRGGRR 378
|
....*
gi 1997926616 448 LYDAN 452
Cdd:PRK15446 379 VFLAG 383
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
58-149 |
1.03e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 41.57 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 58 VTVYDGEGGR-IDDGSVLFADGKVVEVGQTIAAPAgTTVIDGRGKWVTPGIIDIHShLGDYPSpSVQALSDGNEatgpvr 136
Cdd:PRK06151 10 VLGFDDGDHRlLRDGEVVFEGDRILFVGHRFDGEV-DRVIDAGNALVGPGFIDLDA-LSDLDT-TILGLDNGPG------ 80
|
90
....*....|...
gi 1997926616 137 aevWAEHSVWPQD 149
Cdd:PRK06151 81 ---WAKGRVWSRD 90
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
55-168 |
1.07e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 41.20 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 55 VTNVTVYDGEGGRIDDGSVLFADGKVVEVGQtiaAPAGTT---VIDGRGKWVTPGIIDIHSHLGDypspsvqalsDGNEA 131
Cdd:PRK07627 5 IKGGRLIDPAAGTDRQADLYVAAGKIAAIGQ---APAGFNadkTIDASGLIVCPGLVDLSARLRE----------PGYEY 71
|
90 100 110
....*....|....*....|....*....|....*..
gi 1997926616 132 TGPVRAEVWAehsvwpqdpgfsrALAnGGVTTLQILP 168
Cdd:PRK07627 72 KATLESEMAA-------------AVA-GGVTSLVCPP 94
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
54-121 |
1.13e-03 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 41.07 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 54 LVTNVTVYDGEGGR--IDDGSVLFADGKVVEVGQT---IAAPAGTTVIDGRGKWVTPGIIDIHSH----------LGDYP 118
Cdd:PRK07203 3 LIGNGTAITRDPAKpvIEDGAIAIEGNVIVEIGTTdelKAKYPDAEFIDAKGKLIMPGLINSHNHiysglargmmANIPP 82
|
...
gi 1997926616 119 SPS 121
Cdd:PRK07203 83 PPD 85
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
390-447 |
1.46e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 40.85 E-value: 1.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 390 IPDEVAWTWLAINPAKAMGIADRtGSLKPGKMADVVLwngnpLSVYT--RPEKVWIDGAL 447
Cdd:COG1001 284 LDPVTAIQMATLNAAEHFGLKDL-GAIAPGRRADIVL-----LDDLEdfKVEKVYADGKL 337
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
68-114 |
1.65e-03 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 40.75 E-value: 1.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1997926616 68 IDDGSVLFADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSHL 114
Cdd:PRK07228 19 IVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHL 65
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
67-116 |
1.75e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 40.74 E-value: 1.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1997926616 67 RIDDgsVLFADGKVVEVGQTIAA-PAGTTVIDGRGKWVTPGIIDIHSHLGD 116
Cdd:PRK07369 20 RIAD--VLIEDGKIQAIEPHIDPiPPDTQIIDASGLILGPGLVDLYSHSGE 68
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
401-428 |
2.04e-03 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 40.65 E-value: 2.04e-03
10 20
....*....|....*....|....*...
gi 1997926616 401 INPAKAMGIADRTGSLKPGKMADVVLWN 428
Cdd:PRK13985 410 INPAIAHGISEYVGSVEVGKVADLVLWS 437
|
|
| ureC |
PRK13309 |
urease subunit alpha; Reviewed |
399-427 |
2.20e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183966 [Multi-domain] Cd Length: 572 Bit Score: 40.63 E-value: 2.20e-03
10 20
....*....|....*....|....*....
gi 1997926616 399 LAINPAKAMGIADRTGSLKPGKMADVVLW 427
Cdd:PRK13309 412 ITINPAITQGVSHVIGSVEVGKMADLVLW 440
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
51-114 |
2.33e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 40.35 E-value: 2.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1997926616 51 VPT-LVTNVTvydgEGGRIDDGSVLF----ADGKVVEVGQTIAAPAGTTVIDGRGKWVTPGIIDIHSHL 114
Cdd:PRK07583 20 VPAaLLEGGV----PPGDTLEGLVLVdieiADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTHL 84
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
53-168 |
3.05e-03 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 39.84 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926616 53 TLVTNVTVYDGEGGRIDDGSVlfADGKVVEVGQTIAAPAgtTVIDGRGKWVTPGIIDIHSHLGDypspsvqalsdgneat 132
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAV--KGGKIAAIGQDLGDAK--EVMDASGLVVSPGMVDAHTHISE---------------- 64
|
90 100 110
....*....|....*....|....*....|....*.
gi 1997926616 133 gPVRaevwaehSVWPQDPGFSRALANGGVTTLQILP 168
Cdd:PRK08044 65 -PGR-------SHWEGYETGTRAAAKGGITTMIEMP 92
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
395-445 |
3.43e-03 |
|
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.
Pssm-ID: 238631 Cd Length: 325 Bit Score: 39.57 E-value: 3.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1997926616 395 AWTWLAINPAKAMGIADRtGSLKPGKMADVVLWNGNPLsvYTRPEKVWIDG 445
Cdd:cd01306 278 AVALVSANPARAVGLTDR-GSIAPGKRADLILVDDMDG--VPVVRTVWRGG 325
|
|
| |
