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Conserved domains on  [gi|15610236|ref|NP_217615|]
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hypothetical protein Rv3099c [Mycobacterium tuberculosis H37Rv]

Protein Classification

maleylpyruvate isomerase family mycothiol-dependent enzyme( domain architecture ID 11496386)

maleylpyruvate isomerase family protein may be a mycothiol-dependent enzyme similar to the N-terminal domain of Corynebacterium glutamicum mycothiol-dependent maleylpyruvate isomerase (MDMPI), which catalyzes the conversion of maleylpyruvate to fumarylpyruvate

CATH:  3.30.1050.20|1.20.120.450
Gene Ontology:  GO:0046872
PubMed:  17428791
SCOP:  4002268|4001390

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIGR03083 TIGR03083
uncharacterized Actinobacterial protein TIGR03083; This protein family pulls together several ...
 20-253 3.33e-34

uncharacterized Actinobacterial protein TIGR03083; This protein family pulls together several groups of proteins, each very different from the others. They share in common three conserved regions. The first is a region of about 38 amino acids, nearly always at the N-terminus of a protein. This region has a bulky hydrophobic residue, usually Trp, at position 29, and a His residue at position 37 that is invariant, so far, in over 150 instances. The second conserved region has a motif [DE]xxxHxxD. The third conserved region contains a hydrophobic patch and a well-conserved Arg residue. Most examples are found in the Actinobacteria, including the genera Mycobacterium, Corynebacterium, Streptomyces, Nocardia, Frankia, etc. The pattern of near-invariant residues against a backdrop of extreme sequence divergence suggests enzymatic activity and conservation of active site residues.


:

Pssm-ID: 274422 [Multi-domain]  Cd Length: 202  Bit Score: 122.95  E-value: 3.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610236    20 LFAVWHSLDALLDGLLETDWQATSPLPGWDVKAVVSHIIGTESFLLGIAApepdtdvsALAHVRNPIGVMNECWVRHLGT 99
Cdd:TIGR03083   2 ARAERAALAALLAALDPDQWAAPTPCPGWTVRDLLAHLAGRERAAAAVVA--------GLITVRADSDRARERAIEELAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610236   100 ESGVGLLERFRAVTSQRRKVLASLSDDEWNAPTTTPSGPdsygrfMRIRIFDCWMHEQDIRAAVQRPssdDELGGPASPL 179
Cdd:TIGR03083  74 LPPAALLAWFRAGAARLLDALAALDPDAWGPPPRPAGGA------LARRLMEVWVHGWDLARALGRP---DRLPRALAER 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15610236   180 VLDEIAATMGFVVGKLAKAPDGSRVLLELTGPLSrsirvsvdgrarvvddFGGPAPTATIRLDGLQFTRLAGGR 253
Cdd:TIGR03083 145 ALDELLATLPRVARLGGRAPPAAVVLAPTGGTWT----------------FGPGGPAVTVTGPAEDLLLLLTGR 202
 
Name Accession Description Interval E-value
TIGR03083 TIGR03083
uncharacterized Actinobacterial protein TIGR03083; This protein family pulls together several ...
 20-253 3.33e-34

uncharacterized Actinobacterial protein TIGR03083; This protein family pulls together several groups of proteins, each very different from the others. They share in common three conserved regions. The first is a region of about 38 amino acids, nearly always at the N-terminus of a protein. This region has a bulky hydrophobic residue, usually Trp, at position 29, and a His residue at position 37 that is invariant, so far, in over 150 instances. The second conserved region has a motif [DE]xxxHxxD. The third conserved region contains a hydrophobic patch and a well-conserved Arg residue. Most examples are found in the Actinobacteria, including the genera Mycobacterium, Corynebacterium, Streptomyces, Nocardia, Frankia, etc. The pattern of near-invariant residues against a backdrop of extreme sequence divergence suggests enzymatic activity and conservation of active site residues.


Pssm-ID: 274422 [Multi-domain]  Cd Length: 202  Bit Score: 122.95  E-value: 3.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610236    20 LFAVWHSLDALLDGLLETDWQATSPLPGWDVKAVVSHIIGTESFLLGIAApepdtdvsALAHVRNPIGVMNECWVRHLGT 99
Cdd:TIGR03083   2 ARAERAALAALLAALDPDQWAAPTPCPGWTVRDLLAHLAGRERAAAAVVA--------GLITVRADSDRARERAIEELAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610236   100 ESGVGLLERFRAVTSQRRKVLASLSDDEWNAPTTTPSGPdsygrfMRIRIFDCWMHEQDIRAAVQRPssdDELGGPASPL 179
Cdd:TIGR03083  74 LPPAALLAWFRAGAARLLDALAALDPDAWGPPPRPAGGA------LARRLMEVWVHGWDLARALGRP---DRLPRALAER 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15610236   180 VLDEIAATMGFVVGKLAKAPDGSRVLLELTGPLSrsirvsvdgrarvvddFGGPAPTATIRLDGLQFTRLAGGR 253
Cdd:TIGR03083 145 ALDELLATLPRVARLGGRAPPAAVVLAPTGGTWT----------------FGPGGPAVTVTGPAEDLLLLLTGR 202
MDMPI_N pfam11716
Mycothiol maleylpyruvate isomerase N-terminal domain;
20-160 7.31e-22

Mycothiol maleylpyruvate isomerase N-terminal domain;


Pssm-ID: 432021  Cd Length: 139  Bit Score: 88.67  E-value: 7.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610236    20 LFAVWHSLDALLDGLLETDWQATSPLPGWDVKAVVSHIIGTESFLLGIAAPEPDTDVSALAHVrnPIGVMNECWVRHLGT 99
Cdd:pfam11716   1 LRAEWARLAALLAALTDAQWDAPTPCPGWTVRDLVAHLARTARWAAAALAAPAARPGRVVDAA--AASREVDEAVDLAAP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610236   100 ESGVGLLERFRAVTSQRRKVLASLSDDEWNAPTTTPSGPDSYGRFMRIRIFDCWMHEQDIR 160
Cdd:pfam11716  79 LPPEALLALLRAAAARLLAALAALPPDAPAWTFGTPLGPRSAGFWLRRRLMETWVHGLDLA 139
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 154-255 8.60e-03

Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADHs), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176256 [Multi-domain]  Cd Length: 333  Bit Score: 37.22  E-value: 8.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610236 154 MHEQDIRAAVQrpssddELGGPASPLVLDEIAATMGFVVGKLAkaPDGSRVLLELTG-PLSRSIRVSVDGRARVVddfGG 232
Cdd:cd08296 214 TSKEDVAEALQ------ELGGAKLILATAPNAKAISALVGGLA--PRGKLLILGAAGePVAVSPLQLIMGRKSIH---GW 282

                        90       100
                ....*....|....*....|...
gi 15610236 233 PAPTATIRLDGLQFTRLAGGRPM 255
Cdd:cd08296 283 PSGTALDSEDTLKFSALHGVRPM 305
 
Name Accession Description Interval E-value
TIGR03083 TIGR03083
uncharacterized Actinobacterial protein TIGR03083; This protein family pulls together several ...
 20-253 3.33e-34

uncharacterized Actinobacterial protein TIGR03083; This protein family pulls together several groups of proteins, each very different from the others. They share in common three conserved regions. The first is a region of about 38 amino acids, nearly always at the N-terminus of a protein. This region has a bulky hydrophobic residue, usually Trp, at position 29, and a His residue at position 37 that is invariant, so far, in over 150 instances. The second conserved region has a motif [DE]xxxHxxD. The third conserved region contains a hydrophobic patch and a well-conserved Arg residue. Most examples are found in the Actinobacteria, including the genera Mycobacterium, Corynebacterium, Streptomyces, Nocardia, Frankia, etc. The pattern of near-invariant residues against a backdrop of extreme sequence divergence suggests enzymatic activity and conservation of active site residues.


Pssm-ID: 274422 [Multi-domain]  Cd Length: 202  Bit Score: 122.95  E-value: 3.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610236    20 LFAVWHSLDALLDGLLETDWQATSPLPGWDVKAVVSHIIGTESFLLGIAApepdtdvsALAHVRNPIGVMNECWVRHLGT 99
Cdd:TIGR03083   2 ARAERAALAALLAALDPDQWAAPTPCPGWTVRDLLAHLAGRERAAAAVVA--------GLITVRADSDRARERAIEELAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610236   100 ESGVGLLERFRAVTSQRRKVLASLSDDEWNAPTTTPSGPdsygrfMRIRIFDCWMHEQDIRAAVQRPssdDELGGPASPL 179
Cdd:TIGR03083  74 LPPAALLAWFRAGAARLLDALAALDPDAWGPPPRPAGGA------LARRLMEVWVHGWDLARALGRP---DRLPRALAER 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15610236   180 VLDEIAATMGFVVGKLAKAPDGSRVLLELTGPLSrsirvsvdgrarvvddFGGPAPTATIRLDGLQFTRLAGGR 253
Cdd:TIGR03083 145 ALDELLATLPRVARLGGRAPPAAVVLAPTGGTWT----------------FGPGGPAVTVTGPAEDLLLLLTGR 202
MDMPI_N pfam11716
Mycothiol maleylpyruvate isomerase N-terminal domain;
20-160 7.31e-22

Mycothiol maleylpyruvate isomerase N-terminal domain;


Pssm-ID: 432021  Cd Length: 139  Bit Score: 88.67  E-value: 7.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610236    20 LFAVWHSLDALLDGLLETDWQATSPLPGWDVKAVVSHIIGTESFLLGIAAPEPDTDVSALAHVrnPIGVMNECWVRHLGT 99
Cdd:pfam11716   1 LRAEWARLAALLAALTDAQWDAPTPCPGWTVRDLVAHLARTARWAAAALAAPAARPGRVVDAA--AASREVDEAVDLAAP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610236   100 ESGVGLLERFRAVTSQRRKVLASLSDDEWNAPTTTPSGPDSYGRFMRIRIFDCWMHEQDIR 160
Cdd:pfam11716  79 LPPEALLALLRAAAARLLAALAALPPDAPAWTFGTPLGPRSAGFWLRRRLMETWVHGLDLA 139
MDMPI_C pfam07398
MDMPI C-terminal domain; This domain is found at the C-terminus of the mycothiol ...
 178-274 8.24e-08

MDMPI C-terminal domain; This domain is found at the C-terminus of the mycothiol maleylpyruvate isomerase enzyme (MDMPI). The structure of this protein has been solved. This domain appears weakly similar to pfam08608.


Pssm-ID: 429443  Cd Length: 88  Bit Score: 49.00  E-value: 8.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610236   178 PLVLDEIAATMGFVVGKLAKAPDGSRVLLELTGPLSRSIRVSVDGRARVVDdfggpaPTATIRLDGLQFTRLAGGRPMSP 257
Cdd:pfam07398   1 DLAADGVDELLAFVAARPAGGPDGSRVVLDLEGPRTVHLHAGDGGTATAAP------WPATVRGDAADLLLLLWGRLSPA 74

                          90
                  ....*....|....*..
gi 15610236   258 ARsqdVELGGDKELAGH 274
Cdd:pfam07398  75 DT---LSVDGDLALLAR 88
TIGR03086 TIGR03086
TIGR03086 family protein; This family, like pfam07398 and TIGRFAMs family TIGR030834, belongs ...
 27-171 1.36e-05

TIGR03086 family protein; This family, like pfam07398 and TIGRFAMs family TIGR030834, belongs to the larger set of probable enzymes defined in family TIGR03083. Members are found primarily in the Actinobacteria (Mycobacterium, Streptomyces, etc.). The family is uncharacterized.


Pssm-ID: 274424  Cd Length: 180  Bit Score: 44.71  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610236    27 LDALLDGLLETDWQATSPLPGWDVKAVVSHIIGTESFLLGIAAPEPDTDVSALAHVrnpiGVMNECWVrhlgtesgvgll 106
Cdd:TIGR03086   8 LAALVRAVRADQLSRPTPCAGWDVRDLLNHLVGSAEAFAAVKEAGGDGWAGPPADD----PWLGDDPV------------ 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15610236   107 erfRAVTSQRRKVLASLSDDE-WNAPTTTPSGPDSYGRFMRIRIFDCWMHEQDIRAAVQRPSSDDE 171
Cdd:TIGR03086  72 ---AAYAAAADRARAAWADPAaLDATVSLPGGEVPARAALAVHLTELVVHGWDLARATGRDYRLDP 134
DinB_2 pfam12867
DinB superfamily; The DinB family are an uncharacterized family of potential enzymes. The ...
 22-155 1.98e-05

DinB superfamily; The DinB family are an uncharacterized family of potential enzymes. The structure of these proteins is composed of a four helix bundle.


Pssm-ID: 463733  Cd Length: 128  Bit Score: 43.22  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610236    22 AVWHSLDALLDGLLETDWQATSPLPGWDVKAVVSHIIGTESFLLGIAAPEPDTDVSALAHVRNPigvmnecwvrhlgteS 101
Cdd:pfam12867   4 RARARLLALLEGLPDEELNWRPAPGKWSIAWLLGHLADVEEVLLARLRLGEEAPRPAYDPGEPP---------------S 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15610236   102 GVGLLERFRAVTSQRRKVLASLSDDEWNAPTTTPSGPD--SYGRFMRIRIFDCWMH 155
Cdd:pfam12867  69 AAELLAYLAAVRARLLALLAALTDADLARPVTAPPGLGklTLGELLLFVAAHEAHH 124
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 154-255 8.60e-03

Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADHs), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176256 [Multi-domain]  Cd Length: 333  Bit Score: 37.22  E-value: 8.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610236 154 MHEQDIRAAVQrpssddELGGPASPLVLDEIAATMGFVVGKLAkaPDGSRVLLELTG-PLSRSIRVSVDGRARVVddfGG 232
Cdd:cd08296 214 TSKEDVAEALQ------ELGGAKLILATAPNAKAISALVGGLA--PRGKLLILGAAGePVAVSPLQLIMGRKSIH---GW 282

                        90       100
                ....*....|....*....|...
gi 15610236 233 PAPTATIRLDGLQFTRLAGGRPM 255
Cdd:cd08296 283 PSGTALDSEDTLKFSALHGVRPM 305
 
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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