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Conserved domains on  [gi|521255019|ref|WP_020441584|]
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mycothiol conjugate amidase Mca [Corynebacterium terpenotabidum]

Protein Classification

mycothiol conjugate amidase Mca( domain architecture ID 10022448)

mycothiol conjugate amidase Mca recycles conjugated mycothiol (MSH) to the N-acetyl cysteine conjugate and the MSH precursor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
mycothiol_Mca TIGR03446
mycothiol conjugate amidase Mca; Mycobacterium tuberculosis, Corynebacterium glutamicum, and ...
20-300 1.01e-177

mycothiol conjugate amidase Mca; Mycobacterium tuberculosis, Corynebacterium glutamicum, and related species use the thiol mycothiol in place of glutathione. This enzyme, homologous to the (dispensible) MshB enzyme of mycothiol biosynthesis, is described as an amidase that acts on conjugates to mycothiol. It is a detoxification enzyme. [Cellular processes, Detoxification]


:

Pssm-ID: 132487  Cd Length: 283  Bit Score: 491.94  E-value: 1.01e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019   20 LRLLAIHAHPDDESSKGAATMARYADEGCEVMVLTCTGGERGSILNPQMDRPGVAEHMHEIRIEEMAQAAEILGVQHRWL 99
Cdd:TIGR03446   1 LRLMAVHAHPDDESSKGAATMARYAAEGHDVMVVTCTGGERGDILNPAMDKPAVEGRIAEVRREEMAEAAEILGVEHRWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019  100 GYIDSGLPEGDPLPPLPEECFALADTAEATAKVVAVIREFRPHVIITYDENGGYPHPDHIKTHAVSMRAWDVSGDPDYRP 179
Cdd:TIGR03446  81 GFVDSGLPEGDPLPPLPEGCFALEPLEEAAEPLVRVIREFRPHVITTYDENGGYPHPDHIMCHEVSVEAFEAAGDPERYP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019  180 DLGTPWTVQKLYYTHGFIRRRFELLARAEEERGNVTA-SSVLERWN-DVPDIMPRVTTQIACAPWFARRDAALRAHATQI 257
Cdd:TIGR03446 161 EAGEPWAPLKLYYTHGFIRERMEALHEELAERGLESPyAEWLARWLeDRADITARVTTQVECADYFEQRDDALRAHATQI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 521255019  258 DPDGPFFAVATDIQENVWPTEEFELAASRVETTVPEDDLFAGV 300
Cdd:TIGR03446 241 DPNGFFFAVPLEIQRRLWPTEEFELARSRVPTSLPEDDLFAGI 283
 
Name Accession Description Interval E-value
mycothiol_Mca TIGR03446
mycothiol conjugate amidase Mca; Mycobacterium tuberculosis, Corynebacterium glutamicum, and ...
20-300 1.01e-177

mycothiol conjugate amidase Mca; Mycobacterium tuberculosis, Corynebacterium glutamicum, and related species use the thiol mycothiol in place of glutathione. This enzyme, homologous to the (dispensible) MshB enzyme of mycothiol biosynthesis, is described as an amidase that acts on conjugates to mycothiol. It is a detoxification enzyme. [Cellular processes, Detoxification]


Pssm-ID: 132487  Cd Length: 283  Bit Score: 491.94  E-value: 1.01e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019   20 LRLLAIHAHPDDESSKGAATMARYADEGCEVMVLTCTGGERGSILNPQMDRPGVAEHMHEIRIEEMAQAAEILGVQHRWL 99
Cdd:TIGR03446   1 LRLMAVHAHPDDESSKGAATMARYAAEGHDVMVVTCTGGERGDILNPAMDKPAVEGRIAEVRREEMAEAAEILGVEHRWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019  100 GYIDSGLPEGDPLPPLPEECFALADTAEATAKVVAVIREFRPHVIITYDENGGYPHPDHIKTHAVSMRAWDVSGDPDYRP 179
Cdd:TIGR03446  81 GFVDSGLPEGDPLPPLPEGCFALEPLEEAAEPLVRVIREFRPHVITTYDENGGYPHPDHIMCHEVSVEAFEAAGDPERYP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019  180 DLGTPWTVQKLYYTHGFIRRRFELLARAEEERGNVTA-SSVLERWN-DVPDIMPRVTTQIACAPWFARRDAALRAHATQI 257
Cdd:TIGR03446 161 EAGEPWAPLKLYYTHGFIRERMEALHEELAERGLESPyAEWLARWLeDRADITARVTTQVECADYFEQRDDALRAHATQI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 521255019  258 DPDGPFFAVATDIQENVWPTEEFELAASRVETTVPEDDLFAGV 300
Cdd:TIGR03446 241 DPNGFFFAVPLEIQRRLWPTEEFELARSRVPTSLPEDDLFAGI 283
LmbE COG2120
N-acetylglucosaminyl deacetylase, LmbE family [Carbohydrate transport and metabolism];
21-259 1.16e-48

N-acetylglucosaminyl deacetylase, LmbE family [Carbohydrate transport and metabolism];


Pssm-ID: 441723 [Multi-domain]  Cd Length: 201  Bit Score: 160.86  E-value: 1.16e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019  21 RLLAIHAHPDDESSKGAATMARYADEGCEVMVLTCTGGERGSILNPQMDrpgvaEHMHEIRIEEMAQAAEILGV-QHRWL 99
Cdd:COG2120    1 RVLVVAAHPDDEELGCGGTIARLAAAGHEVTVVTLTDGEAGSPGGPPLR-----EELAEIRRAEARAAAAILGVsDVEFL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019 100 GYIDSGLPEgdplpplpeecfalaDTAEATAKVVAVIREFRPHVIITYDENGgyPHPDHIKTHAVSMRAWDVSGDPDyrp 179
Cdd:COG2120   76 GYPDGGLEG---------------PLEELRRALARLIREVRPDVVLTPDPGD--GHPDHRAVGRAVLAAARLAGLPK--- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019 180 dlgtpWTVQKLYYThgfirrrfellaraeeergnvtassvlERWNDvpdimPRVTTQIACAPWFARRDAALRAHATQIDP 259
Cdd:COG2120  136 -----ILGPRLYLY---------------------------EVPSD-----TEPDVAVDITDVLERKLAALAAHASQLDP 178
PIG-L pfam02585
GlcNAc-PI de-N-acetylase; Members of this family are related to PIG-L an ...
23-168 1.37e-33

GlcNAc-PI de-N-acetylase; Members of this family are related to PIG-L an N-acetylglucosaminylphosphatidylinositol de-N-acetylase (EC:3.5.1.89) that catalyzes the second step in GPI biosynthesis.


Pssm-ID: 426852  Cd Length: 128  Bit Score: 119.71  E-value: 1.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019   23 LAIHAHPDDESSKGAATMARYADEGCEVMVLTCTGGERGSILNPQMDRPGVAehmhEIRIEEMAQAAEILGV-QHRWLGY 101
Cdd:pfam02585   1 LVVSAHPDDEELGAGGTIARLAAAGVEVHVVCLTDGEAGSGGGSLEEGEELG----EIRRAEARAAAEILGVdDVEFLDY 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521255019  102 IDSGLPEgdplpplpeecfalADTAEATAKVVAVIREFRPHVIITYDENGGyPHPDHIKTHAVSMRA 168
Cdd:pfam02585  77 PDGGLEY--------------WDLEELLDALADLIRRYRPDVVVTPDPDGG-GHPDHRATGRAVLAA 128
 
Name Accession Description Interval E-value
mycothiol_Mca TIGR03446
mycothiol conjugate amidase Mca; Mycobacterium tuberculosis, Corynebacterium glutamicum, and ...
20-300 1.01e-177

mycothiol conjugate amidase Mca; Mycobacterium tuberculosis, Corynebacterium glutamicum, and related species use the thiol mycothiol in place of glutathione. This enzyme, homologous to the (dispensible) MshB enzyme of mycothiol biosynthesis, is described as an amidase that acts on conjugates to mycothiol. It is a detoxification enzyme. [Cellular processes, Detoxification]


Pssm-ID: 132487  Cd Length: 283  Bit Score: 491.94  E-value: 1.01e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019   20 LRLLAIHAHPDDESSKGAATMARYADEGCEVMVLTCTGGERGSILNPQMDRPGVAEHMHEIRIEEMAQAAEILGVQHRWL 99
Cdd:TIGR03446   1 LRLMAVHAHPDDESSKGAATMARYAAEGHDVMVVTCTGGERGDILNPAMDKPAVEGRIAEVRREEMAEAAEILGVEHRWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019  100 GYIDSGLPEGDPLPPLPEECFALADTAEATAKVVAVIREFRPHVIITYDENGGYPHPDHIKTHAVSMRAWDVSGDPDYRP 179
Cdd:TIGR03446  81 GFVDSGLPEGDPLPPLPEGCFALEPLEEAAEPLVRVIREFRPHVITTYDENGGYPHPDHIMCHEVSVEAFEAAGDPERYP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019  180 DLGTPWTVQKLYYTHGFIRRRFELLARAEEERGNVTA-SSVLERWN-DVPDIMPRVTTQIACAPWFARRDAALRAHATQI 257
Cdd:TIGR03446 161 EAGEPWAPLKLYYTHGFIRERMEALHEELAERGLESPyAEWLARWLeDRADITARVTTQVECADYFEQRDDALRAHATQI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 521255019  258 DPDGPFFAVATDIQENVWPTEEFELAASRVETTVPEDDLFAGV 300
Cdd:TIGR03446 241 DPNGFFFAVPLEIQRRLWPTEEFELARSRVPTSLPEDDLFAGI 283
mycothiol_MshB TIGR03445
N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase; Members of this ...
23-300 2.16e-64

N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase; Members of this protein family are N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase, also called 1D-myo-inosityl-2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase, the MshB protein of mycothiol biosynthesis in Mycobacterium tuberculosis and related species. [Cellular processes, Detoxification]


Pssm-ID: 274584  Cd Length: 284  Bit Score: 204.24  E-value: 2.16e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019   23 LAIHAHPDDESSKGAATMARYADEGCEVMVLTCTGGERGSILNPQMDR--PGVAEHMHEIRIEEMAQAAEILGV-QHRWL 99
Cdd:TIGR03445   1 LLVHAHPDDETLTTGATIARYAARGADVTVVTCTLGEEGEVIGERWAQlaADRADQLGGYRIGELTAALRALGVgDPRFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019  100 G----YIDSGLPeGDPLPPLPEeCFALADTAEATAKVVAVIREFRPHVIITYDENGGYPHPDHIKTHAVSMRAWDVSGDP 175
Cdd:TIGR03445  81 GgagrWRDSGMA-GTPSRSRPR-AFVDADVDEAAGALVAVIREVRPHVVVTYDPNGGYGHPDHIQAHRVTTRAVEAAAEA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019  176 dyrPDLGTPWTVQKLYYTHGFIRRRFELLARAeeeRGNVTASSVLERWNDVPDIMP--RVTTQIACAPWFARRDAALRAH 253
Cdd:TIGR03445 159 ---PLPGTPWQVPKFYWTVTPRSALEEAFARL---RGDLPGEWRLPAAEDVPFGVPddRITTVVDGTAYLAAKRAALRAH 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 521255019  254 ATQID--PDGPFFAVATDIQENVWPTEEFEL---AASRVETTVPEDDLFAGV 300
Cdd:TIGR03445 233 ATQVTvaPSGRAFALSNNIAQPILAEEHYVLvrgEAGPRDPRGWETDLFAGL 284
LmbE COG2120
N-acetylglucosaminyl deacetylase, LmbE family [Carbohydrate transport and metabolism];
21-259 1.16e-48

N-acetylglucosaminyl deacetylase, LmbE family [Carbohydrate transport and metabolism];


Pssm-ID: 441723 [Multi-domain]  Cd Length: 201  Bit Score: 160.86  E-value: 1.16e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019  21 RLLAIHAHPDDESSKGAATMARYADEGCEVMVLTCTGGERGSILNPQMDrpgvaEHMHEIRIEEMAQAAEILGV-QHRWL 99
Cdd:COG2120    1 RVLVVAAHPDDEELGCGGTIARLAAAGHEVTVVTLTDGEAGSPGGPPLR-----EELAEIRRAEARAAAAILGVsDVEFL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019 100 GYIDSGLPEgdplpplpeecfalaDTAEATAKVVAVIREFRPHVIITYDENGgyPHPDHIKTHAVSMRAWDVSGDPDyrp 179
Cdd:COG2120   76 GYPDGGLEG---------------PLEELRRALARLIREVRPDVVLTPDPGD--GHPDHRAVGRAVLAAARLAGLPK--- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019 180 dlgtpWTVQKLYYThgfirrrfellaraeeergnvtassvlERWNDvpdimPRVTTQIACAPWFARRDAALRAHATQIDP 259
Cdd:COG2120  136 -----ILGPRLYLY---------------------------EVPSD-----TEPDVAVDITDVLERKLAALAAHASQLDP 178
PIG-L pfam02585
GlcNAc-PI de-N-acetylase; Members of this family are related to PIG-L an ...
23-168 1.37e-33

GlcNAc-PI de-N-acetylase; Members of this family are related to PIG-L an N-acetylglucosaminylphosphatidylinositol de-N-acetylase (EC:3.5.1.89) that catalyzes the second step in GPI biosynthesis.


Pssm-ID: 426852  Cd Length: 128  Bit Score: 119.71  E-value: 1.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521255019   23 LAIHAHPDDESSKGAATMARYADEGCEVMVLTCTGGERGSILNPQMDRPGVAehmhEIRIEEMAQAAEILGV-QHRWLGY 101
Cdd:pfam02585   1 LVVSAHPDDEELGAGGTIARLAAAGVEVHVVCLTDGEAGSGGGSLEEGEELG----EIRRAEARAAAEILGVdDVEFLDY 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521255019  102 IDSGLPEgdplpplpeecfalADTAEATAKVVAVIREFRPHVIITYDENGGyPHPDHIKTHAVSMRA 168
Cdd:pfam02585  77 PDGGLEY--------------WDLEELLDALADLIRRYRPDVVVTPDPDGG-GHPDHRATGRAVLAA 128
 
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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