|
Name |
Accession |
Description |
Interval |
E-value |
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
43-420 |
0e+00 |
|
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: 532.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 43 VVGKDGFIKAIGPADVIQRqfSGETFEEIIDCSGKCILPGLVDAHTHPVWAGERVHEFAMKLAGATYMEIHQAGGGIHFT 122
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPA--PGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 123 VERTRQATEEELFRSLQQRLQCMMRAGTTLVECKSGYGLDLETELKMLRVIERARRELDIGISATYCGAHSVPKGKTATE 202
Cdd:cd01296 79 VRATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 203 AA-DDIINNHLPKLKELGrngeiHVDNIDVFCEKGVFDLDSTRRILQRGKDIGLQINFHGDELHPMKAAELGAELGAQAI 281
Cdd:cd01296 159 EYiDLVIEEVLPAVAEEN-----LADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 282 SHLEEVSDEGIVAMATARCSAILLPTTAYMLRLKQPRARKMLDEGVIVALGSDFNPNAYCF-SMPMVMHLACVNMRMSMP 360
Cdd:cd01296 234 DHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPGSSPTsSMPLVMHLACRLMRMTPE 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 361 EALAAATINAAYALGKSHTHGSLEVGKQGDLIIINSSRWEHLIYQFGGHHelIEYVIAKG 420
Cdd:cd01296 314 EALTAATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNL--VEYVIKNG 371
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
38-422 |
2.46e-140 |
|
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: 406.03 E-value: 2.46e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 38 EGASLVVgKDGFIKAIGPadviQRQFSGETFEEIIDCSGKCILPGLVDAHTHPVWAGERVHEFAMKLAGATYMEIHQAGG 117
Cdd:TIGR01224 2 EDAVILI-HGGKIVWIGQ----LAALPGEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 118 GIHFTVERTRQATEEELFRSLQQRLQCMMRAGTTLVECKSGYGLDLETELKMLRVIERARRELDIGISATYCGAHSVPKG 197
Cdd:TIGR01224 77 GILSTVRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 198 KTATEAA--DDIINNHLPKLKElgrngEIHVDNIDVFCEKGVFDLDSTRRILQRGKDIGLQINFHGDELHPMKAAELGAE 275
Cdd:TIGR01224 157 FQGRPDDyvDGICEELIPQVAE-----EGLASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 276 LGAQAISHLEEVSDEGIVAMATARCSAILLPTTAYMLRLKQPRARKMLDEGVIVALGSDFNP-NAYCFSMPMVMHLACVN 354
Cdd:TIGR01224 232 LGAVSADHLEHASDAGIKALAEAGTVAVLLPGTTFYLRETYPPARQLIDYGVPVALATDLNPgSSPTLSMQLIMSLACRL 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223972677 355 MRMSMPEALAAATINAAYALGKSHTHGSLEVGKQGDLIIINSSRWEHLIYQFGGHHelIEYVIAKGKL 422
Cdd:TIGR01224 312 MKMTPEEALHAATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPYHYGVNH--VHAVIKNGNI 377
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
35-426 |
3.27e-52 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 179.39 E-value: 3.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 35 AVLEGASLVVgKDGFIKAIGPADVIQRQFSGEtfeeIIDCSGKCILPGLVDAHTHPVWAGERVHEFAMklagatymeihq 114
Cdd:COG1228 24 GVIENGTVLV-EDGKIAAVGPAADLAVPAGAE----VIDATGKTVLPGLIDAHTHLGLGGGRAVEFEA------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 115 aGGGIHFTVERTRQATEeelfrslqqRLQCMMRAGTTLVECKSGYGLDL-----ETELKML---RVIERARreldiGISA 186
Cdd:COG1228 87 -GGGITPTVDLVNPADK---------RLRRALAAGVTTVRDLPGGPLGLrdaiiAGESKLLpgpRVLAAGP-----ALSL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 187 TYcGAHsvpkGKTATEAADdiinnHLPKLKELGrngeihVDNIDVFCEKG--VFDLDSTRRILQRGKDIGLQINFHGDEL 264
Cdd:COG1228 152 TG-GAH----ARGPEEARA-----ALRELLAEG------ADYIKVFAEGGapDFSLEELRAILEAAHALGLPVAAHAHQA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 265 HPMKAAelgAELGAQAISHLEEVSDEGIVAMAtARCSAILLPTTAYMLRL------------------KQPRARKMLDEG 326
Cdd:COG1228 216 DDIRLA---VEAGVDSIEHGTYLDDEVADLLA-EAGTVVLVPTLSLFLALlegaaapvaakarkvreaALANARRLHDAG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 327 VIVALGSDFN-PNAYCFSMPMVMHLAcVNMRMSMPEALAAATINAAYALGKSHTHGSLEVGKQGDLIIINSSRWEHLIYq 405
Cdd:COG1228 292 VPVALGTDAGvGVPPGRSLHRELALA-VEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY- 369
|
410 420
....*....|....*....|.
gi 223972677 406 fgghHELIEYVIAKGKLIYKT 426
Cdd:COG1228 370 ----LEDVRAVMKDGRVVDRS 386
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
24-425 |
1.48e-18 |
|
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: 87.19 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 24 RFLARDAL-----RSLAVLEGASLVVgKDGFIKAIGPADVIQRQFSGEtfeEIIDCSGKCILPGLVDAHTHpvwagervh 98
Cdd:COG0402 1 DLLIRGAWvltmdPAGGVLEDGAVLV-EDGRIAAVGPGAELPARYPAA---EVIDAGGKLVLPGLVNTHTH--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 99 eFAMKL--AGATYMEIHQAGGGIHFTVERtrQATEEELFRSLQQRLQCMMRAGTTLVecksgygLDLETELK--MLRVIE 174
Cdd:COG0402 68 -LPQTLlrGLADDLPLLDWLEEYIWPLEA--RLDPEDVYAGALLALAEMLRSGTTTV-------ADFYYVHPesADALAE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 175 RARrelDIGISATYC-GAHSVPKGKTATEAADDIINNHLPKLKEL--GRNGEIHVdnidVFCEKGVF--DLDSTRRI--L 247
Cdd:COG0402 138 AAA---EAGIRAVLGrGLMDRGFPDGLREDADEGLADSERLIERWhgAADGRIRV----ALAPHAPYtvSPELLRAAaaL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 248 QRGKDIGLQINFHGD--------ELHPMKAAELGAELG--------AQAIsHLeevSDEGIVAMATARCSAILLPTTAYM 311
Cdd:COG0402 211 ARELGLPLHTHLAETrdevewvlELYGKRPVEYLDELGllgprtllAHCV-HL---TDEEIALLAETGASVAHCPTSNLK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 312 LRLKQPRARKMLDEGVIVALGSDFNPNAYCFSMPMVMHLACVNMR--------MSMPEALAAATINAAYALGKSHTHGSL 383
Cdd:COG0402 287 LGSGIAPVPRLLAAGVRVGLGTDGAASNNSLDMFEEMRLAALLQRlrggdptaLSAREALEMATLGGARALGLDDEIGSL 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 223972677 384 EVGKQGDLIIINSSRWE---------HLIYQFGGHHelIEYVIAKGKLIYK 425
Cdd:COG0402 367 EPGKRADLVVLDLDAPHlaplhdplsALVYAADGRD--VRTVWVAGRVVVR 415
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
43-423 |
2.58e-11 |
|
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: 64.96 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 43 VVGKDGFIKAIGPADviqrqfSGETFEEIIDCSGKCILPGLVDAHTH--PVWAGERVHEFamklAGATYMEIHQAgggih 120
Cdd:cd01293 17 IAIEDGRIAAIGPAL------AVPPDAEEVDAKGRLVLPAFVDPHIHldKTFTGGRWPNN----SGGTLLEAIIA----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 121 fTVERTRQATEEELFRSLQQRLQCMMRAGTTL----VECksgyglDLETELKMLRVIERARRE----LDIGISA-----T 187
Cdd:cd01293 82 -WEERKLLLTAEDVKERAERALELAIAHGTTAirthVDV------DPAAGLKALEALLELREEwadlIDLQIVAfpqhgL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 188 YCGAHSVPKGKTATEAADDIINNhLPKLkELGRNGEIHVDNIdvfcekgvFDLDStrrilQRGKDIGLQINFHGDEL--H 265
Cdd:cd01293 155 LSTPGGEELMREALKMGADVVGG-IPPA-EIDEDGEESLDTL--------FELAQ-----EHGLDIDLHLDETDDPGsrT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 266 PMKAAELGAELGAQ---AISHL-------EEVSDEGIVAMATARCSAILLPTTAYMLRLKQ---------PRARKMLDEG 326
Cdd:cd01293 220 LEELAEEAERRGMQgrvTCSHAtalgslpEAEVSRLADLLAEAGISVVSLPPINLYLQGREdttpkrrgvTPVKELRAAG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 327 VIVALGSD-----FNPNAyCFSMPMVMHLACVNMRMSMPEALAAAT----INAAYALGKshTHGSLEVGKQGDLIIINSS 397
Cdd:cd01293 300 VNVALGSDnvrdpWYPFG-SGDMLEVANLAAHIAQLGTPEDLALALdlitGNAARALGL--EDYGIKVGCPADLVLLDAE 376
|
410 420
....*....|....*....|....*.
gi 223972677 398 RWEHLIYqfGGHHELIeyVIAKGKLI 423
Cdd:cd01293 377 DVAEAVA--RQPPRRV--VIRKGRVV 398
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
83-351 |
8.74e-10 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 59.27 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 83 LVDAHTHPVWAGERVHEFAMKLAGATYMEIHQagggihfTVERTRQATEEelfrslqqrlqcMMRAGTTLVECKSGYGLD 162
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEELSPED-------LYEDTLRALEA------------LLAGGVTTVVDMGSTPPP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 163 LETELKMLRVIERARRELDIGISATYCGAHSVPKGKTATEAaddiinnHLPKLKELGRNGEIHVDNIDVFCEKGVFDLDS 242
Cdd:cd01292 62 TTTKAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEA-------LLLELLRRGLELGAVGLKLAGPYTATGLSDES 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 243 TRRILQRGKDIGLQINFH----GDELHPMKAAELGAELGAQ-AISHLEEVSDEGIVAMATARCSAILLPTTAYMLRLK-- 315
Cdd:cd01292 135 LRRVLEEARKLGLPVVIHagelPDPTRALEDLVALLRLGGRvVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRDge 214
|
250 260 270
....*....|....*....|....*....|....*..
gi 223972677 316 -QPRARKMLDEGVIVALGSDFNPNAYCFSMPMVMHLA 351
Cdd:cd01292 215 gAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLL 251
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
46-95 |
1.12e-09 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 60.20 E-value: 1.12e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 223972677 46 KDGFIKAIGPADVIQRQFSGETfeEIIDCSGKCILPGLVDAHTHPVWAGE 95
Cdd:COG1574 33 RDGRIVAVGSDAEVRALAGPAT--EVIDLGGKTVLPGFIDAHVHLLGGGL 80
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
7-425 |
3.98e-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: 54.90 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 7 LLLENAQQVVLVCARgerflardalrslaVLEGASLVVgKDGFIKAIGPADViQRQFSGEtfeEIIDCSGKCILPGLVDA 86
Cdd:cd01298 1 ILIRNGTIVTTDPRR--------------VLEDGDVLV-EDGRIVAVGPALP-LPAYPAD---EVIDAKGKVVMPGLVNT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 87 HTHpvwagervheFAMKL-----AGATYMEIHQAgggihfTVERTRQATEEELFRsLQQRLQC--MMRAGTTLVecksgy 159
Cdd:cd01298 62 HTH----------LAMTLlrglaDDLPLMEWLKD------LIWPLERLLTEEDVY-LGALLALaeMIRSGTTTF------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 160 gldLETELKMLRVIERARRELdiGISATYCGAhSVPKGKTATEAADDIINNHLPKLKE--LGRNGEIHVdnidVFCEKGV 237
Cdd:cd01298 119 ---ADMYFFYPDAVAEAAEEL--GIRAVLGRG-IMDLGTEDVEETEEALAEAERLIREwhGAADGRIRV----ALAPHAP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 238 FDL--DSTRRILQRGKDIGLQINFHG----DELHPMKA----------AELGAeLGAQAI-SHLEEVSDEGIVAMATARC 300
Cdd:cd01298 189 YTCsdELLREVAELAREYGVPLHIHLaeteDEVEESLEkygkrpveylEELGL-LGPDVVlAHCVWLTDEEIELLAETGT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 301 SAILLPTTAYMLRLKQPRARKMLDEGVIVALGSD-----------------------FNPNAYCFSMPMVMHLACVNMR- 356
Cdd:cd01298 268 GVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDgaasnnnldmfeemrlaallqklAHGDPTALPAEEALEMATIGGAk 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223972677 357 -MSMPEAlaaatinaayalgkshthGSLEVGKQGDLIIINSSR---------WEHLIYqfGGHHELIEYVIAKGKLIYK 425
Cdd:cd01298 348 aLGLDEI------------------GSLEVGKKADLILIDLDGphllpvhdpISHLVY--SANGGDVDTVIVNGRVVME 406
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
46-89 |
5.16e-08 |
|
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: 54.71 E-value: 5.16e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 223972677 46 KDGFIKAIGPADviqrqfSGETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:COG0044 21 EDGRIAAIGPDL------AAPEAAEVIDATGLLVLPGLIDLHVH 58
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
43-94 |
1.10e-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: 53.85 E-value: 1.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 223972677 43 VVGKDGFIKAIGPADVIQRQFSGETfeEIIDCSGKCILPGLVDAHTHPVWAG 94
Cdd:cd01300 2 VAVRDGRIVAVGSDAEAKALKGPAT--EVIDLKGKTVLPGFIDSHSHLLLGG 51
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
79-423 |
4.12e-07 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 51.73 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 79 ILPGLVDAHTHpvwagervhefamklagatymeihqagggIHFTVERTRQATEEELFRSLQQRLQCMMRAGTTLVeCKSG 158
Cdd:pfam01979 2 VLPGLIDAHVH-----------------------------LEMGLLRGIPVPPEFAYEALRLGITTMLKSGTTTV-LDMG 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 159 YGldleTELKMLRVIErARRELDIGIsaTYCGAHSVPKGKTATEAADDIINNHLPKL-KELGRNGEIHVDNIDVFcEKGV 237
Cdd:pfam01979 52 AT----TSTGIEALLE-AAEELPLGL--RFLGPGCSLDTDGELEGRKALREKLKAGAeFIKGMADGVVFVGLAPH-GAPT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 238 FDLDSTRRILQRGKDIGLQINFHGDEL-HPMKAAELGAELGAQAISHLE---EVSDEGIVAMATARC------SAILLPT 307
Cdd:pfam01979 124 FSDDELKAALEEAKKYGLPVAIHALETkGEVEDAIAAFGGGIEHGTHLEvaeSGGLLDIIKLILAHGvhlsptEANLLAE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 308 TAYMLRL------------KQPRARKMLDEGVIVALGSDFNPNAYCFSMPMVMHLAC-----VNMRMSMPEALAAATINA 370
Cdd:pfam01979 204 HLKGAGVahcpfsnsklrsGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALelqfdPEGGLSPLEALRMATINP 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 223972677 371 AYALGKSHTHGSLEVGKQGDLIIINSSRWEHLIYQFGGhhELIEYVIAKGKLI 423
Cdd:pfam01979 284 AKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPD--GNVKKVIVKGKIV 334
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
158-424 |
1.33e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 50.22 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 158 GYGLDLETELKMLRVIERAR-RELDIGISATycgahsvpkGKTATEAADDIINNHLPKLKELGRNGEIHVDNIdvfcekG 236
Cdd:pfam07969 241 GTGWPDFEDEALAELVAAAReRGLDVAIHAI---------GDATIDTALDAFEAVAEKLGNQGRVRIEHAQGV------V 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 237 VFDLDSTRRILQRGKDIGLQINFHgdelhPMKAAELGAELGAQAISHLeevsdegivamatarcsaillpttaymlrlkq 316
Cdd:pfam07969 306 PYTYSQIERVAALGGAAGVQPVFD-----PLWGDWLQDRLGAERARGL-------------------------------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 317 PRARKMLDEGVIVALGSDFNPNAYC---FSMPMVMHLACVNM-------RMSMPEALAAATINAAYALGKSHTHGSLEVG 386
Cdd:pfam07969 349 TPVKELLNAGVKVALGSDAPVGPFDpwpRIGAAVMRQTAGGGevlgpdeELSLEEALALYTSGPAKALGLEDRKGTLGVG 428
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 223972677 387 KQGDLIIINSSRW----EHLiyqfggHHELIEYVIAKGKLIY 424
Cdd:pfam07969 429 KDADLVVLDDDPLtvdpPAI------ADIRVRLTVVDGRVVY 464
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
42-89 |
7.82e-06 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 47.88 E-value: 7.82e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 223972677 42 LVVGKDGFIKAIGPADVIQRQFSGETfeEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK09228 33 LLLVEDGRIVAAGPYAELRAQLPADA--EVTDYRGKLILPGFIDTHIH 78
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
46-89 |
1.16e-05 |
|
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: 47.21 E-value: 1.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 223972677 46 KDGFIKAIGPAdviqrqFSGETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:cd01314 22 EDGKIVAIGPN------LEAPGGVEVIDATGKYVLPGGIDPHTH 59
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
46-89 |
1.88e-05 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 46.73 E-value: 1.88e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 223972677 46 KDGFIKAIGPADviqrqfsGETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK09357 25 DDGKIAAIGENI-------EAEGAEVIDATGLVVAPGLVDLHVH 61
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
46-89 |
3.06e-05 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 45.93 E-value: 3.06e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 223972677 46 KDGFIKAIGPADViqrqfsgetfEEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK08323 24 EDGKIAAIGANLG----------DEVIDATGKYVMPGGIDPHTH 57
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
46-186 |
4.54e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 45.31 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 46 KDGFIKAIGPAdviqrqFSGETFEEIIDCSGKCILPGLVDAHTHP---VWaGERVHEfamklagatymeiHQAGGGIH-- 120
Cdd:PRK05985 22 RDGRIAAIGPA------LAAPPGAEVEDGGGALALPGLVDGHIHLdktFW-GDPWYP-------------NEPGPSLRer 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223972677 121 --FTVERTRQATEEELFRSLQQRLQCMMRaGTTLVEC----KSGYGLD-LETelkMLRVIERARRELDIGISA 186
Cdd:PRK05985 82 iaNERRRRAASGHPAAERALALARAAAAA-GTTAMRShvdvDPDAGLRhLEA---VLAARETLRGLIDIQIVA 150
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
36-89 |
5.24e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 45.09 E-value: 5.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 223972677 36 VLEGASLVVgKDGFIKAIGPADviqrqfsgETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:COG1820 13 VLEDGALLI-EDGRIAAIGPGA--------EPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
40-89 |
6.50e-05 |
|
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: 44.97 E-value: 6.50e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 223972677 40 ASLVVgKDGFIKAIGPADviqrqfSGETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:cd01315 18 ADIAV-KGGKIAAIGPDI------ANTEAEEVIDAGGLVVMPGLIDTHVH 60
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
43-98 |
6.93e-05 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 44.63 E-value: 6.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 223972677 43 VVGKDGFIKAIGPADVIQRQfsgetfEEIIDCSGKCILPGLVDAHTHPVWAGERVH 98
Cdd:cd01307 2 VAIENGKIAAVGAALAAPAA------TQIVDAGGCYVSPGWIDLHVHVYQGGTRYG 51
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
70-153 |
1.31e-04 |
|
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: 43.82 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 70 EIIDCSGKCILPGLVDAHTHPVWAGERvhefamklagatymeihqagggihfTVERTRQATEEELFRSLQQrLQCMMRAG 149
Cdd:cd01299 2 QVIDLGGKTLMPGLIDAHTHLGSDPGD-------------------------LPLDLALPVEYRTIRATRQ-ARAALRAG 55
|
....
gi 223972677 150 TTLV 153
Cdd:cd01299 56 FTTV 59
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
37-89 |
1.48e-04 |
|
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: 43.72 E-value: 1.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 223972677 37 LEGASLVVgKDGFIKAIGPADviqrqfSGETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:cd00854 14 LEDGAVLV-EDGKIVAIGPED------ELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
35-89 |
3.37e-04 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 42.59 E-value: 3.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 223972677 35 AVLEGASLVVgKDGFIKAIGPADVIQRQFsgeTFEEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK09045 24 VVLEDHAVAI-RDGRIVAILPRAEARARY---AAAETVELPDHVLIPGLINAHTH 74
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
42-402 |
3.97e-04 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 42.30 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 42 LVVGKDGFIKAIGPADviqrQFSGETFEEIIDCSGKCILPGLVDAHTHPVWAGER-------VHEfamklagatYMEIHQ 114
Cdd:PRK06687 23 ILAVKDSQIVYVGQDK----PAFLEQAEQIIDYQGAWIMPGLVNCHTHSAMTGLRgirddsnLHE---------WLNDYI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 115 AGGGIHFTVERTRQATEEELFRSLQQrlqcmmrAGTTLVECKSGYGLDLETELKMLR----------------------V 172
Cdd:PRK06687 90 WPAESEFTPDMTTNAVKEALTEMLQS-------GTTTFNDMYNPNGVDIQQIYQVVKtskmrcyfsptlfssetettaeT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 173 IERARRELDIGISATYCGAHSVPKGKTATEAADDIINNHLPKLKELgrNGEIHVDNIDVFCEKGVFDLDSTRRILQRGKD 252
Cdd:PRK06687 163 ISRTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKEL--NIPLHVHVAETKEESGIILKRYGKRPLAFLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 253 IGL----QINFHGDELHPMKAAELGAE---LGAQAISHLEEVSDEGIVAMATARCSAILLPTTAymlrLKQPRARKMLDE 325
Cdd:PRK06687 241 LGYldhpSVFAHGVELNEREIERLASSqvaIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDS----VASNNNLDMFEE 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223972677 326 GVIVALGSDFNP-NAYCFSMPMVMHLACVNmrmsmpealaaatinAAYALGKSHTHGSLEVGKQGDLIIINSSRWEHL 402
Cdd:PRK06687 317 GRTAALLQKMKSgDASQFPIETALKVLTIE---------------GAKALGMENQIGSLEVGKQADFLVIQPQGKIHL 379
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
69-425 |
4.13e-04 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 42.56 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 69 EEIIDCSGKCILPGLVDAHTHPVWAGER-------VHEFAMKlagatymeihqagggihfTVERTRQATEEELFRSLQQR 141
Cdd:PRK06380 42 DYIIDATGKVVMPGLINTHAHVGMTASKglfddvdLEEFLMK------------------TFKYDSKRTREGIYNSAKLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 142 LQCMMRAGTTLVecksgygLDLETELKmlrVIERARREldIGISAtYCGAHSVPKGKTATEA-----ADDIINNHlpklk 216
Cdd:PRK06380 104 MYEMINSGITAF-------VDLYYSED---IIAKAAEE--LGIRA-FLSWAVLDEEITTQKGdplnnAENFIREH----- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 217 elgRNGEIHVDNIDVfceKGVF--DLDSTRRILQRGKDIGLQINFHGDELHPmKAAELGAELGAQAISHLEEV---SDEG 291
Cdd:PRK06380 166 ---RNEELVTPSIGV---QGIYvaNDETYLKAKEIAEKYDTIMHMHLSETRK-EVYDHVKRTGERPVEHLEKIgflNSKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 292 IVA---MATARCSAILL---------PTTAYMLRLK-QPRARKMLDEGVIVALGSDFNPNAYCFSMPMVMHLACV---NM 355
Cdd:PRK06380 239 IAAhcvWATYHEIKLLSkngvkvswnSVSNFKLGTGgSPPIPEMLDNGINVTIGTDSNGSNNSLDMFEAMKFSALsvkNE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 356 R-----MSMPEALAAATINAAYALgkSHTHGSLEVGKQGDLIIINSSRWEHLIYQ---------FGGHHELIEYVIAKGK 421
Cdd:PRK06380 319 RwdasiIKAQEILDFATINAAKAL--ELNAGSIEVGKLADLVILDARAPNMIPTRknnivsnivYSLNPLNVDHVIVNGK 396
|
....
gi 223972677 422 LIYK 425
Cdd:PRK06380 397 ILKE 400
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
46-94 |
6.41e-04 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 41.69 E-value: 6.41e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 223972677 46 KDGFIKAIGPADVIQRQfsgetfEEIIDCSGKCILPGLVDAHTHpVWAG 94
Cdd:COG3964 25 KDGKIAAVAKDIDAAEA------KKVIDASGLYVTPGLIDLHTH-VFPG 66
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
24-89 |
8.81e-04 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 41.46 E-value: 8.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223972677 24 RFLARDALRSlaVLEGASLVVgKDGFIKAIGPADVIQRQFSGEtfeEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK07203 8 TAITRDPAKP--VIEDGAIAI-EGNVIVEIGTTDELKAKYPDA---EFIDAKGKLIMPGLINSHNH 67
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
46-89 |
1.00e-03 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 41.06 E-value: 1.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 223972677 46 KDGFIKAIGpadviqrQFSGETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK09060 28 RDGRIAAIG-------DLSGASAGEVIDCRGLHVLPGVIDSQVH 64
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
46-89 |
1.26e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 40.79 E-value: 1.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 223972677 46 KDGFIKAIGpadviqRQFSGETFEEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK02382 25 DGGKITAVG------KDLDGSSSEEVIDARGMLLLPGGIDVHVH 62
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
21-130 |
1.36e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 40.76 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 21 RGERFLARDAlrSLAVLEGASLVVgKDGFIKAIGPAdvIQrqfSGETfeEIIDCSGKCILPGLVDAHTHpVWagervhEF 100
Cdd:PRK08204 7 RGGTVLTMDP--AIGDLPRGDILI-EGDRIAAVAPS--IE---APDA--EVVDARGMIVMPGLVDTHRH-TW------QS 69
|
90 100 110
....*....|....*....|....*....|....*
gi 223972677 101 AMKLAGA-----TYMEIHQAGGGIHFTVERTRQAT 130
Cdd:PRK08204 70 VLRGIGAdwtlqTYFREIHGNLGPMFRPEDVYIAN 104
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
69-89 |
1.45e-03 |
|
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: 40.68 E-value: 1.45e-03
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
46-98 |
1.56e-03 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 40.60 E-value: 1.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 223972677 46 KDGFIKAIGPAdviqrqFSGETFEEIIDCSGKCILPGLVDAHTHPVWAGERVH 98
Cdd:PRK09237 24 EDGKIAAVAGD------IDGSQAKKVIDLSGLYVSPGWIDLHVHVYPGSTPYG 70
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
43-112 |
2.03e-03 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 40.21 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 43 VVGKDGFIKAIGP-----ADVIqrqfsgetfeeIIDCSGKCILPGLVDAHTH---PVWAGERVHEF----AMKLAGATYM 110
Cdd:PLN02942 25 VYVEDGIIVAVAPnlkvpDDVR-----------VIDATGKFVMPGGIDPHTHlamPFMGTETIDDFfsgqAAALAGGTTM 93
|
..
gi 223972677 111 EI 112
Cdd:PLN02942 94 HI 95
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
47-89 |
2.84e-03 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 39.68 E-value: 2.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 223972677 47 DGFIKAIGPADVIQRQFsgetfeEIIDCSGKCILPGLVDAHTH 89
Cdd:TIGR02033 23 GGKIVAVGDNLIPPDAV------EVIDATGKYVLPGGIDVHTH 59
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
34-89 |
3.04e-03 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 39.84 E-value: 3.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 223972677 34 LAVLEGASLVVG---KDGFIKAIGpadviqrQFSGETfEEIIDCSGKCILPGLVDAHTH 89
Cdd:PRK08044 11 TVILENEARVVDiavKGGKIAAIG-------QDLGDA-KEVMDASGLVVSPGMVDAHTH 61
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
36-88 |
3.12e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 39.39 E-value: 3.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 223972677 36 VLEGaSLVVgKDGFIKAIGPAdviqrqfsGETFEEIIDCSGKCILPGLVDAHT 88
Cdd:PRK15446 17 VVDG-SLLI-EDGRIAAIDPG--------ASALPGAIDAEGDYLLPGLVDLHT 59
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
47-89 |
4.29e-03 |
|
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: 39.22 E-value: 4.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 223972677 47 DGFIKAIG-----PADViqrqfsgetfeEIIDCSGKCILPGLVDAHTH 89
Cdd:cd01309 1 DGKIVAVGaeittPADA-----------EVIDAKGKHVTPGLIDAHSH 37
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
37-119 |
4.57e-03 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 39.25 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 37 LEGASLVVGKDGFIKAIGPAdvIQRQFSGETfEEIIDCSGKCILPGLVDAHthpVWAGERVHEFAMKLAGATYMeihQAG 116
Cdd:PRK09059 19 LDEIGTVLIEDGVIVAAGKG--AGNQGAPEG-AEIVDCAGKAVAPGLVDAR---VFVGEPGAEHRETIASASRA---AAA 89
|
...
gi 223972677 117 GGI 119
Cdd:PRK09059 90 GGV 92
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
20-89 |
5.13e-03 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 38.80 E-value: 5.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972677 20 ARGERFLARDALRslaVLEGASLVVGkDGFIKAIGPADVIQRQFSGETfeEIIDCSGKCILPGLVDAHTH 89
Cdd:cd01303 10 SLPELELVEDALR---VVEDGLIVVV-DGNIIAAGAAETLKRAAKPGA--RVIDSPNQFILPGFIDTHIH 73
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
37-89 |
6.42e-03 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 38.58 E-value: 6.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 223972677 37 LEGASLVvgKDGFIKAIG----PADviqrqfsgetfEEIIDCSGKCILPGLVDAHTH 89
Cdd:TIGR00857 4 TEVDILV--EGGRIKKIGklriPPD-----------AEVIDAKGLLVLPGFIDLHVH 47
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
36-91 |
8.04e-03 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 38.44 E-value: 8.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 223972677 36 VLEGASLVvgKDGFIKAIGPADVIQRqfsgetFEEIIDCSGKCILPGLVDAHTHPV 91
Cdd:PRK07228 19 IVDGDVLI--EDDRIAAVGDRLDLED------YDDHIDATGKVVIPGLIQGHIHLC 66
|
|
| |
