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Conserved domains on  [gi|914658656|ref|WP_050649758|]
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alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase [Vibrio sp. J2-31]

Protein Classification

alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase( domain architecture ID 10794164)

alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase catalyzes the hydrolysis of alpha-D-ribose 1-methylphosphonate triphosphate (RPnTP) to form alpha-D-ribose 1-methylphosphonate phosphate (PRPn) and diphosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 1-377 0e+00

phosphonate metabolism protein PhnM; Provisional


:

Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 574.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656   1 MIITNVNLVLENEVVRGSVELRDGVIANMSDSTSQLPGAFDGENGFLMPGLIELHTDNLEKYFTPRPKVNWPPLSAMSAH 80
Cdd:PRK15446   4 MILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGAIDAEGDYLLPGLVDLHTDNLEKHLAPRPGVDWPADAALAAH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  81 DTQLIGSGITTVLDAVALGDYRD-GNRQENL-DQFINTVAESQKRGLTRAEHRIHLRCEVPHSTTVGLFERYVNMPEVQL 158
Cdd:PRK15446  84 DAQLAAAGITTVFDALSVGDEEDgGLRSRDLaRKLIDAIEEARARGLLRADHRLHLRCELTNPDALELFEALLAHPRVDL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 159 VSLMDHAPGQRQFVNIDKYRTYYQGKYNMTDAEMAVYEKDQVAQSQRWSKQNRDEITRQCRDLNIPTASHDDATSAHVTE 238
Cdd:PRK15446 164 VSLMDHTPGQRQFRDLEKYREYYAGKYGLSDEEFDAFVEERIALSARYAPPNRRAIAALARARGIPLASHDDDTPEHVAE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 239 SKELGMVIAEFPTTVEAAKRSHELGLKVMMGAPNVIRGGSHSGNVAAHELASLGVLDILSSDYYPVSLLDAVFTLVNDEr 318
Cdd:PRK15446 244 AHALGVAIAEFPTTLEAARAARALGMSVLMGAPNVVRGGSHSGNVSALDLAAAGLLDILSSDYYPASLLDAAFRLADDG- 322

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 914658656 319 nNLDVAQAVQLATLNPAQALGLTDRGVIEEGKRADLVLAHRLDDHQLVSRVWREGKKVF 377
Cdd:PRK15446 323 -GLDLPQAVALVTANPARAAGLDDRGEIAPGKRADLVRVRRAGGLPVVRAVWRGGRRVF 380
 
Name Accession Description Interval E-value
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 1-377 0e+00

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 574.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656   1 MIITNVNLVLENEVVRGSVELRDGVIANMSDSTSQLPGAFDGENGFLMPGLIELHTDNLEKYFTPRPKVNWPPLSAMSAH 80
Cdd:PRK15446   4 MILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGAIDAEGDYLLPGLVDLHTDNLEKHLAPRPGVDWPADAALAAH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  81 DTQLIGSGITTVLDAVALGDYRD-GNRQENL-DQFINTVAESQKRGLTRAEHRIHLRCEVPHSTTVGLFERYVNMPEVQL 158
Cdd:PRK15446  84 DAQLAAAGITTVFDALSVGDEEDgGLRSRDLaRKLIDAIEEARARGLLRADHRLHLRCELTNPDALELFEALLAHPRVDL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 159 VSLMDHAPGQRQFVNIDKYRTYYQGKYNMTDAEMAVYEKDQVAQSQRWSKQNRDEITRQCRDLNIPTASHDDATSAHVTE 238
Cdd:PRK15446 164 VSLMDHTPGQRQFRDLEKYREYYAGKYGLSDEEFDAFVEERIALSARYAPPNRRAIAALARARGIPLASHDDDTPEHVAE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 239 SKELGMVIAEFPTTVEAAKRSHELGLKVMMGAPNVIRGGSHSGNVAAHELASLGVLDILSSDYYPVSLLDAVFTLVNDEr 318
Cdd:PRK15446 244 AHALGVAIAEFPTTLEAARAARALGMSVLMGAPNVVRGGSHSGNVSALDLAAAGLLDILSSDYYPASLLDAAFRLADDG- 322

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 914658656 319 nNLDVAQAVQLATLNPAQALGLTDRGVIEEGKRADLVLAHRLDDHQLVSRVWREGKKVF 377
Cdd:PRK15446 323 -GLDLPQAVALVTANPARAAGLDDRGEIAPGKRADLVRVRRAGGLPVVRAVWRGGRRVF 380
PhnM COG3454
Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase PhnM [Inorganic ion transport ...
 1-377 0e+00

Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase PhnM [Inorganic ion transport and metabolism];


Pssm-ID: 442677  Cd Length: 383  Bit Score: 573.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656   1 MIITNVNLVLENEVVRGSVELRDGVIANMSDSTSQLPGAFDGENGFLMPGLIELHTDNLEKYFTPRPKVNWPPLSAMSAH 80
Cdd:COG3454    5 LVITNARIVLPDEVIDGSVVIEDGRIAAIDEGASAAPGAIDAEGDYLLPGLVDLHTDNLERHIEPRPGVRWPLDAALLAH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  81 DTQLIGSGITTVLDAVALGDYRDGNRQ-ENLDQFINTVAESQKRGLTRAEHRIHLRCEVPHSTTVGLFERYVNMPEVQLV 159
Cdd:COG3454   85 DAQLAAAGITTVFDALSVGDEPDGGRRlENARALADAIAALRAAGLLRADHRLHLRCEVTSPDALELLEELLDDPRVDLV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 160 SLMDHAPGQRQFVNIDKYRTYYQGKYNMTDAEMAVYEKDQVAQSQRWSKQNRDEITRQCRDLNIPTASHDDATSAHVTES 239
Cdd:COG3454  165 SLMDHTPGQRQFRDLEKYRAYYAGKYGLSDEEFDALVARRRALRARYAAANRAALVALARARGIPLASHDDDTAEHVAES 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 240 KELGMVIAEFPTTVEAAKRSHELGLKVMMGAPNVIRGGSHSGNVAAHELASLGVLDILSSDYYPVSLLDAVFTLVndERN 319
Cdd:COG3454  245 AALGVAIAEFPTTLEAARAARAAGLAVLMGAPNVVRGGSHSGNVSAAELAEAGLLDILSSDYVPASLLAAAFRLA--EDG 322

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 914658656 320 NLDVAQAVQLATLNPAQALGLTDRGVIEEGKRADLVLAHRLDDHQLVSRVWREGKKVF 377
Cdd:COG3454  323 GLDLPEAVALVTSNPARALGLDDRGEIAPGKRADLVRVRRLDGVPVVRAVWVAGRRVY 380
phosphono_phnM TIGR02318
phosphonate metabolism protein PhnM; This family consists of proteins from in the PhnM family. ...
 2-377 0e+00

phosphonate metabolism protein PhnM; This family consists of proteins from in the PhnM family. PhnM is a a protein associated with phosphonate utilization in a number of bacterial species. In Pseudomonas stutzeri WM88, a protein that is part of a system for the oxidation of phosphites (another form of reduced phosphorous compound) scores between trusted and noise cutoffs. [Energy metabolism, Other]


Pssm-ID: 131371  Cd Length: 376  Bit Score: 511.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656    2 IITNVNLVLENEVVRGSVELRDGVIANMSDSTSQLPGAFDGENGFLMPGLIELHTDNLEKYFTPRPKVNWPPLSAMSAHD 81
Cdd:TIGR02318   1 VLSNARLVLEDEVVEGSVVIEDGAIADIGEGPVALAEAIDGEGDLLLPGLIDLHTDNLERHMSPRPGVDWPIDAAIVEHD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656   82 TQLIGSGITTVLDAVALGDYRDG-NRQENLDQFINTVAESQKRGLTRAEHRIHLRCEVPHSTTVGLFERYVNMPEVQLVS 160
Cdd:TIGR02318  81 KQLAAAGITTVFDALALGDTESGgRRPDNLRRMIDAISEARDRGLLRADHRLHLRCELPNEEVLPELEELIDDPRVDLIS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  161 LMDHAPGQRQFVNIDKYRTYYQGKYNMTDAEMAVYEKDQVAQSQRWSKQNRDEITRQCRDLNIPTASHDDATSAHVTESK 240
Cdd:TIGR02318 161 LMDHTPGQRQFRDLEKYREYYRGKRGLSDDEFDEIVEERIARRAEYGLANRSEIAALARARGIPLASHDDDTPEHVAEAH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  241 ELGMVIAEFPTTVEAAKRSHELGLKVMMGAPNVIRGGSHSGNVAAHELASLGVLDILSSDYYPVSLLDAVFTLVnDERNN 320
Cdd:TIGR02318 241 DLGVTISEFPTTLEAAKEARSLGMQILMGAPNIVRGGSHSGNLSARELAHEGLLDVLASDYVPASLLLAAFQLA-DDVEG 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 914658656  321 LDVAQAVQLATLNPAQALGLTDRGVIEEGKRADLVLAHRLDDHQLVSRVWREGKKVF 377
Cdd:TIGR02318 320 IPLPQAVKMVTKNPARAVGLSDRGSIAPGKRADLVRVHRVDGVPRIRAVWRAGRRVY 376
PhnM cd01306
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ...
 48-373 3.49e-157

PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.


Pssm-ID: 238631  Cd Length: 325  Bit Score: 444.80  E-value: 3.49e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  48 MPGLIELHTDNLEKYFTPRPKVNWPPLSAMSAHDTQLIGSGITTVLDAVALGDYRDG-NRQENLDQFINTVAESQKRGLT 126
Cdd:cd01306    1 LPGLIDLHTDNLEKHVMPRPGVDWPMDIALAAHDRQLAAAGITTVFDALSFGDEEGGrRRLRNLRKLIDAIRELHARGVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 127 RAEHRIHLRCEVPHSTTVGLFERYVNMPEVQLVSLMDHAPGQRQFVNIDKYRTYYQGKYNMTDAEMAVYEKDQVAQSQRW 206
Cdd:cd01306   81 RADHRLHLRCELADPAVLPELESLMADPRVHLVSLMDHTPGQRQFRDLEKYREYYAKKYGLSDEEVEEAILERKARAAAY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 207 SKQNRDEITRQCRDLNIPTASHDDATSAHVTESKELGMVIAEFPTTVEAAKRSHELGLKVMMGAPNVIRGGSHSGNVAAH 286
Cdd:cd01306  161 APANRSELAALARARGIPLASHDDDTPEHVAEAHELGVVISEFPTTLEAAKAARELGLQTLMGAPNVVRGGSHSGNVSAR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 287 ELASLGVLDILSSDYYPVSLLDAVFTLVndERNNLDVAQAVQLATLNPAQALGLTDRGVIEEGKRADLVLAHRLDDHQLV 366
Cdd:cd01306  241 ELAAHGLLDILSSDYVPASLLHAAFRLA--DLGGWSLPEAVALVSANPARAVGLTDRGSIAPGKRADLILVDDMDGVPVV 318


                 ....*..
gi 914658656 367 SRVWREG 373
Cdd:cd01306  319 RTVWRGG 325
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 46-376 4.34e-15

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: 75.62  E-value: 4.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656   46 FLMPGLIELHTdnlekYFTPRPKVNwPPLSAMSAHD------TQLIGSGITTVLDAVALGDYrdgnrqenldqFINTVAE 119
Cdd:pfam01979   1 IVLPGLIDAHV-----HLEMGLLRG-IPVPPEFAYEalrlgiTTMLKSGTTTVLDMGATTST-----------GIEALLE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  120 SQKrgltraEHRIHLRCEVPHSTTVGLFERYVNMPEVQLVslmdhapgqrqfvnIDKYRTYYQGKYNMTDAEMAVYEKDQ 199
Cdd:pfam01979  64 AAE------ELPLGLRFLGPGCSLDTDGELEGRKALREKL--------------KAGAEFIKGMADGVVFVGLAPHGAPT 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  200 VAQSQRwskqnrDEITRQCRDLNIPTASHDDATSAHVTESKELGMVIAEFPTTVEAAKRSHELGLKVMMGAPNV------ 273
Cdd:pfam01979 124 FSDDEL------KAALEEAKKYGLPVAIHALETKGEVEDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVhlspte 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  274 ------------------IRGGSHSGNVAAHELASLGVLDILSSDY----YPVSLLDAV---FTLVNDERNNLDVAQAVQ 328
Cdd:pfam01979 198 anllaehlkgagvahcpfSNSKLRSGRIALRKALEDGVKVGLGTDGagsgNSLNMLEELrlaLELQFDPEGGLSPLEALR 277

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  329 LATLNPAQALGLTDR-GVIEEGKRADLVLahrLDDHQL-----------VSRVWREGKKV 376
Cdd:pfam01979 278 MATINPAKALGLDDKvGSIEVGKDADLVV---VDLDPLaaffglkpdgnVKKVIVKGKIV 334
 
Name Accession Description Interval E-value
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 1-377 0e+00

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 574.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656   1 MIITNVNLVLENEVVRGSVELRDGVIANMSDSTSQLPGAFDGENGFLMPGLIELHTDNLEKYFTPRPKVNWPPLSAMSAH 80
Cdd:PRK15446   4 MILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGAIDAEGDYLLPGLVDLHTDNLEKHLAPRPGVDWPADAALAAH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  81 DTQLIGSGITTVLDAVALGDYRD-GNRQENL-DQFINTVAESQKRGLTRAEHRIHLRCEVPHSTTVGLFERYVNMPEVQL 158
Cdd:PRK15446  84 DAQLAAAGITTVFDALSVGDEEDgGLRSRDLaRKLIDAIEEARARGLLRADHRLHLRCELTNPDALELFEALLAHPRVDL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 159 VSLMDHAPGQRQFVNIDKYRTYYQGKYNMTDAEMAVYEKDQVAQSQRWSKQNRDEITRQCRDLNIPTASHDDATSAHVTE 238
Cdd:PRK15446 164 VSLMDHTPGQRQFRDLEKYREYYAGKYGLSDEEFDAFVEERIALSARYAPPNRRAIAALARARGIPLASHDDDTPEHVAE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 239 SKELGMVIAEFPTTVEAAKRSHELGLKVMMGAPNVIRGGSHSGNVAAHELASLGVLDILSSDYYPVSLLDAVFTLVNDEr 318
Cdd:PRK15446 244 AHALGVAIAEFPTTLEAARAARALGMSVLMGAPNVVRGGSHSGNVSALDLAAAGLLDILSSDYYPASLLDAAFRLADDG- 322

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 914658656 319 nNLDVAQAVQLATLNPAQALGLTDRGVIEEGKRADLVLAHRLDDHQLVSRVWREGKKVF 377
Cdd:PRK15446 323 -GLDLPQAVALVTANPARAAGLDDRGEIAPGKRADLVRVRRAGGLPVVRAVWRGGRRVF 380
PhnM COG3454
Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase PhnM [Inorganic ion transport ...
 1-377 0e+00

Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase PhnM [Inorganic ion transport and metabolism];


Pssm-ID: 442677  Cd Length: 383  Bit Score: 573.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656   1 MIITNVNLVLENEVVRGSVELRDGVIANMSDSTSQLPGAFDGENGFLMPGLIELHTDNLEKYFTPRPKVNWPPLSAMSAH 80
Cdd:COG3454    5 LVITNARIVLPDEVIDGSVVIEDGRIAAIDEGASAAPGAIDAEGDYLLPGLVDLHTDNLERHIEPRPGVRWPLDAALLAH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  81 DTQLIGSGITTVLDAVALGDYRDGNRQ-ENLDQFINTVAESQKRGLTRAEHRIHLRCEVPHSTTVGLFERYVNMPEVQLV 159
Cdd:COG3454   85 DAQLAAAGITTVFDALSVGDEPDGGRRlENARALADAIAALRAAGLLRADHRLHLRCEVTSPDALELLEELLDDPRVDLV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 160 SLMDHAPGQRQFVNIDKYRTYYQGKYNMTDAEMAVYEKDQVAQSQRWSKQNRDEITRQCRDLNIPTASHDDATSAHVTES 239
Cdd:COG3454  165 SLMDHTPGQRQFRDLEKYRAYYAGKYGLSDEEFDALVARRRALRARYAAANRAALVALARARGIPLASHDDDTAEHVAES 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 240 KELGMVIAEFPTTVEAAKRSHELGLKVMMGAPNVIRGGSHSGNVAAHELASLGVLDILSSDYYPVSLLDAVFTLVndERN 319
Cdd:COG3454  245 AALGVAIAEFPTTLEAARAARAAGLAVLMGAPNVVRGGSHSGNVSAAELAEAGLLDILSSDYVPASLLAAAFRLA--EDG 322

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 914658656 320 NLDVAQAVQLATLNPAQALGLTDRGVIEEGKRADLVLAHRLDDHQLVSRVWREGKKVF 377
Cdd:COG3454  323 GLDLPEAVALVTSNPARALGLDDRGEIAPGKRADLVRVRRLDGVPVVRAVWVAGRRVY 380
phosphono_phnM TIGR02318
phosphonate metabolism protein PhnM; This family consists of proteins from in the PhnM family. ...
 2-377 0e+00

phosphonate metabolism protein PhnM; This family consists of proteins from in the PhnM family. PhnM is a a protein associated with phosphonate utilization in a number of bacterial species. In Pseudomonas stutzeri WM88, a protein that is part of a system for the oxidation of phosphites (another form of reduced phosphorous compound) scores between trusted and noise cutoffs. [Energy metabolism, Other]


Pssm-ID: 131371  Cd Length: 376  Bit Score: 511.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656    2 IITNVNLVLENEVVRGSVELRDGVIANMSDSTSQLPGAFDGENGFLMPGLIELHTDNLEKYFTPRPKVNWPPLSAMSAHD 81
Cdd:TIGR02318   1 VLSNARLVLEDEVVEGSVVIEDGAIADIGEGPVALAEAIDGEGDLLLPGLIDLHTDNLERHMSPRPGVDWPIDAAIVEHD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656   82 TQLIGSGITTVLDAVALGDYRDG-NRQENLDQFINTVAESQKRGLTRAEHRIHLRCEVPHSTTVGLFERYVNMPEVQLVS 160
Cdd:TIGR02318  81 KQLAAAGITTVFDALALGDTESGgRRPDNLRRMIDAISEARDRGLLRADHRLHLRCELPNEEVLPELEELIDDPRVDLIS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  161 LMDHAPGQRQFVNIDKYRTYYQGKYNMTDAEMAVYEKDQVAQSQRWSKQNRDEITRQCRDLNIPTASHDDATSAHVTESK 240
Cdd:TIGR02318 161 LMDHTPGQRQFRDLEKYREYYRGKRGLSDDEFDEIVEERIARRAEYGLANRSEIAALARARGIPLASHDDDTPEHVAEAH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  241 ELGMVIAEFPTTVEAAKRSHELGLKVMMGAPNVIRGGSHSGNVAAHELASLGVLDILSSDYYPVSLLDAVFTLVnDERNN 320
Cdd:TIGR02318 241 DLGVTISEFPTTLEAAKEARSLGMQILMGAPNIVRGGSHSGNLSARELAHEGLLDVLASDYVPASLLLAAFQLA-DDVEG 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 914658656  321 LDVAQAVQLATLNPAQALGLTDRGVIEEGKRADLVLAHRLDDHQLVSRVWREGKKVF 377
Cdd:TIGR02318 320 IPLPQAVKMVTKNPARAVGLSDRGSIAPGKRADLVRVHRVDGVPRIRAVWRAGRRVY 376
PhnM cd01306
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ...
 48-373 3.49e-157

PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.


Pssm-ID: 238631  Cd Length: 325  Bit Score: 444.80  E-value: 3.49e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  48 MPGLIELHTDNLEKYFTPRPKVNWPPLSAMSAHDTQLIGSGITTVLDAVALGDYRDG-NRQENLDQFINTVAESQKRGLT 126
Cdd:cd01306    1 LPGLIDLHTDNLEKHVMPRPGVDWPMDIALAAHDRQLAAAGITTVFDALSFGDEEGGrRRLRNLRKLIDAIRELHARGVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 127 RAEHRIHLRCEVPHSTTVGLFERYVNMPEVQLVSLMDHAPGQRQFVNIDKYRTYYQGKYNMTDAEMAVYEKDQVAQSQRW 206
Cdd:cd01306   81 RADHRLHLRCELADPAVLPELESLMADPRVHLVSLMDHTPGQRQFRDLEKYREYYAKKYGLSDEEVEEAILERKARAAAY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 207 SKQNRDEITRQCRDLNIPTASHDDATSAHVTESKELGMVIAEFPTTVEAAKRSHELGLKVMMGAPNVIRGGSHSGNVAAH 286
Cdd:cd01306  161 APANRSELAALARARGIPLASHDDDTPEHVAEAHELGVVISEFPTTLEAAKAARELGLQTLMGAPNVVRGGSHSGNVSAR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 287 ELASLGVLDILSSDYYPVSLLDAVFTLVndERNNLDVAQAVQLATLNPAQALGLTDRGVIEEGKRADLVLAHRLDDHQLV 366
Cdd:cd01306  241 ELAAHGLLDILSSDYVPASLLHAAFRLA--DLGGWSLPEAVALVSANPARAVGLTDRGSIAPGKRADLILVDDMDGVPVV 318


                 ....*..
gi 914658656 367 SRVWREG 373
Cdd:cd01306  319 RTVWRGG 325
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 1-377 1.28e-18

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 86.17  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656   1 MIITNVNL-------VLENevvrGSVELRDGVIANM--SDSTSQLPGA--FDGENGFLMPGLIELHT------DNLEKYF 63
Cdd:COG1228   10 LLITNATLvdgtgggVIEN----GTVLVEDGKIAAVgpAADLAVPAGAevIDATGKTVLPGLIDAHThlglggGRAVEFE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  64 TPRPKVNWPPLSAMSAHD-TQLIGSGITTVLDAVAlgdYRDGNRQEnldqfintVAESQKRGLTRAehRIhLRCEVPHST 142
Cdd:COG1228   86 AGGGITPTVDLVNPADKRlRRALAAGVTTVRDLPG---GPLGLRDA--------IIAGESKLLPGP--RV-LAAGPALSL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 143 TVGLFERYVnmPEV-QLVslmdhapgqRQFVN-----IDKYRTYyqGKYNMTDAEMAvyekdqvaqsqrwskqnrdEITR 216
Cdd:COG1228  152 TGGAHARGP--EEArAAL---------RELLAegadyIKVFAEG--GAPDFSLEELR-------------------AILE 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 217 QCRDLNIPTASH----DDATSA---------HVTES--------KELGMVIAeFPTTVEAAKRSHELGLKVMMGAPNVIR 275
Cdd:COG1228  200 AAHALGLPVAAHahqaDDIRLAveagvdsieHGTYLddevadllAEAGTVVL-VPTLSLFLALLEGAAAPVAAKARKVRE 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 276 GgsHSGNVAAheLASLGVLDILSSDYYPV-----SLLDAVFTLVndeRNNLDVAQAVQLATLNPAQALGLTDR-GVIEEG 349
Cdd:COG1228  279 A--ALANARR--LHDAGVPVALGTDAGVGvppgrSLHRELALAV---EAGLTPEEALRAATINAAKALGLDDDvGSLEPG 351

                        410       420       430
                 ....*....|....*....|....*....|...
gi 914658656 350 KRADLVL--AHRLDD---HQLVSRVWREGKKVF 377
Cdd:COG1228  352 KLADLVLldGDPLEDiayLEDVRAVMKDGRVVD 384
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 46-376 4.34e-15

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: 75.62  E-value: 4.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656   46 FLMPGLIELHTdnlekYFTPRPKVNwPPLSAMSAHD------TQLIGSGITTVLDAVALGDYrdgnrqenldqFINTVAE 119
Cdd:pfam01979   1 IVLPGLIDAHV-----HLEMGLLRG-IPVPPEFAYEalrlgiTTMLKSGTTTVLDMGATTST-----------GIEALLE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  120 SQKrgltraEHRIHLRCEVPHSTTVGLFERYVNMPEVQLVslmdhapgqrqfvnIDKYRTYYQGKYNMTDAEMAVYEKDQ 199
Cdd:pfam01979  64 AAE------ELPLGLRFLGPGCSLDTDGELEGRKALREKL--------------KAGAEFIKGMADGVVFVGLAPHGAPT 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  200 VAQSQRwskqnrDEITRQCRDLNIPTASHDDATSAHVTESKELGMVIAEFPTTVEAAKRSHELGLKVMMGAPNV------ 273
Cdd:pfam01979 124 FSDDEL------KAALEEAKKYGLPVAIHALETKGEVEDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVhlspte 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  274 ------------------IRGGSHSGNVAAHELASLGVLDILSSDY----YPVSLLDAV---FTLVNDERNNLDVAQAVQ 328
Cdd:pfam01979 198 anllaehlkgagvahcpfSNSKLRSGRIALRKALEDGVKVGLGTDGagsgNSLNMLEELrlaLELQFDPEGGLSPLEALR 277

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  329 LATLNPAQALGLTDR-GVIEEGKRADLVLahrLDDHQL-----------VSRVWREGKKV 376
Cdd:pfam01979 278 MATINPAKALGLDDKvGSIEVGKDADLVV---VDLDPLaaffglkpdgnVKKVIVKGKIV 334
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
305-374 1.79e-14

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 73.98  E-value: 1.79e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 914658656 305 SLLDAVFTLVndERNNLDVAQAVQLATLNPAQALGLTDR-GVIEEGKRADLVLahrLDDHQLVSRVWREGK 374
Cdd:COG1820  308 TMDDAVRNLV--EWTGLPLEEAVRMASLNPARALGLDDRkGSIAPGKDADLVV---LDDDLNVRATWVGGE 373
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
251-376 3.18e-13

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 70.90  E-value: 3.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 251 TTVEAAKRSHELGLKVMmgapnvIRGGShsgnvAAHELASL--GVLDILSS-------DYYPVSLL------DAVFTLVn 315
Cdd:COG1001  213 TTAEEALEKLRRGMYVM------IREGS-----AAKDLPALlpAVTELNSRrcalctdDRHPDDLLeeghidHVVRRAI- 280

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914658656 316 deRNNLDVAQAVQLATLNPAQALGLTDRGVIEEGKRADLVLahrLDDhqL----VSRVWREGKKV 376
Cdd:COG1001  281 --ELGLDPVTAIQMATLNAAEHFGLKDLGAIAPGRRADIVL---LDD--LedfkVEKVYADGKLV 338
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 305-373 1.19e-10

N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 62.21  E-value: 1.19e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 305 SLLDAVFTLVNdeRNNLDVAQAVQLATLNPAQALGLTDR-GVIEEGKRADLVLahrLDDHQLVSRVWREG 373
Cdd:cd00854  310 TMDQAVRNMVK--WGGCPLEEAVRMASLNPAKLLGLDDRkGSLKPGKDADLVV---LDDDLNVKATWING 374
Amidohydro_3 pfam07969
Amidohydrolase family;
228-377 1.40e-10

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 62.55  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  228 HDDATSAHVTeskelGMVIAEFPTTVEAAKRSHELGLKVMMGAPNVIRGGSHSGNVAAH------ELASLGVLDILSSDY 301
Cdd:pfam07969 293 QGRVRIEHAQ-----GVVPYTYSQIERVAALGGAAGVQPVFDPLWGDWLQDRLGAERARgltpvkELLNAGVKVALGSDA 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  302 yPVSLLD---AVFTLVNDERNN----------LDVAQAVQLATLNPAQALGLTDR-GVIEEGKRADLVLahrLDD----- 362
Cdd:pfam07969 368 -PVGPFDpwpRIGAAVMRQTAGggevlgpdeeLSLEEALALYTSGPAKALGLEDRkGTLGVGKDADLVV---LDDdpltv 443

                         170       180
                  ....*....|....*....|.
gi 914658656  363 ------HQLVSRVWREGKKVF 377
Cdd:pfam07969 444 dppaiaDIRVRLTVVDGRVVY 464
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 313-376 1.32e-08

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: 55.99  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 313 LVNDERNNLDVAQAVQLATLNPAQALGLTDR-GVIEEGKRADLVLaHRLDDHQL------------------VSRVWREG 373
Cdd:COG0402  332 LRGGDPTALSAREALEMATLGGARALGLDDEiGSLEPGKRADLVV-LDLDAPHLaplhdplsalvyaadgrdVRTVWVAG 410


                 ...
gi 914658656 374 KKV 376
Cdd:COG0402  411 RVV 413
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
 317-363 1.91e-08

N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 55.95  E-value: 1.91e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 914658656 317 ERNNLDVAQAVQLATLNPAQALGLTDRGVIEEGKRADLVL--AHRLDDH 363
Cdd:COG3653  436 ERGVLSLEEAVRKLTSLPADRLGLKDRGLLRPGYRADLVVfdPATLADR 484
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 235-377 2.04e-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: 55.40  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 235 HVTESKELGMVIAEFpttveaakrshelGLKVMMGAPNVIRGGSHSGNVAAHELASL----GVLDILSSDYYPVSLLDAV 310
Cdd:cd01309  223 HGAEGYKLADELAKH-------------GIPVIYGPTLTLPKKVEEVNDAIDTNAYLlkkgGVAFAISSDHPVLNIRNLN 289

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 311 FTLVNDERNNLDVAQAVQLATLNPAQALGLTDR-GVIEEGKRADLVL--AHRLDDHQLVSRVWREGKKVF 377
Cdd:cd01309  290 LEAAKAVKYGLSYEEALKAITINPAKILGIEDRvGSLEPGKDADLVVwnGDPLEPTSKPEQVYIDGRLVY 359
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
284-377 2.24e-08

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 55.58  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 284 AAHELASLGVLDILSSDYyPVSLLD---AVFTLVN-----------DERnnLDVAQAVQLATLNPAQALGLTDR-GVIEE 348
Cdd:COG1574  419 PFRSLLDAGAPLAFGSDA-PVEPLDpllGIYAAVTrrtpsgrglgpEER--LTVEEALRAYTIGAAYAAFEEDEkGSLEP 495

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 914658656 349 GKRADLVL---------AHRLDDHQlVSRVWREGKKVF 377
Cdd:COG1574  496 GKLADFVVldrdpltvpPEEIKDIK-VLLTVVGGRVVY 532
AdeC cd01295
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ...
 251-362 4.64e-08

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: 54.54  E-value: 4.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 251 TTVEAAKRSHELGLKVMmgapnvIRGGShsgnvAAHELASLgvLDILSSDYYPVslldavFTLVNDER------------ 318
Cdd:cd01295  164 MTGEEALEKLRLGMYVM------LREGS-----IAKNLEAL--LPAITEKNFRR------FMFCTDDVhpddllseghld 224

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 914658656 319 --------NNLDVAQAVQLATLNPAQALGLTDRGVIEEGKRADLVLahrLDD 362
Cdd:cd01295  225 yivrraieAGIPPEDAIQMATINPAECYGLHDLGAIAPGRIADIVI---LDD 273
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 292-356 6.62e-08

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439814 [Multi-domain]  Cd Length: 439  Bit Score: 53.94  E-value: 6.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 292 GVLDILSSDYYPVS--------------------LLDAVFT-LVNDERnnLDVAQAVQLATLNPAQALGLTDRGVIEEGK 350
Cdd:COG0044  297 GTIDVIATDHAPHTleekelpfaeapngipgletALPLLLTeLVHKGR--LSLERLVELLSTNPARIFGLPRKGRIAVGA 374


                 ....*.
gi 914658656 351 RADLVL 356
Cdd:COG0044  375 DADLVL 380
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 317-363 1.47e-07

D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.


Pssm-ID: 238622 [Multi-domain]  Cd Length: 415  Bit Score: 53.07  E-value: 1.47e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 914658656 317 ERNNLDVAQAVQLATLNPAQALGLTDRGVIEEGKRADLVL--AHRLDDH 363
Cdd:cd01297  331 ERKLLSLEEAVRKMTGLPARVFGLADRGRIAPGYRADIVVfdPDTLADR 379
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 1-356 1.77e-07

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: 52.59  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656   1 MIITNVNLVLEN---EVVRGSVELRDGVIANMSDSTSQLPGA----FDGENGFLMPGLIELHT-----------DNLEky 62
Cdd:cd01298    1 ILIRNGTIVTTDprrVLEDGDVLVEDGRIVAVGPALPLPAYPadevIDAKGKVVMPGLVNTHThlamtllrglaDDLP-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656  63 FTPRPKVNWPPL-SAMSAHDT---------QLIGSGITTVLDAVALgdyrdgnrqeNLDQFINTVAESQKRG-LTRA--- 128
Cdd:cd01298   79 LMEWLKDLIWPLeRLLTEEDVylgallalaEMIRSGTTTFADMYFF----------YPDAVAEAAEELGIRAvLGRGimd 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 129 ---EHRIHLRCEVPHstTVGLFERYVNMPE-VQLVSLMDHAPgqrqfvnidkyrtyyqgkYNMTDAEMAvyekdqvaqsq 204
Cdd:cd01298  149 lgtEDVEETEEALAE--AERLIREWHGAADgRIRVALAPHAP------------------YTCSDELLR----------- 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 205 rwskqnrdEITRQCRDLNIPTASHDDATSAHVTESKEL-GMviaefpTTVEAAkrsHELGLKvmmgAPNVIrgGSHSGNV 283
Cdd:cd01298  198 --------EVAELAREYGVPLHIHLAETEDEVEESLEKyGK------RPVEYL---EELGLL----GPDVV--LAHCVWL 254

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 284 AAHELASLGVLDI-----------LSSDYYPVS-LLDA------------------VFT----------LVNDERNNLDV 323
Cdd:cd01298  255 TDEEIELLAETGTgvahnpasnmkLASGIAPVPeMLEAgvnvglgtdgaasnnnldMFEemrlaallqkLAHGDPTALPA 334

                        410       420       430
                 ....*....|....*....|....*....|...
gi 914658656 324 AQAVQLATLNPAQALGLTDRGVIEEGKRADLVL 356
Cdd:cd01298  335 EEALEMATIGGAKALGLDEIGSLEVGKKADLIL 367
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 292-373 2.43e-06

Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 49.18  E-value: 2.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 292 GVLDILSSDY----YPVSLLDAVFTL-VNDERnnLDVAQAVQLATLNPAQALGL-TDRGVIEEGKRADLV---------L 356
Cdd:cd01296  278 GVPVALGTDFnpgsSPTSSMPLVMHLaCRLMR--MTPEEALTAATINAAAALGLgETVGSLEVGKQADLVildapsyehL 355

                         90
                 ....*....|....*..
gi 914658656 357 AHRLDDHqLVSRVWREG 373
Cdd:cd01296  356 AYRFGVN-LVEYVIKNG 371
PRK07583 PRK07583
cytosine deaminase;
286-374 3.87e-06

cytosine deaminase;


Pssm-ID: 236062  Cd Length: 438  Bit Score: 48.44  E-value: 3.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 286 HELASLGVLDILSSD-----YYPVSLLDAVFTLVNDER-NNLD--VAQAVQLATLNPAQALGLTDRGVIEEGKRADLVL- 356
Cdd:PRK07583 317 HELKAAGIPVAVASDncrdpFYAYGDHDMLEVFREAVRiLHLDhpYDDWPAAVTTTPADIMGLPDLGRIAVGAPADLVLf 396

                         90       100
                 ....*....|....*....|....*
gi 914658656 357 -AHRLDdhQLVSR------VWREGK 374
Cdd:PRK07583 397 kARSFS--ELLSRpqsdriVLRAGK 419
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 284-356 5.16e-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: 48.07  E-value: 5.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 284 AAHELASLGVLDILSSDYyPVSLLDAVFTL---VN------------DERnnLDVAQAVQLATLNPAQALGLTD-RGVIE 347
Cdd:cd01300  394 PFRSLLDAGVPVALGSDA-PVAPPDPLLGIwaaVTrktpgggvlgnpEER--LSLEEALRAYTIGAAYAIGEEDeKGSLE 470


                 ....*....
gi 914658656 348 EGKRADLVL 356
Cdd:cd01300  471 PGKLADFVV 479
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
321-374 6.43e-06

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 47.98  E-value: 6.43e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914658656 321 LDVAQAVQLATLNPAQALGLTDR-GVIEEGKRADLVlAHRLDD------------------HQLVSRVWREGK 374
Cdd:PRK09045 340 LPAHTALRMATLNGARALGLDDEiGSLEPGKQADLV-AVDLSGletqpvydpvsqlvyaagREQVSHVWVAGK 411
DHOase_IIb cd01318
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ...
 292-356 7.96e-06

Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.


Pssm-ID: 238643 [Multi-domain]  Cd Length: 361  Bit Score: 47.33  E-value: 7.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 292 GVLDILSSDYYPVSLLD--------------------AVFTLVNdeRNNLDVAQAVQLATLNPAQALGLTDRGVIEEGKR 351
Cdd:cd01318  240 GRIDVIASDHAPHTLEEkrkgypaapsgipgvetalpLMLTLVN--KGILSLSRVVRLTSHNPARIFGIKNKGRIAEGYD 317


                 ....*
gi 914658656 352 ADLVL 356
Cdd:cd01318  318 ADLTV 322
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 324-356 1.49e-05

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: 46.52  E-value: 1.49e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 914658656 324 AQAVQLATLNPAQALGLTDR-GVIEEGKRADLVL 356
Cdd:cd01299  297 AEALRAATANAAELLGLSDElGVIEAGKLADLLV 330
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
321-356 4.90e-05

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 44.99  E-value: 4.90e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 914658656 321 LDVAQAVQLATLNPAQALGLTDR-GVIEEGKRADLVL 356
Cdd:PRK07228 337 MPARTVFEMATLGGAKAAGFEDEiGSLEEGKKADLAI 373
PRK08418 PRK08418
metal-dependent hydrolase;
295-356 8.66e-05

metal-dependent hydrolase;


Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 44.19  E-value: 8.66e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914658656 295 DILSSDYyPVSLLD----AVFTLVNDERNNLDVaQAVQLATLNPAQALGLtDRGVIEEGKRADLVL 356
Cdd:PRK08418 311 DGLSSNI-SLSLLDelraALLTHANMPLLELAK-ILLLSATRYGAKALGL-NNGEIKEGKDADLSV 373
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 292-356 1.65e-04

Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.


Pssm-ID: 238642 [Multi-domain]  Cd Length: 374  Bit Score: 43.38  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 292 GVLDILSSDYYPVSL----------------LDAVFTLVND---ERNNLDVAQAVQLATLNPAQALGLtDRGVIEEGKRA 352
Cdd:cd01317  257 GTIDAIASDHAPHTDeekdlpfaeappgiigLETALPLLWTllvKGGLLTLPDLIRALSTNPAKILGL-PPGRLEVGAPA 335


                 ....
gi 914658656 353 DLVL 356
Cdd:cd01317  336 DLVL 339
PRK08417 PRK08417
metal-dependent hydrolase;
285-357 1.71e-04

metal-dependent hydrolase;


Pssm-ID: 236262 [Multi-domain]  Cd Length: 386  Bit Score: 43.15  E-value: 1.71e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914658656 285 AHELASLGVLDILssdYYpVSLLdavFT-LVndERNNLDVAQAVQLATLNPAQALGLtDRGVIEEGKRADLVLA 357
Cdd:PRK08417 287 AFDEAAFGIDSIC---EY-FSLC---YTyLV--KEGIITWSELSRFTSYNPAQFLGL-NSGEIEVGKEADLVLF 350
PRK02382 PRK02382
dihydroorotase; Provisional
 292-356 2.82e-04

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 42.72  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 292 GVLDILSSDYYP-------VSLLDA------VFT-----LVNDERNNLDVAQAVQLATLNPAQALGLTDRGVIEEGKRAD 353
Cdd:PRK02382 294 GTIDVVASDHAPhtreekdADIWDApsgvpgVETmlpllLAAVRKNRLPLERVRDVTAANPARIFGLDGKGRIAEGYDAD 373


                 ...
gi 914658656 354 LVL 356
Cdd:PRK02382 374 LVL 376
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 1-94 3.56e-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: 42.28  E-value: 3.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656   1 MIITNVNLVLENEVVRGSVELRDGVIANMSDSTSQLPGA--FDGENGFLMPGLIELHTdnlekyftprpKVNWPPLSAMS 78
Cdd:cd01315    2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEevIDAGGLVVMPGLIDTHV-----------HINEPGRTEWE 70

                         90
                 ....*....|....*....
gi 914658656  79 --AHDTQLIGS-GITTVLD 94
Cdd:cd01315   71 gfETGTKAAAAgGITTIID 89
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
276-356 3.66e-04

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 42.14  E-value: 3.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 276 GGSHSGNVAAHELAsLGVL-DILSSDYYPVSLLD-AVFTLVNDERN----NLDVAQAVQLATLNPAQALGLTDRGVIEEG 349
Cdd:PRK09237 246 TASFSFKVAEAAIA-AGILpDTISTDIYCRNRINgPVYSLATVMSKflalGMPLEEVIAAVTKNAADALRLPELGRLQVG 324


                 ....*..
gi 914658656 350 KRADLVL 356
Cdd:PRK09237 325 SDADLTL 331
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 305-374 6.50e-04

Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.


Pssm-ID: 238633 [Multi-domain]  Cd Length: 387  Bit Score: 41.61  E-value: 6.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 305 SLLDAVFTLVNDERNNLDVAqaVQLATLNPAQALGLTDRGVIEEGKRADLVLahrLDDHQLVSRVWREGK 374
Cdd:cd01308  308 TLLREVREAVKCGDIPLEVA--LRVITSNVARILKLRKKGEIQPGFDADLVI---LDKDLDINSVIAKGQ 372
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 280-356 7.50e-04

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: 41.49  E-value: 7.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 280 SGNVAAHELASLGVLDILSSDY---YPVSLLD----AVFTL-----VNDERNNLDVAQAVQLATLNPAQALGLTDR-GVI 346
Cdd:cd01303  298 SGLFDVRKLLDAGIKVGLGTDVgggTSFSMLDtlrqAYKVSrllgyELGGHAKLSPAEAFYLATLGGAEALGLDDKiGNF 377

                         90
                 ....*....|
gi 914658656 347 EEGKRADLVL 356
Cdd:cd01303  378 EVGKEFDAVV 387
PRK08204 PRK08204
hypothetical protein; Provisional
 317-361 1.22e-03

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 40.76  E-value: 1.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 914658656 317 ERNNLDVAQAVQLATLNPAQALGLTDR-GVIEEGKRADLVLAHRLD 361
Cdd:PRK08204 338 PRLTLTARQVLEWATIEGARALGLEDRiGSLTPGKQADLVLIDATD 383
Cyclic_amidohydrolases cd01302
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ...
 287-376 1.78e-03

Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.


Pssm-ID: 238627 [Multi-domain]  Cd Length: 337  Bit Score: 40.07  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 287 ELASLGVLDILSSDYYPVSL----------------------LDAVFTLVNdeRNNLDVAQAVQLATLNPAQALGLTDRG 344
Cdd:cd01302  213 EGVKNGKIDTIASDHAPHSKeekesgkdiwkappgfpgletrLPILLTEGV--KRGLSLETLVEILSENPARIFGLYPKG 290

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 914658656 345 VIEEGKRADLVL-----AHRLDDHQLVSRV-WR--EGKKV 376
Cdd:cd01302  291 TIAVGYDADLVIvdpkkEWKVTAEEIESKAdWTpfEGMEV 330
Met_dep_hydrolase_D cd01312
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 290-356 1.89e-03

Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238637 [Multi-domain]  Cd Length: 381  Bit Score: 40.13  E-value: 1.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 290 SLGVlDILSSDYyPVSLLDAV--FTLVNDERNNLDVA-QAVQLATLNPAQALGLtDRGVIEEGKRADLVL 356
Cdd:cd01312  284 SLGT-DGLSSNI-SLSLLDELraLLDLHPEEDLLELAsELLLMATLGGARALGL-NNGEIEAGKRADFAV 350
PRK09228 PRK09228
guanine deaminase; Provisional
 317-377 2.34e-03

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 39.79  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 317 ERNNLDVAQAVQLATLNPAQALGLTDR-GVIEEGKRADLV-------------------LAHRL-------DDHqLVSRV 369
Cdd:PRK09228 344 QGYRLSPFQAFYLATLGGARALGLDDRiGNLAPGKEADFVvldpaatpllalrtaraesLEELLfalmtlgDDR-AVAET 422


                 ....*...
gi 914658656 370 WREGKKVF 377
Cdd:PRK09228 423 YVAGRPVY 430
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
 276-356 2.56e-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: 39.62  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 276 GGSHSGNVAAHELAsLGVL-DILSSD-YYPVSLLDAVFTLVNDERNNLDV----AQAVQLATLNPAQALGLTDRGVIEEG 349
Cdd:cd01307  227 TASFSFRVARAAIA-AGLLpDTISSDiHGRNRTNGPVYALATTLSKLLALgmplEEVIEAVTANPARMLGLAEIGTLAVG 305


                 ....*..
gi 914658656 350 KRADLVL 356
Cdd:cd01307  306 YDADLTV 312
PRK09236 PRK09236
dihydroorotase; Reviewed
 292-368 2.99e-03

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 39.47  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 292 GVLDILSSDYYPVSL--------------------LDAVFTLVNDERnnLDVAQAVQLATLNPAQALGLTDRGVIEEGKR 351
Cdd:PRK09236 301 DRIDVIATDHAPHTWeekqgpyfqapsglplvqhaLPALLELVHEGK--LSLEKVVEKTSHAPAILFDIKERGFIREGYW 378

                         90
                 ....*....|....*..
gi 914658656 352 ADLVLAhRLDDHQLVSR 368
Cdd:PRK09236 379 ADLVLV-DLNSPWTVTK 394
PRK09229 PRK09229
N-formimino-L-glutamate deiminase; Validated
 313-376 3.27e-03

N-formimino-L-glutamate deiminase; Validated


Pssm-ID: 236420 [Multi-domain]  Cd Length: 456  Bit Score: 39.45  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 313 LVNDERNNLDVAQAVQL-------ATLNPAQALGLtDRGVIEEGKRADLV--------LAHRLDDHQL-----------V 366
Cdd:PRK09229 342 LRDRRRNVLAAAAQPSVgrrlfdaALAGGAQALGR-AIGGLAVGARADLVvldldhpaLAGREGDALLdrwvfaggdaaV 420

                         90
                 ....*....|
gi 914658656 367 SRVWREGKKV 376
Cdd:PRK09229 421 RDVWVAGRWV 430
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 325-362 3.90e-03

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 39.06  E-value: 3.90e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 914658656 325 QAVQLATLNPAQALGLTDRGVIEEGKRADLVLaHRLDD 362
Cdd:PRK08203 355 EALEWATLGGARVLGRDDIGSLAPGKLADLAL-FDLDE 391
pyrC PRK09357
dihydroorotase; Validated
 312-356 4.19e-03

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 39.02  E-value: 4.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 914658656 312 TLVndERNNLDVAQAVQLATLNPAQALGLTDrGVIEEGKRADLVL 356
Cdd:PRK09357 337 TLV--KTGLLDLEQLLEKMTINPARILGLPA-GPLAEGEPADLVI 378
PRK06189 PRK06189
allantoinase; Provisional
 292-356 5.05e-03

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 38.91  E-value: 5.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 292 GVLDILSSDYYPV---------------------SLLDAVFTLVNDERNnLDVAQAVQLATLNPAQALGLTDRGVIEEGK 350
Cdd:PRK06189 304 GEIDMISSDHSPCppelkegddfflvwggisggqSTLLVMLTEGYIERG-IPLETIARLLATNPAKRFGLPQKGRLEVGA 382


                 ....*.
gi 914658656 351 RADLVL 356
Cdd:PRK06189 383 DADFVL 388
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 218-337 5.39e-03

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: 38.08  E-value: 5.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658656 218 CRDLNIPTASHDDATSAHVTESKEL-------GMVIAE--FPTTVEAAKRSHELGLKVMMG-APNVIRGGSHSGNVAAHE 287
Cdd:cd01292  142 ARKLGLPVVIHAGELPDPTRALEDLvallrlgGRVVIGhvSHLDPELLELLKEAGVSLEVCpLSNYLLGRDGEGAEALRR 221

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 914658656 288 LASLGVLDILSSDYYPVS----LLDAVFTLVNDERNNLDVAQAVQLATLNPAQA 337
Cdd:cd01292  222 LLELGIRVTLGTDGPPHPlgtdLLALLRLLLKVLRLGLSLEEALRLATINPARA 275
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 321-356 6.01e-03

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 38.58  E-value: 6.01e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 914658656 321 LDVAQAVQLATLNPAQALGlTDRGVIEEGKRADLVL 356
Cdd:PRK06038 328 LPARQVLEMATVNGAKALG-INTGMLKEGYLADIII 362
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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