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Conserved domains on  [gi|403399692|sp|A3LZU8|]
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RecName: Full=L-rhamnono-gamma-lactonase

Protein Classification

amidohydrolase family protein( domain architecture ID 10007618)

amidohydrolase family protein similar to 2-pyrone-4,6-dicarboxylic acid (PDC) hydrolase which catalyzes the hydrolysis of PDC to oxalomesaconic acid (OMA), and to Agrobacterium fabrum D-galactarolactone isomerase which catalyzes the isomerization of D-galactaro-1,5-lactone to D-galactaro-1,4-lactone

CATH:  3.20.20.140
EC:  3.1.-.-
Gene Ontology:  GO:0046872|GO:0016787
PubMed:  9144792
SCOP:  3000428

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
114-336 6.49e-27

Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];


:

Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 106.84  E-value: 6.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403399692 114 PLGSAGVEEYVKALKTrnssefHLVKGFRYLIQDKPPLTISDPHFVSSFQWLDSNGYVFDLGIDMrsgglWQFKETLEVF 193
Cdd:COG3618   80 DLDAPDAAAELARLAA------AGVRGVRFNLQGEPDGWLLDPAFRRGLARLAELGLHFDLLVDP-----RQLPALAPLL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403399692 194 KKVPNLKYIINHLTKPcldfdpeTIDSNPDflSWKRLVTEMyITTPNSYMKLSGGFSEVEQDVALDvtstsrHVYPWFKV 273
Cdd:COG3618  149 ARLPDLPVVIDHLGKP-------DIAAGDD--PWFAALLAL-AARPNVWVKLSGLYRESDAGWPYA------DLRPYARA 212
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 403399692 274 VYELWGPERTIFASNWPVCAIPAGqnlTEKWFQVCETLFDsiGMDEDTRRKIYYSNAFKAYNI 336
Cdd:COG3618  213 LLEAFGPDRLMWGSDWPVTLLAPD---YGELLDLLEELLP--DLSEAERRAILGDNAARLYGL 270
 
Name Accession Description Interval E-value
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
114-336 6.49e-27

Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];


Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 106.84  E-value: 6.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403399692 114 PLGSAGVEEYVKALKTrnssefHLVKGFRYLIQDKPPLTISDPHFVSSFQWLDSNGYVFDLGIDMrsgglWQFKETLEVF 193
Cdd:COG3618   80 DLDAPDAAAELARLAA------AGVRGVRFNLQGEPDGWLLDPAFRRGLARLAELGLHFDLLVDP-----RQLPALAPLL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403399692 194 KKVPNLKYIINHLTKPcldfdpeTIDSNPDflSWKRLVTEMyITTPNSYMKLSGGFSEVEQDVALDvtstsrHVYPWFKV 273
Cdd:COG3618  149 ARLPDLPVVIDHLGKP-------DIAAGDD--PWFAALLAL-AARPNVWVKLSGLYRESDAGWPYA------DLRPYARA 212
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 403399692 274 VYELWGPERTIFASNWPVCAIPAGqnlTEKWFQVCETLFDsiGMDEDTRRKIYYSNAFKAYNI 336
Cdd:COG3618  213 LLEAFGPDRLMWGSDWPVTLLAPD---YGELLDLLEELLP--DLSEAERRAILGDNAARLYGL 270
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
109-336 1.09e-13

Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 70.25  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403399692  109 PFAPMPLGSAGVEEYVKALKTRnssefhLVKGFRYLIQ--DKPPLtiSDPHFVSSFQWLDSNGYVFDL----GIDMRSGG 182
Cdd:pfam04909  81 VAVVPLDPEDAAAELERAVGEA------GFRGVRLNPHpgGDPLL--GDRLDRPIYEALEELGLPVDIhtgfGDRPEDTR 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403399692  183 LWQFKETLEVFKKVPNLKYIINHLTKPcldfDPetidsnPDFLSWKRLVTEMYiTTPNSYMKLSGGFSEVEQDVALdvts 262
Cdd:pfam04909 153 AIQPLLLAGVARKFPDLKIVLDHGGGP----WI------PEGLDDPAALALLA-RRPNVYVKLSGLYRDLYFDAPL---- 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 403399692  263 tsrHVYPWFKVVYELWGPERTIFASNWPVCAIPAGQNLTEKWFQVCETlfdsiGMDEDTRRKIYYSNAFKAYNI 336
Cdd:pfam04909 218 ---ADRPYLARLLEAFGPDRILFGSDWPHPPLEISPDDGVLLDLPLLL-----ALSDEEREKILGGNAARLYGL 283
 
Name Accession Description Interval E-value
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
114-336 6.49e-27

Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];


Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 106.84  E-value: 6.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403399692 114 PLGSAGVEEYVKALKTrnssefHLVKGFRYLIQDKPPLTISDPHFVSSFQWLDSNGYVFDLGIDMrsgglWQFKETLEVF 193
Cdd:COG3618   80 DLDAPDAAAELARLAA------AGVRGVRFNLQGEPDGWLLDPAFRRGLARLAELGLHFDLLVDP-----RQLPALAPLL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403399692 194 KKVPNLKYIINHLTKPcldfdpeTIDSNPDflSWKRLVTEMyITTPNSYMKLSGGFSEVEQDVALDvtstsrHVYPWFKV 273
Cdd:COG3618  149 ARLPDLPVVIDHLGKP-------DIAAGDD--PWFAALLAL-AARPNVWVKLSGLYRESDAGWPYA------DLRPYARA 212
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 403399692 274 VYELWGPERTIFASNWPVCAIPAGqnlTEKWFQVCETLFDsiGMDEDTRRKIYYSNAFKAYNI 336
Cdd:COG3618  213 LLEAFGPDRLMWGSDWPVTLLAPD---YGELLDLLEELLP--DLSEAERRAILGDNAARLYGL 270
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
109-336 1.09e-13

Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 70.25  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403399692  109 PFAPMPLGSAGVEEYVKALKTRnssefhLVKGFRYLIQ--DKPPLtiSDPHFVSSFQWLDSNGYVFDL----GIDMRSGG 182
Cdd:pfam04909  81 VAVVPLDPEDAAAELERAVGEA------GFRGVRLNPHpgGDPLL--GDRLDRPIYEALEELGLPVDIhtgfGDRPEDTR 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403399692  183 LWQFKETLEVFKKVPNLKYIINHLTKPcldfDPetidsnPDFLSWKRLVTEMYiTTPNSYMKLSGGFSEVEQDVALdvts 262
Cdd:pfam04909 153 AIQPLLLAGVARKFPDLKIVLDHGGGP----WI------PEGLDDPAALALLA-RRPNVYVKLSGLYRDLYFDAPL---- 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 403399692  263 tsrHVYPWFKVVYELWGPERTIFASNWPVCAIPAGQNLTEKWFQVCETlfdsiGMDEDTRRKIYYSNAFKAYNI 336
Cdd:pfam04909 218 ---ADRPYLARLLEAFGPDRILFGSDWPHPPLEISPDDGVLLDLPLLL-----ALSDEEREKILGGNAARLYGL 283
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
191-336 1.20e-03

5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism];


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 39.96  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403399692 191 EVFKKVPNLKYIINHLtkpCLDFDPETIDsnpdflswkRLVTEMyittPNSYmklsggfseveqdvaLDvTSTSRHVYPW 270
Cdd:COG2159  148 GVAERFPDLKFILAHG---GGPWLPELLG---------RLLKRL----PNVY---------------FD-TSGVFPRPEA 195
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 403399692 271 FKVVYELWGPERTIFASNWPVcaIPAGQNLtekwfqvcETLFDSIGMDEDTRRKIYYSNAFKAYNI 336
Cdd:COG2159  196 LRELLETLGADRILFGSDYPH--WDPPEAL--------EALEELPGLSEEDREKILGGNAARLLGL 251
 
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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