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Conserved domains on  [gi|489932453|ref|WP_003835769|]
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MULTISPECIES: (S)-ureidoglycine aminohydrolase [Citrobacter]

Protein Classification

ura-cupin family protein( domain architecture ID 11496500)

ura-cupin family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ura-cupin TIGR03214
putative allantoin catabolism protein; This model represents a protein containing a tandem ...
 11-261 5.58e-151

putative allantoin catabolism protein; This model represents a protein containing a tandem arrangement of cupin domains (N-terminal part of pfam07883 and C-terminal more distantly related to pfam00190). This protein is found in the vicinity of genes involved in the catabolism of allantoin, a breakdown product of urate and sometimes of urate iteslf. The distribution of pathway components in the genomes in which this family is observed suggests that the function is linked to the allantoate catabolism to glyoxylate pathway (GenProp0686) since it is sometimes found in genomes lacking any elements of the xanthine-to-allantoin pathways (e.g. in Enterococcus faecalis).


:

Pssm-ID: 200251 [Multi-domain]  Cd Length: 252  Bit Score: 421.03  E-value: 5.58e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453   11 RDDLLANRAIVkHGNFALLTPDGLVKNIIPGFENCDVTILSTPKLG--ASFVDYLVTVHQSGGNQSGFGGEGVETFVYVI 88
Cdd:TIGR03214   1 QKQLLTTRAIF-TGNYAVITPDGLVSNIVPGFENTDIWILARPKLGfsATFVQYIVEVHPGGGATTGFGGEGIETFLFVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453   89 SGKIEAKAEGKTFALTQGGYLYCPPGELLTFSNAQAEDSQLFLYKRRYTPVAG-HSPWLVSGNTNQLERIHYEGMDDVIL 167
Cdd:TIGR03214  80 DGEVNVSLGGETHELEEGGYAYLPPGSKWTLENAQDEDARFFLYKKRYQPVEGlHAPEAVVGNERDIEPEAYEGMDDVWA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453  168 LDFLPKELGFDMNMHILSFEPGASHGYIETHVQEHGAYILSGQGVYNLDNQWIPVKKGDYIFMGAYSLQAGYGVGRGEaF 247
Cdd:TIGR03214 160 TTLLPKELAFDMNVHILSFEPGASHPYIETHVMEHGLYVLEGKGVYNLDNDWVPVEAGDYIWMGAYCPQACYAVGRGP-F 238

                         250
                  ....*....|....
gi 489932453  248 SYIYSKDCNRDVEI 261
Cdd:TIGR03214 239 RYLLYKDVNRHPKL 252
 
Name Accession Description Interval E-value
ura-cupin TIGR03214
putative allantoin catabolism protein; This model represents a protein containing a tandem ...
 11-261 5.58e-151

putative allantoin catabolism protein; This model represents a protein containing a tandem arrangement of cupin domains (N-terminal part of pfam07883 and C-terminal more distantly related to pfam00190). This protein is found in the vicinity of genes involved in the catabolism of allantoin, a breakdown product of urate and sometimes of urate iteslf. The distribution of pathway components in the genomes in which this family is observed suggests that the function is linked to the allantoate catabolism to glyoxylate pathway (GenProp0686) since it is sometimes found in genomes lacking any elements of the xanthine-to-allantoin pathways (e.g. in Enterococcus faecalis).


Pssm-ID: 200251 [Multi-domain]  Cd Length: 252  Bit Score: 421.03  E-value: 5.58e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453   11 RDDLLANRAIVkHGNFALLTPDGLVKNIIPGFENCDVTILSTPKLG--ASFVDYLVTVHQSGGNQSGFGGEGVETFVYVI 88
Cdd:TIGR03214   1 QKQLLTTRAIF-TGNYAVITPDGLVSNIVPGFENTDIWILARPKLGfsATFVQYIVEVHPGGGATTGFGGEGIETFLFVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453   89 SGKIEAKAEGKTFALTQGGYLYCPPGELLTFSNAQAEDSQLFLYKRRYTPVAG-HSPWLVSGNTNQLERIHYEGMDDVIL 167
Cdd:TIGR03214  80 DGEVNVSLGGETHELEEGGYAYLPPGSKWTLENAQDEDARFFLYKKRYQPVEGlHAPEAVVGNERDIEPEAYEGMDDVWA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453  168 LDFLPKELGFDMNMHILSFEPGASHGYIETHVQEHGAYILSGQGVYNLDNQWIPVKKGDYIFMGAYSLQAGYGVGRGEaF 247
Cdd:TIGR03214 160 TTLLPKELAFDMNVHILSFEPGASHPYIETHVMEHGLYVLEGKGVYNLDNDWVPVEAGDYIWMGAYCPQACYAVGRGP-F 238

                         250
                  ....*....|....
gi 489932453  248 SYIYSKDCNRDVEI 261
Cdd:TIGR03214 239 RYLLYKDVNRHPKL 252
AllE COG3257
Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];
2-261 5.84e-143

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 442488 [Multi-domain]  Cd Length: 262  Bit Score: 401.12  E-value: 5.84e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453   2 GYLNNVTGY--RDDLLANRAIVKHgNFALLTPDGLVKNIIPGFENCDVTILSTPKLGASFVDYLVTVHQSGGNQSGFGGE 79
Cdd:COG3257    1 TYYAPKGGLppQTDLLTTRAVFTE-AYAVIPPDDIVTSVLPGWENTRVWILARPLSGATFSQYIVEVAPGGGSDRPEPDP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453  80 GVETFVYVISGKIEAKAEGKTFALTQGGYLYCPPGELLTFSNAQAEDSQLFLYKRRYTPVAGHS-PWLVSGNTNQLERIH 158
Cdd:COG3257   80 GAETFLFVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRNAGDEPARFHWIRKRYEPVEGLEaPEAFVGNEADVEPTP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453 159 YEGMDDVILLDFLPKELGFDMNMHILSFEPGASHGYIETHVQEHGAYILSGQGVYNLDNQWIPVKKGDYIFMGAYSLQAG 238
Cdd:COG3257  160 MPGTEGATTRFLLPEDLRFDMHVNIVTFEPGGSIPFVETHVMEHGLYVLEGKGVYRLNNDWVEVEAGDFIWMRAYCPQAC 239

                        250       260
                 ....*....|....*....|...
gi 489932453 239 YGVGRGEaFSYIYSKDCNRDVEI 261
Cdd:COG3257  240 YAGGPGP-FRYLLYKDVNRHPEL 261
PRK11171 PRK11171
(S)-ureidoglycine aminohydrolase;
1-261 1.73e-141

(S)-ureidoglycine aminohydrolase;


Pssm-ID: 183011 [Multi-domain]  Cd Length: 266  Bit Score: 397.73  E-value: 1.73e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453   1 MGYLNNVTGY--RDDLLANRAIVKHgNFALLTPDGLVKNIIPGFENCDVTILSTPKLGASFVDYLVTVHQSGGNQSGFGG 78
Cdd:PRK11171   2 MGYYAPVGGLppQTDLLTTRAVVTE-AYAVIPPDDIVTSVLPGWENTRAWVLARPGLGATFSQYLVEVEPGGGSDQPEPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453  79 EGVETFVYVISGKIEAKAEGKTFALTQGGYLYCPPGELLTFSNAQAEDSQLFLYKRRYTPVAGHS-PWLVSGNTNQLERI 157
Cdd:PRK11171  81 EGAETFLFVVEGEITLTLEGKTHALSEGGYAYLPPGSDWTLRNAGAEDARFHWIRKRYEPVEGHEaPEAFVGNESDIEPI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453 158 HYEGMDDVILLDFL--PKELGFDMNMHILSFEPGASHGYIETHVQEHGAYILSGQGVYNLDNQWIPVKKGDYIFMGAYSL 235
Cdd:PRK11171 161 PMPGTDGVWATTRLvdPEDLRFDMHVNIVTFEPGASIPFVETHVMEHGLYVLEGKGVYRLNNDWVEVEAGDFIWMRAYCP 240

                        250       260
                 ....*....|....*....|....*.
gi 489932453 236 QAGYGVGRGEaFSYIYSKDCNRDVEI 261
Cdd:PRK11171 241 QACYAGGPGP-FRYLLYKDVNRHPEL 265
cupin_UGlyAH_N cd02211
(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family ...
 35-150 9.51e-55

(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family includes the N-terminal cupin domain of (S)-ureidoglycine aminohydrolase (UGlyAH), an enzyme that converts (S)-ureidoglycine into (S)-ureidoglycolate and ammonia, providing the final substrate to the ureide pathway. The ureide pathway has recently been identified as the metabolic route of purine catabolism in plants and some bacteria where, uric acid, which is a major product of the early stage of purine catabolism, is degraded into glyoxylate and ammonia via stepwise reactions by seven different enzymes. Thus, this pathway has a possible physiological role in mobilization of purine ring nitrogen for further assimilation. This enzyme from Arabidopsis thaliana(AtUGlyAH) has been shown to bind a Mn2+ ion, via the C-terminal cupin domain, which acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. The structure of AtUGlyAH shows a bi-cupin fold with a conserved "jelly roll-like" beta-barrel fold and an octameric functional unit. Several structural homologs of UGlyAH, including the Escherichia coli ortholog YlbA (also known as GlxB6), also exhibit similar features.


Pssm-ID: 380341 [Multi-domain]  Cd Length: 117  Bit Score: 171.93  E-value: 9.51e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453  35 VKNIIPGFENCDVTILSTPKLGASFVDYLVTVHQSGGNQSGFGGEGVETFVYVISGKIEAKAEGKTFALTQGGYLYCPPG 114
Cdd:cd02211    1 VTSVLPGWENTRASVLASPKLGATFVQYLVEVEPGGGSTAPEGGEGIERFLYVLEGEVELTVGGETHTLTAGGYAYLPPG 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489932453 115 ELLTFSNAQAEDSQLFLYKRRYTPVAG-HSPWLVSGN 150
Cdd:cd02211   81 TKHSLRNAGDEPARLLWYKKRYEPLEGgAAPEVVVGN 117
Cupin_3 pfam05899
EutQ-like cupin domain; This entry represents the cupin domain, with a conserved jelly ...
 55-114 1.42e-08

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: 50.37  E-value: 1.42e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489932453   55 LGASFVDYLVTVHQSGGNQSGFGGEgvETFVYVISGKIEAKAE-GKTFALTQGGYLYCPPG 114
Cdd:pfam05899   1 LSPLGVFSWGIWECTPGKFRWTYEE--DETCYILSGEVTVTPEgGKTVTLRAGDLVVLPKG 59
 
Name Accession Description Interval E-value
ura-cupin TIGR03214
putative allantoin catabolism protein; This model represents a protein containing a tandem ...
 11-261 5.58e-151

putative allantoin catabolism protein; This model represents a protein containing a tandem arrangement of cupin domains (N-terminal part of pfam07883 and C-terminal more distantly related to pfam00190). This protein is found in the vicinity of genes involved in the catabolism of allantoin, a breakdown product of urate and sometimes of urate iteslf. The distribution of pathway components in the genomes in which this family is observed suggests that the function is linked to the allantoate catabolism to glyoxylate pathway (GenProp0686) since it is sometimes found in genomes lacking any elements of the xanthine-to-allantoin pathways (e.g. in Enterococcus faecalis).


Pssm-ID: 200251 [Multi-domain]  Cd Length: 252  Bit Score: 421.03  E-value: 5.58e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453   11 RDDLLANRAIVkHGNFALLTPDGLVKNIIPGFENCDVTILSTPKLG--ASFVDYLVTVHQSGGNQSGFGGEGVETFVYVI 88
Cdd:TIGR03214   1 QKQLLTTRAIF-TGNYAVITPDGLVSNIVPGFENTDIWILARPKLGfsATFVQYIVEVHPGGGATTGFGGEGIETFLFVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453   89 SGKIEAKAEGKTFALTQGGYLYCPPGELLTFSNAQAEDSQLFLYKRRYTPVAG-HSPWLVSGNTNQLERIHYEGMDDVIL 167
Cdd:TIGR03214  80 DGEVNVSLGGETHELEEGGYAYLPPGSKWTLENAQDEDARFFLYKKRYQPVEGlHAPEAVVGNERDIEPEAYEGMDDVWA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453  168 LDFLPKELGFDMNMHILSFEPGASHGYIETHVQEHGAYILSGQGVYNLDNQWIPVKKGDYIFMGAYSLQAGYGVGRGEaF 247
Cdd:TIGR03214 160 TTLLPKELAFDMNVHILSFEPGASHPYIETHVMEHGLYVLEGKGVYNLDNDWVPVEAGDYIWMGAYCPQACYAVGRGP-F 238

                         250
                  ....*....|....
gi 489932453  248 SYIYSKDCNRDVEI 261
Cdd:TIGR03214 239 RYLLYKDVNRHPKL 252
AllE COG3257
Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];
2-261 5.84e-143

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 442488 [Multi-domain]  Cd Length: 262  Bit Score: 401.12  E-value: 5.84e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453   2 GYLNNVTGY--RDDLLANRAIVKHgNFALLTPDGLVKNIIPGFENCDVTILSTPKLGASFVDYLVTVHQSGGNQSGFGGE 79
Cdd:COG3257    1 TYYAPKGGLppQTDLLTTRAVFTE-AYAVIPPDDIVTSVLPGWENTRVWILARPLSGATFSQYIVEVAPGGGSDRPEPDP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453  80 GVETFVYVISGKIEAKAEGKTFALTQGGYLYCPPGELLTFSNAQAEDSQLFLYKRRYTPVAGHS-PWLVSGNTNQLERIH 158
Cdd:COG3257   80 GAETFLFVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRNAGDEPARFHWIRKRYEPVEGLEaPEAFVGNEADVEPTP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453 159 YEGMDDVILLDFLPKELGFDMNMHILSFEPGASHGYIETHVQEHGAYILSGQGVYNLDNQWIPVKKGDYIFMGAYSLQAG 238
Cdd:COG3257  160 MPGTEGATTRFLLPEDLRFDMHVNIVTFEPGGSIPFVETHVMEHGLYVLEGKGVYRLNNDWVEVEAGDFIWMRAYCPQAC 239

                        250       260
                 ....*....|....*....|...
gi 489932453 239 YGVGRGEaFSYIYSKDCNRDVEI 261
Cdd:COG3257  240 YAGGPGP-FRYLLYKDVNRHPEL 261
PRK11171 PRK11171
(S)-ureidoglycine aminohydrolase;
1-261 1.73e-141

(S)-ureidoglycine aminohydrolase;


Pssm-ID: 183011 [Multi-domain]  Cd Length: 266  Bit Score: 397.73  E-value: 1.73e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453   1 MGYLNNVTGY--RDDLLANRAIVKHgNFALLTPDGLVKNIIPGFENCDVTILSTPKLGASFVDYLVTVHQSGGNQSGFGG 78
Cdd:PRK11171   2 MGYYAPVGGLppQTDLLTTRAVVTE-AYAVIPPDDIVTSVLPGWENTRAWVLARPGLGATFSQYLVEVEPGGGSDQPEPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453  79 EGVETFVYVISGKIEAKAEGKTFALTQGGYLYCPPGELLTFSNAQAEDSQLFLYKRRYTPVAGHS-PWLVSGNTNQLERI 157
Cdd:PRK11171  81 EGAETFLFVVEGEITLTLEGKTHALSEGGYAYLPPGSDWTLRNAGAEDARFHWIRKRYEPVEGHEaPEAFVGNESDIEPI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453 158 HYEGMDDVILLDFL--PKELGFDMNMHILSFEPGASHGYIETHVQEHGAYILSGQGVYNLDNQWIPVKKGDYIFMGAYSL 235
Cdd:PRK11171 161 PMPGTDGVWATTRLvdPEDLRFDMHVNIVTFEPGASIPFVETHVMEHGLYVLEGKGVYRLNNDWVEVEAGDFIWMRAYCP 240

                        250       260
                 ....*....|....*....|....*.
gi 489932453 236 QAGYGVGRGEaFSYIYSKDCNRDVEI 261
Cdd:PRK11171 241 QACYAGGPGP-FRYLLYKDVNRHPEL 265
cupin_UGlyAH_N cd02211
(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family ...
 35-150 9.51e-55

(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family includes the N-terminal cupin domain of (S)-ureidoglycine aminohydrolase (UGlyAH), an enzyme that converts (S)-ureidoglycine into (S)-ureidoglycolate and ammonia, providing the final substrate to the ureide pathway. The ureide pathway has recently been identified as the metabolic route of purine catabolism in plants and some bacteria where, uric acid, which is a major product of the early stage of purine catabolism, is degraded into glyoxylate and ammonia via stepwise reactions by seven different enzymes. Thus, this pathway has a possible physiological role in mobilization of purine ring nitrogen for further assimilation. This enzyme from Arabidopsis thaliana(AtUGlyAH) has been shown to bind a Mn2+ ion, via the C-terminal cupin domain, which acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. The structure of AtUGlyAH shows a bi-cupin fold with a conserved "jelly roll-like" beta-barrel fold and an octameric functional unit. Several structural homologs of UGlyAH, including the Escherichia coli ortholog YlbA (also known as GlxB6), also exhibit similar features.


Pssm-ID: 380341 [Multi-domain]  Cd Length: 117  Bit Score: 171.93  E-value: 9.51e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453  35 VKNIIPGFENCDVTILSTPKLGASFVDYLVTVHQSGGNQSGFGGEGVETFVYVISGKIEAKAEGKTFALTQGGYLYCPPG 114
Cdd:cd02211    1 VTSVLPGWENTRASVLASPKLGATFVQYLVEVEPGGGSTAPEGGEGIERFLYVLEGEVELTVGGETHTLTAGGYAYLPPG 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489932453 115 ELLTFSNAQAEDSQLFLYKRRYTPVAG-HSPWLVSGN 150
Cdd:cd02211   81 TKHSLRNAGDEPARLLWYKKRYEPLEGgAAPEVVVGN 117
cupin_UGlyAH_C cd02212
(S)-ureidoglycine aminohydrolase and related proteins, C-terminal cupin domain; This family ...
 165-257 2.63e-49

(S)-ureidoglycine aminohydrolase and related proteins, C-terminal cupin domain; This family includes the C-terminal cupin domain of (S)-Ureidoglycine aminohydrolase (UGlyAH), an enzyme that converts (S)-ureidoglycine into (S)-ureidoglycolate and ammonia, providing the final substrate to the ureide pathway. The ureide pathway has recently been identified as the metabolic route of purine catabolism in plants and some bacteria where, uric acid, which is a major product of the early stage of purine catabolism, is degraded into glyoxylate and ammonia via stepwise reactions by seven different enzymes. Thus, this pathway has a possible physiological role in mobilization of purine ring nitrogen for further assimilation. This enzyme from Arabidopsis thaliana(AtUGlyAH) has been shown to bind a Mn2+ ion,via the C-terminal cupin domain, which acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. The structure of AtUGlyAH shows a bi-cupin fold with a conserved "jelly roll-like" beta-barrel fold and an octameric functional unit. Several structural homologs of UGlyAH, including the Escherichia coli ortholog YlbA (also known as GlxB6), also exhibit similar features.


Pssm-ID: 380342 [Multi-domain]  Cd Length: 92  Bit Score: 157.27  E-value: 2.63e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453 165 VILLDFLPKELGFDMNMHILSFEPGASHGYIETHVQEHGAYILSGQGVYNLDNQWIPVKKGDYIFMGAYSLQAGYGVGRg 244
Cdd:cd02212    1 FELRKLLPDSDGFDMNVNIMTFEPGASLPFVETHVMEHGLYMLEGQGIYRLGDDWYPVQAGDFIWMAPYCPQWFYALGR- 79

                         90
                 ....*....|...
gi 489932453 245 EAFSYIYSKDCNR 257
Cdd:cd02212   80 EPFRYLLYKDVNR 92
Cupin_3 pfam05899
EutQ-like cupin domain; This entry represents the cupin domain, with a conserved jelly ...
 55-114 1.42e-08

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: 50.37  E-value: 1.42e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489932453   55 LGASFVDYLVTVHQSGGNQSGFGGEgvETFVYVISGKIEAKAE-GKTFALTQGGYLYCPPG 114
Cdd:pfam05899   1 LSPLGVFSWGIWECTPGKFRWTYEE--DETCYILSGEVTVTPEgGKTVTLRAGDLVVLPKG 59
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 186-229 9.86e-07

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: 45.90  E-value: 9.86e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 489932453 186 FEPGashGYI--ETHVQEHGAYILSGQGVYNLDNQWIPVKKGDYIF 229
Cdd:cd02222   24 IEPG---GHTplHTHPWEHEVYVLRGKGVVVIGGEEYPVKPGDVVY 66
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
178-232 2.86e-05

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 42.14  E-value: 2.86e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489932453 178 DMNMHILSFEPGASHGYiETHVQEHGAYILSGQGVYNLDNQWIPVKKGDYIFMGA 232
Cdd:COG1917   22 ELEVVRVTFEPGARTPW-HSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPP 75
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 182-229 3.94e-05

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: 40.70  E-value: 3.94e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 489932453  182 HILSFEPGASHGYIETHVQEHGAYILSGQGVYNLDNQWIPVKKGDYIF 229
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVY 48
cupin_TM1287-like cd02221
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ...
 187-229 6.57e-05

Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial proteins homologous to TM1287 decarboxylase, a Thermotoga maritima manganese-containing cupin thought to catalyze the conversion of oxalate to formate and carbon dioxide, due to its similarity to oxalate decarboxylase (OXDC) from Bacillus subtilis. TM1287 shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold and forms a homodimer.


Pssm-ID: 380350 [Multi-domain]  Cd Length: 93  Bit Score: 40.92  E-value: 6.57e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 489932453 187 EPGASHGYietHVQEHGA---YILSGQGVYNLDNQWIPVKKGDYIF 229
Cdd:cd02221   27 PPGSSIGY---HQHEGEFeiyYILSGEGLYTDNGKEYEVKAGDVTF 69
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
162-229 1.33e-03

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 37.43  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932453 162 MDDVILLDFLPKELGF---------DMNMHILSFEPGAShgyIETHVQEHGA---YILSGQGVYNLDNQWIPVKKGDYIF 229
Cdd:COG0662    1 MQDVNIEELKAIGWGSyevlgeggeRLSVKRITVPPGAE---LSLHVHPHRDeffYVLEGTGEVTIGDEEVELKAGDSVY 77
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
79-126 1.68e-03

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 37.30  E-value: 1.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489932453  79 EGVETFVYVISGKIEAKAEGKTFALTQGGYLYCPPGELLTFSNAQAED 126
Cdd:COG3837   48 SAEEEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLRNRGDEP 95
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
178-232 1.72e-03

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 37.30  E-value: 1.72e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489932453 178 DMNMHILSFEPGASHGYIETHV-QEHGAYILSGQGVYNLDNQWIPVKKGDYIFMGA 232
Cdd:COG3837   27 RLGVNLITLPPGASSSPYHAHSaEEEFVYVLEGELTLRIGGEEYVLEPGDSVGFPA 82
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
84-115 3.28e-03

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 35.98  E-value: 3.28e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 489932453  84 FVYVISGKIEAKAEGKTFALTQGGYLYCPPGE 115
Cdd:COG1917   46 LIYVLEGEGEVEVGGEEYELKPGDVVFIPPGV 77
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 179-232 5.09e-03

XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380339 [Multi-domain]  Cd Length: 90  Bit Score: 35.18  E-value: 5.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489932453 179 MNMHILSFEPGASHGYIETH-VQEHGaYILSGQGVYNLDNQWIPVKKGDYIFMGA 232
Cdd:cd02209   16 MEPFLVTLPPGGSGGEPYSHeGEEFG-YVLEGELELTVGGETYVLEAGDSIYFDS 69
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 181-246 5.15e-03

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: 34.77  E-value: 5.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489932453 181 MHILSFEPGASHGYIETHVQEHGAYILSGQGVYNLDNQ-WIPVKKGDYIFMGAYSLQAGYGVGRGEA 246
Cdd:cd02208    1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDDGeTVELKAGDIVLIPPGVPHSFVNTSDEPA 67
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 85-126 5.25e-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: 35.50  E-value: 5.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 489932453  85 VYVISGKIEAKAEGKTFALTQGGYLYCPPGELLTFSNAQAED 126
Cdd:cd02222   41 VYVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPHQFRNTGDEP 82
cupin_HP0902-like cd02230
Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes ...
 65-115 5.46e-03

Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.


Pssm-ID: 380358 [Multi-domain]  Cd Length: 83  Bit Score: 35.18  E-value: 5.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489932453  65 TVHQS-GGNQSGFG---GEGVET-------FVYVISGKIEAKAEGKTFALTQGGYLYCPPGE 115
Cdd:cd02230    4 TLVQDdGLRVTLFAfdaGQELSEhtapgdaTVQVLEGEAEFTIGGETVTLKAGELIVMPANV 65
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 79-122 6.05e-03

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: 34.54  E-value: 6.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 489932453   79 EGVETFVYVISGKIEAKAEGKTFALTQGGYLYCPPGELLTFSNA 122
Cdd:pfam07883  17 PGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNT 60
cupin_Pac13-like cd20295
monomeric dehydratase Pac13 and related proteins, cupin domain; This family includes a small ...
 205-228 8.60e-03

monomeric dehydratase Pac13 and related proteins, cupin domain; This family includes a small monomeric dehydratase Pac13 that mediates the formation of the 3'-deoxynucleotide of pacidamycins, which are uradyl peptide antibiotics (UPAs). Pac13 is involved in the formation of the unique 3'-deoxyuridine moiety found in these UPAs; it catalyzes the dehydration of uridine-5'-aldehyde. The similarity of the 3'-deoxy pacidamycin moiety with synthetic anti-retrovirals, offers a potential opportunity for the utilization of Pac13 in the biocatalytic generation of antiviral compounds. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380429 [Multi-domain]  Cd Length: 101  Bit Score: 34.89  E-value: 8.60e-03
                         10        20
                 ....*....|....*....|....
gi 489932453 205 YILSGQGVYNLDNQWIPVKKGDYI 228
Cdd:cd20295   46 YVLEGEGIFELDGEAVPVKPGDLV 69
 
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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