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Conserved domains on  [gi|2720677831|ref|WP_342028483|]
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MULTISPECIES: amidohydrolase family protein [Mesorhizobium]

Protein Classification

amidohydrolase family protein( domain architecture ID 330)

metal-dependent amidohydrolase family protein having a conserved metal binding site, usually involving four histidines and one aspartic acid residue

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-dependent_hydrolases super family cl00281
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 10-152 4.77e-33

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.


The actual alignment was detected with superfamily member cd01299:

Pssm-ID: 469705 [Multi-domain]  Cd Length: 342  Bit Score: 119.32  E-value: 4.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  10 IEHGNLIKATTANRVREAGAFVVPTNITFAVVARDGARYGMSAESLEKVSFVLDAGLSALETLQSAGVTMGYGSDLL--G 87
Cdd:cd01299   197 IEHGFLIDDETIELMKEKGIFLVPTLATYEALAAEGAAPGLPADSAEKVALVLEAGRDALRRAHKAGVKIAFGTDAGfpV 276

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2720677831  88 QMHRHQSEEFLLRGRVLK-PRDVIRSATVDAARVLNMEGLIGTIAPGAHADLIAVYGNPLKDLAIL 152
Cdd:cd01299   277 PPHGWNARELELLVKAGGtPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDGDPLEDIAVL 342
 
Name Accession Description Interval E-value
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 10-152 4.77e-33

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: 119.32  E-value: 4.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  10 IEHGNLIKATTANRVREAGAFVVPTNITFAVVARDGARYGMSAESLEKVSFVLDAGLSALETLQSAGVTMGYGSDLL--G 87
Cdd:cd01299   197 IEHGFLIDDETIELMKEKGIFLVPTLATYEALAAEGAAPGLPADSAEKVALVLEAGRDALRRAHKAGVKIAFGTDAGfpV 276

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2720677831  88 QMHRHQSEEFLLRGRVLK-PRDVIRSATVDAARVLNMEGLIGTIAPGAHADLIAVYGNPLKDLAIL 152
Cdd:cd01299   277 PPHGWNARELELLVKAGGtPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDGDPLEDIAVL 342
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 10-165 2.01e-25

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 100.04  E-value: 2.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  10 IEHGNLIKATTANRVREAG-AFVVPTnitfaVVARDGARYGMSAESLEKVSFVLDAGLSALETLQSAGVTMGYGSDLLGQ 88
Cdd:COG1228   229 IEHGTYLDDEVADLLAEAGtVVLVPT-----LSLFLALLEGAAAPVAAKARKVREAALANARRLHDAGVPVALGTDAGVG 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  89 MH--RHQSEEFLLRGRV-LKPRDVIRSATVDAARVLNMEGLIGTIAPGAHADLIAVYGNPLKDLAILSDParlRKIIKGG 165
Cdd:COG1228   304 VPpgRSLHRELALAVEAgLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAYLEDV---RAVMKDG 380
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 24-165 2.16e-12

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: 63.29  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  24 VREAGAFVVPTNITFAVVARDGARYGMSAESLEKvsfvLDAGLSALETLQSAGVTMGYGSDLLGQMH--------RHQSE 95
Cdd:pfam01979 186 ILAHGVHLSPTEANLLAEHLKGAGVAHCPFSNSK----LRSGRIALRKALEDGVKVGLGTDGAGSGNslnmleelRLALE 261

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  96 EFLLRGRVLKPRDVIRSATVDAARVLNMEGLIGTIAPGAHADLIAVYGNPLKDLAILSDPARLRKIIKGG 165
Cdd:pfam01979 262 LQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKKVIVKG 331
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
62-141 4.76e-07

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 48.37  E-value: 4.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  62 LDAGLSALETLQSAGVTMGYGSD---------LLGQMhRHQSeefLL------RGRVLKPRDVIRSATVDAARVLNMEGL 126
Cdd:PRK09045  287 LASGFCPVAKLLQAGVNVALGTDgaasnndldLFGEM-RTAA---LLakavagDATALPAHTALRMATLNGARALGLDDE 362

                          90
                  ....*....|....*
gi 2720677831 127 IGTIAPGAHADLIAV 141
Cdd:PRK09045  363 IGSLEPGKQADLVAV 377
 
Name Accession Description Interval E-value
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 10-152 4.77e-33

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: 119.32  E-value: 4.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  10 IEHGNLIKATTANRVREAGAFVVPTNITFAVVARDGARYGMSAESLEKVSFVLDAGLSALETLQSAGVTMGYGSDLL--G 87
Cdd:cd01299   197 IEHGFLIDDETIELMKEKGIFLVPTLATYEALAAEGAAPGLPADSAEKVALVLEAGRDALRRAHKAGVKIAFGTDAGfpV 276

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2720677831  88 QMHRHQSEEFLLRGRVLK-PRDVIRSATVDAARVLNMEGLIGTIAPGAHADLIAVYGNPLKDLAIL 152
Cdd:cd01299   277 PPHGWNARELELLVKAGGtPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDGDPLEDIAVL 342
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 10-165 2.01e-25

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 100.04  E-value: 2.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  10 IEHGNLIKATTANRVREAG-AFVVPTnitfaVVARDGARYGMSAESLEKVSFVLDAGLSALETLQSAGVTMGYGSDLLGQ 88
Cdd:COG1228   229 IEHGTYLDDEVADLLAEAGtVVLVPT-----LSLFLALLEGAAAPVAAKARKVREAALANARRLHDAGVPVALGTDAGVG 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  89 MH--RHQSEEFLLRGRV-LKPRDVIRSATVDAARVLNMEGLIGTIAPGAHADLIAVYGNPLKDLAILSDParlRKIIKGG 165
Cdd:COG1228   304 VPpgRSLHRELALAVEAgLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAYLEDV---RAVMKDG 380
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 24-165 2.16e-12

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: 63.29  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  24 VREAGAFVVPTNITFAVVARDGARYGMSAESLEKvsfvLDAGLSALETLQSAGVTMGYGSDLLGQMH--------RHQSE 95
Cdd:pfam01979 186 ILAHGVHLSPTEANLLAEHLKGAGVAHCPFSNSK----LRSGRIALRKALEDGVKVGLGTDGAGSGNslnmleelRLALE 261

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  96 EFLLRGRVLKPRDVIRSATVDAARVLNMEGLIGTIAPGAHADLIAVYGNPLKDLAILSDPARLRKIIKGG 165
Cdd:pfam01979 262 LQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKKVIVKG 331
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
9-165 4.60e-11

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 59.81  E-value: 4.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831   9 RIEHGNLIKATTANRVREAGAFVVPtNITFAVVARDGARYGMSAESLekvsfvldAGLSALETLQSAGVTMGYGSD---- 84
Cdd:COG1574   369 RIEHAQLVDPDDLARFAELGVIASM-QPTHATSDGDWAEDRLGPERA--------ARAYPFRSLLDAGAPLAFGSDapve 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  85 ----LLGqMH---RHQSEEfllrGRVLKP------RDVIRSATVDAARVLNMEGLIGTIAPGAHADLIAVYGNPLKdlai 151
Cdd:COG1574   440 pldpLLG-IYaavTRRTPS----GRGLGPeerltvEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLT---- 510

                         170
                  ....*....|....*....
gi 2720677831 152 lSDPARLRKI-----IKGG 165
Cdd:COG1574   511 -VPPEEIKDIkvlltVVGG 528
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 65-141 2.48e-10

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: 57.53  E-value: 2.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  65 GLSALETLQSAGVTMGYGSD---------LLGQM------HRHQSeeflLRGRVLKPRDVIRSATVDAARVLNMEGLIGT 129
Cdd:COG0402   290 GIAPVPRLLAAGVRVGLGTDgaasnnsldMFEEMrlaallQRLRG----GDPTALSAREALEMATLGGARALGLDDEIGS 365

                          90
                  ....*....|..
gi 2720677831 130 IAPGAHADLIAV 141
Cdd:COG0402   366 LEPGKRADLVVL 377
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 72-141 8.25e-08

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: 50.28  E-value: 8.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  72 LQSAGVTMGYG---------SDLLGQM------HRHQSeeflLRGRVLKPRDVIRSATVDAARVLNMEGlIGTIAPGAHA 136
Cdd:cd01298   289 MLEAGVNVGLGtdgaasnnnLDMFEEMrlaallQKLAH----GDPTALPAEEALEMATIGGAKALGLDE-IGSLEVGKKA 363


                  ....*
gi 2720677831 137 DLIAV 141
Cdd:cd01298   364 DLILI 368
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
62-141 4.76e-07

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 48.37  E-value: 4.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  62 LDAGLSALETLQSAGVTMGYGSD---------LLGQMhRHQSeefLL------RGRVLKPRDVIRSATVDAARVLNMEGL 126
Cdd:PRK09045  287 LASGFCPVAKLLQAGVNVALGTDgaasnndldLFGEM-RTAA---LLakavagDATALPAHTALRMATLNGARALGLDDE 362

                          90
                  ....*....|....*
gi 2720677831 127 IGTIAPGAHADLIAV 141
Cdd:PRK09045  363 IGSLEPGKQADLVAV 377
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 9-139 2.88e-06

YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 45.76  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831   9 RIEHGNLIKATTANRVREAGAFVVpTNITFAvvARDGARYGMSAESLEKVSFvldagLSALETLQSAGVTMGYGSD---- 84
Cdd:cd01300   343 RIEHAQLVSPDDIPRFAKLGVIAS-VQPNHL--YSDGDAAEDRRLGEERAKR-----SYPFRSLLDAGVPVALGSDapva 414

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2720677831  85 ----LLGqMH----RHQSEEFLLRGR--VLKPRDVIRSATVDAARVLNMEGLIGTIAPGAHADLI 139
Cdd:cd01300   415 ppdpLLG-IWaavtRKTPGGGVLGNPeeRLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFV 478
PRK08204 PRK08204
hypothetical protein; Provisional
 82-156 2.97e-06

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 45.76  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  82 GSDLLGQM------HR------HQSEEFLLRGRV-LKPRDVIRSATVDAARVLNMEGLIGTIAPGAHADLIAVYGNPLkD 148
Cdd:PRK08204  307 GGDMFTQMrfalqaERardnavHLREGGMPPPRLtLTARQVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDATDL-N 385


                  ....*...
gi 2720677831 149 LAILSDPA 156
Cdd:PRK08204  386 LAPVHDPV 393
Amidohydro_3 pfam07969
Amidohydrolase family;
9-165 1.29e-05

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 44.06  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831   9 RIEHGNLIKATT---ANRVREAGAFV-VPTNITFAVVARDGARYGMSAeslekvsfvlDAGLSALETLQSAGVTMGYGSD 84
Cdd:pfam07969 297 RIEHAQGVVPYTysqIERVAALGGAAgVQPVFDPLWGDWLQDRLGAER----------ARGLTPVKELLNAGVKVALGSD 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  85 LLGQ------------MHR-HQSEEFLLRGRVLKPRDVIRSATVDAARVLNMEGLIGTIAPGAHADLIAVYGNPLKdlai 151
Cdd:pfam07969 367 APVGpfdpwprigaavMRQtAGGGEVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLT---- 442

                         170
                  ....*....|....*....
gi 2720677831 152 lSDPARLRKI-----IKGG 165
Cdd:pfam07969 443 -VDPPAIADIrvrltVVDG 460
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 60-141 1.68e-05

Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.


Pssm-ID: 238628 [Multi-domain]  Cd Length: 429  Bit Score: 43.81  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  60 FVLDAGLSALETLQSAGVTMGYGSDLLG-------QMHRH-----QSEEFLLRGRV-LKPRDVIRSATVDAARVLNMEGL 126
Cdd:cd01303   294 LFLGSGLFDVRKLLDAGIKVGLGTDVGGgtsfsmlDTLRQaykvsRLLGYELGGHAkLSPAEAFYLATLGGAEALGLDDK 373

                          90
                  ....*....|....*
gi 2720677831 127 IGTIAPGAHADLIAV 141
Cdd:cd01303   374 IGNFEVGKEFDAVVI 388
PRK12394 PRK12394
metallo-dependent hydrolase;
108-138 2.42e-05

metallo-dependent hydrolase;


Pssm-ID: 183497 [Multi-domain]  Cd Length: 379  Bit Score: 43.21  E-value: 2.42e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2720677831 108 DVIRSATVDAARVLNMEGLIGTIAPGAHADL 138
Cdd:PRK12394  305 DVINACTHTPAVLMGMAAEIGTLAPGAFADI 335
PRK09228 PRK09228
guanine deaminase; Provisional
 62-141 6.00e-05

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 42.10  E-value: 6.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  62 LDAGLSALETLQSAGVTMGYGSDLLG----QMHRHQSEEFL---LRGRVLKPRDVIRSATVDAARVLNMEGLIGTIAPGA 134
Cdd:PRK09228  299 LGSGLFDLKRADAAGVRVGLGTDVGGgtsfSMLQTMNEAYKvqqLQGYRLSPFQAFYLATLGGARALGLDDRIGNLAPGK 378


                  ....*..
gi 2720677831 135 HADLIAV 141
Cdd:PRK09228  379 EADFVVL 385
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 104-147 8.64e-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: 41.53  E-value: 8.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2720677831 104 LKPRDVIRSATVDAARVLNMEGLIGTIAPGAHADLIAVYGNPLK 147
Cdd:cd01309   300 LSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLE 343
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
108-141 8.43e-04

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 38.54  E-value: 8.43e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2720677831 108 DVIRSATVDAARVLNMEGLIGTIAPGAHADLIAV 141
Cdd:COG1820   326 EAVRMASLNPARALGLDDRKGSIAPGKDADLVVL 359
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 104-165 9.47e-04

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: 38.39  E-value: 9.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2720677831 104 LKPRDVIRSATVDAARVLNMEGLIGTIAPGAHADLIAVYGNPLKDLAILSDPARLRKIIKGG 165
Cdd:cd01296   310 MTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNLVEYVIKNG 371
PRK07213 PRK07213
chlorohydrolase; Provisional
 62-147 2.03e-03

chlorohydrolase; Provisional


Pssm-ID: 235969 [Multi-domain]  Cd Length: 375  Bit Score: 37.32  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2720677831  62 LDAGLSALETLQSAGVTMGYGSD--------LLGQMhrhqseEFLLRGRVLKPRDVIRSATVDAARVLNMEGLiGTIAPG 133
Cdd:PRK07213  262 FNVGLPPLNEMLEKGILLGIGTDnfmanspsIFREM------EFIYKLYHIEPKEILKMATINGAKILGLINV-GLIEEG 334

                          90
                  ....*....|....
gi 2720677831 134 AHADLIAVYGNPLK 147
Cdd:PRK07213  335 FKADFTFIKPTNIK 348
AdeC cd01295
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ...
 104-153 4.60e-03

Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.


Pssm-ID: 238620 [Multi-domain]  Cd Length: 422  Bit Score: 36.43  E-value: 4.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2720677831 104 LKPRDVIRSATVDAARVLNMEGLiGTIAPGAHADLIAVygNPLKDLAILS 153
Cdd:cd01295   235 IPPEDAIQMATINPAECYGLHDL-GAIAPGRIADIVIL--DDLENFNITT 281
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
104-165 7.36e-03

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 35.85  E-value: 7.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2720677831 104 LKPRDVIRSATVDAARVLNMEGLiGTIAPGAHADLIAVygNPLKDLAIlsdparlRKIIKGG 165
Cdd:COG1001   284 LDPVTAIQMATLNAAEHFGLKDL-GAIAPGRRADIVLL--DDLEDFKV-------EKVYADG 335
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
103-141 8.96e-03

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 35.75  E-value: 8.96e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2720677831 103 VLKPRDVIRSATVDAARVLNMEGLIGTIAPGAHADLIAV 141
Cdd:PRK07228  336 AMPARTVFEMATLGGAKAAGFEDEIGSLEEGKKADLAIL 374
PRK12393 PRK12393
amidohydrolase; Provisional
 108-165 9.99e-03

amidohydrolase; Provisional


Pssm-ID: 237088 [Multi-domain]  Cd Length: 457  Bit Score: 35.43  E-value: 9.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2720677831 108 DVIRSATVDAARVLNMEGlIGTIAPGAHADLiAVYG------NPLKDLAI----LSDPARLRKIIKGG 165
Cdd:PRK12393  359 DVVHWGTAGGARVLGLDA-IGTLAVGQAADL-AIYDlddprfFGLHDPAIapvaCGGPAPVKALLVNG 424
 
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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