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Conserved domains on  [gi|1277938128|gb|PIV37151|]
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MAG: chlorohydrolase [Sulfurimonas sp. CG02_land_8_20_14_3_00_36_67]

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;
1-402 0e+00

metal-dependent hydrolase;


:

Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 570.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128   1 MQIIVPHFILMSD---SIVTERAIAFEKTILKIAPLEELLQEFPHAKITTlAKNSLLMPGLINAHVHLEFSANKTHLSYG 77
Cdd:PRK08418    1 MKIIGASYIFTCDenfEILEDGAVVFDDKILEIGDYENLKKKYPNAKIQF-FKNSVLLPAFINPHTHLEFSANKTTLDYG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  78 DFISWLYSVIENREELIGGCDTACMAQAIDSMLACGITTFGAVSSHGMDLQACADAPQNVIFFNELIGSQATMADALFND 157
Cdd:PRK08418   80 DFIPWLGSVINHREDLLEKCKGALIQQAINEMLKSGVGTIGAISSFGIDLEICAKSPLRVVFFNEILGSNASAVDELYQD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 158 FSARLDASKSVTREGFHTGVAIHSPYSVHPVLIKKALAIVKSEKLKLTAHFMESKAEREWLDKSEGDFKEFFESLLKQNT 237
Cdd:PRK08418  160 FLARFEESKKFKSKKFIPAIAIHSPYSVHPILAKKALQLAKKENLLVSTHFLESKAEREWLEESKGWFKKFFEKFLKEPK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 238 CVSDSAEFLEHFNAIPTLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKL 317
Cdd:PRK08418  240 PLYTPKEFLELFKGLRTLFTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDGLSSNISL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 318 DLFEEMKISLFMHSDAPLLEFAKALLKGATLDAAKALGLNTGEIAVGKNADMIVLDLDATPTP--ELAIHLLLHRYNVSK 395
Cdd:PRK08418  320 SLLDELRAALLTHANMPLLELAKILLLSATRYGAKALGLNNGEIKEGKDADLSVFELPEECTKkeQLPLQFILHAKEVKK 399

                  ....*..
gi 1277938128 396 VYINGKL 402
Cdd:PRK08418  400 LFIGGKE 406
 
Name Accession Description Interval E-value
PRK08418 PRK08418
metal-dependent hydrolase;
1-402 0e+00

metal-dependent hydrolase;


Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 570.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128   1 MQIIVPHFILMSD---SIVTERAIAFEKTILKIAPLEELLQEFPHAKITTlAKNSLLMPGLINAHVHLEFSANKTHLSYG 77
Cdd:PRK08418    1 MKIIGASYIFTCDenfEILEDGAVVFDDKILEIGDYENLKKKYPNAKIQF-FKNSVLLPAFINPHTHLEFSANKTTLDYG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  78 DFISWLYSVIENREELIGGCDTACMAQAIDSMLACGITTFGAVSSHGMDLQACADAPQNVIFFNELIGSQATMADALFND 157
Cdd:PRK08418   80 DFIPWLGSVINHREDLLEKCKGALIQQAINEMLKSGVGTIGAISSFGIDLEICAKSPLRVVFFNEILGSNASAVDELYQD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 158 FSARLDASKSVTREGFHTGVAIHSPYSVHPVLIKKALAIVKSEKLKLTAHFMESKAEREWLDKSEGDFKEFFESLLKQNT 237
Cdd:PRK08418  160 FLARFEESKKFKSKKFIPAIAIHSPYSVHPILAKKALQLAKKENLLVSTHFLESKAEREWLEESKGWFKKFFEKFLKEPK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 238 CVSDSAEFLEHFNAIPTLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKL 317
Cdd:PRK08418  240 PLYTPKEFLELFKGLRTLFTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDGLSSNISL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 318 DLFEEMKISLFMHSDAPLLEFAKALLKGATLDAAKALGLNTGEIAVGKNADMIVLDLDATPTP--ELAIHLLLHRYNVSK 395
Cdd:PRK08418  320 SLLDELRAALLTHANMPLLELAKILLLSATRYGAKALGLNNGEIKEGKDADLSVFELPEECTKkeQLPLQFILHAKEVKK 399

                  ....*..
gi 1277938128 396 VYINGKL 402
Cdd:PRK08418  400 LFIGGKE 406
Met_dep_hydrolase_D cd01312
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
27-401 1.52e-114

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: 339.43  E-value: 1.52e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  27 ILKIAPLEELLQEFPHAKITTLaKNSLLMPGLINAHVHLEFSANKTHLSYGDFISWLYSVIENREELIG-GCDTAcMAQA 105
Cdd:cd01312     3 ILEVGDYEKLEKRYPGAKHEFF-PNGVLLPGLINAHTHLEFSANVAQFTYGRFRAWLLSVINSRDELLKqPWEEA-IRQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 106 IDSMLACGITTFGAVSSHGMDLQACADAPQNVIFFNELIGSQATMADALFNDFSARLDASKSVTREGFHTGVAIHSPYSV 185
Cdd:cd01312    81 IRQMLESGTTSIGAISSDGSLLPALASSGLRGVFFNEVIGSNPSAIDFKGETFLERFKRSKSFESQLFIPAISPHAPYSV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 186 HPVLIKKALAIVKSEKLKLTAHFMESKAEREWLDKSEGDFKEFFESLLK--QNTCVSDSAEFLEHFNAI--PTLFTHVVQ 261
Cdd:cd01312   161 HPELAQDLIDLAKKLNLPLSTHFLESKEEREWLEESKGWFKHFWESFLKlpKPKKLATAIDFLDMLGGLgtRVSFVHCVY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 262 ANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMHSDAPLLEFAKA 341
Cdd:cd01312   241 ANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDGLSSNISLSLLDELRALLDLHPEEDLLELASE 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277938128 342 LLKGATLDAAKALGLNTGEIAVGKNADMIVLDLDATPTPELAIHL-LLHRYNVSKVYINGK 401
Cdd:cd01312   321 LLLMATLGGARALGLNNGEIEAGKRADFAVFELPGPGIKEQAPLQfILHAKEVRHLFISGK 381
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
20-402 5.03e-75

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: 239.34  E-value: 5.03e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  20 AIAFEK-TILKIAPLEELLQEFPHAKITTlAKNSLLMPGLINAHVHLEFSANKTHLSYGDFISWLYSVIENREE-LIGGC 97
Cdd:COG0402    23 AVLVEDgRIAAVGPGAELPARYPAAEVID-AGGKLVLPGLVNTHTHLPQTLLRGLADDLPLLDWLEEYIWPLEArLDPED 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  98 DTACMAQAIDSMLACGITTFGAVSSHGMD-----LQACADAPQNVIFFNELIG-----SQATMADALFNDFSARLDASKS 167
Cdd:COG0402   102 VYAGALLALAEMLRSGTTTVADFYYVHPEsadalAEAAAEAGIRAVLGRGLMDrgfpdGLREDADEGLADSERLIERWHG 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 168 VTREGFHTGVAIHSPYSVHPVLIKKALAIVKSEKLKLTAHFMESKAEREWLDKSEGDfkeffesllkqntcvsDSAEFLE 247
Cdd:COG0402   182 AADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLELYGK----------------RPVEYLD 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 248 HFNAI--PTLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKI 325
Cdd:COG0402   246 ELGLLgpRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDGAASNNSLDMFEEMRL 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 326 SLFMH----SDAPLLEfAKALLKGATLDAAKALGLN--TGEIAVGKNADMIVLDLDA---TPTPELAIHLLL--HRYNVS 394
Cdd:COG0402   326 AALLQrlrgGDPTALS-AREALEMATLGGARALGLDdeIGSLEPGKRADLVVLDLDAphlAPLHDPLSALVYaaDGRDVR 404

                  ....*...
gi 1277938128 395 KVYINGKL 402
Cdd:COG0402   405 TVWVAGRV 412
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
53-402 1.10e-39

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: 144.57  E-value: 1.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  53 LLMPGLINAHVHLEFSANKTHLSYGDFISWlysvienreeligGCDTACMAqaidsMLACGITTFGAVS-SHGMDLQACA 131
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYE-------------ALRLGITT-----MLKSGTTTVLDMGaTTSTGIEALL 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 132 DAPQNVIFFNELIGSQATMA--------DALFNDFSARLDASKSVTREGFHTGVAIHSPYSVHPVLIKKALAIVKSEKLK 203
Cdd:pfam01979  63 EAAEELPLGLRFLGPGCSLDtdgelegrKALREKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLP 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 204 LTAHFMESKAEREWLDKSEGDFKEFFESLlkqntcvsDSAEFLEHFNAIPTLFTHVVQANKSELSTLAK--NGHTVIHCP 281
Cdd:pfam01979 143 VAIHALETKGEVEDAIAAFGGGIEHGTHL--------EVAESGGLLDIIKLILAHGVHLSPTEANLLAEhlKGAGVAHCP 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 282 ISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMHSDAPLLEFAKALLKGATLDAAKALGL--NTG 359
Cdd:pfam01979 215 FSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFDPEGGLSPLEALRMATINPAKALGLddKVG 294
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1277938128 360 EIAVGKNADMIVLDLDATPtpelAIHLLLHRYNVSKVYINGKL 402
Cdd:pfam01979 295 SIEVGKDADLVVVDLDPLA----AFFGLKPDGNVKKVIVKGKI 333
 
Name Accession Description Interval E-value
PRK08418 PRK08418
metal-dependent hydrolase;
1-402 0e+00

metal-dependent hydrolase;


Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 570.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128   1 MQIIVPHFILMSD---SIVTERAIAFEKTILKIAPLEELLQEFPHAKITTlAKNSLLMPGLINAHVHLEFSANKTHLSYG 77
Cdd:PRK08418    1 MKIIGASYIFTCDenfEILEDGAVVFDDKILEIGDYENLKKKYPNAKIQF-FKNSVLLPAFINPHTHLEFSANKTTLDYG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  78 DFISWLYSVIENREELIGGCDTACMAQAIDSMLACGITTFGAVSSHGMDLQACADAPQNVIFFNELIGSQATMADALFND 157
Cdd:PRK08418   80 DFIPWLGSVINHREDLLEKCKGALIQQAINEMLKSGVGTIGAISSFGIDLEICAKSPLRVVFFNEILGSNASAVDELYQD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 158 FSARLDASKSVTREGFHTGVAIHSPYSVHPVLIKKALAIVKSEKLKLTAHFMESKAEREWLDKSEGDFKEFFESLLKQNT 237
Cdd:PRK08418  160 FLARFEESKKFKSKKFIPAIAIHSPYSVHPILAKKALQLAKKENLLVSTHFLESKAEREWLEESKGWFKKFFEKFLKEPK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 238 CVSDSAEFLEHFNAIPTLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKL 317
Cdd:PRK08418  240 PLYTPKEFLELFKGLRTLFTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDGLSSNISL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 318 DLFEEMKISLFMHSDAPLLEFAKALLKGATLDAAKALGLNTGEIAVGKNADMIVLDLDATPTP--ELAIHLLLHRYNVSK 395
Cdd:PRK08418  320 SLLDELRAALLTHANMPLLELAKILLLSATRYGAKALGLNNGEIKEGKDADLSVFELPEECTKkeQLPLQFILHAKEVKK 399

                  ....*..
gi 1277938128 396 VYINGKL 402
Cdd:PRK08418  400 LFIGGKE 406
Met_dep_hydrolase_D cd01312
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
27-401 1.52e-114

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: 339.43  E-value: 1.52e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  27 ILKIAPLEELLQEFPHAKITTLaKNSLLMPGLINAHVHLEFSANKTHLSYGDFISWLYSVIENREELIG-GCDTAcMAQA 105
Cdd:cd01312     3 ILEVGDYEKLEKRYPGAKHEFF-PNGVLLPGLINAHTHLEFSANVAQFTYGRFRAWLLSVINSRDELLKqPWEEA-IRQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 106 IDSMLACGITTFGAVSSHGMDLQACADAPQNVIFFNELIGSQATMADALFNDFSARLDASKSVTREGFHTGVAIHSPYSV 185
Cdd:cd01312    81 IRQMLESGTTSIGAISSDGSLLPALASSGLRGVFFNEVIGSNPSAIDFKGETFLERFKRSKSFESQLFIPAISPHAPYSV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 186 HPVLIKKALAIVKSEKLKLTAHFMESKAEREWLDKSEGDFKEFFESLLK--QNTCVSDSAEFLEHFNAI--PTLFTHVVQ 261
Cdd:cd01312   161 HPELAQDLIDLAKKLNLPLSTHFLESKEEREWLEESKGWFKHFWESFLKlpKPKKLATAIDFLDMLGGLgtRVSFVHCVY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 262 ANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMHSDAPLLEFAKA 341
Cdd:cd01312   241 ANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDGLSSNISLSLLDELRALLDLHPEEDLLELASE 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277938128 342 LLKGATLDAAKALGLNTGEIAVGKNADMIVLDLDATPTPELAIHL-LLHRYNVSKVYINGK 401
Cdd:cd01312   321 LLLMATLGGARALGLNNGEIEAGKRADFAVFELPGPGIKEQAPLQfILHAKEVRHLFISGK 381
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
20-402 5.03e-75

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: 239.34  E-value: 5.03e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  20 AIAFEK-TILKIAPLEELLQEFPHAKITTlAKNSLLMPGLINAHVHLEFSANKTHLSYGDFISWLYSVIENREE-LIGGC 97
Cdd:COG0402    23 AVLVEDgRIAAVGPGAELPARYPAAEVID-AGGKLVLPGLVNTHTHLPQTLLRGLADDLPLLDWLEEYIWPLEArLDPED 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  98 DTACMAQAIDSMLACGITTFGAVSSHGMD-----LQACADAPQNVIFFNELIG-----SQATMADALFNDFSARLDASKS 167
Cdd:COG0402   102 VYAGALLALAEMLRSGTTTVADFYYVHPEsadalAEAAAEAGIRAVLGRGLMDrgfpdGLREDADEGLADSERLIERWHG 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 168 VTREGFHTGVAIHSPYSVHPVLIKKALAIVKSEKLKLTAHFMESKAEREWLDKSEGDfkeffesllkqntcvsDSAEFLE 247
Cdd:COG0402   182 AADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLELYGK----------------RPVEYLD 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 248 HFNAI--PTLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKI 325
Cdd:COG0402   246 ELGLLgpRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDGAASNNSLDMFEEMRL 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 326 SLFMH----SDAPLLEfAKALLKGATLDAAKALGLN--TGEIAVGKNADMIVLDLDA---TPTPELAIHLLL--HRYNVS 394
Cdd:COG0402   326 AALLQrlrgGDPTALS-AREALEMATLGGARALGLDdeIGSLEPGKRADLVVLDLDAphlAPLHDPLSALVYaaDGRDVR 404

                  ....*...
gi 1277938128 395 KVYINGKL 402
Cdd:COG0402   405 TVWVAGRV 412
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
8-402 7.40e-49

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: 170.85  E-value: 7.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128   8 FILMSDSIVTERAIAFEK-TILKIAPLEELLQEfpHAKITTLAKNSLLMPGLINAHVHLEFSANKTHLSYGDFISWLYSV 86
Cdd:cd01298     9 VTTDPRRVLEDGDVLVEDgRIVAVGPALPLPAY--PADEVIDAKGKVVMPGLVNTHTHLAMTLLRGLADDLPLMEWLKDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  87 IENREELIGGCDTACMAQ-AIDSMLACGITTFgaVSSHGMDLQACADAPQNV--------IFFNELIGSQATMADALFNd 157
Cdd:cd01298    87 IWPLERLLTEEDVYLGALlALAEMIRSGTTTF--ADMYFFYPDAVAEAAEELgiravlgrGIMDLGTEDVEETEEALAE- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 158 fSARL-DASKSVTREGFHTGVAIHSPYSVHPVLIKKALAIVKSEKLKLTAHFMESKAEREWLDKSEGdfkeffesllkqn 236
Cdd:cd01298   164 -AERLiREWHGAADGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESLEKYG------------- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 237 tcvSDSAEFLEHFNAI--PTLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSN 314
Cdd:cd01298   230 ---KRPVEYLEELGLLgpDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDGAASN 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 315 YKLDLFEEMKISLFMH----SDAPLLEFAKAlLKGATLDAAKALGLN-TGEIAVGKNADMIVLDLDA---TPTPELAIHL 386
Cdd:cd01298   307 NNLDMFEEMRLAALLQklahGDPTALPAEEA-LEMATIGGAKALGLDeIGSLEVGKKADLILIDLDGphlLPVHDPISHL 385
                         410
                  ....*....|....*...
gi 1277938128 387 LL--HRYNVSKVYINGKL 402
Cdd:cd01298   386 VYsaNGGDVDTVIVNGRV 403
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
53-402 1.10e-39

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: 144.57  E-value: 1.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  53 LLMPGLINAHVHLEFSANKTHLSYGDFISWlysvienreeligGCDTACMAqaidsMLACGITTFGAVS-SHGMDLQACA 131
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYE-------------ALRLGITT-----MLKSGTTTVLDMGaTTSTGIEALL 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 132 DAPQNVIFFNELIGSQATMA--------DALFNDFSARLDASKSVTREGFHTGVAIHSPYSVHPVLIKKALAIVKSEKLK 203
Cdd:pfam01979  63 EAAEELPLGLRFLGPGCSLDtdgelegrKALREKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLP 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 204 LTAHFMESKAEREWLDKSEGDFKEFFESLlkqntcvsDSAEFLEHFNAIPTLFTHVVQANKSELSTLAK--NGHTVIHCP 281
Cdd:pfam01979 143 VAIHALETKGEVEDAIAAFGGGIEHGTHL--------EVAESGGLLDIIKLILAHGVHLSPTEANLLAEhlKGAGVAHCP 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 282 ISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMHSDAPLLEFAKALLKGATLDAAKALGL--NTG 359
Cdd:pfam01979 215 FSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFDPEGGLSPLEALRMATINPAKALGLddKVG 294
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1277938128 360 EIAVGKNADMIVLDLDATPtpelAIHLLLHRYNVSKVYINGKL 402
Cdd:pfam01979 295 SIEVGKDADLVVVDLDPLA----AFFGLKPDGNVKKVIVKGKI 333
PRK06687 PRK06687
TRZ/ATZ family protein;
54-401 1.44e-32

TRZ/ATZ family protein;


Pssm-ID: 180657 [Multi-domain]  Cd Length: 419  Bit Score: 127.04  E-value: 1.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  54 LMPGLINAHVHLEFSANKTHLSYGDFISWLYSVIENRE-ELIGGCDTACMAQAIDSMLACGITTFGAV-SSHGMDL---- 127
Cdd:PRK06687   56 IMPGLVNCHTHSAMTGLRGIRDDSNLHEWLNDYIWPAEsEFTPDMTTNAVKEALTEMLQSGTTTFNDMyNPNGVDIqqiy 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 128 QACADAPQNVIFFNELIGSQATMADALFNDFSARLDASKSVTREGFHTGVAIHSPYSVHPVLIKKALAIVKSEKLKLTAH 207
Cdd:PRK06687  136 QVVKTSKMRCYFSPTLFSSETETTAETISRTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVH 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 208 FMESKAEREWLDKSEGDFK-EFFESLlkqntcvsdsaEFLEHfnaiPTLFTHVVQANKSELSTLAKNGHTVIHCPISNRL 286
Cdd:PRK06687  216 VAETKEESGIILKRYGKRPlAFLEEL-----------GYLDH----PSVFAHGVELNEREIERLASSQVAIAHNPISNLK 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 287 LGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMHS----DAPLLEFAKAlLKGATLDAAKALGLNT--GE 360
Cdd:PRK06687  281 LASGIAPIIQLQKAGVAVGIATDSVASNNNLDMFEEGRTAALLQKmksgDASQFPIETA-LKVLTIEGAKALGMENqiGS 359
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1277938128 361 IAVGKNADMIVLD----LDATPTPELAIHLL--LHRYNVSKVYINGK 401
Cdd:PRK06687  360 LEVGKQADFLVIQpqgkIHLQPQENMLSHLVyaVKSSDVDDVYIAGE 406
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
41-406 3.54e-27

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 111.90  E-value: 3.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  41 PHAKITTLAKNSLLMPGLINAHVHLEFSANK-----THLSygDFI--SWLYSVIENREELIGGCDTAcmaqaIDSMLACG 113
Cdd:PRK06380   39 EEADYIIDATGKVVMPGLINTHAHVGMTASKglfddVDLE--EFLmkTFKYDSKRTREGIYNSAKLG-----MYEMINSG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 114 ITTFgavsshgMDLQACADAPQNVIffnELIGSQATMADALFN-DFSAR----LDASKSVTREGFHT-----GVAIHSPY 183
Cdd:PRK06380  112 ITAF-------VDLYYSEDIIAKAA---EELGIRAFLSWAVLDeEITTQkgdpLNNAENFIREHRNEelvtpSIGVQGIY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 184 SVHPVLIKKALAIVKSEKLKLTAHFMESKaerewldksegdfKEFFESLLKQntcvsdSAEFLEHFNAIPTLFT-----H 258
Cdd:PRK06380  182 VANDETYLKAKEIAEKYDTIMHMHLSETR-------------KEVYDHVKRT------GERPVEHLEKIGFLNSkliaaH 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 259 VVQANKSELSTLAKNGHTVIHCPISNRLLGNE-TLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMHS----DA 333
Cdd:PRK06380  243 CVWATYHEIKLLSKNGVKVSWNSVSNFKLGTGgSPPIPEMLDNGINVTIGTDSNGSNNSLDMFEAMKFSALSVKnerwDA 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 334 PLLEfAKALLKGATLDAAKALGLNTGEIAVGKNADMIVLDLDAT---PTPELA----IHLLLHRYNVSKVYINGKLEKGN 406
Cdd:PRK06380  323 SIIK-AQEILDFATINAAKALELNAGSIEVGKLADLVILDARAPnmiPTRKNNivsnIVYSLNPLNVDHVIVNGKILKEN 401
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
49-402 4.16e-27

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 111.77  E-value: 4.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  49 AKNSLLMPGLINAHVHLEFSANKthlSYGDFI---SWLYSVIENREELIGGCDTAcmaqaIDSMLAC------GITTFGA 119
Cdd:PRK06038   48 AKGSVVMPGLVNTHTHAAMTLFR---GYADDLplaEWLNDHIWPAEAKLTAEDVY-----AGSLLAClemiksGTTSFAD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 120 VSSHgMDlqacaDAPQNViffnELIGSQAT----MADaLFNDFSAR--LDASKSVTREgFH--------TGVAIHSPYSV 185
Cdd:PRK06038  120 MYFY-MD-----EVAKAV----EESGLRAAlsygMID-LGDDEKGEaeLKEGKRFVKE-WHgaadgrikVMYGPHAPYTC 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 186 HPVLIKKALAIVKSEKLKLTAHFMESKAEREWLDKSEGdfKEFFESLlkqntcvsDSAEFLEHfnaiPTLFTHVVQANKS 265
Cdd:PRK06038  188 SEEFLSKVKKLANKDGVGIHIHVLETEAELNQMKEQYG--MCSVNYL--------DDIGFLGP----DVLAAHCVWLSDG 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 266 ELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMH---SDAPLLEFAKAL 342
Cdd:PRK06038  254 DIEILRERGVNVSHNPVSNMKLASGIAPVPKLLERGVNVSLGTDGCASNNNLDMFEEMKTAALLHkvnTMDPTALPARQV 333
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277938128 343 LKGATLDAAKALGLNTGEIAVGKNADMIVLDLDA---TPTPELAIHLLLHRY--NVSKVYINGKL 402
Cdd:PRK06038  334 LEMATVNGAKALGINTGMLKEGYLADIIIVDMNKphlTPVRDVPSHLVYSASgsDVDTTIVDGRI 398
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
27-402 2.68e-25

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 106.92  E-value: 2.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  27 ILKIAPLEELLQEFPHAKITTLAkNSLLMPGLINAHVHLEFS-----ANKTHLsygdfISWLYSVI---ENR---EELIG 95
Cdd:PRK09045   38 IVAILPRAEARARYAAAETVELP-DHVLIPGLINAHTHAAMSllrglADDLPL-----MTWLQDHIwpaEGAwvsEEFVR 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  96 -GCDTAcMAQaidsMLACGITTF-----------GAVSSHGMDLQACA---DAPqnviffnelIGSQATMADALFNDFSA 160
Cdd:PRK09045  112 dGTLLA-IAE----MLRGGTTCFndmyffpeaaaEAAHQAGMRAQIGMpvlDFP---------TAWASDADEYLAKGLEL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 161 RlDASKSVTRegFHTGVAIHSPYSVHPVLIKKALAIVKSEKLKLTAHFMESKAErewLDKSEgdfKEFFE---------S 231
Cdd:PRK09045  178 H-DQWRHHPL--ISTAFAPHAPYTVSDENLERIRTLAEQLDLPIHIHLHETAQE---IADSL---KQHGQrplarlarlG 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 232 LLKQNT-CVsdsaeflehfnaiptlftHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDG 310
Cdd:PRK09045  249 LLGPRLiAV------------------HMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGTDG 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 311 LSSNYKLDLFEEMKISLF----MHSDAPLLEfAKALLKGATLDAAKALGLN--TGEIAVGKNADMIVLDLDA---TPTPE 381
Cdd:PRK09045  311 AASNNDLDLFGEMRTAALlakaVAGDATALP-AHTALRMATLNGARALGLDdeIGSLEPGKQADLVAVDLSGletQPVYD 389
                         410       420
                  ....*....|....*....|...
gi 1277938128 382 LAIHLL--LHRYNVSKVYINGKL 402
Cdd:PRK09045  390 PVSQLVyaAGREQVSHVWVAGKQ 412
PRK15493 PRK15493
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
50-401 2.44e-24

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


Pssm-ID: 185390 [Multi-domain]  Cd Length: 435  Bit Score: 103.98  E-value: 2.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  50 KNSLLMPGLINAHVHLEFSANKthlSYGD---FISWLYSVIENRE-ELIGGCDTACMAQAIDSMLACGITTFGAV-SSHG 124
Cdd:PRK15493   53 KGKWVLPGLVNTHTHVVMSLLR---GIGDdmlLQPWLETRIWPLEsQFTPELAVASTELGLLEMVKSGTTSFSDMfNPIG 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 125 MDLQACADAPQNViffneliGSQATMADALFNdFSARLDASKSVT----------REG--FHTGVAIHSPYSVHPVLIKK 192
Cdd:PRK15493  130 VDQDAIMETVSRS-------GMRAAVSRTLFS-FGTKEDEKKAIEeaekyvkryyNESgmLTTMVAPHSPYTCSTELLEE 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 193 ALAIVKSEKLKLTAHFMESKAEREWLDKSEGDFK-EFFES--LLKQntcvsdsaeflehfnaiPTLFTHVVQANKSELST 269
Cdd:PRK15493  202 CARIAVENQTMVHIHLSETEREVRDIEAQYGKRPvEYAAScgLFKR-----------------PTVIAHGVVLNDNERAF 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 270 LAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFM----HSDAPLLEFAKAlLKG 345
Cdd:PRK15493  265 LAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEEMRIATLLqkgiHQDATALPVETA-LTL 343
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277938128 346 ATLDAAKALGL-NTGEIAVGKNADMIVLDLDATPTPELAIHLLLHRY------NVSKVYINGK 401
Cdd:PRK15493  344 ATKGAAEVIGMkQTGSLEVGKCADFITIDPSNKPHLQPADEVLSHLVyaasgkDISDVIINGK 406
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
49-374 1.71e-21

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 95.64  E-value: 1.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  49 AKNSLLMPGLINAHVHLEFSANKTHLSYGDFISWLYSVIENREELIGGCDTACMAQ-AIDSMLACGITTFGAVSSHgmdL 127
Cdd:PRK08393   47 ASGSVVSPGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPRERKLKRKDIYWGAYlGLLEMIKSGTTTFVDMYFH---M 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 128 QACADAPQNV----------IFFNELIGSQATMADAL-FNDFSARLDASKsvtregFHTGVAIHSPYSVHPVLIKKALAI 196
Cdd:PRK08393  124 EEVAKATLEVglrgylsygmVDLGDEEKREKEIKETEkLMEFIEKLNSPR------VHFVFGPHAPYTCSLALLKWVREK 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 197 VKSEKLKLTAHFMESKAEREWLDKSEGdfkeffesllKQNTCVSDSAEFLEHfnaiPTLFTHVVQANKSELSTLAKNGHT 276
Cdd:PRK08393  198 AREWNKLITIHLSETMDEIKQIREKYG----------KSPVVLLDEIGFLNE----DVIAAHGVWLSSRDIRILASAGVT 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 277 VIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMHSDA---PLLEFAKALLKGATLDAAKA 353
Cdd:PRK08393  264 VAHNPASNMKLGSGVMPLRKLLNAGVNVALGTDGAASNNNLDMLREMKLAALLHKVHnldPTIADAETVFRMATQNGAKA 343
                         330       340
                  ....*....|....*....|.
gi 1277938128 354 LGLNTGEIAVGKNADMIVLDL 374
Cdd:PRK08393  344 LGLKAGVIKEGYLADIAVIDF 364
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
6-400 5.34e-20

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: 91.19  E-value: 5.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128   6 PHFILMSDSIVTER--AIAFEKTILKIAPLEELL--QEFPHAKITTLaKNSLLMPGLINAHVHLEFSANkTHLSYGD-FI 80
Cdd:cd01303    12 PELELVEDALRVVEdgLIVVVDGNIIAAGAAETLkrAAKPGARVIDS-PNQFILPGFIDTHIHAPQYAN-IGSGLGEpLL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  81 SWL----------YSVIENREELIGGcdtacmaqAIDSMLACGITT---FGAVSSHGMDL--QACADAPQNVIffnelIG 145
Cdd:cd01303    90 DWLetytfpeeakFADPAYAREVYGR--------FLDELLRNGTTTacyFATIHPESTEAlfEEAAKRGQRAI-----AG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 146 SqaTMADALFNDFsaRLDASKSVTREG--FHTGVAIHSPySVHPVlIKKALAIVKSEKL-----KLTA---------HFM 209
Cdd:cd01303   157 K--VCMDRNAPEY--YRDTAESSYRDTkrLIERWHGKSG-RVKPA-ITPRFAPSCSEELlaalgKLAKehpdlhiqtHIS 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 210 ESKAEREWLdksegdfKEFFESllkqntcVSDSAEFLEHFNAI--PTLFTHVVQANKSELSTLAKNGHTVIHCPISNRLL 287
Cdd:cd01303   231 ENLDEIAWV-------KELFPG-------ARDYLDVYDKYGLLteKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFL 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 288 GNETLNIKELAENNIPWIVATDgLSSNYKLDLFEEM----KIS--LFMHSDAPLLEFAKALLKGATLDAAKALGLN--TG 359
Cdd:cd01303   297 GSGLFDVRKLLDAGIKVGLGTD-VGGGTSFSMLDTLrqayKVSrlLGYELGGHAKLSPAEAFYLATLGGAEALGLDdkIG 375
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1277938128 360 EIAVGKNADMIVLDLDATPTP--------ELAIHLLLHRY-----NVSKVYING 400
Cdd:cd01303   376 NFEVGKEFDAVVIDPSATPLLadrmfrveSLEEALFKFLYlgddrNIREVYVAG 429
Met_dep_hydrolase_E cd01313
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
51-401 1.81e-17

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: 83.66  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  51 NSLLMPGLINAHVHlEFS---ANKTHL---SYGDFISW---LYSVIE--NREELiggcdTACMAQAIDSMLACGITTFGA 119
Cdd:cd01313    37 GGALLPGMPNLHSH-AFQramAGLTEYrgsAADSFWTWrelMYRFAArlTPEQI-----EAIARQLYIEMLLAGITAVGE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 120 V-----SSHGMDLQACADAPQNVIFFNELIGSQATMADALF---------------------NDFSARLDASKSVTREGF 173
Cdd:cd01313   111 FhyvhhDPDGTPYADPAELAQRVIAAASDAGIGITLLPVLYaragfggpapnpgqrrfingyEDFLGLLEKALRAVKEHA 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 174 HT--GVAIHSPYSVHPVLIKKALAIVkSEKLKLTAHFMESKAEREWLDKSEGDFKEffeSLLKQNTCVSdsaeflEHFNA 251
Cdd:cd01313   191 AAriGVAPHSLRAVPAEQLAALAALA-SEKAPVHIHLAEQPKEVDDCLAAHGRRPV---ELLLDHGHLD------ARWCL 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 252 IptlftHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDglsSNYKLDLFEEMKISLF--- 328
Cdd:cd01313   261 V-----HATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSD---SNARIDLLEELRQLEYsqr 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 329 --------MHSDAPLLefAKALLKGATLDAAKALGLNTGEIAVGKNADMIVLDLD----ATPTPELAIHLLL---HRYNV 393
Cdd:cd01313   333 lrdrarnvLATAGGSS--ARALLDAALAGGAQALGLATGALEAGARADLLSLDLDhpslAGALPDTLLDAWVfaaGDREV 410

                  ....*...
gi 1277938128 394 SKVYINGK 401
Cdd:cd01313   411 RDVVVGGR 418
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
258-401 4.78e-17

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 82.35  E-value: 4.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 258 HVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMH---SDAP 334
Cdd:PRK07228  255 HCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGADGAPCNNTLDPFTEMRQAALIQkvdRLGP 334
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277938128 335 LLEFAKALLKGATLDAAKALGL--NTGEIAVGKNADMIVLDLD---ATPTPELAI--HLLL--HRYNVSKVYINGK 401
Cdd:PRK07228  335 TAMPARTVFEMATLGGAKAAGFedEIGSLEEGKKADLAILDLDglhATPSHGVDVlsHLVYaaHGSDVETTMVDGK 410
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
58-353 3.75e-15

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: 75.06  E-value: 3.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  58 LINAHVHLEFSANKTHLSYGDFISWLYSVIENREELIggcdtacmAQAIDSMLACGITTFGAVSSHGMDLQACADAPQNV 137
Cdd:cd01292     1 FIDTHVHLDGSALRGTRLNLELKEAEELSPEDLYEDT--------LRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 138 IFFNELIGSQATMADALFNDFSARLDASKSVTRE--------GFHtGVAIHSPYSVHPV---LIKKALAIVKSEKLKLTA 206
Cdd:cd01292    73 EAARASAGIRVVLGLGIPGVPAAVDEDAEALLLEllrrglelGAV-GLKLAGPYTATGLsdeSLRRVLEEARKLGLPVVI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 207 HFMESKAEREwldksegDFKEFFESLLKQNTCVsdsaeflehfnaiptlFTHVVQANKSELSTLAKNGHTVIHCPISNRL 286
Cdd:cd01292   152 HAGELPDPTR-------ALEDLVALLRLGGRVV----------------IGHVSHLDPELLELLKEAGVSLEVCPLSNYL 208
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 287 LGNE---TLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMHSdapLLEFAKALLKGATLDAAKA 353
Cdd:cd01292   209 LGRDgegAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLR---LGLSLEEALRLATINPARA 275
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
12-402 2.54e-14

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 73.84  E-value: 2.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  12 SDSIVTERAIAFEK-TILKIAPLEELlqEFPHAKITTLAKNSLLMPGLINAHVHLEFSANKTH-LSYGDFISWLYSVIEN 89
Cdd:COG1228    22 GGGVIENGTVLVEDgKIAAVGPAADL--AVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVeFEAGGGITPTVDLVNP 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  90 reeliggcdtacMAQAIDSMLACGITTfgavsshgmdlqaCADAPqnviffneliGSQATMADALfndfsarlDASKSVT 169
Cdd:COG1228   100 ------------ADKRLRRALAAGVTT-------------VRDLP----------GGPLGLRDAI--------IAGESKL 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 170 REG---FHTGVAIHSPYSVHPVLIKKALAIVKsEKLKLTAHFMESKAEREWLDKSEGDFKEFFESllkqntcvsdsaefl 246
Cdd:COG1228   137 LPGprvLAAGPALSLTGGAHARGPEEARAALR-ELLAEGADYIKVFAEGGAPDFSLEELRAILEA--------------- 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 247 EHFNAIPtLFTHVVQAnkSELSTLAKNGHTVI-HCPisnrLLGNETlnIKELAENNIPWIVATDGLSSNYKLDLFEEMKI 325
Cdd:COG1228   201 AHALGLP-VAAHAHQA--DDIRLAVEAGVDSIeHGT----YLDDEV--ADLLAEAGTVVLVPTLSLFLALLEGAAAPVAA 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 326 SLF---------------------MHSDAP---------LLEFAKAL---------LKGATLDAAKALGL--NTGEIAVG 364
Cdd:COG1228   272 KARkvreaalanarrlhdagvpvaLGTDAGvgvppgrslHRELALAVeagltpeeaLRAATINAAKALGLddDVGSLEPG 351
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1277938128 365 KNADMIVLDLDatPTPELAihlllHRYNVSKVYINGKL 402
Cdd:COG1228   352 KLADLVLLDGD--PLEDIA-----YLEDVRAVMKDGRV 382
PRK12393 PRK12393
amidohydrolase; Provisional
256-376 1.06e-12

amidohydrolase; Provisional


Pssm-ID: 237088 [Multi-domain]  Cd Length: 457  Bit Score: 69.33  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 256 FTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEEMKISLFMH----- 330
Cdd:PRK12393  272 FAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDGAASNESADMLSEAHAAWLLHraegg 351
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1277938128 331 SDAPLLEfakALLKGATLDAAKALGLN-TGEIAVGKNADMIVLDLDA 376
Cdd:PRK12393  352 ADATTVE---DVVHWGTAGGARVLGLDaIGTLAVGQAADLAIYDLDD 395
PRK09229 PRK09229
N-formimino-L-glutamate deiminase; Validated
258-401 1.17e-11

N-formimino-L-glutamate deiminase; Validated


Pssm-ID: 236420 [Multi-domain]  Cd Length: 456  Bit Score: 66.03  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 258 HVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDglsSNYKLDLFEEMKislfmhsdapLLE 337
Cdd:PRK09229  271 HATHLTDAETARLARSGAVAGLCPTTEANLGDGIFPAVDYLAAGGRFGIGSD---SHVSIDLVEELR----------LLE 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 338 F--------------------AKALLKGATLDAAKALGLNTGEIAVGKNADMIVLDLDATPTPELAIHLLLHRY------ 391
Cdd:PRK09229  338 YgqrlrdrrrnvlaaaaqpsvGRRLFDAALAGGAQALGRAIGGLAVGARADLVVLDLDHPALAGREGDALLDRWvfaggd 417
                         170
                  ....*....|.
gi 1277938128 392 -NVSKVYINGK 401
Cdd:PRK09229  418 aAVRDVWVAGR 428
PRK09228 PRK09228
guanine deaminase; Provisional
27-379 3.74e-10

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 61.36  E-value: 3.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  27 ILKIAPLEELLQEFP-HAKITTLaKNSLLMPGLINAHVH---LEFSAnkthlSYGD-FISWLysviENR---EEliggCD 98
Cdd:PRK09228   41 IVAAGPYAELRAQLPaDAEVTDY-RGKLILPGFIDTHIHypqTDMIA-----SYGEqLLDWL----NTYtfpEE----RR 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  99 TACMAQA-------IDSMLACGITT---FGavSSHgmdlQACADApqnviFFNE-------LIGSQATM----ADALFND 157
Cdd:PRK09228  107 FADPAYArevaeffLDELLRNGTTTalvFG--TVH----PQSVDA-----LFEAaearnmrMIAGKVLMdrnaPDGLRDT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 158 FSARLDASKSVTREgFH----TGVAI---HSPYSVHPVLikKALAIVKSEK--LKLTAHFMESKAEREWLdksegdfKEF 228
Cdd:PRK09228  176 AESGYDDSKALIER-WHgkgrLLYAItprFAPTSTPEQL--EAAGALAREHpdVWIQTHLSENLDEIAWV-------KEL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 229 FesllkqntcvSDSAEFL---EHFNAI--PTLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIP 303
Cdd:PRK09228  246 F----------PEARDYLdvyERYGLLgpRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVR 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 304 WIVATD--GLSSnykLDLFEEM----KIS-LFMHSDAPLlefakALLKGATLDAAKALGLN--TGEIAVGKNADMIVLDL 374
Cdd:PRK09228  316 VGLGTDvgGGTS---FSMLQTMneayKVQqLQGYRLSPF-----QAFYLATLGGARALGLDdrIGNLAPGKEADFVVLDP 387

                  ....*
gi 1277938128 375 DATPT 379
Cdd:PRK09228  388 AATPL 392
PRK07203 PRK07203
putative aminohydrolase SsnA;
20-401 7.77e-10

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 60.33  E-value: 7.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  20 AIAFE-KTILKIAPLEELLQEFPHAKITTlAKNSLLMPGLINAHVHLeFSAnkthLSYG---------DFISwlysVIEN 89
Cdd:PRK07203   23 AIAIEgNVIVEIGTTDELKAKYPDAEFID-AKGKLIMPGLINSHNHI-YSG----LARGmmanippppDFIS----ILKN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  90 ---------REELIGGCDTACMAQAIDsmlaCGITTFgavsshgMDLQACadapqnvifFNELIGSQATMADALFN---- 156
Cdd:PRK07203   93 lwwrldralTLEDVYYSALICSLEAIK----NGVTTV-------FDHHAS---------PNYIGGSLFTIADAAKKvglr 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 157 ------------------------DFSARLDASKSVTREGfHTGvaIHSPYSVHPVLIKKALAIVKSEKLKLTAHFMESK 212
Cdd:PRK07203  153 amlcyetsdrdgekelqegveeniRFIKHIDEAKDDMVEA-MFG--LHASFTLSDATLEKCREAVKETGRGYHIHVAEGI 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 213 AEREwldksegdfkeffESLLKQNTcvsDSAEFLEHFNAI--PTLFTHVVQANKSELSTLAKNGHTVIHCPISNrlLGNE 290
Cdd:PRK07203  230 YDVS-------------DSHKKYGK---DIVERLADFGLLgeKTLAAHCIYLSDEEIDLLKETDTFVVHNPESN--MGNA 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 291 --TLNIKELAENNIPWIVATDGlssnYKLDLFEEMKISLFMHSDA--PLLE-----FAKALLKGATLdAAKALGLNTGEI 361
Cdd:PRK07203  292 vgYNPVLEMIKNGILLGLGTDG----YTSDMFESYKVANFKHKHAggDPNVgwpesPAMLFENNNKI-AERYFGAKFGIL 366
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1277938128 362 AVGKNADMIVLDLDAtPTP----ELAIHLL--LHRYNVSKVYINGK 401
Cdd:PRK07203  367 EEGAKADLIIVDYNP-PTPlnedNINGHILfgMNGGSVDTTIVNGK 411
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
176-401 7.66e-09

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 57.17  E-value: 7.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 176 GVAIHSPYSVHPVLIKKALAIVKSEKLKLTAHFMESkaerewLDksEGDFkeffesllkqntCvsdsaefLEHFNAIP-- 253
Cdd:PRK08203  202 ALAPCSPFSVSRELMRESAALARRLGVRLHTHLAET------LD--EEAF------------C-------LERFGMRPvd 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 254 -----------TLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNYKLDLFEE 322
Cdd:PRK08203  255 yledlgwlgpdVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDGSASNDGSNLIGE 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 323 MKISLFMhsdAPLLEFAKAL-----LKGATLDAAKALGLN-TGEIAVGKNADMIVLDLDatptpELA---IH-----LLL 388
Cdd:PRK08203  335 ARQALLL---QRLRYGPDAMtareaLEWATLGGARVLGRDdIGSLAPGKLADLALFDLD-----ELRfagAHdpvaaLVL 406
                         250
                  ....*....|....*.
gi 1277938128 389 ---HRynVSKVYINGK 401
Cdd:PRK08203  407 cgpPR--ADRVMVGGR 420
archeal_chlorohydrolases cd01305
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ...
53-353 9.66e-08

Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. They have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. Some members of this subgroup are predicted to be chlorohyrolases.


Pssm-ID: 238630 [Multi-domain]  Cd Length: 263  Bit Score: 52.79  E-value: 9.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  53 LLMPGLINAHVHLefsankthlsyGDFIswLYSVIENR--EELIGGCDTA---CMAQAIDSMLACGITTFgAVSSHGMDL 127
Cdd:cd01305     1 ILIPALVNAHTHL-----------GDSA--IKEVGDGLplDDLVAPPDGLkhrLLAQADDRELAEAMRKV-LRDMRETGI 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 128 QACADAPQNVIFFNELIGSQATMADALFNDFSARLDASKSVTREGFHT-GVAIHSPYSVHpvlIKKALAIVKSEKLKLTA 206
Cdd:cd01305    67 GAFADFREGGVEGIELLRRALGKLPVPFEVILGRPTEPDDPEILLEVAdGLGLSSANDVD---LEDILELLRRRGKLFAI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 207 HFMESKAEREWLDksegdfkefFESLLKqntcvsdsaefLEhfnaiPTLFTHVVQANKSELSTLAKNGHTVIHCPISNRL 286
Cdd:cd01305   144 HASETRESVGMTD---------IERALD-----------LE-----PDLLVHGTHLTDEDLELVRENGVPVVLCPRSNLY 198
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277938128 287 LGNETLNIKELAENNIPWIVATDGLSSNyKLDLFEEMKislFMH--SDAPLLEFAKALLKGATLDAAKA 353
Cdd:cd01305   199 FGVGIPPVAELLKLGIKVLLGTDNVMVN-EPDMWAEME---FLAkySRLQGYLSPLEILRMATVNAAEF 263
PRK07213 PRK07213
chlorohydrolase; Provisional
253-371 1.09e-07

chlorohydrolase; Provisional


Pssm-ID: 235969 [Multi-domain]  Cd Length: 375  Bit Score: 53.50  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 253 PTLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENNIPWIVATDGLSSNyKLDLFEEMKISL-FMHS 331
Cdd:PRK07213  228 PDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMLEKGILLGIGTDNFMAN-SPSIFREMEFIYkLYHI 306
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1277938128 332 DApllefaKALLKGATLDAAKALGL-NTGEIAVGKNADMIV 371
Cdd:PRK07213  307 EP------KEILKMATINGAKILGLiNVGLIEEGFKADFTF 341
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
27-400 5.71e-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: 51.10  E-value: 5.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  27 ILKIAPLEELLQEFPHAKITTLAKNSLLMPGLINAHVHLEFSANKTH--------LSYGDfISW-----LYSVIENREEl 93
Cdd:cd01296     8 IAAVGPAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDefaarlagASYEE-ILAagggiLSTVRATRAA- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128  94 iggCDTACMAQA---IDSMLACGITTFGAVSSHGMDLQacadapqnviffNELigsqaTMADALfndfsARLDASKSVT- 169
Cdd:cd01296    86 ---SEDELFASAlrrLARMLRHGTTTVEVKSGYGLDLE------------TEL-----KMLRVI-----RRLKEEGPVDl 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 170 REGFHTGVAIHSPYSVHP----VLIKKALAIVKSEKLkltAHFMESKAErewldksEGDFKeffesllkqntcVSDSAEF 245
Cdd:cd01296   141 VSTFLGAHAVPPEYKGREeyidLVIEEVLPAVAEENL---ADFCDVFCE-------KGAFS------------LEQSRRI 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 246 L--------------EHFNAIP----------TLFTHVVQANKSELSTLAKNGHTVIHCPISNRLLGNETLNIKELAENN 301
Cdd:cd01296   199 LeaakeaglpvkihaDELSNIGgaelaaelgaLSADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAG 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 302 IPWIVATDGLSSNYKLDlfeemKISLFMHsdaplleFAKALLK--------GATLDAAKALGL--NTGEIAVGKNADMIV 371
Cdd:cd01296   279 VPVALGTDFNPGSSPTS-----SMPLVMH-------LACRLMRmtpeealtAATINAAAALGLgeTVGSLEVGKQADLVI 346
                         410       420       430
                  ....*....|....*....|....*....|
gi 1277938128 372 LDldaTPTP-ELAIHLLLHryNVSKVYING 400
Cdd:cd01296   347 LD---APSYeHLAYRFGVN--LVEYVIKNG 371
PRK08204 PRK08204
hypothetical protein; Provisional
318-406 2.16e-06

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 49.62  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 318 DLFEEMKISLFMH----------------SDAPLLefAKALLKGATLDAAKALGLN--TGEIAVGKNADMIVL---DLDA 376
Cdd:PRK08204  309 DMFTQMRFALQAErardnavhlreggmppPRLTLT--ARQVLEWATIEGARALGLEdrIGSLTPGKQADLVLIdatDLNL 386
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1277938128 377 TPT--PELAIHLLLHRYNVSKVYINGKLEKGN 406
Cdd:PRK08204  387 APVhdPVGAVVQSAHPGNVDSVMVAGRAVKRN 418
Amidohydro_3 pfam07969
Amidohydrolase family;
294-401 1.70e-05

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 46.76  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 294 IKELAENNIPWIVATDGLssnykLDLFEEMK--ISLFMHSDAPLLEFAKA--------LLKGATLDAAKALGL--NTGEI 361
Cdd:pfam07969 351 VKELLNAGVKVALGSDAP-----VGPFDPWPriGAAVMRQTAGGGEVLGPdeelsleeALALYTSGPAKALGLedRKGTL 425
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1277938128 362 AVGKNADMIVLDLDATPTPELAIHLLLhrynVSKVYINGK 401
Cdd:pfam07969 426 GVGKDADLVVLDDDPLTVDPPAIADIR----VRLTVVDGR 461
PRK06151 PRK06151
N-ethylammeline chlorohydrolase; Provisional
267-376 2.20e-05

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180428 [Multi-domain]  Cd Length: 488  Bit Score: 46.57  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 267 LSTLAKNGHTVIHCPI-SNRllGNETLN-IKELAENNIPWIVATDglssNYKLDLFEEMKISLfMH-------SDAPlle 337
Cdd:PRK06151  295 LALLAEHGVSIVHCPLvSAR--HGSALNsFDRYREAGINLALGTD----TFPPDMVMNMRVGL-ILgrvvegdLDAA--- 364
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1277938128 338 FAKALLKGATLDAAKALGL-NTGEIAVGKNADMIVLDLDA 376
Cdd:PRK06151  365 SAADLFDAATLGGARALGRdDLGRLAPGAKADIVVFDLDG 404
PLN02795 PLN02795
allantoinase
6-65 2.93e-05

allantoinase


Pssm-ID: 178392 [Multi-domain]  Cd Length: 505  Bit Score: 45.92  E-value: 2.93e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277938128   6 PHFILMSDSIVTERAI---AFE---KTILKIAPLEELLQEFPHAKITTLaKNSLLMPGLINAHVHL 65
Cdd:PLN02795   44 PHFVLYSKRVVTPAGVipgAVEvegGRIVSVTKEEEAPKSQKKPHVLDY-GNAVVMPGLIDVHVHL 108
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
295-402 8.08e-05

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: 44.22  E-value: 8.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 295 KELAENNIPWIVATDgLSSNYKLDLFEE-------------MKISLfmHSDAP-------LLEFAKAL---------LKG 345
Cdd:cd01309   232 DELAKHGIPVIYGPT-LTLPKKVEEVNDaidtnayllkkggVAFAI--SSDHPvlnirnlNLEAAKAVkyglsyeeaLKA 308
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277938128 346 ATLDAAKALGLN--TGEIAVGKNADMIVLD---LDATPTPELaihlllhrynvskVYINGKL 402
Cdd:cd01309   309 ITINPAKILGIEdrVGSLEPGKDADLVVWNgdpLEPTSKPEQ-------------VYIDGRL 357
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
346-401 2.23e-04

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 43.16  E-value: 2.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1277938128 346 ATLDAAKALGL--NTGEIAVGKNADMIVLDldatptpelaihlllHRYNVSKVYINGK 401
Cdd:COG1820   331 ASLNPARALGLddRKGSIAPGKDADLVVLD---------------DDLNVRATWVGGE 373
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
343-400 2.24e-04

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


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 42.95  E-value: 2.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277938128 343 LKGATLDAAKALGLN--TGEIAVGKNADMIVLDLDatptpelaihlllhrYNVSKVYING 400
Cdd:cd00854   330 VRMASLNPAKLLGLDdrKGSLKPGKDADLVVLDDD---------------LNVKATWING 374
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
343-401 2.44e-04

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 43.25  E-value: 2.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277938128 343 LKGATLDAAKALGL--NTGEIAVGKNADMIVLDLDATPTPELAIHLLlhryNVSKVYINGK 401
Cdd:COG1574   473 LRAYTIGAAYAAFEedEKGSLEPGKLADFVVLDRDPLTVPPEEIKDI----KVLLTVVGGR 529
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
343-375 2.41e-03

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


Pssm-ID: 238624 [Multi-domain]  Cd Length: 342  Bit Score: 39.58  E-value: 2.41e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1277938128 343 LKGATLDAAKALGL--NTGEIAVGKNADMIVLDLD 375
Cdd:cd01299   300 LRAATANAAELLGLsdELGVIEAGKLADLLVVDGD 334
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
346-402 3.34e-03

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 39.70  E-value: 3.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1277938128 346 ATLDAAKALGL-NTGEIAVGKNADMIVLDlDatptpelaihllLHRYNVSKVYINGKL 402
Cdd:COG1001   293 ATLNAAEHFGLkDLGAIAPGRRADIVLLD-D------------LEDFKVEKVYADGKL 337
 
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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