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Conserved domains on  [gi|1565696180|ref|WP_129045677|]
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carboxymuconolactone decarboxylase family protein [Companilactobacillus metriopterae]

Protein Classification

carboxymuconolactone decarboxylase family protein( domain architecture ID 10001777)

carboxymuconolactone decarboxylase (CMD) family protein similar to alkyl hydroperoxide reductase AhpD, which is required for the reduction of the AhpC active site cysteine residues to regenerate its enzyme activity; carboxymuconolactone d

CATH:  1.20.1290.10
Gene Ontology:  GO:0051920
PubMed:  9495744
SCOP:  4000771

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YurZ COG0599
Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone ...
 14-125 3.66e-36

Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone decarboxylase family [General function prediction only];


:

Pssm-ID: 440364  Cd Length: 114  Bit Score: 119.67  E-value: 3.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696180  14 KQTLSKVDGSSAKgVMESLDNIAPDVGKYiFEFAFGDIYNRPGLDLKQREMVTITSLLTQGDtENQLKVHINGSLNVGLT 93
Cdd:COG0599     1 EEVLKEVEEYVPR-ALEALAEFAPEFAEA-FEALFGDVWARGALDPKTRELITLAALAALGC-EPCLKAHVRAALNAGAT 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1565696180  94 QREIIETFIHCLPYVGFPKVLNAISVAKEVFE 125
Cdd:COG0599    78 REEIAEALLVAAVYAGFPAALNALRAALEVLE 109
 
Name Accession Description Interval E-value
YurZ COG0599
Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone ...
 14-125 3.66e-36

Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone decarboxylase family [General function prediction only];


Pssm-ID: 440364  Cd Length: 114  Bit Score: 119.67  E-value: 3.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696180  14 KQTLSKVDGSSAKgVMESLDNIAPDVGKYiFEFAFGDIYNRPGLDLKQREMVTITSLLTQGDtENQLKVHINGSLNVGLT 93
Cdd:COG0599     1 EEVLKEVEEYVPR-ALEALAEFAPEFAEA-FEALFGDVWARGALDPKTRELITLAALAALGC-EPCLKAHVRAALNAGAT 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1565696180  94 QREIIETFIHCLPYVGFPKVLNAISVAKEVFE 125
Cdd:COG0599    78 REEIAEALLVAAVYAGFPAALNALRAALEVLE 109
CMD pfam02627
Carboxymuconolactone decarboxylase family; Carboxymuconolactone decarboxylase (CMD) EC:4.1.1. ...
 37-122 9.08e-23

Carboxymuconolactone decarboxylase family; Carboxymuconolactone decarboxylase (CMD) EC:4.1.1.44 is involved in protocatechuate catabolism. In some bacteria a gene fusion event leads to expression of CMD with a hydrolase involved in the same pathway. In these bifunctional proteins CMD represents the C-terminal domain, pfam00561 represents the N-terminal domain.


Pssm-ID: 460628 [Multi-domain]  Cd Length: 84  Bit Score: 84.67  E-value: 9.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696180  37 PDVGKYIFEFAFGDIYNrPGLDLKQREMVTITSLLTQGDtENQLKVHINGSLNVGLTQREIIETFIHCLPYVGFPKVLNA 116
Cdd:pfam02627   1 PELLAALTALAFGLLWD-GGLDPKTRELIALAVSAANGC-AYCLDAHTRAALKAGVTEEEIAEVLAWAAAYAGGPAARAA 78


                  ....*.
gi 1565696180 117 ISVAKE 122
Cdd:pfam02627  79 LAAAEE 84
 
Name Accession Description Interval E-value
YurZ COG0599
Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone ...
 14-125 3.66e-36

Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone decarboxylase family [General function prediction only];


Pssm-ID: 440364  Cd Length: 114  Bit Score: 119.67  E-value: 3.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696180  14 KQTLSKVDGSSAKgVMESLDNIAPDVGKYiFEFAFGDIYNRPGLDLKQREMVTITSLLTQGDtENQLKVHINGSLNVGLT 93
Cdd:COG0599     1 EEVLKEVEEYVPR-ALEALAEFAPEFAEA-FEALFGDVWARGALDPKTRELITLAALAALGC-EPCLKAHVRAALNAGAT 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1565696180  94 QREIIETFIHCLPYVGFPKVLNAISVAKEVFE 125
Cdd:COG0599    78 REEIAEALLVAAVYAGFPAALNALRAALEVLE 109
CMD pfam02627
Carboxymuconolactone decarboxylase family; Carboxymuconolactone decarboxylase (CMD) EC:4.1.1. ...
 37-122 9.08e-23

Carboxymuconolactone decarboxylase family; Carboxymuconolactone decarboxylase (CMD) EC:4.1.1.44 is involved in protocatechuate catabolism. In some bacteria a gene fusion event leads to expression of CMD with a hydrolase involved in the same pathway. In these bifunctional proteins CMD represents the C-terminal domain, pfam00561 represents the N-terminal domain.


Pssm-ID: 460628 [Multi-domain]  Cd Length: 84  Bit Score: 84.67  E-value: 9.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565696180  37 PDVGKYIFEFAFGDIYNrPGLDLKQREMVTITSLLTQGDtENQLKVHINGSLNVGLTQREIIETFIHCLPYVGFPKVLNA 116
Cdd:pfam02627   1 PELLAALTALAFGLLWD-GGLDPKTRELIALAVSAANGC-AYCLDAHTRAALKAGVTEEEIAEVLAWAAAYAGGPAARAA 78


                  ....*.
gi 1565696180 117 ISVAKE 122
Cdd:pfam02627  79 LAAAEE 84
 
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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