|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
2-342 |
0e+00 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 625.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 2 ALAELLLSGCTTAADHHYLFPGGLEQAIDVQAGVVEELGMRAMLTRGSMSLGEKDGGLPPQQTVQEAETILADSERLIAR 81
Cdd:PRK08203 110 ALAELLLSGCTTSSDHHYLFPNGLRDALDDQIEAAREIGMRFHATRGSMSLGESDGGLPPDSVVEDEDAILADSQRLIDR 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 82 YHQRGDGARVQIALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRTVDYLDSVGWLGPRTWLA 161
Cdd:PRK08203 190 YHDPGPGAMLRIALAPCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAFCLERFGMRPVDYLEDLGWLGPDVWLA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 162 HGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASNMILEARQALYLQRLRYGAE 241
Cdd:PRK08203 270 HCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDGSASNDGSNLIGEARQALLLQRLRYGPD 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 242 RITPELALGWATRGSARLLGRSDIGELAPGKQADLALFKLDELRFSGSHDPLSALLLCAADRADRVMVGGAWRVVDGAVE 321
Cdd:PRK08203 350 AMTAREALEWATLGGARVLGRDDIGSLAPGKLADLALFDLDELRFAGAHDPVAALVLCGPPRADRVMVGGRWVVRDGQLT 429
|
330 340
....*....|....*....|.
gi 777183254 322 GLDLAALIARHREAASALIAG 342
Cdd:PRK08203 430 TLDLAALIARHRAAARRLAAG 450
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
2-320 |
3.34e-131 |
|
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: 380.39 E-value: 3.34e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 2 ALAELLLSGCTTAADHHYLFPggleqaiDVQAGVVEELGMRAMLTRGSMSLGEKDgglppqqtVQEAETILADSERLIAR 81
Cdd:cd01298 106 ALAEMIRSGTTTFADMYFFYP-------DAVAEAAEELGIRAVLGRGIMDLGTED--------VEETEEALAEAERLIRE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 82 YHQRGDGaRVQIALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRTVDYLDSVGWLGPRTWLA 161
Cdd:cd01298 171 WHGAADG-RIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESLEKYGKRPVEYLEELGLLGPDVVLA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 162 HGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASNMILEARQALYLQRLRYGAE 241
Cdd:cd01298 250 HCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDGAASNNNLDMFEEMRLAALLQKLAHGDP 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 242 R-ITPELALGWATRGSARLLGRSDIGELAPGKQADLALFKLDELRFSGSHDPLSALL-LCAADRADRVMVGGAWRVVDGA 319
Cdd:cd01298 330 TaLPAEEALEMATIGGAKALGLDEIGSLEVGKKADLILIDLDGPHLLPVHDPISHLVySANGGDVDTVIVNGRVVMEDGE 409
|
.
gi 777183254 320 V 320
Cdd:cd01298 410 L 410
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
2-317 |
2.97e-124 |
|
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: 362.99 E-value: 2.97e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 2 ALAELLLSGCTTAADHHYLFPGGLEQAIDVqagvVEELGMRAMLTRGSMslgekDGGLPPQQtVQEAETILADSERLIAR 81
Cdd:COG0402 109 ALAEMLRSGTTTVADFYYVHPESADALAEA----AAEAGIRAVLGRGLM-----DRGFPDGL-REDADEGLADSERLIER 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 82 YHQRGDGaRVQIALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRTVDYLDSVGWLGPRTWLA 161
Cdd:COG0402 179 WHGAADG-RIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLELYGKRPVEYLDELGLLGPRTLLA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 162 HGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASNMILEARQALYLQRLRYG-A 240
Cdd:COG0402 258 HCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDGAASNNSLDMFEEMRLAALLQRLRGGdP 337
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 777183254 241 ERITPELALGWATRGSARLLGRSD-IGELAPGKQADLALFKLDELRFSGSHDPLSALLLCAADRA-DRVMVGGAWRVVD 317
Cdd:COG0402 338 TALSAREALEMATLGGARALGLDDeIGSLEPGKRADLVVLDLDAPHLAPLHDPLSALVYAADGRDvRTVWVAGRVVVRD 416
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
1-341 |
3.38e-107 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 320.86 E-value: 3.38e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 1 MALAELLLSGCTTAADHHYLF-PGGLEQAIDVQAGVVEELGMRAMLTRGSMSLGEKD-GGLPPQQTVQEAETILADSERL 78
Cdd:PRK12393 110 IGLVELLRSGCTTVADHHYLYhPGMPFDTGDILFDEAEALGMRFVLCRGGATQTRGDhPGLPTALRPETLDQMLADVERL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 79 IARYHQRGDGARVQIALAPCSP-FSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRTVDYLDSVGWLGPR 157
Cdd:PRK12393 190 VSRYHDASPDSLRRVVVAPTTPtFSLPPELLREVARAARGMGLRLHSHLSETVDYVDFCREKYGMTPVQFVAEHDWLGPD 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 158 TWLAHGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASNMILEARQALYLQRLR 237
Cdd:PRK12393 270 VWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDGAASNESADMLSEAHAAWLLHRAE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 238 YGAERITPELALGWATRGSARLLGRSDIGELAPGKQADLALFKLDELRFSGSHDPLSALLLCAADRADR-VMVGGAWRVV 316
Cdd:PRK12393 350 GGADATTVEDVVHWGTAGGARVLGLDAIGTLAVGQAADLAIYDLDDPRFFGLHDPAIAPVACGGPAPVKaLLVNGRPVVE 429
|
330 340
....*....|....*....|....*
gi 777183254 317 DGAVEGLDLAALIARHREAASALIA 341
Cdd:PRK12393 430 NGAIPGLDLAELRHDARAAVRRLLQ 454
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
4-341 |
2.89e-67 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 217.95 E-value: 2.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 4 AELLLSGCTTAAD----HHYlfpgglEQAIdvQAgvVEELGMRAMLTRGSMSLGeKDGGLPPQQTVQEAetiLADSERLI 79
Cdd:PRK07228 108 GELIESGTTTIVDmesvHHT------DSAF--EA--AGESGIRAVLGKVMMDYG-DDVPEGLQEDTEAS---LAESVRLL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 80 ARYHQRGDGaRVQIALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRTVDYLDSVGWLGPRTW 159
Cdd:PRK07228 174 EKWHGADNG-RIRYAFTPRFAVSCTEELLRGVRDLADEYGVRIHTHASENRGEIETVEEETGMRNIHYLDEVGLTGEDLI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 160 LAHGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASNMILEARQALYLQR-LRY 238
Cdd:PRK07228 253 LAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGADGAPCNNTLDPFTEMRQAALIQKvDRL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 239 GAERITPELALGWATRGSARLLGRSD-IGELAPGKQADLALFKLDELRFSGSH--DPLSALLLCA-ADRADRVMVGGAWR 314
Cdd:PRK07228 333 GPTAMPARTVFEMATLGGAKAAGFEDeIGSLEEGKKADLAILDLDGLHATPSHgvDVLSHLVYAAhGSDVETTMVDGKIV 412
|
330 340
....*....|....*....|....*..
gi 777183254 315 VVDGAVEGLDLAALIARHREAASALIA 341
Cdd:PRK07228 413 MEDGELTTIDADAVRREANRSIKRLLK 439
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
1-334 |
4.50e-56 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 188.58 E-value: 4.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 1 MALAELLLSGCTTAADHhYLFPggleqaiDVQAGVVEELGMRAMLtrgsmslgekdgGLP----PQQTVQEAETILADSE 76
Cdd:PRK09045 116 LAIAEMLRGGTTCFNDM-YFFP-------EAAAEAAHQAGMRAQI------------GMPvldfPTAWASDADEYLAKGL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 77 RLIARYHqrgDGARVQIALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRTVDYLDSVGWLGP 156
Cdd:PRK09045 176 ELHDQWR---HHPLISTAFAPHAPYTVSDENLERIRTLAEQLDLPIHIHLHETAQEIADSLKQHGQRPLARLARLGLLGP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 157 RTWLAHGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASNMILEARQALYLQRL 236
Cdd:PRK09045 253 RLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGTDGAASNNDLDLFGEMRTAALLAKA 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 237 RYG-AERITPELALGWATRGSARLLGRSD-IGELAPGKQADLALFKLDELRFSGSHDPLSALLLCAA-DRADRVMVGGAW 313
Cdd:PRK09045 333 VAGdATALPAHTALRMATLNGARALGLDDeIGSLEPGKQADLVAVDLSGLETQPVYDPVSQLVYAAGrEQVSHVWVAGKQ 412
|
330 340
....*....|....*....|.
gi 777183254 314 RVVDGAVEGLDLAALIARHRE 334
Cdd:PRK09045 413 LLDDRELTTLDEAELLARARQ 433
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
1-325 |
1.08e-48 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 168.65 E-value: 1.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 1 MALAELLLSGCTTAADHHYlfPGGLEqaIDVQAGVVEELGMRAMLTRGSMSlgekdgglPPQQTVqeAETIlaDSERLIA 80
Cdd:PRK06687 107 EALTEMLQSGTTTFNDMYN--PNGVD--IQQIYQVVKTSKMRCYFSPTLFS--------SETETT--AETI--SRTRSII 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 81 RYHQRGDGARVQIALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRTVDYLDSVGWLGPRTWL 160
Cdd:PRK06687 171 DEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIILKRYGKRPLAFLEELGYLDHPSVF 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 161 AHGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASNMILEARQALYLQRLRYG- 239
Cdd:PRK06687 251 AHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDSVASNNNLDMFEEGRTAALLQKMKSGd 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 240 AERITPELALGWATRGSARLLGRSD-IGELAPGKQAD-LALFKLDELRFSGSHDPLSALLLCA-ADRADRVMVGGAWRVV 316
Cdd:PRK06687 331 ASQFPIETALKVLTIEGAKALGMENqIGSLEVGKQADfLVIQPQGKIHLQPQENMLSHLVYAVkSSDVDDVYIAGEQVVK 410
|
....*....
gi 777183254 317 DGAVEGLDL 325
Cdd:PRK06687 411 QGQVLTVEL 419
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
1-341 |
3.49e-48 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 167.62 E-value: 3.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 1 MALAELLLSGCTTAADHhYLFpggleqaIDVQAGVVEELGMRAMLTRGSMSLGEKdgglppqqtvQEAETILADSERLIA 80
Cdd:PRK06038 104 LACLEMIKSGTTSFADM-YFY-------MDEVAKAVEESGLRAALSYGMIDLGDD----------EKGEAELKEGKRFVK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 81 RYHQRGDGaRVQIALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRTVDYLDSVGWLGPRTWL 160
Cdd:PRK06038 166 EWHGAADG-RIKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQMKEQYGMCSVNYLDDIGFLGPDVLA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 161 AHGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASNMILEARQALYLQRLRYGA 240
Cdd:PRK06038 245 AHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIAPVPKLLERGVNVSLGTDGCASNNNLDMFEEMKTAALLHKVNTMD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 241 ERITPELA-LGWATRGSARLLGrSDIGELAPGKQADLALFKLDELRFSGSHDPLSALLLCA--ADrADRVMVGGAWRVVD 317
Cdd:PRK06038 325 PTALPARQvLEMATVNGAKALG-INTGMLKEGYLADIIIVDMNKPHLTPVRDVPSHLVYSAsgSD-VDTTIVDGRILMED 402
|
330 340
....*....|....*....|....
gi 777183254 318 GAVEGLDLAALIARHREAASALIA 341
Cdd:PRK06038 403 YKVLCMDEQDVMEDAKKAAEELVS 426
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
3-278 |
7.75e-47 |
|
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: 163.99 E-value: 7.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 3 LAELLLSGCTTA---ADHHYlfpggleQAIDVQAGVVEELGMRAMLTRGSMSLgekdggLPPQQTVQEAETILADSERLI 79
Cdd:cd01303 117 LDELLRNGTTTAcyfATIHP-------ESTEALFEEAAKRGQRAIAGKVCMDR------NAPEYYRDTAESSYRDTKRLI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 80 ARYHQRGDgaRVQIALAPCSPFSVTPEIMRASAEVAARH-DVRLHTHLAETLDEEDFCLQRFGLRTvDYLD---SVGWLG 155
Cdd:cd01303 184 ERWHGKSG--RVKPAITPRFAPSCSEELLAALGKLAKEHpDLHIQTHISENLDEIAWVKELFPGAR-DYLDvydKYGLLT 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 156 PRTWLAHGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASnMILEARQALYLQR 235
Cdd:cd01303 261 EKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDVGGGTSFS-MLDTLRQAYKVSR 339
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 777183254 236 LR----YGAERITPELALGWATRGSARLLGRSD-IGELAPGKQADLAL 278
Cdd:cd01303 340 LLgyelGGHAKLSPAEAFYLATLGGAEALGLDDkIGNFEVGKEFDAVV 387
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
2-284 |
6.44e-46 |
|
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: 159.20 E-value: 6.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 2 ALAELLLSGCTTAADHHYLFPGGLEQAIDVQAGVVeeLGMRAMLTRGSMSlgekdgglppqqTVQEAETILADSERLIAR 81
Cdd:pfam01979 35 GITTMLKSGTTTVLDMGATTSTGIEALLEAAEELP--LGLRFLGPGCSLD------------TDGELEGRKALREKLKAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 82 Y---HQRGDGaRVQIALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRT-----VDYLDSVGW 153
Cdd:pfam01979 101 AefiKGMADG-VVFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKGEVEDAIAAFGGGIehgthLEVAESGGL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 154 LGP-RTWLAHGIHFNAEEIRRLGEA--GTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASNMILEARQA 230
Cdd:pfam01979 180 LDIiKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLA 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 777183254 231 LYLQRLRYGAerITPELALGWATRGSARLLGRSD-IGELAPGKQADLALFKLDEL 284
Cdd:pfam01979 260 LELQFDPEGG--LSPLEALRMATINPAKALGLDDkVGSIEVGKDADLVVVDLDPL 312
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
1-339 |
4.94e-44 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 156.50 E-value: 4.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 1 MALAELLLSGCTTAADHHYlfpggleqAIDVQAGVVEELGMRAMLTRGSMSLGEKDgglPPQQTVQEAETILADSERLia 80
Cdd:PRK08393 103 LGLLEMIKSGTTTFVDMYF--------HMEEVAKATLEVGLRGYLSYGMVDLGDEE---KREKEIKETEKLMEFIEKL-- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 81 ryhqrgDGARVQIALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRTVDYLDSVGWLGPRTWL 160
Cdd:PRK08393 170 ------NSPRVHFVFGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIKQIREKYGKSPVVLLDEIGFLNEDVIA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 161 AHGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASNMILEARQALYLQRLRYGA 240
Cdd:PRK08393 244 AHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTDGAASNNNLDMLREMKLAALLHKVHNLD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 241 ERIT-PELALGWATRGSARLLGRsDIGELAPGKQADLALFKLDELRFSGSHDPLSALLLCA-ADRADRVMVGGAWRVVDG 318
Cdd:PRK08393 324 PTIAdAETVFRMATQNGAKALGL-KAGVIKEGYLADIAVIDFNRPHLRPINNPISHLVYSAnGNDVETTIVDGKIVMLDG 402
|
330 340
....*....|....*....|.
gi 777183254 319 AVEGLDLAALIARHREAASAL 339
Cdd:PRK08393 403 EVLTLDEEKILDKFLKVIEKL 423
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
3-312 |
5.62e-43 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 153.81 E-value: 5.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 3 LAELLLSGCTTA---ADHHylfpgglEQAIDVQAGVVEELGMRaMLTRGSMSlgekDGGLPPQQTvQEAETILADSERLI 79
Cdd:PRK09228 121 LDELLRNGTTTAlvfGTVH-------PQSVDALFEAAEARNMR-MIAGKVLM----DRNAPDGLR-DTAESGYDDSKALI 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 80 ARYHQRGdgaRVQIALAPCSPFSVTPEIMRASAEVAARH-DVRLHTHLAETLDEEDFCLQRFGLRTvDYLD---SVGWLG 155
Cdd:PRK09228 188 ERWHGKG---RLLYAITPRFAPTSTPEQLEAAGALAREHpDVWIQTHLSENLDEIAWVKELFPEAR-DYLDvyeRYGLLG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 156 PRTWLAHGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASnMILEARQALYLQR 235
Cdd:PRK09228 264 PRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVGLGTDVGGGTSFS-MLQTMNEAYKVQQ 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 236 LRygAERITPELALGWATRGSARLLGRSD-IGELAPGKQADLALFK-----LDELRFSGSHDP---LSALLLCAADRA-D 305
Cdd:PRK09228 343 LQ--GYRLSPFQAFYLATLGGARALGLDDrIGNLAPGKEADFVVLDpaatpLLALRTARAESLeelLFALMTLGDDRAvA 420
|
....*..
gi 777183254 306 RVMVGGA 312
Cdd:PRK09228 421 ETYVAGR 427
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
2-342 |
4.48e-42 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 152.50 E-value: 4.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 2 ALAELLLSGCTTA---ADHHYLFPGGLEQAIDVQAGVVEELGMRAMLT---RGSMSLGEKDGGLPPQQTVQEAETILADS 75
Cdd:PRK06151 112 AFAQLLRNGITTAmpiASLFYRQWAETYAEFAAAAEAAGRLGLRVYLGpayRSGGSVLEADGSLEVVFDEARGLAGLEEA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 76 ERLIARYHQRGDGaRVQIALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRTVDYLDSVGWLG 155
Cdd:PRK06151 192 IAFIKRVDGAHNG-LVRGMLAPDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLHGTTPLEWLADVGLLG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 156 PRTWLAHGIHF---------NAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDgSASNDasnMILE 226
Cdd:PRK06151 271 PRLLIPHATYIsgsprlnysGGDDLALLAEHGVSIVHCPLVSARHGSALNSFDRYREAGINLALGTD-TFPPD---MVMN 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 227 ARQALYLQRLRYGA-ERITPELALGWATRGSARLLGRSDIGELAPGKQADLALFKLDELRFSGSHDPLSALLLCAADRAD 305
Cdd:PRK06151 347 MRVGLILGRVVEGDlDAASAADLFDAATLGGARALGRDDLGRLAPGAKADIVVFDLDGLHMGPVFDPIRTLVTGGSGRDV 426
|
330 340 350
....*....|....*....|....*....|....*...
gi 777183254 306 R-VMVGGAWRVVDGAVEGLDLAALIARHREAASALIAG 342
Cdd:PRK06151 427 RaVFVDGRVVMEDGRLPGVDLAALRAQAQQQFDKLVAD 464
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
1-339 |
8.66e-36 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 134.41 E-value: 8.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 1 MALAELLLSGCTTAADhhyLF-PGGLEQaiDVQAGVVEELGMRAMLTRGSMSLGEKDGglpPQQTVQEAEtiladseRLI 79
Cdd:PRK15493 108 LGLLEMVKSGTTSFSD---MFnPIGVDQ--DAIMETVSRSGMRAAVSRTLFSFGTKED---EKKAIEEAE-------KYV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 80 ARYHQRGDgaRVQIALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRTVDYLDSVGWLGPRTW 159
Cdd:PRK15493 173 KRYYNESG--MLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCGLFKRPTV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 160 LAHGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASNMILEARQALYLQR-LRY 238
Cdd:PRK15493 251 IAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEEMRIATLLQKgIHQ 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 239 GAERITPELALGWATRGSARLLGRSDIGELAPGKQAD-LALFKLDELRFSGSHDPLSALLLCAA--DRADrVMVGGAWRV 315
Cdd:PRK15493 331 DATALPVETALTLATKGAAEVIGMKQTGSLEVGKCADfITIDPSNKPHLQPADEVLSHLVYAASgkDISD-VIINGKRVV 409
|
330 340
....*....|....*....|....
gi 777183254 316 VDGAVEGLDLAALIARHREAASAL 339
Cdd:PRK15493 410 WNGECKTLDEERIIFEASRYKRGL 433
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
2-311 |
4.49e-33 |
|
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: 238638 [Multi-domain] Cd Length: 418 Bit Score: 126.80 E-value: 4.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 2 ALAELLLSGCTTAADHHYLF--PGG--------LEQAIdVQAGvvEELGMRAMLTRgsmSLGEKDG-GLPPQQTVQE--- 67
Cdd:cd01313 96 LYIEMLLAGITAVGEFHYVHhdPDGtpyadpaeLAQRV-IAAA--SDAGIGITLLP---VLYARAGfGGPAPNPGQRrfi 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 68 --AETILADSERLIAryhQRGDGARVQIALAPCSPFSVTPEIMRASAEVAARhDVRLHTHLAETLDEEDFCLQRFGLRTV 145
Cdd:cd01313 170 ngYEDFLGLLEKALR---AVKEHAAARIGVAPHSLRAVPAEQLAALAALASE-KAPVHIHLAEQPKEVDDCLAAHGRRPV 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 146 DYLDSVGWLGPRTWLAHGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDgsaSNDASNMIL 225
Cdd:cd01313 246 ELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSD---SNARIDLLE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 226 EARQALYLQRLR-------YGAERITPELALGWATRGSARLLGRsDIGELAPGKQADLALFKLDELRFSGSHDP--LSAL 296
Cdd:cd01313 323 ELRQLEYSQRLRdrarnvlATAGGSSARALLDAALAGGAQALGL-ATGALEAGARADLLSLDLDHPSLAGALPDtlLDAW 401
|
330
....*....|....*.
gi 777183254 297 LLCAADRADR-VMVGG 311
Cdd:cd01313 402 VFAAGDREVRdVVVGG 417
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
94-283 |
1.44e-32 |
|
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: 124.87 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 94 ALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFC----------LQRF--------GLRTVDYLDSVGWLG 155
Cdd:cd01312 151 AISPHAPYSVHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLeeskgwfkhfWESFlklpkpkkLATAIDFLDMLGGLG 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 156 PRTWLAHGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASNMILEARQALYLQR 235
Cdd:cd01312 231 TRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDGLSSNISLSLLDELRALLDLHP 310
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 777183254 236 lRYGAERITPELALGwATRGSARLLGRsDIGELAPGKQADLALFKLDE 283
Cdd:cd01312 311 -EEDLLELASELLLM-ATLGGARALGL-NNGEIEAGKRADFAVFELPG 355
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
57-342 |
1.45e-32 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 126.12 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 57 GGLPPQQT----VQEAETILADSERLIARYHQRGDgarVQIALAPCSPFSVTPEIMRASAEVAARhDVRLHTHLAETLDE 132
Cdd:PRK09229 166 GGQPPNPGqrrfINDPDGFLRLLEALRRALAALPG---ARLGLAPHSLRAVTPDQLAAVLALAAP-DGPVHIHIAEQTKE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 133 EDFCLQRFGLRTVDYLDSVGWLGPRTWLAHGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGV 212
Cdd:PRK09229 242 VDDCLAWSGARPVEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPTTEANLGDGIFPAVDYLAAGGRFGIGS 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 213 DGSASNDASNmilEARQALYLQRLR--------YGAERITPELALGWATRGSARLLGRsDIGELAPGKQADLALFKLDEL 284
Cdd:PRK09229 322 DSHVSIDLVE---ELRLLEYGQRLRdrrrnvlaAAAQPSVGRRLFDAALAGGAQALGR-AIGGLAVGARADLVVLDLDHP 397
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 777183254 285 RFSG--SHDPLSALLLCAADRA-DRVMVGGAWRVVDGAveGLDLAALIARHREAASALIAG 342
Cdd:PRK09229 398 ALAGreGDALLDRWVFAGGDAAvRDVWVAGRWVVRDGR--HRLREAIAAAFRAALAALLAA 456
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
72-341 |
1.47e-32 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 125.89 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 72 LADSERLIARYHQRGDGArVQIALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLA-ETLDEEDfclqrfglRTVDYLDS 150
Cdd:PRK08204 168 REDIRRVKKRYFSSDDGL-LTLGLAIRGPEFSSWEVARADFRLARELGLPISMHQGfGPWGATP--------RGVEQLHD 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 151 VGWLGPRTWLAHGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDgSASNDASNMILEARQA 230
Cdd:PRK08204 239 AGLLGPDLNLVHGNDLSDDELKLLADSGGSFSVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVD-VVTSTGGDMFTQMRFA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 231 LYLQRLRYGAER------------ITPELALGWATRGSARLLGRSD-IGELAPGKQADLALFKLDELRFSGSHDPLSALL 297
Cdd:PRK08204 318 LQAERARDNAVHlreggmppprltLTARQVLEWATIEGARALGLEDrIGSLTPGKQADLVLIDATDLNLAPVHDPVGAVV 397
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 777183254 298 LCAADR-ADRVMVGGAWRVVDGAVEGLDLAALIARHREAASALIA 341
Cdd:PRK08204 398 QSAHPGnVDSVMVAGRAVKRNGKLLGVDLERLRRLAAASRDRLLS 442
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
9-339 |
4.09e-31 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 121.97 E-value: 4.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 9 SGCTTAADHHyLFPGGLEQAIDVQAGVVEELGMRAMLtrgSMSLGEKDGglppqqtVQEAETILADSERLIaRYHQRGDG 88
Cdd:PRK07203 120 NGVTTVFDHH-ASPNYIGGSLFTIADAAKKVGLRAML---CYETSDRDG-------EKELQEGVEENIRFI-KHIDEAKD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 89 ARVQIALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRTVDYLDSVGWLGPRTWLAHGIHFNA 168
Cdd:PRK07203 188 DMVEAMFGLHASFTLSDATLEKCREAVKETGRGYHIHVAEGIYDVSDSHKKYGKDIVERLADFGLLGEKTLAAHCIYLSD 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 169 EEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSasndASNMILEARQALYLQRLRYGaeritpELA 248
Cdd:PRK07203 268 EEIDLLKETDTFVVHNPESNMGNAVGYNPVLEMIKNGILLGLGTDGY----TSDMFESYKVANFKHKHAGG------DPN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 249 LGWATR------GSARLLGR---SDIGELAPGKQADLALFKLDelrfsgSHDPLSA------LLLCAADR-ADRVMVGGA 312
Cdd:PRK07203 338 VGWPESpamlfeNNNKIAERyfgAKFGILEEGAKADLIIVDYN------PPTPLNEdninghILFGMNGGsVDTTIVNGK 411
|
330 340
....*....|....*....|....*..
gi 777183254 313 WRVVDGAVEGLDLAALIARHREAASAL 339
Cdd:PRK07203 412 VVMEDRKFLNFDEESIYARARKAAAKL 438
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-278 |
2.24e-24 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 102.65 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 1 MALAELLLSGCTTAADHHYlfpggleqAIDVQAGVVEELGMRAMLTRGSmslgekdggLPPQQTVQEAETiLADSERLIa 80
Cdd:PRK06380 102 LGMYEMINSGITAFVDLYY--------SEDIIAKAAEELGIRAFLSWAV---------LDEEITTQKGDP-LNNAENFI- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 81 RYHQRGDgaRVQIALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRTVDYLDSVGWLGPRTWL 160
Cdd:PRK06380 163 REHRNEE--LVTPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETRKEVYDHVKRTGERPVEHLEKIGFLNSKLIA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 161 AHGIHFNAEEIRRLGEAGTGICHCPSSNMRLAS-GICPTVELEAAGAPIGLGVDGSASNDASNMILEAR-QALYLQRLRY 238
Cdd:PRK06380 241 AHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTgGSPPIPEMLDNGINVTIGTDSNGSNNSLDMFEAMKfSALSVKNERW 320
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 777183254 239 GAERITPELALGWATRGSARLLgRSDIGELAPGKQADLAL 278
Cdd:PRK06380 321 DASIIKAQEILDFATINAAKAL-ELNAGSIEVGKLADLVI 359
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
94-283 |
4.43e-19 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 87.33 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 94 ALAPCSPFSVTPEIMRASAEVAARHDVRLHTHLAET------LDE-----EDFcLQRFGL------RTVDYLDSvgWLGP 156
Cdd:PRK08418 178 AIAIHSPYSVHPILAKKALQLAKKENLLVSTHFLESkaerewLEEskgwfKKF-FEKFLKepkplyTPKEFLEL--FKGL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 157 RTWLAHGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASNMILEARQALYLqrl 236
Cdd:PRK08418 255 RTLFTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDGLSSNISLSLLDELRAALLT--- 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 777183254 237 rYGAERITpELA---LGWATRGSARLLGrSDIGELAPGKQADLALFKLDE 283
Cdd:PRK08418 332 -HANMPLL-ELAkilLLSATRYGAKALG-LNNGEIKEGKDADLSVFELPE 378
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
1-259 |
2.32e-14 |
|
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: 72.37 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 1 MALAELLLSGCTTAADHHYLFPGGLEQAIDVQAgvveelgmrAMLTRGSMSLGEKDGGLPPQQTVQEAETILADSERLIA 80
Cdd:cd01292 39 RALEALLAGGVTTVVDMGSTPPPTTTKAAIEAV---------AEAARASAGIRVVLGLGIPGVPAAVDEDAEALLLELLR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 81 RYHQRGDGArvqIALA-PCSPFSVTPEIMRASAEVAARHDVRLHTHLAETLDEEdfclqRFGLRTVDYLDsvgwLGPRTW 159
Cdd:cd01292 110 RGLELGAVG---LKLAgPYTATGLSDESLRRVLEEARKLGLPVVIHAGELPDPT-----RALEDLVALLR----LGGRVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 160 LAHGIHFNAEEIRRLGEAGTGICHCPSSNMRLAS---GICPTVELEAAGAPIGLGVDGSASNDASNMILEARQALYLQRL 236
Cdd:cd01292 178 IGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRdgeGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRL 257
|
250 260
....*....|....*....|...
gi 777183254 237 rygaeRITPELALGWATRGSARL 259
Cdd:cd01292 258 -----GLSLEEALRLATINPARA 275
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
2-319 |
1.87e-13 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 70.37 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 2 ALAELLLSGCTTAADHH-YLFpgGLEQAIDvqAGVVEELGMRAMLTRG---SMSLGEKDGGlpPQQTVQEAETILADSER 77
Cdd:COG1228 103 RLRRALAAGVTTVRDLPgGPL--GLRDAII--AGESKLLPGPRVLAAGpalSLTGGAHARG--PEEARAALRELLAEGAD 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 78 LIARYHQRGDGARvqialapcspfsvTPEIMRASAEVAARHDVRLHTHlAETLDEEDFCLqRFGLRTVDyldsvgwlgpr 157
Cdd:COG1228 177 YIKVFAEGGAPDF-------------SLEELRAILEAAHALGLPVAAH-AHQADDIRLAV-EAGVDSIE----------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 158 twlaHGIHFNAEEIRRLGEAGTgICHCPSSNMRLASGICPTVE------------------LEAAGAPIGLGVDGSASND 219
Cdd:COG1228 231 ----HGTYLDDEVADLLAEAGT-VVLVPTLSLFLALLEGAAAPvaakarkvreaalanarrLHDAGVPVALGTDAGVGVP 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 220 A-SNMILEARQAlylqrlryGAERITPELALGWATRGSARLLGRSD-IGELAPGKQADLALFkldelrfsgSHDPLSAll 297
Cdd:COG1228 306 PgRSLHRELALA--------VEAGLTPEEALRAATINAAKALGLDDdVGSLEPGKLADLVLL---------DGDPLED-- 366
|
330 340
....*....|....*....|..
gi 777183254 298 LCAADRADRVMVGGawRVVDGA 319
Cdd:COG1228 367 IAYLEDVRAVMKDG--RVVDRS 386
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
95-236 |
1.22e-08 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are 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. They 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. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 55.10 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 95 LAPCSPFSVTPEIMRasaEVAARHDVRLHTHLAETLDEedfclqrfglRTVDYLDSVGWLGPRTwLAHGIHFNAEEIRRL 174
Cdd:cd01305 117 LGLSSANDVDLEDIL---ELLRRRGKLFAIHASETRES----------VGMTDIERALDLEPDL-LVHGTHLTDEDLELV 182
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 777183254 175 GEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASnMILEARQALYLQRL 236
Cdd:cd01305 183 RENGVPVVLCPRSNLYFGVGIPPVAELLKLGIKVLLGTDNVMVNEPD-MWAEMEFLAKYSRL 243
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
162-286 |
1.79e-07 |
|
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: 52.26 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 162 HGIHFNAEEIRRLGEAGTGICHCPSSNMRLASGICPTVELEAAGAPIGLGVD-GSASNDASNMILEARQALYLQRLryga 240
Cdd:cd01296 235 HLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDfNPGSSPTSSMPLVMHLACRLMRM---- 310
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 777183254 241 eriTPELALGWATRGSARLLGRS-DIGELAPGKQADLALFKLDELRF 286
Cdd:cd01296 311 ---TPEEALTAATINAAAALGLGeTVGSLEVGKQADLVILDAPSYEH 354
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
103-288 |
7.54e-07 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 50.42 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 103 VTPEIMRASAEVAARHDVRLHTHLAETLDEEDFCLQRFGLRTVDYLDSVGwLGPrTWLAHGIHFNAEEIRRLGEAGTGIC 182
Cdd:PRK07213 176 YSDEELKFICKECKREKKIFSIHAAEHKGSVEYSLEKYGMTEIERLINLG-FKP-DFIVHATHPSNDDLELLKENNIPVV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 183 HCPSSNMRLASGICPTVELEAAGAPIGLGVDGSASNDASnmILeaRQALYLQRLRYgaerITPELALGWATRGSARLLGR 262
Cdd:PRK07213 254 VCPRANASFNVGLPPLNEMLEKGILLGIGTDNFMANSPS--IF--REMEFIYKLYH----IEPKEILKMATINGAKILGL 325
|
170 180
....*....|....*....|....*.
gi 777183254 263 SDIGELAPGKQADLALFKLDELRFSG 288
Cdd:PRK07213 326 INVGLIEEGFKADFTFIKPTNIKFSK 351
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
103-316 |
1.41e-06 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 49.80 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 103 VTPEIMRASAEVAARHDVRLHTH------LAETLDeedfCLQRfglrtvdYLDSVGWLGPRTWLAHGIHFNAEEIRRLGE 176
Cdd:COG1574 318 LDPEELRELVRAADAAGLQVAVHaigdaaVDEVLD----AYEA-------ARAANGRRDRRHRIEHAQLVDPDDLARFAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 177 AGTGIC----HCPS----SNMRL----ASGICPTVELEAAGAPIGLGVDGSASNDASNMILEA---RQALYLQRLrYGAE 241
Cdd:COG1574 387 LGVIASmqptHATSdgdwAEDRLgperAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAavtRRTPSGRGL-GPEE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 242 RITPELALGWATRGSARLLGRSD-IGELAPGKQADLALFkldelrfsgSHDPLSalllCAAD-----RADRVMVGGawRV 315
Cdd:COG1574 466 RLTVEEALRAYTIGAAYAAFEEDeKGSLEPGKLADFVVL---------DRDPLT----VPPEeikdiKVLLTVVGG--RV 530
|
.
gi 777183254 316 V 316
Cdd:COG1574 531 V 531
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
230-322 |
5.27e-05 |
|
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: 44.60 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 230 ALYLQRLRYGAERITPELALGWATRGSARLLGRSDIGELAPGKQADLALFKLDELRFSGSHDPLSAlllcAADRADRVMV 309
Cdd:cd01297 322 TRVLGHYVRERKLLSLEEAVRKMTGLPARVFGLADRGRIAPGYRADIVVFDPDTLADRATFTRPNQ----PAEGIEAVLV 397
|
90
....*....|...
gi 777183254 310 GGAWRVVDGAVEG 322
Cdd:cd01297 398 NGVPVVRDGAFTG 410
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
106-316 |
1.97e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 42.90 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 106 EIMRASAEVAArhDVRLHTHLAETLDEEDFCLQR-------FGLRTVDYLDSVGWLGPRTwlahgihfnAEEIRRLG--- 175
Cdd:pfam07969 254 ELVAAARERGL--DVAIHAIGDATIDTALDAFEAvaeklgnQGRVRIEHAQGVVPYTYSQ---------IERVAALGgaa 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 176 --EAGTGICHCPSSNMRL----ASGICPTVELEAAGAPIGLGVDGSAS--NDASNMI-LEARQALYLQRLRYGAERITPE 246
Cdd:pfam07969 323 gvQPVFDPLWGDWLQDRLgaerARGLTPVKELLNAGVKVALGSDAPVGpfDPWPRIGaAVMRQTAGGGEVLGPDEELSLE 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 777183254 247 LALGWATRGSARLLGRSD-IGELAPGKQADLALFKLDELRFSGSHDplsalllcAADRADRVMVGGawRVV 316
Cdd:pfam07969 403 EALALYTSGPAKALGLEDrKGTLGVGKDADLVVLDDDPLTVDPPAI--------ADIRVRLTVVDG--RVV 463
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
201-312 |
4.79e-04 |
|
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: 41.53 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 201 LEAAGAPIGLGVDGSASNdASNMILEARQALylqrlRYGAeriTPELALGWATRGSARLLGRSD-IGELAPGKQADLALF 279
Cdd:cd01309 267 LKKGGVAFAISSDHPVLN-IRNLNLEAAKAV-----KYGL---SYEEALKAITINPAKILGIEDrVGSLEPGKDADLVVW 337
|
90 100 110
....*....|....*....|....*....|...
gi 777183254 280 kldelrfsgSHDPLSALllcaaDRADRVMVGGA 312
Cdd:cd01309 338 ---------NGDPLEPT-----SKPEQVYIDGR 356
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
103-278 |
4.80e-04 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 41.91 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 103 VTPEIMRASAEVAARHDVRLHTH------LAETLDeedfclqrfGLRTVdyLDSVGWLGPRTWLAHGIHFNAEEIRRLGE 176
Cdd:cd01300 292 ISPEELEELVRAADEAGLQVAIHaigdraVDTVLD---------ALEAA--LKDNPRADHRHRIEHAQLVSPDDIPRFAK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 177 AGTG----ICHCPSS---------NMRLASGICPTVELEAAGAPIGLGVDGSASNDASNMILEA---RQALYLQRLRYGA 240
Cdd:cd01300 361 LGVIasvqPNHLYSDgdaaedrrlGEERAKRSYPFRSLLDAGVPVALGSDAPVAPPDPLLGIWAavtRKTPGGGVLGNPE 440
|
170 180 190
....*....|....*....|....*....|....*....
gi 777183254 241 ERITPELALGWATRGSARLLGRSD-IGELAPGKQADLAL 278
Cdd:cd01300 441 ERLSLEEALRAYTIGAAYAIGEEDeKGSLEPGKLADFVV 479
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
201-276 |
1.39e-03 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 39.97 E-value: 1.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 777183254 201 LEAAGAPIGLGVDGSASNdasnmILEARQALYLQ-RLRYGaerITPELALGWATRGSARLLGRSD-IGELAPGKQADL 276
Cdd:cd01299 259 AHKAGVKIAFGTDAGFPV-----PPHGWNARELElLVKAG---GTPAEALRAATANAAELLGLSDeLGVIEAGKLADL 328
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
245-285 |
1.52e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 40.08 E-value: 1.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 777183254 245 PELALGWATRGSARLLGRSDIGELAPGKQADLALFK-LDELR 285
Cdd:COG1001 286 PVTAIQMATLNAAEHFGLKDLGAIAPGRRADIVLLDdLEDFK 327
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
253-321 |
5.51e-03 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 38.55 E-value: 5.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 777183254 253 TR-GSARLLGRSDIGELAPGKQADLALFKLDELRFSGSHdplSALLLCAADRADRVMVGGAWRVVDGAVE 321
Cdd:cd01304 436 TRaGPAKLLGLSDKGHLGVGADADIAIYDDDPDQVDPSD---YEKVEKAFSRAAYVLKDGEIVVKDGEVV 502
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
252-286 |
8.91e-03 |
|
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: 37.69 E-value: 8.91e-03
10 20 30
....*....|....*....|....*....|....*
gi 777183254 252 ATRGSARLLGRSDIGELAPGKQADLALFKLDELRF 286
Cdd:cd01307 286 VTANPARMLGLAEIGTLAVGYDADLTVFDLKDGRV 320
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
243-280 |
9.63e-03 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 37.59 E-value: 9.63e-03
10 20 30
....*....|....*....|....*....|....*...
gi 777183254 243 ITPELALGWATRGSARLLGRSDIGELAPGKQADLALFK 280
Cdd:cd01295 235 IPPEDAIQMATINPAECYGLHDLGAIAPGRIADIVILD 272
|
|
| |
