|
Name |
Accession |
Description |
Interval |
E-value |
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
61-431 |
3.07e-169 |
|
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: 479.45 E-value: 3.07e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 61 IHVVDGRIRDFGPAERVAVglPKGAEPRVLDAAGGAVVPGFVDCHTHLLYSGSRADEYPMRVAGASYGEISSRGGGVTRT 140
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPA--PGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 141 IRESSDATSSELKQALTVRLAKALLNGTTTAEIKTGYWVDPEGEGAALGIIAEVSASQPVDLVQTFHVALGTPARFGGAG 220
Cdd:cd01296 79 VRATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 221 EYARYVIDYVLPSVA--SHARFCDVVCDVGAFSHDEARQILHAAGRRGLNFKIHADEFSAAGGAELAAELGAVSADHLCF 298
Cdd:cd01296 159 EYIDLVIEEVLPAVAeeNLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSADHLEH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 299 LGKDTAQTLAKAQTVAVLLPATCHYLLAPkFADARHLIDGGVAIALGTDHGPGS-PTLSMPFVMGLACSWLRMDPAEALV 377
Cdd:cd01296 239 TSDEGIAALAEAGTVAVLLPGTAFSLRET-YPPARKLIDAGVPVALGTDFNPGSsPTSSMPLVMHLACRLMRMTPEEALT 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 14028431 378 AATCNAAHAIGAASTAGQIAIGRPADLVVLKTPTYRDLAYLIDQNLIRYTLKDG 431
Cdd:cd01296 318 AATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNLVEYVIKNG 371
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
56-433 |
3.86e-108 |
|
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: 324.36 E-value: 3.86e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 56 IRNAAIHVVDGRIRDFGPAervaVGLPKGAEPRVLDAAGGAVVPGFVDCHTHLLYSGSRADEYPMRVAGASYGEISSRGG 135
Cdd:TIGR01224 1 IEDAVILIHGGKIVWIGQL----AALPGEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 136 GVTRTIRESSDATSSELKQALTVRLAKALLNGTTTAEIKTGYWVDPEGEGAALGIIAEVSASQPVDLVQTFHVALGTPAR 215
Cdd:TIGR01224 77 GILSTVRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 216 FGG-AGEYARYVIDYVLPSVASH--ARFCDVVCDVGAFSHDEARQILHAAGRRGLNFKIHADEFSAAGGAELAAELGAVS 292
Cdd:TIGR01224 157 FQGrPDDYVDGICEELIPQVAEEglASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAKLGAVS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 293 ADHLCFLGKDTAQTLAKAQTVAVLLPATcHYLLAPKFADARHLIDGGVAIALGTDHGPG-SPTLSMPFVMGLACSWLRMD 371
Cdd:TIGR01224 237 ADHLEHASDAGIKALAEAGTVAVLLPGT-TFYLRETYPPARQLIDYGVPVALATDLNPGsSPTLSMQLIMSLACRLMKMT 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028431 372 PAEALVAATCNAAHAIGAASTAGQIAIGRPADLVVLKTPTYRDLAYLIDQNLIRYTLKDGAV 433
Cdd:TIGR01224 316 PEEALHAATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPYHYGVNHVHAVIKNGNI 377
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
56-434 |
3.03e-58 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 195.95 E-value: 3.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 56 IRNAAIHVVDGRIRDFGPAERVAVglPKGAEprVLDAAGGAVVPGFVDCHTHLLYSGSRADEYPMrvagasygeissrGG 135
Cdd:COG1228 26 IENGTVLVEDGKIAAVGPAADLAV--PAGAE--VIDATGKTVLPGLIDAHTHLGLGGGRAVEFEA-------------GG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 136 GVTRTIressdatssELKQALTVRLAKALLNGTTTAEIKTGYWV-----DPEGEGAALGIIAEVSASQPVDLVQTFHVal 210
Cdd:COG1228 89 GITPTV---------DLVNPADKRLRRALAAGVTTVRDLPGGPLglrdaIIAGESKLLPGPRVLAAGPALSLTGGAHA-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 211 GTPArfgGAGEYARYVIDYvlpsvasHARFCDVVCDVG--AFSHDEARQILHAAGRRGLNFKIHADEFSAAGGAELAAEL 288
Cdd:COG1228 158 RGPE---EARAALRELLAE-------GADYIKVFAEGGapDFSLEELRAILEAAHALGLPVAAHAHQADDIRLAVEAGVD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 289 gavSADHLCFLGKDTAQTLAKAQTVaVLLPATCHYL-----------------LAPKFADARHLIDGGVAIALGTDHGPG 351
Cdd:COG1228 228 ---SIEHGTYLDDEVADLLAEAGTV-VLVPTLSLFLallegaaapvaakarkvREAALANARRLHDAGVPVALGTDAGVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 352 S-PTLSMPFVMGLACSWlRMDPAEALVAATCNAAHAIGAASTAGQIAIGRPADLVVLKTPTYRDLAYLidqNLIRYTLKD 430
Cdd:COG1228 304 VpPGRSLHRELALAVEA-GLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAYL---EDVRAVMKD 379
|
....
gi 14028431 431 GAVF 434
Cdd:COG1228 380 GRVV 383
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
56-407 |
6.63e-24 |
|
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: 102.98 E-value: 6.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 56 IRNAAIHVVDGRIRDFGPAERVAVGLPkGAEprVLDAAGGAVVPGFVDCHTHLLYSGSR--ADEYP--------MRVAGA 125
Cdd:COG0402 19 LEDGAVLVEDGRIAAVGPGAELPARYP-AAE--VIDAGGKLVLPGLVNTHTHLPQTLLRglADDLPlldwleeyIWPLEA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 126 SYGEissrgggvtRTIRESSDATSSELkqaltvrlakaLLNGTTTA-EIktgYWVDPEGEGAALGIIAEV---------- 194
Cdd:COG0402 96 RLDP---------EDVYAGALLALAEM-----------LRSGTTTVaDF---YYVHPESADALAEAAAEAgiravlgrgl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 195 -SASQPVDLVQTFHVALGTPARFggAGEYARYVIDYVLPSVASHArfcdvvcdVGAFSHDEARQILHAAGRRGLNFKIHA 273
Cdd:COG0402 153 mDRGFPDGLREDADEGLADSERL--IERWHGAADGRIRVALAPHA--------PYTVSPELLRAAAALARELGLPLHTHL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 274 DEfSAAGGAELAAELGA---------------VSADHLCFLGKDTAQTLAKAQTVAVLLPaTCHYLLAPKFADARHLIDG 338
Cdd:COG0402 223 AE-TRDEVEWVLELYGKrpveyldelgllgprTLLAHCVHLTDEEIALLAETGASVAHCP-TSNLKLGSGIAPVPRLLAA 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14028431 339 GVAIALGTDHGPGSPTLSMPFVMGLA--------CSWLRMDPAEALVAATCNAAHAIGAASTAGQIAIGRPADLVVL 407
Cdd:COG0402 301 GVRVGLGTDGAASNNSLDMFEEMRLAallqrlrgGDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVL 377
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
97-431 |
4.20e-17 |
|
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: 82.16 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 97 VVPGFVDCHTHLLYSGSRADEYPMRVA--GASYGEISSRGGGVTrTIRESSDATSSELKqaltvRLAKALLNgtttaeik 174
Cdd:pfam01979 2 VLPGLIDAHVHLEMGLLRGIPVPPEFAyeALRLGITTMLKSGTT-TVLDMGATTSTGIE-----ALLEAAEE-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 175 tgYWVDPEGEGAALGIIAEVSASQPVDLVQTFHVALGTPARFGGAGeyaryvidyVLPSVASHARFcdvvcdvgAFSHDE 254
Cdd:pfam01979 68 --LPLGLRFLGPGCSLDTDGELEGRKALREKLKAGAEFIKGMADGV---------VFVGLAPHGAP--------TFSDDE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 255 ARQILHAAGRRGLNFKIHADE--------------------FSAAGGAELAAELGAVSADHLCFLGKDTAQTLAK-AQTV 313
Cdd:pfam01979 129 LKAALEEAKKYGLPVAIHALEtkgevedaiaafgggiehgtHLEVAESGGLLDIIKLILAHGVHLSPTEANLLAEhLKGA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 314 AVLLPATCHYLLAPKFADARHLIDGGVAIALGTDHGPGSPTLSMPFVMGLACSWLR-----MDPAEALVAATCNAAHAIG 388
Cdd:pfam01979 209 GVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFdpeggLSPLEALRMATINPAKALG 288
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 14028431 389 AASTAGQIAIGRPADLVVLKTPTYRDLAYLIDQNLIRYTLKDG 431
Cdd:pfam01979 289 LDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKKVIVKG 331
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
61-433 |
2.10e-14 |
|
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: 74.59 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 61 IHVVDGRIRDFGPAERVAVGLPkgaeprVLDAAGGAVVPGFVDCHTHL---LYSGsradeyPMRVagasygeisSRGGGV 137
Cdd:cd01293 17 IAIEDGRIAAIGPALAVPPDAE------EVDAKGRLVLPAFVDPHIHLdktFTGG------RWPN---------NSGGTL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 138 TRTIRESSDATSSELKQALTVR----LAKALLNGTTTaeIKTGYWVDPEGEGAALGIIAEVSAS-------QPVDLVQtf 206
Cdd:cd01293 76 LEAIIAWEERKLLLTAEDVKERaeraLELAIAHGTTA--IRTHVDVDPAAGLKALEALLELREEwadlidlQIVAFPQ-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 207 HVALGTParfgGAGEYARYVIDyvlpsvashaRFCDVVCDVGAFSHDEA-----RQILHAAGRRGLNFKIHADEFSAAGG 281
Cdd:cd01293 152 HGLLSTP----GGEELMREALK----------MGADVVGGIPPAEIDEDgeeslDTLFELAQEHGLDIDLHLDETDDPGS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 282 AE---------LAAELGAVSADHLCFLG-------KDTAQTLAKAQ-TVAVLLPATCHYLLAPKFADARH-------LID 337
Cdd:cd01293 218 RTleelaeeaeRRGMQGRVTCSHATALGslpeaevSRLADLLAEAGiSVVSLPPINLYLQGREDTTPKRRgvtpvkeLRA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 338 GGVAIALGTDH-----GP-GSPtlSMPFVMGLACSWLRMDPAE----ALVAATCNAAHAIGAAStaGQIAIGRPADLVVL 407
Cdd:cd01293 298 AGVNVALGSDNvrdpwYPfGSG--DMLEVANLAAHIAQLGTPEdlalALDLITGNAARALGLED--YGIKVGCPADLVLL 373
|
410 420
....*....|....*....|....*.
gi 14028431 408 KTPTYRDLayLIDQNLIRYTLKDGAV 433
Cdd:cd01293 374 DAEDVAEA--VARQPPRRVVIRKGRV 397
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
56-409 |
6.11e-12 |
|
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: 66.84 E-value: 6.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 56 IRNAAIHVVDGRIRDFGPAERvavgLPKGAEPRVLDAAGGAVVPGFVDCHTHLLYSGSR--AD---------EYPMRVAG 124
Cdd:cd01298 17 LEDGDVLVEDGRIVAVGPALP----LPAYPADEVIDAKGKVVMPGLVNTHTHLAMTLLRglADdlplmewlkDLIWPLER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 125 ASYGEIssrgggvtrtIRESSDATSSELkqaltvrlakaLLNGTTT-AEIktgYWVDPEGEGAA---LGI---IAEVSAS 197
Cdd:cd01298 93 LLTEED----------VYLGALLALAEM-----------IRSGTTTfADM---YFFYPDAVAEAaeeLGIravLGRGIMD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 198 QPVDLVQTFHVALGTPARFggAGEYARYVIDYVLPSVASHArfcdvvcdVGAFSHDEARQILHAAGRRGLNFKIHADEFS 277
Cdd:cd01298 149 LGTEDVEETEEALAEAERL--IREWHGAADGRIRVALAPHA--------PYTCSDELLREVAELAREYGVPLHIHLAETE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 278 AAGGAELAA--ELGAVSADHLCFLGKDT------------AQTLAKAQTVAVLLPATcHYLLAPKFADARHLIDGGVAIA 343
Cdd:cd01298 219 DEVEESLEKygKRPVEYLEELGLLGPDVvlahcvwltdeeIELLAETGTGVAHNPAS-NMKLASGIAPVPEMLEAGVNVG 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14028431 344 LGTDHGPGSPTLSMPFVMGLAcsWL----------RMDPAEALVAATCNAAHAIGAASTaGQIAIGRPADLVVLKT 409
Cdd:cd01298 298 LGTDGAASNNNLDMFEEMRLA--ALlqklahgdptALPAEEALEMATIGGAKALGLDEI-GSLEVGKKADLILIDL 370
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
101-384 |
1.29e-11 |
|
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: 64.66 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 101 FVDCHTHLLYSGSRadeypmrvagasygeissrGGGVTRTIRESSDATSSELKQALTVRLAKALLNGTTTAEIKTGYwVD 180
Cdd:cd01292 1 FIDTHVHLDGSALR-------------------GTRLNLELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGST-PP 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 181 PEGEGAALGIIAEVSASQPVDLVQTFHVALGTPARFGGA-----GEYARYVIDYVLPSVASHarfcdVVCDVGAFSHDEA 255
Cdd:cd01292 61 PTTTKAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDaeallLELLRRGLELGAVGLKLA-----GPYTATGLSDESL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 256 RQILHAAGRRGLNFKIHADEFSAAGGAE-----LAAELGAVSADHLCFLGKDTAQTLAKAQTVAVLLPATCHYLLAPK-- 328
Cdd:cd01292 136 RRVLEEARKLGLPVVIHAGELPDPTRALedlvaLLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRDGeg 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 14028431 329 FADARHLIDGGVAIALGTDHGPGSPTLSMPFVMGLAC--SWLRMDPAEALVAATCNAA 384
Cdd:cd01292 216 AEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLkvLRLGLSLEEALRLATINPA 273
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
88-433 |
4.00e-09 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 58.31 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 88 RVLDAAGGAVVPGFVDCHTHLLYSGSRADEY--------------------PMRVAGASYGEISSRGGGVTRTIRESSDA 147
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLRELrlpdvlpnavvkgqagrtpkGRWLVGEGWDEAQFAETRFPYALADLDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 148 ------------TSSELkqALTVRLAKALLNGTTTAEIKTGYWVDPEGEGAaLGIIAE-----VSASQPVDLVQTFHVAL 210
Cdd:pfam07969 81 apdgpvllralhTHAAV--ANSAALDLAGITKATEDPPGGEIARDANGEGL-TGLLREgayalPPLLAREAEAAAVAAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 211 GTPARFG-----GAGEYARYVIDYVL---------------------------------------------PSVASHARF 240
Cdd:pfam07969 158 AALPGFGitsvdGGGGNVHSLDDYEPlreltaaeklkelldaperlglphsiyelrigamklfadgvlgsrTAALTEPYF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 241 CDVVCDVGAFSHDEARQILHAAGRRGLNFKIHADE--------FSAAGGAELAAELGAVSADHLCFLGKDTAQT---LAK 309
Cdd:pfam07969 238 DAPGTGWPDFEDEALAELVAAARERGLDVAIHAIGdatidtalDAFEAVAEKLGNQGRVRIEHAQGVVPYTYSQierVAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 310 AQTVAVLLPATCHYLL-----------APKFADARHLIDGGVAIALGTDhGPGSPTLSMPFVMGLACSW----------- 367
Cdd:pfam07969 318 LGGAAGVQPVFDPLWGdwlqdrlgaerARGLTPVKELLNAGVKVALGSD-APVGPFDPWPRIGAAVMRQtagggevlgpd 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028431 368 LRMDPAEALVAATCNAAHAIGAASTAGQIAIGRPADLVVLktptyrDLAYL------IDQNLIRYTLKDGAV 433
Cdd:pfam07969 397 EELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVL------DDDPLtvdppaIADIRVRLTVVDGRV 462
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
65-406 |
5.04e-08 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 54.62 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 65 DGRIRDFGPAERVavglPKGAEprVLDAAGGAVVPGFVDCHTHLlysGsrADEYPMRVAGASYGEISsrgGGVTRTIReS 144
Cdd:cd01309 1 DGKIVAVGAEITT----PADAE--VIDAKGKHVTPGLIDAHSHL---G--LDEEGGVRETSDANEET---DPVTPHVR-A 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 145 SDA---TSSELKQALT-------VRLAKALLNGTTTAEIKTgYWVDPEGEgaalGIIAEVSasqpvdlvqtFHVALG-TP 213
Cdd:cd01309 66 IDGinpDDEAFKRARAggvttvqVLPGSANLIGGQGVVIKT-DGGTIEDM----FIKAPAG----------LKMALGeNP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 214 ARFGG----------------------AGEYARYVIDYVLPSVASHARfcDVVCDVGA---------FSH-DEARQILhA 261
Cdd:cd01309 131 KRVYGgkgkepatrmgvaallrdafikAQEYGRKYDLGKNAKKDPPER--DLKLEALLpvlkgeipvRIHaHRADDIL-T 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 262 AGRrglnfkiHADEFsaaggaelaaeLGAVSADHlCFLGKDTAQTLAKAQTVAVLLPATCHY-----LLAPKFADARHLI 336
Cdd:cd01309 208 AIR-------IAKEF-----------GIKITIEH-GAEGYKLADELAKHGIPVIYGPTLTLPkkveeVNDAIDTNAYLLK 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 337 DGGVAIALGTDHgPGSPTLSMPFVMGLACSwLRMDPAEALVAATCNAAHAIGAASTAGQIAIGRPADLVV 406
Cdd:cd01309 269 KGGVAFAISSDH-PVLNIRNLNLEAAKAVK-YGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVV 336
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
56-407 |
1.09e-07 |
|
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 132012 [Multi-domain] Cd Length: 401 Bit Score: 53.80 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 56 IRNAAIHVVDGRIRDFGPAERVAVGLPKGAEprVLDAAGGAVVPGFVDCHTHllysgsradeYPMRVAGASYGEissrgg 135
Cdd:TIGR02967 4 FEDGLLVVENGRIVAVGDYAELKETLPAGVE--IDDYRGHLIMPGFIDTHIH----------YPQTEMIASYGE------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 136 GV-----TRTIRESSDATSSELKQALTVRLAKALL-NGTTTAeiktGYW--VDPEG--------EGAALGII-------- 191
Cdd:TIGR02967 66 QLlewleKYTFPTEARFADPDHAEEVAEFFLDELLrNGTTTA----LVFatVHPESvdalfeaaLKRGMRMIagkvlmdr 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 192 ---------AEVSASQPVDLVQTFH------VAL-------GTPARFGGAGEYARyviDYvlPSVASHARFCDvvcdvga 249
Cdd:TIGR02967 142 napdylrdtAESSYDESKALIERWHgkgrllYAVtprfaptSSPEQLAAAGELAK---EY--PDVYVQTHLSE------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 250 fSHDE----------ARQILHAAGRRGLnfkihadefsaaggaelaAELGAVSAdHLCFLGKDTAQTLAKAQTVAVLLPa 319
Cdd:TIGR02967 210 -NKDEiawvkelfpeAKDYLDVYDHYGL------------------LGRRSVFA-HCIHLSDEECQRLAETGAAIAHCP- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 320 TCHYLLAPKFADARHLIDGGVAIALGTDHGPGsPTLSMPFVMGLA--CSWL---RMDPAEALVAATCNAAHAIGAASTAG 394
Cdd:TIGR02967 269 TSNLFLGSGLFNLKKALEHGVRVGLGTDVGGG-TSFSMLQTLREAykVSQLqgaRLSPFEAFYLATLGGARALDLDDRIG 347
|
410
....*....|...
gi 14028431 395 QIAIGRPADLVVL 407
Cdd:TIGR02967 348 NFEPGKEADFVVL 360
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
55-115 |
2.51e-07 |
|
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: 52.79 E-value: 2.51e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028431 55 SIRNAAIHVVDGRIRDFGPaervavGLPKGAEPRVLDAAGGAVVPGFVDCHTHL----------LYSGSRA 115
Cdd:COG0044 12 GLERADVLIEDGRIAAIGP------DLAAPEAAEVIDATGLLVLPGLIDLHVHLrepglehkedIETGTRA 76
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
56-129 |
1.09e-06 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 50.57 E-value: 1.09e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14028431 56 IRNAAIHVVDGRIRDFGPAERVAVGLPKGAEprVLDAAGGAVVPGFVDCHTHllysgsradeYP-MRVAgASYGE 129
Cdd:PRK09228 29 IEDGLLLVEDGRIVAAGPYAELRAQLPADAE--VTDYRGKLILPGFIDTHIH----------YPqTDMI-ASYGE 90
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
56-413 |
2.65e-06 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 49.61 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 56 IRNAAIHVVDGRIRDFGPAERVAvglpkgAEPRVLDAAGGAVVPGFVDCHTHL---LYSGsRADE-----------YPMR 121
Cdd:PRK07228 19 IVDGDVLIEDDRIAAVGDRLDLE------DYDDHIDATGKVVIPGLIQGHIHLcqtLFRG-IADDlelldwlkdriWPLE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 122 VA--GAS--------YGEISsRGGGVTRTIRESSDATSSELKQALTV----RLAKALLNgtttaeiktgywvdpEGEGAA 187
Cdd:PRK07228 92 AAhdAESmyysallgIGELI-ESGTTTIVDMESVHHTDSAFEAAGESgiraVLGKVMMD---------------YGDDVP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 188 LGIIAEVSAS--QPVDLVQTFHvalgtpARFGGAGEYAryvidyVLPsvashaRFCdVVCdvgafSHDEARQILHAAGRR 265
Cdd:PRK07228 156 EGLQEDTEASlaESVRLLEKWH------GADNGRIRYA------FTP------RFA-VSC-----TEELLRGVRDLADEY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 266 GLNFKIHADEfsaaggaeLAAELGAVSAD----------------------HLCFLGKDTAQTLAKAQTVAVLLPAtCHY 323
Cdd:PRK07228 212 GVRIHTHASE--------NRGEIETVEEEtgmrnihyldevgltgedlilaHCVWLDEEEREILAETGTHVTHCPS-SNL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 324 LLAPKFADARHLIDGGVAIALGTDHGPGSPTLSMPFVMGLAcSWL---------RMDPAEALVAATCNAAHAIGAASTAG 394
Cdd:PRK07228 283 KLASGIAPVPDLLERGINVALGADGAPCNNTLDPFTEMRQA-ALIqkvdrlgptAMPARTVFEMATLGGAKAAGFEDEIG 361
|
410
....*....|....*....
gi 14028431 395 QIAIGRPADLVVLKTPTYR 413
Cdd:PRK07228 362 SLEEGKKADLAILDLDGLH 380
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
60-406 |
3.19e-06 |
|
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: 49.23 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 60 AIHVVDGRIRDFGPAERVAvgLPKGAEPRVLDAAGGAVVPGFVDCHTHLLYSGSRADEYPMRvaGASYGEISS------- 132
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAK--ALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLS--GVTSKEEALarireda 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 133 ---------RGGGVTRT-IRESSDATSSELKQALTVR------------------LAKALLNGTTTAEIKTGYWVDPEGE 184
Cdd:cd01300 77 aaappgewiLGFGWDESlLGEGRYPTRAELDAVSPDRpvlllrrdghsawvnsaaLRLAGITRDTPDPPGGEIVRDADGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 185 gaALGIIAEVSASQPVDLVQTFHVALGTPARFGGAGEYARY----VID-------------------------YVLPSVA 235
Cdd:cd01300 157 --PTGVLVEAAAALVLEAVPPPTPEERRAALRAAARELASLgvttVHDagggaaddieayrrlaaageltlrvRVALYVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 236 SHARFCD---------------------VVCDvGA-----------------------FSHDEARQILHAAGRRGLNFKI 271
Cdd:cd01300 235 PLAEDLLeelgarkngagddrlrlggvkLFAD-GSlgsrtaalsepyldspgtgglllISPEELEELVRAADEAGLQVAI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 272 HA----------DEFSAAGGAELAAELGAvSADHLCFLGKDTAQTLAKAQTVAVLLPATCHY--------LLAPKFADA- 332
Cdd:cd01300 314 HAigdravdtvlDALEAALKDNPRADHRH-RIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSdgdaaedrRLGEERAKRs 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 333 ---RHLIDGGVAIALGTDHGPGSP----------TLSMPFVMGLACSWLRMDPAEALVAATCNAAHAIGAASTAGQIAIG 399
Cdd:cd01300 393 ypfRSLLDAGVPVALGSDAPVAPPdpllgiwaavTRKTPGGGVLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPG 472
|
....*..
gi 14028431 400 RPADLVV 406
Cdd:cd01300 473 KLADFVV 479
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
329-408 |
3.40e-06 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 48.83 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 329 FADARHLIDGGVAIALGTDHG-PGSPTLSMPFVMGLACSWLrMDPAEALVAATCNAAHAIGAASTAGQIAIGRPADLVVL 407
Cdd:cd01299 253 RDALRRAHKAGVKIAFGTDAGfPVPPHGWNARELELLVKAG-GTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVV 331
|
.
gi 14028431 408 K 408
Cdd:cd01299 332 D 332
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
60-112 |
4.61e-06 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 48.64 E-value: 4.61e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 14028431 60 AIHVVDGRIRDFGPAERVAvGLpKGAEPRVLDAAGGAVVPGFVDCHTHLLYSG 112
Cdd:COG1574 29 AVAVRDGRIVAVGSDAEVR-AL-AGPATEVIDLGGKTVLPGFIDAHVHLLGGG 79
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
39-108 |
9.88e-06 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 47.67 E-value: 9.88e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 39 DEFGPGPQRGGLKHlksirnAAIHVVDGRIRDFGPAERVAVGLPKgaeprvLDAAGGAVVPGFVDCHTHL 108
Cdd:PRK07583 27 GGVPPGDTLEGLVL------VDIEIADGKIAAILPAGGAPDELPA------VDLKGRMVWPCFVDMHTHL 84
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
56-107 |
1.00e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 47.40 E-value: 1.00e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 14028431 56 IRNAAIHVVDGRIRDFGPAERVAVglpkgaepRVLDAAGGAVVPGFVDCHTH 107
Cdd:COG1820 14 LEDGALLIEDGRIAAIGPGAEPDA--------EVIDLGGGYLAPGFIDLHVH 57
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
351-407 |
1.05e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 47.40 E-value: 1.05e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 14028431 351 GSpTLSMPFVMGLACSWLRMDPAEALVAATCNAAHAIGAASTAGQIAIGRPADLVVL 407
Cdd:COG1820 304 GS-TLTMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVL 359
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
66-410 |
1.16e-05 |
|
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238637 [Multi-domain] Cd Length: 381 Bit Score: 47.44 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 66 GRIRDFGPAERVAVGLPKgaePRVLDAAGGAVVPGFVDCHTHLLYSGSRADeypmrvagASYGEISSRGGGVtrtIRESS 145
Cdd:cd01312 1 DKILEVGDYEKLEKRYPG---AKHEFFPNGVLLPGLINAHTHLEFSANVAQ--------FTYGRFRAWLLSV---INSRD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 146 DATSSELKQALTVRLAKALLNGTTTAeiktgywvdpeGEGAALGIIAEVSASQPVDLVqTFHVALGT-PAR--FGGAGEY 222
Cdd:cd01312 67 ELLKQPWEEAIRQGIRQMLESGTTSI-----------GAISSDGSLLPALASSGLRGV-FFNEVIGSnPSAidFKGETFL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 223 ARYV------IDYVLPSVASHARFcDVVCDVGAFSHDEARQ-----ILH-------------AAG---------RRGLNF 269
Cdd:cd01312 135 ERFKrsksfeSQLFIPAISPHAPY-SVHPELAQDLIDLAKKlnlplSTHfleskeerewleeSKGwfkhfwesfLKLPKP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 270 KIHA------DEFSAAGGAelaaelgaVSADHLCFLGKDTAQTLAKAQTVAVLLPATcHYLLAPKFADARHLIDGGVAIA 343
Cdd:cd01312 214 KKLAtaidflDMLGGLGTR--------VSFVHCVYANLEEAEILASRGASIALCPRS-NRLLNGGKLDVSELKKAGIPVS 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028431 344 LGTDHGPGSPTLSMPFVMGLACSWLRMD-----PAEALVAATCNAAHAIGAAStaGQIAIGRPADLVVLKTP 410
Cdd:cd01312 285 LGTDGLSSNISLSLLDELRALLDLHPEEdllelASELLLMATLGGARALGLNN--GEIEAGKRADFAVFELP 354
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
57-107 |
1.16e-05 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 47.48 E-value: 1.16e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 14028431 57 RNAAIHVVDGRIrdfgpaerVAVG-LPKGAEPRVLDAAGGAVVPGFVDCHTH 107
Cdd:COG3653 20 FRADVAIKGGRI--------VAVGdLAAAEAARVIDATGLVVAPGFIDIHTH 63
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
59-115 |
1.26e-05 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 47.47 E-value: 1.26e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14028431 59 AAIHVVDGRIrdfgpaerVAVGLPKGAEprVLDAAGGAVVPGFVDCHTHL------------LYSGSRA 115
Cdd:PRK08323 19 ADVLIEDGKI--------AAIGANLGDE--VIDATGKYVMPGGIDPHTHMempfggtvssddFETGTRA 77
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
58-409 |
1.64e-05 |
|
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: 46.89 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 58 NAAIHVVDGRIRDFGPAERVAVGLPKGAepRVLDAAGGAVVPGFVDCHTHllysgsradeYP-MRVAGASYGE-----IS 131
Cdd:cd01303 26 DGLIVVVDGNIIAAGAAETLKRAAKPGA--RVIDSPNQFILPGFIDTHIH----------APqYANIGSGLGEplldwLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 132 srgggvTRTIREssDATSSELKQALTV--RLAKALL-NGTTTAEiktgYW--VDPEG------EGAALGIIA-------- 192
Cdd:cd01303 94 ------TYTFPE--EAKFADPAYAREVygRFLDELLrNGTTTAC----YFatIHPEStealfeEAAKRGQRAiagkvcmd 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 193 -----------EVSASQPVDLVQTFHVALG------TPaRF---------GGAGEYARyviDYVLPSVASHARFCDVVCD 246
Cdd:cd01303 162 rnapeyyrdtaESSYRDTKRLIERWHGKSGrvkpaiTP-RFapscseellAALGKLAK---EHPDLHIQTHISENLDEIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 247 VGAFSHDEARQILHAAGRRGLnfkihadefsaaggaelaAELGAVSAdHLCFLGKDTAQTLAKAQTVAVLLPaTCHYLLA 326
Cdd:cd01303 238 WVKELFPGARDYLDVYDKYGL------------------LTEKTVLA-HCVHLSEEEFNLLKERGASVAHCP-TSNLFLG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 327 PKFADARHLIDGGVAIALGTDHGPGSpTLSMPFVMGLA--CSWLR---------MDPAEALVAATCNAAHAIGAASTAGQ 395
Cdd:cd01303 298 SGLFDVRKLLDAGIKVGLGTDVGGGT-SFSMLDTLRQAykVSRLLgyelgghakLSPAEAFYLATLGGAEALGLDDKIGN 376
|
410
....*....|....
gi 14028431 396 IAIGRPADLVVLKT 409
Cdd:cd01303 377 FEVGKEFDAVVIDP 390
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
61-115 |
2.03e-05 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 46.73 E-value: 2.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14028431 61 IHVVDGRIRDFGPAERvavglpkGAEPRVLDAAGGAVVPGFVDCHTHL----------LYSGSRA 115
Cdd:PRK09357 22 VLIDDGKIAAIGENIE-------AEGAEVIDATGLVVAPGLVDLHVHLrepgqedketIETGSRA 79
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
54-107 |
3.65e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 45.65 E-value: 3.65e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 14028431 54 KSIRNAAIHVVDGRIRDFGPAErvavglPKGAEPRVLDAAGGAVVPGFVDCHTH 107
Cdd:cd00854 12 GGLEDGAVLVEDGKIVAIGPED------ELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
59-108 |
5.25e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 45.31 E-value: 5.25e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 14028431 59 AAIHVVDGRIRDFGPAERVAVGLPkgaeprVLDAAGGAVVPGFVDCHTHL 108
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAE------VEDGGGALALPGLVDGHIHL 60
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
54-115 |
1.00e-04 |
|
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: 44.52 E-value: 1.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028431 54 KSIRNAAIHVVDGRIRDFGPaervavGLPKGAEPRVLDAAGGAVVPGFVDCHTHL------------LYSGSRA 115
Cdd:cd01314 12 DGSFKADILIEDGKIVAIGP------NLEAPGGVEVIDATGKYVLPGGIDPHTHLelpfmgtvtaddFESGTRA 79
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
56-115 |
1.99e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 43.45 E-value: 1.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 56 IRNAAIHVVDGRIRDFGPAERVAvglpkGAEprVLDAAGGAVVPGFVDCHTHLLYSGSRA 115
Cdd:PRK08204 21 LPRGDILIEGDRIAAVAPSIEAP-----DAE--VVDARGMIVMPGLVDTHRHTWQSVLRG 73
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
56-107 |
2.71e-04 |
|
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: 43.05 E-value: 2.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028431 56 IRNAaiHVVDG----------RIRDFGPAERVAVGLPKGAepRVLDAAGGAVVPGFVDCHTH 107
Cdd:cd01297 4 IRNG--TVVDGtgappftadvGIRDGRIAAIGPILSTSAR--EVIDAAGLVVAPGFIDVHTH 61
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
58-269 |
2.83e-04 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 42.83 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 58 NAAIHVVDGRIRDfgpaervAVGLPKGAEPRVLDAAGGAVVPGFVDCHTHLLYSGSradeypmrvAGASYGEISSRGGGV 137
Cdd:PRK12394 22 INNLRIINDIIVD-------ADKYPVASETRIIHADGCIVTPGLIDYHAHVFYDGT---------EGGVRPDMYMPPNGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 138 TRTIRESSDATSS-ELKQALTVRLA----KALLNGTTTAEIKTGYW--VDP-------------EGEGAALG-------- 189
Cdd:PRK12394 86 TTVVDAGSAGTANfDAFYRTVICASkvriKAFLTVSPPGQTWSGYQenYDPdnidenkihalfrQYRNVLQGlklrvqte 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 190 IIAEVsASQPvdLVQTFHVA--LGTPArfggageyARYVIDYVLPS--VASHARFCDVVCDV----GAFSHDEARQILHA 261
Cdd:PRK12394 166 DIAEY-GLKP--LTETLRIAndLRCPV--------AVHSTHPVLPMkeLVSLLRRGDIIAHAfhgkGSTILTEEGAVLAE 234
|
250
....*....|.
gi 14028431 262 ---AGRRGLNF 269
Cdd:PRK12394 235 vrqARERGVIF 245
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
56-107 |
4.37e-04 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 42.39 E-value: 4.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 14028431 56 IRNAAIHVVDGRIrdfgpaerVAVGLPKGAEPRVLDAAGGAVVPGFVDCHTH 107
Cdd:COG1001 22 ILEGDIAIAGGRI--------AGVGDYIGEATEVIDAAGRYLVPGFIDGHVH 65
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
325-405 |
5.23e-04 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 42.21 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 325 LAPKFADARHLIDGGVAIALGTDHGPGSPTLSMPFVMGLAC--------SWLRMDPAEALVAATCNAAHAIGAASTAGQI 396
Cdd:PRK09045 287 LASGFCPVAKLLQAGVNVALGTDGAASNNDLDLFGEMRTAAllakavagDATALPAHTALRMATLNGARALGLDDEIGSL 366
|
....*....
gi 14028431 397 AIGRPADLV 405
Cdd:PRK09045 367 EPGKQADLV 375
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
56-112 |
5.37e-04 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 42.23 E-value: 5.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 14028431 56 IRNAAIHVVDGRIRDFGPAERVAVGLPkgaEPRVLDAAGGAVVPGFVDCHTHlLYSG 112
Cdd:PRK07203 19 IEDGAIAIEGNVIVEIGTTDELKAKYP---DAEFIDAKGKLIMPGLINSHNH-IYSG 71
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
55-108 |
6.56e-04 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 41.89 E-value: 6.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 14028431 55 SIRNAAIHVVDGRIRdfgpaeRVAVGLPKGAEPRVLDAAGGAVVPGFVDCHTHL 108
Cdd:cd01315 14 GVREADIAVKGGKIA------AIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHI 61
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
59-108 |
9.53e-04 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 41.37 E-value: 9.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 14028431 59 AAIHVVDGRIRDFGPaervavGLPKGAEPRVLDAAGGAVVPGFVDCHTHL 108
Cdd:PLN02942 23 ADVYVEDGIIVAVAP------NLKVPDDVRVIDATGKFVMPGGIDPHTHL 66
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
56-106 |
9.99e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 41.32 E-value: 9.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 14028431 56 IRNAAIHVVDGRIRDFGPAERVAVGlpkgaeprVLDAAGGAVVPGFVDCHT 106
Cdd:PRK15446 17 VVDGSLLIEDGRIAAIDPGASALPG--------AIDAEGDYLLPGLVDLHT 59
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
53-107 |
1.27e-03 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 41.22 E-value: 1.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 14028431 53 LKSIRNAAIhvVDGRIrdfgpaerVAVGLPKGAEPRVLDAAGGAVVPGFVDCHTH 107
Cdd:PRK09061 35 LDAVRDVGI--KGGKI--------AAVGTAAIEGDRTIDATGLVVAPGFIDLHAH 79
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
56-120 |
1.50e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 40.89 E-value: 1.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14028431 56 IRNAAIHVVDGRIrdfgpaERVAVGLPKGAEpRVLDAAGGAVVPGFVDCHTHL---LYSGSrADEYPM 120
Cdd:PRK06038 19 LKKGSVVIEDGTI------TEVSESTPGDAD-TVIDAKGSVVMPGLVNTHTHAamtLFRGY-ADDLPL 78
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
56-115 |
1.67e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 40.61 E-value: 1.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 56 IRNAAIHVVDGRIRDFGPAervavGLPKGAEPRVLDAAGGAVVPGFVDCHTHLLYSGSRA 115
Cdd:PRK08203 21 IADGGLVVEGGRIVEVGPG-----GALPQPADEVFDARGHVVTPGLVNTHHHFYQTLTRA 75
|
|
| PLN02795 |
PLN02795 |
allantoinase |
56-178 |
1.92e-03 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 40.53 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 56 IRNAAIHVVDGRIRDFGPAERVAVGLPKgaePRVLDAAGGAVVPGFVDCHTHLlysgsraDEyPMRV--AGASYGEISSR 133
Cdd:PLN02795 59 VIPGAVEVEGGRIVSVTKEEEAPKSQKK---PHVLDYGNAVVMPGLIDVHVHL-------NE-PGRTewEGFPTGTKAAA 127
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 14028431 134 GGGVTRTIR---ESSDATSSELKQALTVRLAKAllngttTAEIKTGYW 178
Cdd:PLN02795 128 AGGITTLVDmplNSFPSTTSVETLELKIEAAKG------KLYVDVGFW 169
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
61-141 |
2.46e-03 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 40.02 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 61 IHVVDGRIRDFGPAERVAvGLPKGAEprVLDAAGGAVVPGFVDCHTHLLYSGSradEYPMRVAGASYgeiSSRGGGVTRT 140
Cdd:PRK09059 25 VLIEDGVIVAAGKGAGNQ-GAPEGAE--IVDCAGKAVAPGLVDARVFVGEPGA---EHRETIASASR---AAAAGGVTSI 95
|
.
gi 14028431 141 I 141
Cdd:PRK09059 96 I 96
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
61-153 |
3.06e-03 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 39.84 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028431 61 IHVVDGRIrdfgpaerVAVGLPKGAEPRVLDAAGGAVVPGFVDCHTHLLYSGSRADEypmrvaGASYGEISSRGGGVTRT 140
Cdd:PRK08044 23 IAVKGGKI--------AAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWE------GYETGTRAAAKGGITTM 88
|
90 100
....*....|....*....|
gi 14028431 141 IR-------ESSDATSSELK 153
Cdd:PRK08044 89 IEmplnqlpATVDRASIELK 108
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
61-111 |
4.77e-03 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 39.28 E-value: 4.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 14028431 61 IHVVDGRIRDFGPaervavgLPKGAEPRVLDAAGGAVVPGFVDCHTHLLYS 111
Cdd:PRK12393 28 IRIRDGRIAAIGA-------LTPLPGERVIDATDCVVYPGWVNTHHHLFQS 71
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
56-108 |
4.90e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 39.23 E-value: 4.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028431 56 IRNAA---------IHVVDGRIRDFGPaervavGLPKGAePRVLDAAGGAVVPGFVDCHTHL 108
Cdd:PRK07572 6 VRNANlpdgrtgidIGIAGGRIAAVEP------GLQAEA-AEEIDAAGRLVSPPFVDPHFHM 60
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
366-407 |
5.43e-03 |
|
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: 38.71 E-value: 5.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 14028431 366 SWLRMDPAEALVAATCNAAHAIGAASTAGQIAIGRPADLVVL 407
Cdd:cd00854 320 KWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVL 361
|
|
| |
