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Conserved domains on  [gi|446463143|ref|WP_000540997|]
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MULTISPECIES: (S)-ureidoglycine aminohydrolase [Enterobacteriaceae]

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 5.92e-145

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: 406.01  E-value: 5.92e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143   11 REDLLANRAIVkHGNFALLTPDGLVKNIIPGFENCDATILSTPKLG--ASFVDYLVTLHQNGGNQQGFGGEGIETFLYVI 88
Cdd:TIGR03214   1 QKQLLTTRAIF-TGNYAVITPDGLVSNIVPGFENTDIWILARPKLGfsATFVQYIVEVHPGGGATTGFGGEGIETFLFVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143   89 SGNITAKAEGKTFALSEGGYLYCPPGSLMTFVNAQAEDSQIFLYKRRYVPVEGY-APWLVSGNASELERIHYEGMDDVIL 167
Cdd:TIGR03214  80 DGEVNVSLGGETHELEEGGYAYLPPGSKWTLENAQDEDARFFLYKKRYQPVEGLhAPEAVVGNERDIEPEAYEGMDDVWA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143  168 LDFLPKELGFDMNMHILSFAPGASHGYIETHVQEHGAYILSGQGVYNLDNNWIPVKKGDYIFMGAYSLQAGYGVGRGEaF 247
Cdd:TIGR03214 160 TTLLPKELAFDMNVHILSFEPGASHPYIETHVMEHGLYVLEGKGVYNLDNDWVPVEAGDYIWMGAYCPQACYAVGRGP-F 238

                         250
                  ....*....|....
gi 446463143  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 5.92e-145

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: 406.01  E-value: 5.92e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143   11 REDLLANRAIVkHGNFALLTPDGLVKNIIPGFENCDATILSTPKLG--ASFVDYLVTLHQNGGNQQGFGGEGIETFLYVI 88
Cdd:TIGR03214   1 QKQLLTTRAIF-TGNYAVITPDGLVSNIVPGFENTDIWILARPKLGfsATFVQYIVEVHPGGGATTGFGGEGIETFLFVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143   89 SGNITAKAEGKTFALSEGGYLYCPPGSLMTFVNAQAEDSQIFLYKRRYVPVEGY-APWLVSGNASELERIHYEGMDDVIL 167
Cdd:TIGR03214  80 DGEVNVSLGGETHELEEGGYAYLPPGSKWTLENAQDEDARFFLYKKRYQPVEGLhAPEAVVGNERDIEPEAYEGMDDVWA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143  168 LDFLPKELGFDMNMHILSFAPGASHGYIETHVQEHGAYILSGQGVYNLDNNWIPVKKGDYIFMGAYSLQAGYGVGRGEaF 247
Cdd:TIGR03214 160 TTLLPKELAFDMNVHILSFEPGASHPYIETHVMEHGLYVLEGKGVYNLDNDWVPVEAGDYIWMGAYCPQACYAVGRGP-F 238

                         250
                  ....*....|....
gi 446463143  248 SYIYSKDCNRDVEI 261
Cdd:TIGR03214 239 RYLLYKDVNRHPKL 252
PRK11171 PRK11171
(S)-ureidoglycine aminohydrolase;
1-261 3.26e-136

(S)-ureidoglycine aminohydrolase;


Pssm-ID: 183011 [Multi-domain]  Cd Length: 266  Bit Score: 384.25  E-value: 3.26e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143   1 MGYLNNVTGY--REDLLANRAIVKHgNFALLTPDGLVKNIIPGFENCDATILSTPKLGASFVDYLVTLHQNGGNQQGFGG 78
Cdd:PRK11171   2 MGYYAPVGGLppQTDLLTTRAVVTE-AYAVIPPDDIVTSVLPGWENTRAWVLARPGLGATFSQYLVEVEPGGGSDQPEPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143  79 EGIETFLYVISGNITAKAEGKTFALSEGGYLYCPPGSLMTFVNAQAEDSQIFLYKRRYVPVEGY-APWLVSGNASELERI 157
Cdd:PRK11171  81 EGAETFLFVVEGEITLTLEGKTHALSEGGYAYLPPGSDWTLRNAGAEDARFHWIRKRYEPVEGHeAPEAFVGNESDIEPI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143 158 HYEGMDDVILLDFL--PKELGFDMNMHILSFAPGASHGYIETHVQEHGAYILSGQGVYNLDNNWIPVKKGDYIFMGAYSL 235
Cdd:PRK11171 161 PMPGTDGVWATTRLvdPEDLRFDMHVNIVTFEPGASIPFVETHVMEHGLYVLEGKGVYRLNNDWVEVEAGDFIWMRAYCP 240

                        250       260
                 ....*....|....*....|....*.
gi 446463143 236 QAGYGVGRGEaFSYIYSKDCNRDVEI 261
Cdd:PRK11171 241 QACYAGGPGP-FRYLLYKDVNRHPEL 265
AllE COG3257
Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];
2-261 1.68e-134

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 442488 [Multi-domain]  Cd Length: 262  Bit Score: 379.94  E-value: 1.68e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143   2 GYLNNVTGY--REDLLANRAIVKHgNFALLTPDGLVKNIIPGFENCDATILSTPKLGASFVDYLVTLHQNGGNQQGFGGE 79
Cdd:COG3257    1 TYYAPKGGLppQTDLLTTRAVFTE-AYAVIPPDDIVTSVLPGWENTRVWILARPLSGATFSQYIVEVAPGGGSDRPEPDP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143  80 GIETFLYVISGNITAKAEGKTFALSEGGYLYCPPGSLMTFVNAQAEDSQIFLYKRRYVPVEGY-APWLVSGNASELERIH 158
Cdd:COG3257   80 GAETFLFVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRNAGDEPARFHWIRKRYEPVEGLeAPEAFVGNEADVEPTP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143 159 YEGMDDVILLDFLPKELGFDMNMHILSFAPGASHGYIETHVQEHGAYILSGQGVYNLDNNWIPVKKGDYIFMGAYSLQAG 238
Cdd:COG3257  160 MPGTEGATTRFLLPEDLRFDMHVNIVTFEPGGSIPFVETHVMEHGLYVLEGKGVYRLNNDWVEVEAGDFIWMRAYCPQAC 239

                        250       260
                 ....*....|....*....|...
gi 446463143 239 YGVGRGEaFSYIYSKDCNRDVEI 261
Cdd:COG3257  240 YAGGPGP-FRYLLYKDVNRHPEL 261
cupin_UGlyAH_C cd02212
(S)-ureidoglycine aminohydrolase and related proteins, C-terminal cupin domain; This family ...
 165-257 9.79e-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: 156.11  E-value: 9.79e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143 165 VILLDFLPKELGFDMNMHILSFAPGASHGYIETHVQEHGAYILSGQGVYNLDNNWIPVKKGDYIFMGAYSLQAGYGVGRg 244
Cdd:cd02212    1 FELRKLLPDSDGFDMNVNIMTFEPGASLPFVETHVMEHGLYMLEGQGIYRLGDDWYPVQAGDFIWMAPYCPQWFYALGR- 79

                         90
                 ....*....|...
gi 446463143 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 ...
 81-136 8.76e-06

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: 42.66  E-value: 8.76e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446463143   81 IETFlYVISGNITAKAE-GKTFALSEGGYLYCPPGSlmtfvnAQAEDSQIFlYKRRY 136
Cdd:pfam05899  26 DETC-YILSGEVTVTPEgGKTVTLRAGDLVVLPKGL------SGTWDVLET-VRKHY 74
 
Name Accession Description Interval E-value
ura-cupin TIGR03214
putative allantoin catabolism protein; This model represents a protein containing a tandem ...
 11-261 5.92e-145

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: 406.01  E-value: 5.92e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143   11 REDLLANRAIVkHGNFALLTPDGLVKNIIPGFENCDATILSTPKLG--ASFVDYLVTLHQNGGNQQGFGGEGIETFLYVI 88
Cdd:TIGR03214   1 QKQLLTTRAIF-TGNYAVITPDGLVSNIVPGFENTDIWILARPKLGfsATFVQYIVEVHPGGGATTGFGGEGIETFLFVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143   89 SGNITAKAEGKTFALSEGGYLYCPPGSLMTFVNAQAEDSQIFLYKRRYVPVEGY-APWLVSGNASELERIHYEGMDDVIL 167
Cdd:TIGR03214  80 DGEVNVSLGGETHELEEGGYAYLPPGSKWTLENAQDEDARFFLYKKRYQPVEGLhAPEAVVGNERDIEPEAYEGMDDVWA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143  168 LDFLPKELGFDMNMHILSFAPGASHGYIETHVQEHGAYILSGQGVYNLDNNWIPVKKGDYIFMGAYSLQAGYGVGRGEaF 247
Cdd:TIGR03214 160 TTLLPKELAFDMNVHILSFEPGASHPYIETHVMEHGLYVLEGKGVYNLDNDWVPVEAGDYIWMGAYCPQACYAVGRGP-F 238

                         250
                  ....*....|....
gi 446463143  248 SYIYSKDCNRDVEI 261
Cdd:TIGR03214 239 RYLLYKDVNRHPKL 252
PRK11171 PRK11171
(S)-ureidoglycine aminohydrolase;
1-261 3.26e-136

(S)-ureidoglycine aminohydrolase;


Pssm-ID: 183011 [Multi-domain]  Cd Length: 266  Bit Score: 384.25  E-value: 3.26e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143   1 MGYLNNVTGY--REDLLANRAIVKHgNFALLTPDGLVKNIIPGFENCDATILSTPKLGASFVDYLVTLHQNGGNQQGFGG 78
Cdd:PRK11171   2 MGYYAPVGGLppQTDLLTTRAVVTE-AYAVIPPDDIVTSVLPGWENTRAWVLARPGLGATFSQYLVEVEPGGGSDQPEPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143  79 EGIETFLYVISGNITAKAEGKTFALSEGGYLYCPPGSLMTFVNAQAEDSQIFLYKRRYVPVEGY-APWLVSGNASELERI 157
Cdd:PRK11171  81 EGAETFLFVVEGEITLTLEGKTHALSEGGYAYLPPGSDWTLRNAGAEDARFHWIRKRYEPVEGHeAPEAFVGNESDIEPI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143 158 HYEGMDDVILLDFL--PKELGFDMNMHILSFAPGASHGYIETHVQEHGAYILSGQGVYNLDNNWIPVKKGDYIFMGAYSL 235
Cdd:PRK11171 161 PMPGTDGVWATTRLvdPEDLRFDMHVNIVTFEPGASIPFVETHVMEHGLYVLEGKGVYRLNNDWVEVEAGDFIWMRAYCP 240

                        250       260
                 ....*....|....*....|....*.
gi 446463143 236 QAGYGVGRGEaFSYIYSKDCNRDVEI 261
Cdd:PRK11171 241 QACYAGGPGP-FRYLLYKDVNRHPEL 265
AllE COG3257
Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];
2-261 1.68e-134

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 442488 [Multi-domain]  Cd Length: 262  Bit Score: 379.94  E-value: 1.68e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143   2 GYLNNVTGY--REDLLANRAIVKHgNFALLTPDGLVKNIIPGFENCDATILSTPKLGASFVDYLVTLHQNGGNQQGFGGE 79
Cdd:COG3257    1 TYYAPKGGLppQTDLLTTRAVFTE-AYAVIPPDDIVTSVLPGWENTRVWILARPLSGATFSQYIVEVAPGGGSDRPEPDP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143  80 GIETFLYVISGNITAKAEGKTFALSEGGYLYCPPGSLMTFVNAQAEDSQIFLYKRRYVPVEGY-APWLVSGNASELERIH 158
Cdd:COG3257   80 GAETFLFVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRNAGDEPARFHWIRKRYEPVEGLeAPEAFVGNEADVEPTP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143 159 YEGMDDVILLDFLPKELGFDMNMHILSFAPGASHGYIETHVQEHGAYILSGQGVYNLDNNWIPVKKGDYIFMGAYSLQAG 238
Cdd:COG3257  160 MPGTEGATTRFLLPEDLRFDMHVNIVTFEPGGSIPFVETHVMEHGLYVLEGKGVYRLNNDWVEVEAGDFIWMRAYCPQAC 239

                        250       260
                 ....*....|....*....|...
gi 446463143 239 YGVGRGEaFSYIYSKDCNRDVEI 261
Cdd:COG3257  240 YAGGPGP-FRYLLYKDVNRHPEL 261
cupin_UGlyAH_C cd02212
(S)-ureidoglycine aminohydrolase and related proteins, C-terminal cupin domain; This family ...
 165-257 9.79e-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: 156.11  E-value: 9.79e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143 165 VILLDFLPKELGFDMNMHILSFAPGASHGYIETHVQEHGAYILSGQGVYNLDNNWIPVKKGDYIFMGAYSLQAGYGVGRg 244
Cdd:cd02212    1 FELRKLLPDSDGFDMNVNIMTFEPGASLPFVETHVMEHGLYMLEGQGIYRLGDDWYPVQAGDFIWMAPYCPQWFYALGR- 79

                         90
                 ....*....|...
gi 446463143 245 EAFSYIYSKDCNR 257
Cdd:cd02212   80 EPFRYLLYKDVNR 92
cupin_UGlyAH_N cd02211
(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family ...
 35-150 4.61e-47

(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: 152.67  E-value: 4.61e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143  35 VKNIIPGFENCDATILSTPKLGASFVDYLVTLHQNGGNQQGFGGEGIETFLYVISGNITAKAEGKTFALSEGGYLYCPPG 114
Cdd:cd02211    1 VTSVLPGWENTRASVLASPKLGATFVQYLVEVEPGGGSTAPEGGEGIERFLYVLEGEVELTVGGETHTLTAGGYAYLPPG 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446463143 115 SLMTFVNAQAEDSQIFLYKRRYVPVEG-YAPWLVSGN 150
Cdd:cd02211   81 TKHSLRNAGDEPARLLWYKKRYEPLEGgAAPEVVVGN 117
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 172-229 3.49e-06

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: 44.36  E-value: 3.49e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143 172 PKELGFDMNMHILSFAPGashGYI--ETHVQEHGAYILSGQGVYNLDNNWIPVKKGDYIF 229
Cdd:cd02222   10 PEDGAPNFAMRYFEIEPG---GHTplHTHPWEHEVYVLRGKGVVVIGGEEYPVKPGDVVY 66
Cupin_3 pfam05899
EutQ-like cupin domain; This entry represents the cupin domain, with a conserved jelly ...
 81-136 8.76e-06

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: 42.66  E-value: 8.76e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446463143   81 IETFlYVISGNITAKAE-GKTFALSEGGYLYCPPGSlmtfvnAQAEDSQIFlYKRRY 136
Cdd:pfam05899  26 DETC-YILSGEVTVTPEgGKTVTLRAGDLVVLPKGL------SGTWDVLET-VRKHY 74
cupin_TM1287-like cd02221
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ...
 165-229 3.11e-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: 41.69  E-value: 3.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446463143 165 VILLDFLPKElgfDMNMHILSFA-----PGASHGYietHVQEHGA---YILSGQGVYNLDNNWIPVKKGDYIF 229
Cdd:cd02221    3 VTVYHLLTPE---ELKGKGRLFArvtlpPGSSIGY---HQHEGEFeiyYILSGEGLYTDNGKEYEVKAGDVTF 69
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 182-229 6.98e-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: 39.93  E-value: 6.98e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 446463143  182 HILSFAPGASHGYIETHVQEHGAYILSGQGVYNLDNNWIPVKKGDYIF 229
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVY 48
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
178-232 1.02e-04

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 40.60  E-value: 1.02e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446463143 178 DMNMHILSFAPGASHGYiETHVQEHGAYILSGQGVYNLDNNWIPVKKGDYIFMGA 232
Cdd:COG1917   22 ELEVVRVTFEPGARTPW-HSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPP 75
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
84-121 8.54e-04

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 37.91  E-value: 8.54e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446463143  84 FLYVISGNITAKAEGKTFALSEGGYLYCPPGSLMTFVN 121
Cdd:COG1917   46 LIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRN 83
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
82-126 2.75e-03

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 36.53  E-value: 2.75e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446463143  82 ETFLYVISGNITAKAEGKTFALSEGGYLYCPPGSLMTFVNAQAED 126
Cdd:COG3837   51 EEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLRNRGDEP 95
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
162-229 4.56e-03

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 35.89  E-value: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463143 162 MDDVILLDFLPKELGF---------DMNMHILSFAPGAShgyIETHVQEHGA---YILSGQGVYNLDNNWIPVKKGDYIF 229
Cdd:COG0662    1 MQDVNIEELKAIGWGSyevlgeggeRLSVKRITVPPGAE---LSLHVHPHRDeffYVLEGTGEVTIGDEEVELKAGDSVY 77
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 82-130 4.71e-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: 35.15  E-value: 4.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446463143  82 ETFLYVISGNITAKAE-GKTFALSEGGYLYCPPGSLMTFVNAQAEDSQIF 130
Cdd:cd02208   21 DEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFL 70
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
178-232 7.44e-03

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 35.38  E-value: 7.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446463143 178 DMNMHILSFAPGASHGYIETHV-QEHGAYILSGQGVYNLDNNWIPVKKGDYIFMGA 232
Cdd:COG3837   27 RLGVNLITLPPGASSSPYHAHSaEEEFVYVLEGELTLRIGGEEYVLEPGDSVGFPA 82
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 181-246 8.51e-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: 34.38  E-value: 8.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446463143 181 MHILSFAPGASHGYIETHVQEHGAYILSGQGVYNLD-NNWIPVKKGDYIFMGAYSLQAGYGVGRGEA 246
Cdd:cd02208    1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSDEPA 67
 
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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