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Conserved domains on  [gi|390192580|gb|AFL67635|]
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cytosine deaminase-like metal-dependent hydrolase [Sulfurospirillum barnesii SES-3]

Protein Classification

metal-dependent hydrolase( domain architecture ID 10793094)

metal-dependent hydrolase similar to Nitratiruptor sp. aminodeoxyfutalosine deaminase that catalyzes the deamination of aminodeoxyfutalosine (AFL) into futalosine (FL), a step in the biosynthesis of menaquinone (MK, vitamin K2)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08418 PRK08418
metal-dependent hydrolase;
1-406 0e+00

metal-dependent hydrolase;


:

Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 645.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   1 MTLITADFILTCNEHFEIIEEGAVLFDAQILEVGKASILKEKHPTVTcIETPKNSVLLPGLINSHVHLEFSANQSMLHYG 80
Cdd:PRK08418   1 MKIIGASYIFTCDENFEILEDGAVVFDDKILEIGDYENLKKKYPNAK-IQFFKNSVLLPAFINPHTHLEFSANKTTLDYG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  81 DFIPWLQSVIAHRDELSALATTELITCKLTEMLKSGTTSLGAISSFGADLEACVNAPQRVVYFNEVLGSVPSAVDVMYND 160
Cdd:PRK08418  80 DFIPWLGSVINHREDLLEKCKGALIQQAINEMLKSGVGTIGAISSFGIDLEICAKSPLRVVFFNEILGSNASAVDELYQD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 161 FRGRLEASKEFTCKHFIPAISVHSPYSTHPILAKKALKLAEDEDCVVSTHFMESQAERAWIDEGSGDFQTFFTAFNPHAK 240
Cdd:PRK08418 160 FLARFEESKKFKSKKFIPAIAIHSPYSVHPILAKKALQLAKKENLLVSTHFLESKAEREWLEESKGWFKKFFEKFLKEPK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 241 PMCTSLEYLALFENNATLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEKIKLTLGTDGLSSNISL 320
Cdd:PRK08418 240 PLYTPKEFLELFKGLRTLFTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDGLSSNISL 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 321 SLWDEMRSALMMHTNMELNALARTLLQSVTCNAAHALKLPCGALKEGLASDMIVVTLPQSC-ELSTLPLHLILHTHTTHL 399
Cdd:PRK08418 320 SLLDELRAALLTHANMPLLELAKILLLSATRYGAKALGLNNGEIKEGKDADLSVFELPEECtKKEQLPLQFILHAKEVKK 399


                 ....*..
gi 390192580 400 TFIDGKQ 406
Cdd:PRK08418 400 LFIGGKE 406
 
Name Accession Description Interval E-value
PRK08418 PRK08418
metal-dependent hydrolase;
1-406 0e+00

metal-dependent hydrolase;


Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 645.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   1 MTLITADFILTCNEHFEIIEEGAVLFDAQILEVGKASILKEKHPTVTcIETPKNSVLLPGLINSHVHLEFSANQSMLHYG 80
Cdd:PRK08418   1 MKIIGASYIFTCDENFEILEDGAVVFDDKILEIGDYENLKKKYPNAK-IQFFKNSVLLPAFINPHTHLEFSANKTTLDYG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  81 DFIPWLQSVIAHRDELSALATTELITCKLTEMLKSGTTSLGAISSFGADLEACVNAPQRVVYFNEVLGSVPSAVDVMYND 160
Cdd:PRK08418  80 DFIPWLGSVINHREDLLEKCKGALIQQAINEMLKSGVGTIGAISSFGIDLEICAKSPLRVVFFNEILGSNASAVDELYQD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 161 FRGRLEASKEFTCKHFIPAISVHSPYSTHPILAKKALKLAEDEDCVVSTHFMESQAERAWIDEGSGDFQTFFTAFNPHAK 240
Cdd:PRK08418 160 FLARFEESKKFKSKKFIPAIAIHSPYSVHPILAKKALQLAKKENLLVSTHFLESKAEREWLEESKGWFKKFFEKFLKEPK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 241 PMCTSLEYLALFENNATLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEKIKLTLGTDGLSSNISL 320
Cdd:PRK08418 240 PLYTPKEFLELFKGLRTLFTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDGLSSNISL 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 321 SLWDEMRSALMMHTNMELNALARTLLQSVTCNAAHALKLPCGALKEGLASDMIVVTLPQSC-ELSTLPLHLILHTHTTHL 399
Cdd:PRK08418 320 SLLDELRAALLTHANMPLLELAKILLLSATRYGAKALGLNNGEIKEGKDADLSVFELPEECtKKEQLPLQFILHAKEVKK 399


                 ....*..
gi 390192580 400 TFIDGKQ 406
Cdd:PRK08418 400 LFIGGKE 406
Met_dep_hydrolase_D cd01312
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 29-405 5.66e-135

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: 391.81  E-value: 5.66e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  29 QILEVGKASILKEKHPTvTCIETPKNSVLLPGLINSHVHLEFSANQSMLHYGDFIPWLQSVIAHRDELSALATTELITCK 108
Cdd:cd01312    2 KILEVGDYEKLEKRYPG-AKHEFFPNGVLLPGLINAHTHLEFSANVAQFTYGRFRAWLLSVINSRDELLKQPWEEAIRQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 109 LTEMLKSGTTSLGAISSFGADLEACVNAPQRVVYFNEVLGSVPSAVDVMYNDFRGRLEASKEFTCKHFIPAISVHSPYST 188
Cdd:cd01312   81 IRQMLESGTTSIGAISSDGSLLPALASSGLRGVFFNEVIGSNPSAIDFKGETFLERFKRSKSFESQLFIPAISPHAPYSV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 189 HPILAKKALKLAEDEDCVVSTHFMESQAERAWIDEGSGDFQTFFTAFNPHAKPMC--TSLEYLALFE--NNATLFTHGVQ 264
Cdd:cd01312  161 HPELAQDLIDLAKKLNLPLSTHFLESKEEREWLEESKGWFKHFWESFLKLPKPKKlaTAIDFLDMLGglGTRVSFVHCVY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 265 ASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEKIKLTLGTDGLSSNISLSLWDEMRSALMMHTNMELNALART 344
Cdd:cd01312  241 ANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDGLSSNISLSLLDELRALLDLHPEEDLLELASE 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 390192580 345 LLQSVTCNAAHALKLPCGALKEGLASDMIVVTLPQSCELSTLPLHLILHTHTTHLTFIDGK 405
Cdd:cd01312  321 LLLMATLGGARALGLNNGEIEAGKRADFAVFELPGPGIKEQAPLQFILHAKEVRHLFISGK 381
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 2-406 9.67e-83

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: 259.37  E-value: 9.67e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   2 TLITADFILTCNEHFEIIEEGAVLFDA-QILEVGKASILKEKHPTVTCIETPkNSVLLPGLINSHVHLEFSANQSMLHYG 80
Cdd:COG0402    2 LLIRGAWVLTMDPAGGVLEDGAVLVEDgRIAAVGPGAELPARYPAAEVIDAG-GKLVLPGLVNTHTHLPQTLLRGLADDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  81 DFIPWLQSVI----AHRDELSALATTELitcKLTEMLKSGTTSLGAISSFG-----ADLEACVNAPQRVVYFNEVLG-SV 150
Cdd:COG0402   81 PLLDWLEEYIwpleARLDPEDVYAGALL---ALAEMLRSGTTTVADFYYVHpesadALAEAAAEAGIRAVLGRGLMDrGF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 151 PSA----VDVMYNDFRGRLEASKEFTCKHFIPAISVHSPYSTHPILAKKALKLAEDEDCVVSTHFMESQAERAWIDEGSG 226
Cdd:COG0402  158 PDGlredADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLELYG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 227 dfqtfftafnphakpmCTSLEYLALFE--NNATLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEK 304
Cdd:COG0402  238 ----------------KRPVEYLDELGllGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAG 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 305 IKLTLGTDGLSSNISLSLWDEMRSALMMH--TNMELNAL-ARTLLQSVTCNAAHALKLP--CGALKEGLASDMIVVTLPQ 379
Cdd:COG0402  302 VRVGLGTDGAASNNSLDMFEEMRLAALLQrlRGGDPTALsAREALEMATLGGARALGLDdeIGSLEPGKRADLVVLDLDA 381

                        410       420       430
                 ....*....|....*....|....*....|....
gi 390192580 380 sceLSTLPLHLIL-------HTHTTHLTFIDGKQ 406
Cdd:COG0402  382 ---PHLAPLHDPLsalvyaaDGRDVRTVWVAGRV 412
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 56-405 3.29e-34

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: 129.93  E-value: 3.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   56 VLLPGLINSHVHLEFSANQSMLHYGDFIPWlqsviahrdelsALATTelitckLTEMLKSGTTSLGAISSFGAD-----L 130
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYE------------ALRLG------ITTMLKSGTTTVLDMGATTSTgiealL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  131 EACVNAP--QRVVYFNEVLGSVPSAVDVM--YNDFRGRLEASKEFTCKHFIPAISVHSPYSTHPILAKKALKLAEDEDCV 206
Cdd:pfam01979  63 EAAEELPlgLRFLGPGCSLDTDGELEGRKalREKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  207 VSTHFMESQAERAWIDEGSGDFQTFftafnphakpmCTSLEYL---ALFENNATLFTHGVQASKEELETISKQ--NATLT 281
Cdd:pfam01979 143 VAIHALETKGEVEDAIAAFGGGIEH-----------GTHLEVAesgGLLDIIKLILAHGVHLSPTEANLLAEHlkGAGVA 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  282 HCPVSNRLLGVGKLDVERVENEKIKLTLGTDGLSSNISLSLWDEMRSALMMHTNMELNALARTLLQSVTCNAAHALKLPC 361
Cdd:pfam01979 212 HCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFDPEGGLSPLEALRMATINPAKALGLDD 291

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 390192580  362 --GALKEGLASDMIVVTLPQSCELSTLplhliLHTHTTHLTFIDGK 405
Cdd:pfam01979 292 kvGSIEVGKDADLVVVDLDPLAAFFGL-----KPDGNVKKVIVKGK 332
 
Name Accession Description Interval E-value
PRK08418 PRK08418
metal-dependent hydrolase;
1-406 0e+00

metal-dependent hydrolase;


Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 645.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   1 MTLITADFILTCNEHFEIIEEGAVLFDAQILEVGKASILKEKHPTVTcIETPKNSVLLPGLINSHVHLEFSANQSMLHYG 80
Cdd:PRK08418   1 MKIIGASYIFTCDENFEILEDGAVVFDDKILEIGDYENLKKKYPNAK-IQFFKNSVLLPAFINPHTHLEFSANKTTLDYG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  81 DFIPWLQSVIAHRDELSALATTELITCKLTEMLKSGTTSLGAISSFGADLEACVNAPQRVVYFNEVLGSVPSAVDVMYND 160
Cdd:PRK08418  80 DFIPWLGSVINHREDLLEKCKGALIQQAINEMLKSGVGTIGAISSFGIDLEICAKSPLRVVFFNEILGSNASAVDELYQD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 161 FRGRLEASKEFTCKHFIPAISVHSPYSTHPILAKKALKLAEDEDCVVSTHFMESQAERAWIDEGSGDFQTFFTAFNPHAK 240
Cdd:PRK08418 160 FLARFEESKKFKSKKFIPAIAIHSPYSVHPILAKKALQLAKKENLLVSTHFLESKAEREWLEESKGWFKKFFEKFLKEPK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 241 PMCTSLEYLALFENNATLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEKIKLTLGTDGLSSNISL 320
Cdd:PRK08418 240 PLYTPKEFLELFKGLRTLFTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDGLSSNISL 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 321 SLWDEMRSALMMHTNMELNALARTLLQSVTCNAAHALKLPCGALKEGLASDMIVVTLPQSC-ELSTLPLHLILHTHTTHL 399
Cdd:PRK08418 320 SLLDELRAALLTHANMPLLELAKILLLSATRYGAKALGLNNGEIKEGKDADLSVFELPEECtKKEQLPLQFILHAKEVKK 399


                 ....*..
gi 390192580 400 TFIDGKQ 406
Cdd:PRK08418 400 LFIGGKE 406
Met_dep_hydrolase_D cd01312
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 29-405 5.66e-135

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: 391.81  E-value: 5.66e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  29 QILEVGKASILKEKHPTvTCIETPKNSVLLPGLINSHVHLEFSANQSMLHYGDFIPWLQSVIAHRDELSALATTELITCK 108
Cdd:cd01312    2 KILEVGDYEKLEKRYPG-AKHEFFPNGVLLPGLINAHTHLEFSANVAQFTYGRFRAWLLSVINSRDELLKQPWEEAIRQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 109 LTEMLKSGTTSLGAISSFGADLEACVNAPQRVVYFNEVLGSVPSAVDVMYNDFRGRLEASKEFTCKHFIPAISVHSPYST 188
Cdd:cd01312   81 IRQMLESGTTSIGAISSDGSLLPALASSGLRGVFFNEVIGSNPSAIDFKGETFLERFKRSKSFESQLFIPAISPHAPYSV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 189 HPILAKKALKLAEDEDCVVSTHFMESQAERAWIDEGSGDFQTFFTAFNPHAKPMC--TSLEYLALFE--NNATLFTHGVQ 264
Cdd:cd01312  161 HPELAQDLIDLAKKLNLPLSTHFLESKEEREWLEESKGWFKHFWESFLKLPKPKKlaTAIDFLDMLGglGTRVSFVHCVY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 265 ASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEKIKLTLGTDGLSSNISLSLWDEMRSALMMHTNMELNALART 344
Cdd:cd01312  241 ANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDGLSSNISLSLLDELRALLDLHPEEDLLELASE 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 390192580 345 LLQSVTCNAAHALKLPCGALKEGLASDMIVVTLPQSCELSTLPLHLILHTHTTHLTFIDGK 405
Cdd:cd01312  321 LLLMATLGGARALGLNNGEIEAGKRADFAVFELPGPGIKEQAPLQFILHAKEVRHLFISGK 381
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 2-406 9.67e-83

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: 259.37  E-value: 9.67e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   2 TLITADFILTCNEHFEIIEEGAVLFDA-QILEVGKASILKEKHPTVTCIETPkNSVLLPGLINSHVHLEFSANQSMLHYG 80
Cdd:COG0402    2 LLIRGAWVLTMDPAGGVLEDGAVLVEDgRIAAVGPGAELPARYPAAEVIDAG-GKLVLPGLVNTHTHLPQTLLRGLADDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  81 DFIPWLQSVI----AHRDELSALATTELitcKLTEMLKSGTTSLGAISSFG-----ADLEACVNAPQRVVYFNEVLG-SV 150
Cdd:COG0402   81 PLLDWLEEYIwpleARLDPEDVYAGALL---ALAEMLRSGTTTVADFYYVHpesadALAEAAAEAGIRAVLGRGLMDrGF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 151 PSA----VDVMYNDFRGRLEASKEFTCKHFIPAISVHSPYSTHPILAKKALKLAEDEDCVVSTHFMESQAERAWIDEGSG 226
Cdd:COG0402  158 PDGlredADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLELYG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 227 dfqtfftafnphakpmCTSLEYLALFE--NNATLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEK 304
Cdd:COG0402  238 ----------------KRPVEYLDELGllGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAG 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 305 IKLTLGTDGLSSNISLSLWDEMRSALMMH--TNMELNAL-ARTLLQSVTCNAAHALKLP--CGALKEGLASDMIVVTLPQ 379
Cdd:COG0402  302 VRVGLGTDGAASNNSLDMFEEMRLAALLQrlRGGDPTALsAREALEMATLGGARALGLDdeIGSLEPGKRADLVVLDLDA 381

                        410       420       430
                 ....*....|....*....|....*....|....
gi 390192580 380 sceLSTLPLHLIL-------HTHTTHLTFIDGKQ 406
Cdd:COG0402  382 ---PHLAPLHDPLsalvyaaDGRDVRTVWVAGRV 412
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 2-406 4.41e-45

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: 160.83  E-value: 4.41e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   2 TLITADFILTCNEhFEIIEEGAVLF-DAQILEVGKAsILKEKHPTVTCIETpKNSVLLPGLINSHVHLefsaNQSMLH-Y 79
Cdd:cd01298    1 ILIRNGTIVTTDP-RRVLEDGDVLVeDGRIVAVGPA-LPLPAYPADEVIDA-KGKVVMPGLVNTHTHL----AMTLLRgL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  80 GD---FIPWLQSVI-----AHRDELSALATteLITCklTEMLKSGTTS-LGAISSFGADL-EACVNAPQRVVYFNEVLGS 149
Cdd:cd01298   74 ADdlpLMEWLKDLIwplerLLTEEDVYLGA--LLAL--AEMIRSGTTTfADMYFFYPDAVaEAAEELGIRAVLGRGIMDL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 150 VPSAVDVMyndfRGRLEASKEF--TCKHFI-----PAISVHSPYSTHPILAKKALKLAEDEDCVVSTHFMESQAERAWID 222
Cdd:cd01298  150 GTEDVEET----EEALAEAERLirEWHGAAdgrirVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESL 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 223 EGSGdfqtfftafnphakpmCTSLEYLA---LFENNaTLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVER 299
Cdd:cd01298  226 EKYG----------------KRPVEYLEelgLLGPD-VVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPE 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 300 VENEKIKLTLGTDGLSSNISLSLWDEMRSALMMH--TNMELNAL-ARTLLQSVTCNAAHALKLPC-GALKEGLASDMIVV 375
Cdd:cd01298  289 MLEAGVNVGLGTDGAASNNNLDMFEEMRLAALLQklAHGDPTALpAEEALEMATIGGAKALGLDEiGSLEVGKKADLILI 368

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 390192580 376 TL--PQSCELSTLPLHLILHTHTT--HLTFIDGKQ 406
Cdd:cd01298  369 DLdgPHLLPVHDPISHLVYSANGGdvDTVIVNGRV 403
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 56-405 3.29e-34

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: 129.93  E-value: 3.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   56 VLLPGLINSHVHLEFSANQSMLHYGDFIPWlqsviahrdelsALATTelitckLTEMLKSGTTSLGAISSFGAD-----L 130
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYE------------ALRLG------ITTMLKSGTTTVLDMGATTSTgiealL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  131 EACVNAP--QRVVYFNEVLGSVPSAVDVM--YNDFRGRLEASKEFTCKHFIPAISVHSPYSTHPILAKKALKLAEDEDCV 206
Cdd:pfam01979  63 EAAEELPlgLRFLGPGCSLDTDGELEGRKalREKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  207 VSTHFMESQAERAWIDEGSGDFQTFftafnphakpmCTSLEYL---ALFENNATLFTHGVQASKEELETISKQ--NATLT 281
Cdd:pfam01979 143 VAIHALETKGEVEDAIAAFGGGIEH-----------GTHLEVAesgGLLDIIKLILAHGVHLSPTEANLLAEHlkGAGVA 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  282 HCPVSNRLLGVGKLDVERVENEKIKLTLGTDGLSSNISLSLWDEMRSALMMHTNMELNALARTLLQSVTCNAAHALKLPC 361
Cdd:pfam01979 212 HCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFDPEGGLSPLEALRMATINPAKALGLDD 291

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 390192580  362 --GALKEGLASDMIVVTLPQSCELSTLplhliLHTHTTHLTFIDGK 405
Cdd:pfam01979 292 kvGSIEVGKDADLVVVDLDPLAAFFGL-----KPDGNVKKVIVKGK 332
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
 14-401 3.37e-31

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 123.37  E-value: 3.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  14 EHFEIIEEGAVLFDAQILEVGKaSILKekhPTVTCIETpKNSVLLPGLINSHVHLEFSANQSMLHYGDFIPWLQSVIAHR 93
Cdd:PRK08393  14 ENLKVIRADVLIEGNKIVEVKR-NINK---PADTVIDA-SGSVVSPGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  94 D-ELSALATTELITCKLTEMLKSGTTS-------------------LGAISSFG-ADLEacvNAPQRVVYFNEVLgsvps 152
Cdd:PRK08393  89 ErKLKRKDIYWGAYLGLLEMIKSGTTTfvdmyfhmeevakatlevgLRGYLSYGmVDLG---DEEKREKEIKETE----- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 153 avdvMYNDFRGRLEASKeftcKHFIpaISVHSPYSTHPILAKKALKLAEDEDCVVSTHFMESQAERAWIDEGSGdfqtff 232
Cdd:PRK08393 161 ----KLMEFIEKLNSPR----VHFV--FGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIKQIREKYG------ 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 233 tafnphaKPMCTSLEYLALFeNNATLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEKIKLTLGTD 312
Cdd:PRK08393 225 -------KSPVVLLDEIGFL-NEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTD 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 313 GLSSNISLSLWDEMRSALMMHTNMELN---ALARTLLQSVTCNAAHALKLPCGALKEGLASDMIVVTLPQScelstlplH 389
Cdd:PRK08393 297 GAASNNNLDMLREMKLAALLHKVHNLDptiADAETVFRMATQNGAKALGLKAGVIKEGYLADIAVIDFNRP--------H 368

                        410
                 ....*....|...
gi 390192580 390 LI-LHTHTTHLTF 401
Cdd:PRK08393 369 LRpINNPISHLVY 381
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 3-391 1.46e-30

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 121.78  E-value: 1.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   3 LITADFILTCNEhfEIIEEGAVLF-DAQILEVGKASilKEKHPTVtcIETpKNSVLLPGLINSHVHLEFSANQSmlhYGD 81
Cdd:PRK06038   5 IIKNAYVLTMDA--GDLKKGSVVIeDGTITEVSEST--PGDADTV--IDA-KGSVVMPGLVNTHTHAAMTLFRG---YAD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  82 FIP---WLQSVI----AHRDELSALATTeLITCklTEMLKSGTTSLgaissfgADLEACVNAPQRVVYFNEVLGSVPSAV 154
Cdd:PRK06038  75 DLPlaeWLNDHIwpaeAKLTAEDVYAGS-LLAC--LEMIKSGTTSF-------ADMYFYMDEVAKAVEESGLRAALSYGM 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 155 DVMYNDFRGRLEASKEftcKHFIPA--------ISV----HSPYSTHPILAKKALKLAEDEDCVVSTHFMESQAERAWID 222
Cdd:PRK06038 145 IDLGDDEKGEAELKEG---KRFVKEwhgaadgrIKVmygpHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQMK 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 223 EGSGdfqtfftafnphakpMCtSLEYL---ALFENNaTLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVER 299
Cdd:PRK06038 222 EQYG---------------MC-SVNYLddiGFLGPD-VLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIAPVPK 284

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 300 VENEKIKLTLGTDGLSSNISLSLWDEMRSALMMH--TNMELNAL-ARTLLQSVTCNAAHALKLPCGALKEGLASDMIVVT 376
Cdd:PRK06038 285 LLERGVNVSLGTDGCASNNNLDMFEEMKTAALLHkvNTMDPTALpARQVLEMATVNGAKALGINTGMLKEGYLADIIIVD 364

                        410
                 ....*....|....*..
gi 390192580 377 L--PQSCELSTLPLHLI 391
Cdd:PRK06038 365 MnkPHLTPVRDVPSHLV 381
PRK06687 PRK06687
TRZ/ATZ family protein;
9-401 2.30e-27

TRZ/ATZ family protein;


Pssm-ID: 180657 [Multi-domain]  Cd Length: 419  Bit Score: 112.41  E-value: 2.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   9 ILTCNEHFEIIEEGA-VLFDAQILEVG--KASILKEKHPTVTCietpKNSVLLPGLINSHVHLEFSANQSMLHYGDFIPW 85
Cdd:PRK06687   9 IVTCDQDFHVYLDGIlAVKDSQIVYVGqdKPAFLEQAEQIIDY----QGAWIMPGLVNCHTHSAMTGLRGIRDDSNLHEW 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  86 LQSVI-AHRDELSALATTELITCKLTEMLKSGTTSLGAI-SSFGADLE---ACVNAPQRVVYFNEVLGSVPS-AVDVMYN 159
Cdd:PRK06687  85 LNDYIwPAESEFTPDMTTNAVKEALTEMLQSGTTTFNDMyNPNGVDIQqiyQVVKTSKMRCYFSPTLFSSETeTTAETIS 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 160 DFRGRLEASKEFTCKHFIPAISVHSPYSTHPILAKKALKLAEDEDCVVSTHFMESQAERAWIDEGSGDfqtfftafnpha 239
Cdd:PRK06687 165 RTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIILKRYGK------------ 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 240 KPMcTSLEYLALFENNAtLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEKIKLTLGTDGLSSNIS 319
Cdd:PRK06687 233 RPL-AFLEELGYLDHPS-VFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDSVASNNN 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 320 LSLWDEMRSALMMHTNMELNALARTL---LQSVTCNAAHALKL--PCGALKEGLASDMIVVTlPQScELSTLPLHLILht 394
Cdd:PRK06687 311 LDMFEEGRTAALLQKMKSGDASQFPIetaLKVLTIEGAKALGMenQIGSLEVGKQADFLVIQ-PQG-KIHLQPQENML-- 386


                 ....*..
gi 390192580 395 htTHLTF 401
Cdd:PRK06687 387 --SHLVY 391
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 16-375 1.76e-25

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: 107.36  E-value: 1.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  16 FEIIEEGAVLF-DAQILEVGKASILKEKHPTVTCIETPKNSVLLPGLINSHVHLEFSANqSMLHYGD-FIPWLQSVI--- 90
Cdd:cd01303   21 LRVVEDGLIVVvDGNIIAAGAAETLKRAAKPGARVIDSPNQFILPGFIDTHIHAPQYAN-IGSGLGEpLLDWLETYTfpe 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  91 --AHRDELSAlatTELITCKLTEMLKSGTTS---LGAISSFGADL--EACVNAPQRVVyfnevLGSVpsavdVM-YNDFR 162
Cdd:cd01303  100 eaKFADPAYA---REVYGRFLDELLRNGTTTacyFATIHPESTEAlfEEAAKRGQRAI-----AGKV-----CMdRNAPE 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 163 GRLEASKEFT--CKHFI-----------PAISVH-SPYSTHPILAkkAL-KLAEDE-DCVVSTHFMESQAERAWIdegsg 226
Cdd:cd01303  167 YYRDTAESSYrdTKRLIerwhgksgrvkPAITPRfAPSCSEELLA--ALgKLAKEHpDLHIQTHISENLDEIAWV----- 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 227 dfQTFFtafnphakPMCTSleYLALFEN-----NATLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVE 301
Cdd:cd01303  240 --KELF--------PGARD--YLDVYDKyglltEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLL 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 302 NEKIKLTLGTDgLSSNISLSLWDEMRSALMM--HTNMELNALART----LLQSVTCNAAHALKL--PCGALKEGLASDMI 373
Cdd:cd01303  308 DAGIKVGLGTD-VGGGTSFSMLDTLRQAYKVsrLLGYELGGHAKLspaeAFYLATLGGAEALGLddKIGNFEVGKEFDAV 386


                 ..
gi 390192580 374 VV 375
Cdd:cd01303  387 VI 388
PRK15493 PRK15493
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
9-375 7.01e-23

bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;


Pssm-ID: 185390 [Multi-domain]  Cd Length: 435  Bit Score: 99.75  E-value: 7.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   9 ILTCNEHFEIIEEGAVLF-DAQILEVGKASILKekHPTVTCIETPKNSVLLPGLINSHVHLEFSANQSMLHYGDFIPWLQ 87
Cdd:PRK15493  10 IVTMNEQNEVIENGYIIVeNDQIIDVNSGEFAS--DFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  88 SVI-----AHRDELsALATTELitcKLTEMLKSGTTSLGAI-SSFGADLEACVNAPQRVvyfnevlGSVPSAVDVMYN-- 159
Cdd:PRK15493  88 TRIwplesQFTPEL-AVASTEL---GLLEMVKSGTTSFSDMfNPIGVDQDAIMETVSRS-------GMRAAVSRTLFSfg 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 160 ---DFRGRLEASKEFTCKHF------IPAISVHSPYSTHPILAKKALKLAEDEDCVVSTHFMESQAERAWIDEGSGDfqt 230
Cdd:PRK15493 157 tkeDEKKAIEEAEKYVKRYYnesgmlTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGK--- 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 231 fftafnphaKPmctsLEYLA---LFENnATLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEKIKL 307
Cdd:PRK15493 234 ---------RP----VEYAAscgLFKR-PTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKV 299

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 390192580 308 TLGTDGLSSNISLSLWDEMRSALMMHTNMELNALA---RTLLQSVTCNAAHALKLP-CGALKEGLASDMIVV 375
Cdd:PRK15493 300 GIATDSVASNNNLDMFEEMRIATLLQKGIHQDATAlpvETALTLATKGAAEVIGMKqTGSLEVGKCADFITI 371
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
 2-375 8.13e-23

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 99.57  E-value: 8.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   2 TLITADFILTCNEHFEIIEeGAVLFDA-QILEVGKASILKEKhptvtcIETPKNSVLLPGLINSHVHLEFSANQSMLHYG 80
Cdd:PRK06380   3 ILIKNAWIVTQNEKREILQ-GNVYIEGnKIVYVGDVNEEADY------IIDATGKVVMPGLINTHAHVGMTASKGLFDDV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  81 DfipwLQSVIAHRDELSALATTELI--TCKL--TEMLKSGTTSLgaissfgADLEACVNAPQRvvyfnevlgsvpSAVDV 156
Cdd:PRK06380  76 D----LEEFLMKTFKYDSKRTREGIynSAKLgmYEMINSGITAF-------VDLYYSEDIIAK------------AAEEL 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 157 MYNDFRGRLEASKEFTCK---------HFI----------PAISVHSPYSTHPILAKKALKLAEDEDCVVSTHFMESQAE 217
Cdd:PRK06380 133 GIRAFLSWAVLDEEITTQkgdplnnaeNFIrehrneelvtPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETRKE 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 218 rawidegsgdfqtfftAFNPHAKPMCTSLEYLAL--FENNATLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVG-K 294
Cdd:PRK06380 213 ----------------VYDHVKRTGERPVEHLEKigFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTGgS 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 295 LDVERVENEKIKLTLGTDGLSSNISLSLWDEMRSALMMHTNMELNAL---ARTLLQSVTCNAAHALKLPCGALKEGLASD 371
Cdd:PRK06380 277 PPIPEMLDNGINVTIGTDSNGSNNSLDMFEAMKFSALSVKNERWDASiikAQEILDFATINAAKALELNAGSIEVGKLAD 356


                 ....
gi 390192580 372 MIVV 375
Cdd:PRK06380 357 LVIL 360
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
2-406 2.67e-21

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 95.36  E-value: 2.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   2 TLITADFILTCNEHFEIIEEGAVLF-DAQILEVGKASILKEKHPTVTCIETPkNSVLLPGLINSHVHlefSANQSMLHYG 80
Cdd:PRK09045   9 LLIEARWIVPVEPAGVVLEDHAVAIrDGRIVAILPRAEARARYAAAETVELP-DHVLIPGLINAHTH---AAMSLLRGLA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  81 DFIP---WLQSVI-----AHRDELSALATTELitcKLTEMLKSGTTSLGAISSFG-ADLEACVNAPQRVVYFNEVLgSVP 151
Cdd:PRK09045  85 DDLPlmtWLQDHIwpaegAWVSEEFVRDGTLL---AIAEMLRGGTTCFNDMYFFPeAAAEAAHQAGMRAQIGMPVL-DFP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 152 SAVDVMYND-FRGRLEASKEFtcKHFiPAISV----HSPYSTHPILAKKALKLAEDEDCVVSTHFMESQAErawIDEGSG 226
Cdd:PRK09045 161 TAWASDADEyLAKGLELHDQW--RHH-PLISTafapHAPYTVSDENLERIRTLAEQLDLPIHIHLHETAQE---IADSLK 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 227 DFQTfftafnphaKPMcTSLEYLALFENNaTLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEKIK 306
Cdd:PRK09045 235 QHGQ---------RPL-ARLARLGLLGPR-LIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVN 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 307 LTLGTDGLSSNISLSLWDEMRSALMMHTNMELNAL---ARTLLQSVTCNAAHALKL--PCGALKEGLASDMIVVTLPqsc 381
Cdd:PRK09045 304 VALGTDGAASNNDLDLFGEMRTAALLAKAVAGDATalpAHTALRMATLNGARALGLddEIGSLEPGKQADLVAVDLS--- 380

                        410       420       430
                 ....*....|....*....|....*....|...
gi 390192580 382 ELSTLPL-----HLILHT---HTTHlTFIDGKQ 406
Cdd:PRK09045 381 GLETQPVydpvsQLVYAAgreQVSH-VWVAGKQ 412
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 61-354 2.20e-19

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: 87.39  E-value: 2.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  61 LINSHVHLEFSANQsmLHYGDFIPWLQSVIAHRDELSALATTelitckLTEMLKSGTTSLGAISSFGAD----------L 130
Cdd:cd01292    1 FIDTHVHLDGSALR--GTRLNLELKEAEELSPEDLYEDTLRA------LEALLAGGVTTVVDMGSTPPPtttkaaieavA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 131 EACVNAP-QRVVYFNEVLGSVPSAVDVMYNDFRGRLEASKEFtckhFIPAISVHSPYSTH---PILAKKALKLAEDEDCV 206
Cdd:cd01292   73 EAARASAgIRVVLGLGIPGVPAAVDEDAEALLLELLRRGLEL----GAVGLKLAGPYTATglsDESLRRVLEEARKLGLP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 207 VSTHFMESQAERAWIDEGsgdfqtfftafnphakpmctsleYLALFENNATLFTHGVQASKEELETISKQNATLTHCPVS 286
Cdd:cd01292  149 VVIHAGELPDPTRALEDL-----------------------VALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLS 205

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 390192580 287 NRLLGVGKLDVERVEN---EKIKLTLGTDGLSSNISLSLWDEMRSALMMhtnMELNALARTLLQSVTCNAA 354
Cdd:cd01292  206 NYLLGRDGEGAEALRRlleLGIRVTLGTDGPPHPLGTDLLALLRLLLKV---LRLGLSLEEALRLATINPA 273
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
2-405 7.48e-17

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 81.97  E-value: 7.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   2 TLITADFILTCNEHfEIIEEGAVLF-DAQILEVGKASILKE--KHPTVTCietpknSVLLPGLINSHVHLefsaNQSmLH 78
Cdd:PRK07228   3 ILIKNAGIVTMNAK-REIVDGDVLIeDDRIAAVGDRLDLEDydDHIDATG------KVVIPGLIQGHIHL----CQT-LF 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  79 YG-----DFIPWLQSVI-----AHRDE---LSALATTelitcklTEMLKSGTTSL-------GAISSFGADLEACVNAPQ 138
Cdd:PRK07228  71 RGiaddlELLDWLKDRIwpleaAHDAEsmyYSALLGI-------GELIESGTTTIvdmesvhHTDSAFEAAGESGIRAVL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 139 RVV---YFNEVLG--------SVPSAVDVM---YNDFRGRLEASkeftckhFIPAISVhspySTHPILAKKALKLAEDED 204
Cdd:PRK07228 144 GKVmmdYGDDVPEglqedteaSLAESVRLLekwHGADNGRIRYA-------FTPRFAV----SCTEELLRGVRDLADEYG 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 205 CVVSTHFMESQAERAWIDEGSGDFQTFFtafnphakpmctsLEYLALFENNATLfTHGVQASKEELETISKQNATLTHCP 284
Cdd:PRK07228 213 VRIHTHASENRGEIETVEEETGMRNIHY-------------LDEVGLTGEDLIL-AHCVWLDEEEREILAETGTHVTHCP 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 285 VSNRLLGVGKLDVERVENEKIKLTLGTDGLSSNISLSLWDEMRSALMMHTNMELNAL---ARTLLQSVTCNAAHALKLP- 360
Cdd:PRK07228 279 SSNLKLASGIAPVPDLLERGINVALGADGAPCNNTLDPFTEMRQAALIQKVDRLGPTampARTVFEMATLGGAKAAGFEd 358

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 390192580 361 -CGALKEGLASDMIVVTLPQsceLSTLPLHLI-LHTHTTH--------LTFIDGK 405
Cdd:PRK07228 359 eIGSLEEGKKADLAILDLDG---LHATPSHGVdVLSHLVYaahgsdveTTMVDGK 410
PRK09228 PRK09228
guanine deaminase; Provisional
 16-375 4.79e-16

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 79.46  E-value: 4.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  16 FEIIEEGAVLFDAQ-ILEVGKASILKEKHPTVTCIETPKNSVLLPGLINSHVHleFSANQSMLHYGD-FIPWLQSVI--- 90
Cdd:PRK09228  26 LRYIEDGLLLVEDGrIVAAGPYAELRAQLPADAEVTDYRGKLILPGFIDTHIH--YPQTDMIASYGEqLLDWLNTYTfpe 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  91 -------AHRDELSALAttelitckLTEMLKSGTTSlgaISSFGADLEACVNApqrvvYFNE--------VLGSV----- 150
Cdd:PRK09228 104 errfadpAYAREVAEFF--------LDELLRNGTTT---ALVFGTVHPQSVDA-----LFEAaearnmrmIAGKVlmdrn 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 151 -PSAV----DVMYNDF---------RGRLeaskeftckHFipAISVH-SPYSTHPILAKKALKLAEDEDCVVSTHFMESQ 215
Cdd:PRK09228 168 aPDGLrdtaESGYDDSkalierwhgKGRL---------LY--AITPRfAPTSTPEQLEAAGALAREHPDVWIQTHLSENL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 216 AERAWIDEgsgdfqtFFtafnphakPMCTSleYLALFEN-----NATLFTHGVQASKEELETISKQNATLTHCPVSNRLL 290
Cdd:PRK09228 237 DEIAWVKE-------LF--------PEARD--YLDVYERygllgPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFL 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 291 GVGKLDVERVENEKIKLTLGTD-GLSSniSLSLWDEMRSA--LMMHTNMELNALArtLLQSVTCNAAHALKLP--CGALK 365
Cdd:PRK09228 300 GSGLFDLKRADAAGVRVGLGTDvGGGT--SFSMLQTMNEAykVQQLQGYRLSPFQ--AFYLATLGGARALGLDdrIGNLA 375

                        410
                 ....*....|
gi 390192580 366 EGLASDMIVV 375
Cdd:PRK09228 376 PGKEADFVVL 385
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 1-377 2.63e-13

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 71.04  E-value: 2.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   1 MTLITADFILTCNEHFEIIEEGAVLF-DAQILEVGKASilKEKHPTVTCIETpKNSVLLPGLINSHVHLEFSANQSMLHY 79
Cdd:PRK08203   3 LWIKNPLAIVTMDAARREIADGGLVVeGGRIVEVGPGG--ALPQPADEVFDA-RGHVVTPGLVNTHHHFYQTLTRALPAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  80 GD---FiPWLQS---VIAHRD-ELSALATTelitCKLTEMLKSG-TTSLGAISSF----GADLEACVNAPQRV-VYFNEV 146
Cdd:PRK08203  80 QDaelF-PWLTTlypVWARLTpEMVRVATQ----TALAELLLSGcTTSSDHHYLFpnglRDALDDQIEAAREIgMRFHAT 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 147 LGSV----------PsavDVMYNDFRGRLEASKEFTCKHFIPA------ISVH--SPYSTHPILAKKALKLAEDEDCVVS 208
Cdd:PRK08203 155 RGSMslgesdgglpP---DSVVEDEDAILADSQRLIDRYHDPGpgamlrIALApcSPFSVSRELMRESAALARRLGVRLH 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 209 THFMESQAERAWIDEGSGdfqtfftafnphakpmCTSLEYLalfE-----NNATLFTHGVQASKEELETISKQNATLTHC 283
Cdd:PRK08203 232 THLAETLDEEAFCLERFG----------------MRPVDYL---EdlgwlGPDVWLAHCVHLDDAEIARLARTGTGVAHC 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 284 PVSNRLLGVGKLDVERVENEKIKLTLGTDGLSSNISLSLWDEMRSALMMH------TNMElnalARTLLQSVTCNAAHAL 357
Cdd:PRK08203 293 PCSNMRLASGIAPVRELRAAGVPVGLGVDGSASNDGSNLIGEARQALLLQrlrygpDAMT----AREALEWATLGGARVL 368

                        410       420
                 ....*....|....*....|.
gi 390192580 358 KLP-CGALKEGLASDMIVVTL 377
Cdd:PRK08203 369 GRDdIGSLAPGKLADLALFDL 389
PRK12393 PRK12393
amidohydrolase; Provisional
 53-379 2.38e-12

amidohydrolase; Provisional


Pssm-ID: 237088 [Multi-domain]  Cd Length: 457  Bit Score: 68.17  E-value: 2.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  53 KNSVLLPGLINSHVHLeFsanQSMLH------YGDFIPWLQSV----IAHRDELSALATTELitcKLTEMLKSGTTS--- 119
Cdd:PRK12393  53 TDCVVYPGWVNTHHHL-F---QSLLKgvpagiNQSLTAWLAAVpyrfRARFDEDLFRLAARI---GLVELLRSGCTTvad 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 120 ------------LGAI-----SSFGADLEACVNAPQRVVYFNEVLGS--VPSAVDVMYND---FRGRLEASKEFTCKHFI 177
Cdd:PRK12393 126 hhylyhpgmpfdTGDIlfdeaEALGMRFVLCRGGATQTRGDHPGLPTalRPETLDQMLADverLVSRYHDASPDSLRRVV 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 178 PAISVhSPYSTHPILAKKALKLAEDEDCVVSTHFMESQaerawidegsgDFQTFftafnPHAKPMCTSLEYLALFE--NN 255
Cdd:PRK12393 206 VAPTT-PTFSLPPELLREVARAARGMGLRLHSHLSETV-----------DYVDF-----CREKYGMTPVQFVAEHDwlGP 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 256 ATLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEKIKLTLGTDGLSSNISLSLWDEMRSALMMHtN 335
Cdd:PRK12393 269 DVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDGAASNESADMLSEAHAAWLLH-R 347

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 390192580 336 MELNALARTLLQSV---TCNAAHALKLP-CGALKEGLASDMIVVTLPQ 379
Cdd:PRK12393 348 AEGGADATTVEDVVhwgTAGGARVLGLDaIGTLAVGQAADLAIYDLDD 395
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 1-405 8.40e-12

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 66.14  E-value: 8.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   1 MTLITADFILTcNEHFEIIEEGAVLF-DAQILEVGKASILKEKHPTVTcIETpKNSVLLPGLINSHVHLEFSANQSM-LH 78
Cdd:COG1228    9 TLLITNATLVD-GTGGGVIENGTVLVeDGKIAAVGPAADLAVPAGAEV-IDA-TGKTVLPGLIDAHTHLGLGGGRAVeFE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  79 YGDFIPWLQSVIAHRDELsalattelitckLTEMLKSGTTSLGAISSFGADLEACVNAPQ-RVVYFNEVLGSVPsAVDVm 157
Cdd:COG1228   86 AGGGITPTVDLVNPADKR------------LRRALAAGVTTVRDLPGGPLGLRDAIIAGEsKLLPGPRVLAAGP-ALSL- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 158 YNDFRGRLEAskefTCKHFIPAisvhspysthpILAKKA--LKLAEDEDcvvSTHFmeSQAERAWIDEGSGDFQTFFTAf 235
Cdd:COG1228  152 TGGAHARGPE----EARAALRE-----------LLAEGAdyIKVFAEGG---APDF--SLEELRAILEAAHALGLPVAA- 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 236 npHAkpmCTSLEYLALFENNATLFTHGVQASKEELETISKQNA-----TLTHCPVSNRLLGVGKLDVERVENEK------ 304
Cdd:COG1228  211 --HA---HQADDIRLAVEAGVDSIEHGTYLDDEVADLLAEAGTvvlvpTLSLFLALLEGAAAPVAAKARKVREAalanar 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 305 ------IKLTLGTD-GLSSNISLSLWDEMRSALMMH-TNMElnalartLLQSVTCNAAHALKLP--CGALKEGLASDMIV 374
Cdd:COG1228  286 rlhdagVPVALGTDaGVGVPPGRSLHRELALAVEAGlTPEE-------ALRAATINAAKALGLDddVGSLEPGKLADLVL 358

                        410       420       430
                 ....*....|....*....|....*....|.
gi 390192580 375 VTLPqscelstlPLHLILHTHTTHLTFIDGK 405
Cdd:COG1228  359 LDGD--------PLEDIAYLEDVRAVMKDGR 381
archeal_chlorohydrolases cd01305
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ...
 258-354 1.52e-10

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: 61.26  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 258 LFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEKIKLTLGTDGLSSNiSLSLWDEMRSAlMMHTNME 337
Cdd:cd01305  167 LLVHGTHLTDEDLELVRENGVPVVLCPRSNLYFGVGIPPVAELLKLGIKVLLGTDNVMVN-EPDMWAEMEFL-AKYSRLQ 244

                         90
                 ....*....|....*..
gi 390192580 338 LNALARTLLQSVTCNAA 354
Cdd:cd01305  245 GYLSPLEILRMATVNAA 261
Met_dep_hydrolase_E cd01313
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 54-377 3.48e-09

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: 58.24  E-value: 3.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  54 NSVLLPGLINSHVH---------LEFSANQSmlhyGDFIPWLQSVIAHRDELSAlATTELITCKL-TEMLKSGTTSLGAI 123
Cdd:cd01313   37 GGALLPGMPNLHSHafqramaglTEYRGSAA----DSFWTWRELMYRFAARLTP-EQIEAIARQLyIEMLLAGITAVGEF 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 124 -----SSFG---ADL----EACVNAPQ---------RVVYFNEVLGSVPSAVDVM-----YNDFRGRLE--ASKEFTCKH 175
Cdd:cd01313  112 hyvhhDPDGtpyADPaelaQRVIAAASdagigitllPVLYARAGFGGPAPNPGQRrfingYEDFLGLLEkaLRAVKEHAA 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 176 FIPAISVHSPYSTHPILAKKALKLAeDEDCVVSTHFMESQAERAWIDEGSGdfqtfftafnphAKPMCTSLEYLALfeNN 255
Cdd:cd01313  192 ARIGVAPHSLRAVPAEQLAALAALA-SEKAPVHIHLAEQPKEVDDCLAAHG------------RRPVELLLDHGHL--DA 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 256 ATLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEKIKLTLGTDglsSNISLSLWDEMRsALMMHTN 335
Cdd:cd01313  257 RWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSD---SNARIDLLEELR-QLEYSQR 332

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 390192580 336 MELNA----------LARTLLQSVTCNAAHALKLPCGALKEGLASDMIVVTL 377
Cdd:cd01313  333 LRDRArnvlataggsSARALLDAALAGGAQALGLATGALEAGARADLLSLDL 384
PRK07213 PRK07213
chlorohydrolase; Provisional
 255-375 1.60e-08

chlorohydrolase; Provisional


Pssm-ID: 235969 [Multi-domain]  Cd Length: 375  Bit Score: 55.81  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 255 NATLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEKIKLTLGTDGLSSNiSLSLWDEMRSAL-MMH 333
Cdd:PRK07213 227 KPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMLEKGILLGIGTDNFMAN-SPSIFREMEFIYkLYH 305

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 390192580 334 TNmelnalARTLLQSVTCNAAHALKLP-CGALKEGLASDMIVV 375
Cdd:PRK07213 306 IE------PKEILKMATINGAKILGLInVGLIEEGFKADFTFI 342
PRK07203 PRK07203
putative aminohydrolase SsnA;
1-375 5.85e-08

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 54.56  E-value: 5.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580   1 MTLITADFILTCNEHFEIIEEGAVLFD-AQILEVGKASILKEKHPTVTCIETpKNSVLLPGLINSHVHLEFSANQSMLHY 79
Cdd:PRK07203   1 MLLIGNGTAITRDPAKPVIEDGAIAIEgNVIVEIGTTDELKAKYPDAEFIDA-KGKLIMPGLINSHNHIYSGLARGMMAN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  80 G----DFIPWLQSVIAHRDE--------LSALATtelitckLTEMLKSGTT-------SLGAIS-SFGADLEACVNAPQR 139
Cdd:PRK07203  80 IppppDFISILKNLWWRLDRaltledvyYSALIC-------SLEAIKNGVTtvfdhhaSPNYIGgSLFTIADAAKKVGLR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 140 VVYFNEVlgsvpSAVDVMyndfRGRLEASKEFTckHFIPAISV------------HSPYSthpiLAKKALKLAEDEDCVV 207
Cdd:PRK07203 153 AMLCYET-----SDRDGE----KELQEGVEENI--RFIKHIDEakddmveamfglHASFT----LSDATLEKCREAVKET 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 208 STHFMESQAerawidEGSGDFQtfftafNPHAKPMCTSLEYLALFE--NNATLFTHGVQASKEELETISKQNATLTHCPV 285
Cdd:PRK07203 218 GRGYHIHVA------EGIYDVS------DSHKKYGKDIVERLADFGllGEKTLAAHCIYLSDEEIDLLKETDTFVVHNPE 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 286 SNRLLGVGKLDVERVENEKIKLTLGTDGLSSNIslslWDEMRSALMMHTNM--ELNA----LARTLLQSVTCNAAHALKL 359
Cdd:PRK07203 286 SNMGNAVGYNPVLEMIKNGILLGLGTDGYTSDM----FESYKVANFKHKHAggDPNVgwpeSPAMLFENNNKIAERYFGA 361

                        410
                 ....*....|....*.
gi 390192580 360 PCGALKEGLASDMIVV 375
Cdd:PRK07203 362 KFGILEEGAKADLIIV 377
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 27-378 4.04e-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: 51.49  E-value: 4.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  27 DAQILEVGKASILKEKHPTVTCIETPKNSVLLPGLINSHVHL--------EFSANQSMLHYGDfIPW-----LQSVIAHR 93
Cdd:cd01296    5 DGRIAAVGPAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLvfagdrvdEFAARLAGASYEE-ILAagggiLSTVRATR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580  94 ----DELSALATTelitcKLTEMLKSGTTSLGAISSFGADLEACV-----------NAPQRVVyfNEVLG--SVPSavdv 156
Cdd:cd01296   84 aaseDELFASALR-----RLARMLRHGTTTVEVKSGYGLDLETELkmlrvirrlkeEGPVDLV--STFLGahAVPP---- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 157 mynDFRGRlEASKEFTCKHFIPAIsvhspysthpilakKALKLAEDEDcvvsthfmesqaerAWIDEGSGDF---QTFFT 233
Cdd:cd01296  153 ---EYKGR-EEYIDLVIEEVLPAV--------------AEENLADFCD--------------VFCEKGAFSLeqsRRILE 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 234 A-------FNPHAKpmctSLEY-----LALfENNATLFTHGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVE 301
Cdd:cd01296  201 AakeaglpVKIHAD----ELSNiggaeLAA-ELGALSADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLI 275

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 302 NEKIKLTLGTD--GLSSNISLSLwdemrsaLMMH---TNMELNALarTLLQSVTCNAAHALKL--PCGALKEGLASDMIV 374
Cdd:cd01296  276 DAGVPVALGTDfnPGSSPTSSMP-------LVMHlacRLMRMTPE--EALTAATINAAAALGLgeTVGSLEVGKQADLVI 346


                 ....
gi 390192580 375 VTLP 378
Cdd:cd01296  347 LDAP 350
PRK09229 PRK09229
N-formimino-L-glutamate deiminase; Validated
 261-395 4.49e-06

N-formimino-L-glutamate deiminase; Validated


Pssm-ID: 236420 [Multi-domain]  Cd Length: 456  Bit Score: 48.69  E-value: 4.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390192580 261 HGVQASKEELETISKQNATLTHCPVSNRLLGVGKLDVERVENEKIKLTLGTDglsSNISLSLWDEMRsalMMHTNMEL-- 338
Cdd:PRK09229 271 HATHLTDAETARLARSGAVAGLCPTTEANLGDGIFPAVDYLAAGGRFGIGSD---SHVSIDLVEELR---LLEYGQRLrd 344

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 390192580 339 ---NALA--------RTLLQSVTCNAAHALKLPCGALKEGLASDMIVVTLpQSCELSTLPLHLILHTH 395
Cdd:PRK09229 345 rrrNVLAaaaqpsvgRRLFDAALAGGAQALGRAIGGLAVGARADLVVLDL-DHPALAGREGDALLDRW 411
 
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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