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Conserved domains on  [gi|506439068|ref|WP_015958785|]
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ethanolamine utilization acetate kinase EutQ [Klebsiella pneumoniae]

Protein Classification

ethanolamine utilization acetate kinase EutQ( domain architecture ID 10015128)

ethanolamine utilization acetate kinase EutQ is involved in polyamine and ethanolamine degradation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15457 PRK15457
ethanolamine utilization acetate kinase EutQ;
1-229 1.95e-160

ethanolamine utilization acetate kinase EutQ;


:

Pssm-ID: 185354 [Multi-domain]  Cd Length: 233  Bit Score: 442.84  E-value: 1.95e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506439068   1 MKKLITANDIRAAHARGEQAMSVVLRASIITPEAREVAELLGFTITE----DDGAAPAATAADSDKTESQRIRETILAQL 76
Cdd:PRK15457   1 MKKLITANDIREAHARGEQAMSVVLRASIITPEAREVADLLGFTITEcdesIPVTASVPASVPADKTESQRIRETIIAQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506439068  77 PEGQFTESLVAQLMEKVMKEKQSLEQEAMQPGFDSVTGKGGIKVIDGSSVKFGRFDGAQPHCVGLTDLVTDQDGSSMAAG 156
Cdd:PRK15457  81 PEGQFTESLVAQLMEKVMKEKQSLEQGAMQPSFKSVTGKGGIKVIDGSSVKFGRFDGAEPHCVGLTDLVTGDDGSSMAAG 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506439068 157 FMQWENAFFPWTLNYDEIDMVLEGELHVRHQGETLVAKAGDVVFIPKGSSIEFGTPSTVRFLYVAWPANWQSL 229
Cdd:PRK15457 161 FMQWENAFFPWTLNYDEIDMVLEGELHVRHEGETMIAKAGDVMFIPKGSSIEFGTPSSVRFLYVAWPANWQSL 233
 
Name Accession Description Interval E-value
PRK15457 PRK15457
ethanolamine utilization acetate kinase EutQ;
1-229 1.95e-160

ethanolamine utilization acetate kinase EutQ;


Pssm-ID: 185354 [Multi-domain]  Cd Length: 233  Bit Score: 442.84  E-value: 1.95e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506439068   1 MKKLITANDIRAAHARGEQAMSVVLRASIITPEAREVAELLGFTITE----DDGAAPAATAADSDKTESQRIRETILAQL 76
Cdd:PRK15457   1 MKKLITANDIREAHARGEQAMSVVLRASIITPEAREVADLLGFTITEcdesIPVTASVPASVPADKTESQRIRETIIAQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506439068  77 PEGQFTESLVAQLMEKVMKEKQSLEQEAMQPGFDSVTGKGGIKVIDGSSVKFGRFDGAQPHCVGLTDLVTDQDGSSMAAG 156
Cdd:PRK15457  81 PEGQFTESLVAQLMEKVMKEKQSLEQGAMQPSFKSVTGKGGIKVIDGSSVKFGRFDGAEPHCVGLTDLVTGDDGSSMAAG 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506439068 157 FMQWENAFFPWTLNYDEIDMVLEGELHVRHQGETLVAKAGDVVFIPKGSSIEFGTPSTVRFLYVAWPANWQSL 229
Cdd:PRK15457 161 FMQWENAFFPWTLNYDEIDMVLEGELHVRHEGETMIAKAGDVMFIPKGSSIEFGTPSSVRFLYVAWPANWQSL 233
EutQ pfam06249
Ethanolamine utilization protein EutQ; The eut operon of Salmonella typhimurium encodes ...
 81-228 4.18e-81

Ethanolamine utilization protein EutQ; The eut operon of Salmonella typhimurium encodes proteins involved in the cobalamin-dependent degradation of ethanolamine. The role of EutQ in this process is unclear.


Pssm-ID: 114941  Cd Length: 152  Bit Score: 239.01  E-value: 4.18e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506439068   81 FTESLVAQLMEKVMKEKQSLEQEAMQPGFDSVT---GKGGIKVIDGSSVKFGRFDGAQPHCVGLT-DLVTDQDGSSMAAG 156
Cdd:pfam06249   1 ISKELLEQLVRKVIKEKLGLEQGAMSPSFKKVTdksGIGSIKLPDVKVVKFGRLDTGNPHDVVYTkDLVTLEESPRLGAG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506439068  157 FMQWENAFFPWTLNYDEIDMVLEGELHVRHQGETLVAKAGDVVFIPKGSSIEFGTPSTVRFLYVAWPANWQS 228
Cdd:pfam06249  81 LMEMKETTFPWTLNYDEIDYVIEGRLDVRIDGRTVSAKAGDVIFIPKGSKIEFSVTSYAKFLYVTYPANWQS 152
EutQ COG4766
Ethanolamine utilization protein EutQ, cupin superfamily (function unknown) [Amino acid ...
 107-227 5.82e-56

Ethanolamine utilization protein EutQ, cupin superfamily (function unknown) [Amino acid transport and metabolism];


Pssm-ID: 443798  Cd Length: 123  Bit Score: 174.40  E-value: 5.82e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506439068 107 PGFDSVTGKGGIKVidgsSVKFGRFD-GAQPHCVGLTDLVTDQDGSSMAAGFMQWENAFFPWTLNYDEIDMVLEGELHVR 185
Cdd:COG4766    6 PPFEKEVDPSGIKV----SVKDERFDtGGPGDKVYLKDVVTLEESSRMGAGFMRLEKTTFPWTLTYDEVDYVLEGTLTIE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 506439068 186 HQGETLVAKAGDVVFIPKGSSIEFGTPSTVRFLYVAWPANWQ 227
Cdd:COG4766   82 IDGETVTAGPGDVIYIPKGSSITFSTPEKARFFYVTYPANWA 123
cupin_EutQ cd02228
Clostridium difficile EutQ and related proteins, cupin domain; This family includes bacterial ...
 139-222 2.60e-43

Clostridium difficile EutQ and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to ethanolamine utilization protein EutQ found in Clostridium difficile, as well as in other bacteria, including the enteric pathogens Salmonella enterica and Enterococcus faecalis. EutQ is encoded by the eutQ gene which is part of the eut (ethanolamine utilization) operon found to be essential during anoxic growth of S. enterica on ethanolamine and tetrathionate. In C. difficile, inability to utilize ethanolamine results in greater virulence and a shorter time to morbidity in the animal model, suggesting that, in contrast to other intestinal pathogens, the metabolism of ethanolamine can delay the onset of disease. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. In contrast to the metal-binding catalytic cupins, the EutQ family does not possess the histidine residues that are responsible for metal coordination in the oxidoreductase and epimerase classes of cupins.


Pssm-ID: 380357 [Multi-domain]  Cd Length: 84  Bit Score: 140.72  E-value: 2.60e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506439068 139 VGLTDLVTDQDGSSMAAGFMQWENAFFPWTLNYDEIDMVLEGELHVRHQGETLVAKAGDVVFIPKGSSIEFGTPSTVRFL 218
Cdd:cd02228    1 VFLKDVVTSEEGSPMSAGFMELEKKSFPWTLTYDEIKYVLEGELEITDDGQTVTAKPGDVLFIPKGSKITFSTPDYAKFF 80


                 ....
gi 506439068 219 YVAW 222
Cdd:cd02228   81 YVTY 84
 
Name Accession Description Interval E-value
PRK15457 PRK15457
ethanolamine utilization acetate kinase EutQ;
1-229 1.95e-160

ethanolamine utilization acetate kinase EutQ;


Pssm-ID: 185354 [Multi-domain]  Cd Length: 233  Bit Score: 442.84  E-value: 1.95e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506439068   1 MKKLITANDIRAAHARGEQAMSVVLRASIITPEAREVAELLGFTITE----DDGAAPAATAADSDKTESQRIRETILAQL 76
Cdd:PRK15457   1 MKKLITANDIREAHARGEQAMSVVLRASIITPEAREVADLLGFTITEcdesIPVTASVPASVPADKTESQRIRETIIAQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506439068  77 PEGQFTESLVAQLMEKVMKEKQSLEQEAMQPGFDSVTGKGGIKVIDGSSVKFGRFDGAQPHCVGLTDLVTDQDGSSMAAG 156
Cdd:PRK15457  81 PEGQFTESLVAQLMEKVMKEKQSLEQGAMQPSFKSVTGKGGIKVIDGSSVKFGRFDGAEPHCVGLTDLVTGDDGSSMAAG 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506439068 157 FMQWENAFFPWTLNYDEIDMVLEGELHVRHQGETLVAKAGDVVFIPKGSSIEFGTPSTVRFLYVAWPANWQSL 229
Cdd:PRK15457 161 FMQWENAFFPWTLNYDEIDMVLEGELHVRHEGETMIAKAGDVMFIPKGSSIEFGTPSSVRFLYVAWPANWQSL 233
EutQ pfam06249
Ethanolamine utilization protein EutQ; The eut operon of Salmonella typhimurium encodes ...
 81-228 4.18e-81

Ethanolamine utilization protein EutQ; The eut operon of Salmonella typhimurium encodes proteins involved in the cobalamin-dependent degradation of ethanolamine. The role of EutQ in this process is unclear.


Pssm-ID: 114941  Cd Length: 152  Bit Score: 239.01  E-value: 4.18e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506439068   81 FTESLVAQLMEKVMKEKQSLEQEAMQPGFDSVT---GKGGIKVIDGSSVKFGRFDGAQPHCVGLT-DLVTDQDGSSMAAG 156
Cdd:pfam06249   1 ISKELLEQLVRKVIKEKLGLEQGAMSPSFKKVTdksGIGSIKLPDVKVVKFGRLDTGNPHDVVYTkDLVTLEESPRLGAG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506439068  157 FMQWENAFFPWTLNYDEIDMVLEGELHVRHQGETLVAKAGDVVFIPKGSSIEFGTPSTVRFLYVAWPANWQS 228
Cdd:pfam06249  81 LMEMKETTFPWTLNYDEIDYVIEGRLDVRIDGRTVSAKAGDVIFIPKGSKIEFSVTSYAKFLYVTYPANWQS 152
EutQ COG4766
Ethanolamine utilization protein EutQ, cupin superfamily (function unknown) [Amino acid ...
 107-227 5.82e-56

Ethanolamine utilization protein EutQ, cupin superfamily (function unknown) [Amino acid transport and metabolism];


Pssm-ID: 443798  Cd Length: 123  Bit Score: 174.40  E-value: 5.82e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506439068 107 PGFDSVTGKGGIKVidgsSVKFGRFD-GAQPHCVGLTDLVTDQDGSSMAAGFMQWENAFFPWTLNYDEIDMVLEGELHVR 185
Cdd:COG4766    6 PPFEKEVDPSGIKV----SVKDERFDtGGPGDKVYLKDVVTLEESSRMGAGFMRLEKTTFPWTLTYDEVDYVLEGTLTIE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 506439068 186 HQGETLVAKAGDVVFIPKGSSIEFGTPSTVRFLYVAWPANWQ 227
Cdd:COG4766   82 IDGETVTAGPGDVIYIPKGSSITFSTPEKARFFYVTYPANWA 123
cupin_EutQ cd02228
Clostridium difficile EutQ and related proteins, cupin domain; This family includes bacterial ...
 139-222 2.60e-43

Clostridium difficile EutQ and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to ethanolamine utilization protein EutQ found in Clostridium difficile, as well as in other bacteria, including the enteric pathogens Salmonella enterica and Enterococcus faecalis. EutQ is encoded by the eutQ gene which is part of the eut (ethanolamine utilization) operon found to be essential during anoxic growth of S. enterica on ethanolamine and tetrathionate. In C. difficile, inability to utilize ethanolamine results in greater virulence and a shorter time to morbidity in the animal model, suggesting that, in contrast to other intestinal pathogens, the metabolism of ethanolamine can delay the onset of disease. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. In contrast to the metal-binding catalytic cupins, the EutQ family does not possess the histidine residues that are responsible for metal coordination in the oxidoreductase and epimerase classes of cupins.


Pssm-ID: 380357 [Multi-domain]  Cd Length: 84  Bit Score: 140.72  E-value: 2.60e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506439068 139 VGLTDLVTDQDGSSMAAGFMQWENAFFPWTLNYDEIDMVLEGELHVRHQGETLVAKAGDVVFIPKGSSIEFGTPSTVRFL 218
Cdd:cd02228    1 VFLKDVVTSEEGSPMSAGFMELEKKSFPWTLTYDEIKYVLEGELEITDDGQTVTAKPGDVLFIPKGSKITFSTPDYAKFF 80


                 ....
gi 506439068 219 YVAW 222
Cdd:cd02228   81 YVTY 84
COG3450 COG3450
Predicted enzyme of the cupin superfamily [General function prediction only];
165-220 1.76e-07

Predicted enzyme of the cupin superfamily [General function prediction only];


Pssm-ID: 442673  Cd Length: 108  Bit Score: 48.05  E-value: 1.76e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 506439068 165 FPWTLNYDEIDMVLEGELHVRHQ-GETLVAKAGDVVFIPKGSSIEFGTPSTVRFLYV 220
Cdd:COG3450   50 FRWDYDEDEFCYILEGRVTVTDDdGEPVEFGAGDSFVFPAGFKGTWEVLETVRKHYV 106
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
172-226 7.95e-07

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 46.55  E-value: 7.95e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 506439068 172 DEIDMVLEGELHVRHQGETLVAKAGDVVFIPKGS--SIEFGTPSTVRFLYVAWPANW 226
Cdd:COG3837   51 EEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVphRLRNRGDEPARYLVVGTRAPY 107
cupin_QDO_C cd20281
quercetinase, C-terminal cupin domain; This family contains the C-terminal domain of ...
 176-220 1.39e-06

quercetinase, C-terminal cupin domain; This family contains the C-terminal domain of quercetinase (also known as quercetin 2,3-dioxygenase, 2,3QD, QDO and YxaG; EC 1.13.11.24), a mononuclear copper-dependent dioxygenase that catalyzes the cleavage of the flavonol quercetin (5,7,3',4'-tetrahydroxyflavonol) heterocyclic ring to produce 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. This family includes Aspergillus japonicus quercetin 2,3-dioxygenase (QDO), a homodimer that shows oxygenase activity with Cu2+. The dioxygen binds to the metal ion of the Cu-QDO-quercetin complex, yielding a Cu2+-superoxo quercetin radical intermediate, which forms a Cu2+-alkylperoxo complex that evolves into an endoperoxide intermediate that decomposes to the product. Quercetinase is a bicupin with two tandem cupin beta-barrel domains, only the C-terminal domain is included in this alignment. The pirins, which also belong to the cupin domain family, have been shown to catalyze a reaction involving quercetin and may have a function similar to that of quercetinase.


Pssm-ID: 380417  Cd Length: 114  Bit Score: 45.66  E-value: 1.39e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 506439068 176 MVLEGELHVRHQGETLVAKAGDVVFIPKGSSIEF--GTPSTvRFLYV 220
Cdd:cd20281   55 QVLEGQLVVEVGGETATLITGDVVFIPGGTSFSYwsEAAFT-KFLYV 100
cupin_TM1112-like cd02227
Thermotoga maritima TM1112 and related proteins, cupin domain; This family includes bacterial ...
 165-220 3.43e-06

Thermotoga maritima TM1112 and related proteins, cupin domain; This family includes bacterial and plant proteins homologous to TM1112, a Thermotoga maritima protein of unknown function with a cupin beta barrel domain. TM1112 (also known as DUF861) is a subfamily of RmlC-like cupins with a conserved "jelly roll-like" beta-barrel fold; structures indicate that a monomer is the biologically-relevant form.


Pssm-ID: 380356 [Multi-domain]  Cd Length: 69  Bit Score: 43.34  E-value: 3.43e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 506439068 165 FPWTLNYDEIDMVLEGELHVR-HQGETLVAKAGDVVFIPKGSSIEFGTPSTVRFLYV 220
Cdd:cd02227   12 FPWNYDEDEFCYILEGEVRVTpEDGEPVTFKAGDLVVFPAGFSGTWEVLEPVRKHYV 68
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
171-224 6.26e-06

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 43.68  E-value: 6.26e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 506439068 171 YDEIDMVLEGELHVRHQGETLVAKAGDVVFIPKGS--SIEFGTPSTVRFLYVAWPA 224
Cdd:COG1917   43 GEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVphAFRNLGDEPAVLLVVFSPG 98
cupin_YP766765-like cd20299
Rhizobium leguminosarum YP_766765.1 and related proteins, cupin domain; This family includes ...
 172-218 1.53e-05

Rhizobium leguminosarum YP_766765.1 and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to Rhizobium leguminosarum YP_766765.1, a protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380433 [Multi-domain]  Cd Length: 90  Bit Score: 42.27  E-value: 1.53e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 506439068 172 DEIDMVLEGELHVRHQGETLVAKAGDVVFIPKGS--SIEFGTPSTVRFL 218
Cdd:cd20299   38 EKVYVVLEGELTVTTDGEEVVLGPGDSCYIPPGEtrSIDNRTNGPATML 86
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 170-220 1.03e-04

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 39.39  E-value: 1.03e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 506439068 170 NYDEIDMVLEGELHVRHQ-GETLVAKAGDVVFIPKGSSIEFGTPS--TVRFLYV 220
Cdd:cd02208   19 EQDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSdePAVFLVV 72
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 172-220 1.44e-04

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 39.16  E-value: 1.44e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 506439068  172 DEIDMVLEGELHVRHQGETLVAKAGDVVFIPKGSSIEFGTPST--VRFLYV 220
Cdd:pfam07883  20 DEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDepARLLDV 70
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
172-224 1.51e-04

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 40.12  E-value: 1.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 506439068 172 DEIDMVLEGELHVRHQGETLVAKAGDVVFIPKGSSIEFGTPSTV--RFLYVAWPA 224
Cdd:COG0662   49 DEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGDEplELLEVQAPA 103
Cupin_3 pfam05899
EutQ-like cupin domain; This entry represents the cupin domain, with a conserved jelly ...
 165-206 2.63e-04

EutQ-like cupin domain; This entry represents the cupin domain, with a conserved jelly roll-like beta-barrel fold capable of homodimerization found in bacteria, plant and fungi. It is present in EutQ family from the eut operon, involved in ethanolamine degradation. EutQ is essential during anoxic growth and has acetate kinase activity. The cupin domain from EutQ does not possess the His residues responsible for metal coordination in other classes of cupins. This domain is also found in (S)-ureidoglycine aminohydrolase (UGlyAH) from E.coli, which is involved in the anaerobic nitrogen utilization via the assimilation of allantoin. It catalyzes the deamination of allantoin to produce S-ureidoglycolate and ammonia from S-ureidoglycine.


Pssm-ID: 399116 [Multi-domain]  Cd Length: 74  Bit Score: 38.43  E-value: 2.63e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 506439068  165 FPWTLNYDEIDMVLEGELHVR-HQGETLVAKAGDVVFIPKGSS 206
Cdd:pfam05899  19 FRWTYEEDETCYILSGEVTVTpEGGKTVTLRAGDLVVLPKGLS 61
cupin_SPO2919-like cd02224
Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase ...
 172-207 6.21e-04

Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase with a cupin domain; This family includes proteins similar to sugar phosphate isomerase SPO2919 from Silicibacter pomeroyi and Afe_0303 from Acidithiobacillus ferrooxidans, but are as yet uncharacterized. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380353 [Multi-domain]  Cd Length: 105  Bit Score: 38.24  E-value: 6.21e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 506439068 172 DEIDMVLEGELHVRHQGETLVAKAGDVVFIPKGSSI 207
Cdd:cd02224   40 EEFVYVLSGEGTLRLDGEEVLPRPGDFVGFPAGTGV 75
cupin_YdbB-like cd02226
Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial ...
 172-204 2.21e-03

Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial proteins homologous to YdbB, a Bacillus subtilis protein of unknown function. It also includes protein Nmb1881 From Neisseria meningitidis, also of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380355 [Multi-domain]  Cd Length: 94  Bit Score: 36.27  E-value: 2.21e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 506439068 172 DEIDMVLEGELHVRHQGETLVAKAGDVVFIPKG 204
Cdd:cd02226   44 DELFLVLEGELTIDFRDRDVTLGPGEFFVVPKG 76
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 172-229 7.04e-03

quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known as quercetin 2,3-dioxygenase, 2,3QD, QDO and YxaG; EC 1.13.11.24), a mononuclear copper-dependent dioxygenase that catalyzes the cleavage of the flavonol quercetin (5,7,3',4'-tetrahydroxyflavonol) heterocyclic ring to produce 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. Bacillus subtilis quercetin 2,3-dioxygenase (QDO) is a homodimer that shows oxygenase activity with several divalent metals such as Mn2+, Co2+, Fe2+, and Cu2+, although the preferred one appears to be Mn2+. The dioxygen binds to the metal ion of the Cu-QDO-quercetin complex, yielding a Cu2+-superoxo quercetin radical intermediate, which then forms a Cu2+-alkylperoxo complex which then evolves into endoperoxide intermediate that decomposes to the product. Quercetinase is a bicupin with two tandem cupin beta-barrel domains, both of which are included in this alignment model. The pirins, which also belong to the cupin domain family, have been shown to catalyze a reaction involving quercetin and may have a function similar to that of quercetinase.


Pssm-ID: 380345 [Multi-domain]  Cd Length: 122  Bit Score: 35.59  E-value: 7.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 506439068 172 DEIDMVLEGELHVRHQGETLVAKAGDVVFIPKGS--SIEFGTPSTvRFLYVAWPANWQSL 229
Cdd:cd02215   54 HETFYVLEGRLQLWLDGESRLLTPGDFASVPPGTihAYRMLSPDT-RFLGVITPGGFERF 112
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 167-208 7.38e-03

Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and eukaryotic cupin domains of proteins homologous to oxalate decarboxylase (OxDC; EC 4.1.1.2) such as MSMEG_2254, a putative OxDC from Mycobacterium smegmatis. OxDC is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues.


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 35.64  E-value: 7.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 506439068 167 WTLNYDEIDMVLEGE-----LHVRHQGETLVAKAGDVVFIPKGS--SIE 208
Cdd:cd20306   51 WHPNANELGYVISGEarvsiLDPTGSLDTFTVKPGQVVFIPQGWlhWIE 99
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 174-204 8.25e-03

pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380366 [Multi-domain]  Cd Length: 104  Bit Score: 34.75  E-value: 8.25e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 506439068 174 IDMVLEGELHVRHQGETLVAKAGDVVFIPKG 204
Cdd:cd02238   50 IGYVLSGRFEFTIGGETRILKPGDSYYIPPN 80
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 176-202 8.94e-03

Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380351 [Multi-domain]  Cd Length: 91  Bit Score: 34.35  E-value: 8.94e-03
                         10        20
                 ....*....|....*....|....*..
gi 506439068 176 MVLEGELHVRHQGETLVAKAGDVVFIP 202
Cdd:cd02222   42 YVLRGKGVVVIGGEEYPVKPGDVVYIP 68
 
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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