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Conserved domains on  [gi|1906352649|ref|WP_189120964|]
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bifunctional allantoicase/(S)-ureidoglycine aminohydrolase [Nocardioides luteus]

Protein Classification

(S)-ureidoglycine aminohydrolase family protein( domain architecture ID 11485243)

(S)-ureidoglycine aminohydrolase family protein similar to (S)-ureidoglycine aminohydrolase, which hydrolyzes (S)-2-ureidoglycine to yield (S)-ureidoglycolate and ammonia in the ureide pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAH_UGLYAH2 NF040771
bifunctional allantoicase/(S)-ureidoglycine aminohydrolase, UGLYAH2 family; The UGLYAH2 family ...
 11-277 0e+00

bifunctional allantoicase/(S)-ureidoglycine aminohydrolase, UGLYAH2 family; The UGLYAH2 family acts primarily as allantoicase (allantoate amidinohydrolase, EC 3.5.3.4), while unrelated to the AllC family of allantoicase enzymes. It belongs to a broader family of enzymes with (S)-ureidoglycine aminohydrolase activity (EC 3.5.3.26) carried out at the same active site. However, Puggioni, et al. consider that activity secondary, as (S)-ureidoglycine is an unstable compound expected only as a product of allantoate amidohydrolase (AAH) activity, and AAH is nearly always absent when UGLYAH2 is present. UGLYAH2 is an acronym for (S)-ureidoglycine aminohydrolase type 2.


:

Pssm-ID: 468730  Cd Length: 267  Bit Score: 596.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  11 YYAPTGGHPSQRELTTDRAVFTEAYAVLPRGTMRDIVTSKLPFWDETRLWVIARPLSGFAETFSQYIVEVSPGGGSDKPE 90
Cdd:NF040771    1 YYAPPGGLPPQTDLLTDRAVFTEAYAVIPKGVMRDIVTSFLPFWEGTRAWVLARPLSGFAETFSQYIMEVAPGGGSDRPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  91 LDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTSDQVARFHWIRKAYQRVEGIDLPEPFVTNETDVE 170
Cdd:NF040771   81 PDPGAEGVLFVVEGELTLTIDGEEHELTPGGYAYLPPGADWTLRNGGDAPARFHWIRKAYEPVEGLDAPEAFVTNERDIE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649 171 GGEMPGTDGAWKTQRFVDPDDVRHDMHVNIVSFEPGGAIPFPETHVMEHGLYVLEGKAVYLLNKDWVEVQEGDFMWLRAF 250
Cdd:NF040771  161 PTPMPDTDGAWATTRFVDPADLRHDMHVNIVTFEPGGVIPFAETHVMEHGLYVLEGKAVYRLNQDWVEVEAGDFMWLRAF 240

                         250       260
                  ....*....|....*....|....*..
gi 1906352649 251 CPQACYAGGPGRFRYLLYKDVNRHAVL 277
Cdd:NF040771  241 CPQACYAGGPGPFRYLLYKDVNRHMPL 267
 
Name Accession Description Interval E-value
AAH_UGLYAH2 NF040771
bifunctional allantoicase/(S)-ureidoglycine aminohydrolase, UGLYAH2 family; The UGLYAH2 family ...
 11-277 0e+00

bifunctional allantoicase/(S)-ureidoglycine aminohydrolase, UGLYAH2 family; The UGLYAH2 family acts primarily as allantoicase (allantoate amidinohydrolase, EC 3.5.3.4), while unrelated to the AllC family of allantoicase enzymes. It belongs to a broader family of enzymes with (S)-ureidoglycine aminohydrolase activity (EC 3.5.3.26) carried out at the same active site. However, Puggioni, et al. consider that activity secondary, as (S)-ureidoglycine is an unstable compound expected only as a product of allantoate amidohydrolase (AAH) activity, and AAH is nearly always absent when UGLYAH2 is present. UGLYAH2 is an acronym for (S)-ureidoglycine aminohydrolase type 2.


Pssm-ID: 468730  Cd Length: 267  Bit Score: 596.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  11 YYAPTGGHPSQRELTTDRAVFTEAYAVLPRGTMRDIVTSKLPFWDETRLWVIARPLSGFAETFSQYIVEVSPGGGSDKPE 90
Cdd:NF040771    1 YYAPPGGLPPQTDLLTDRAVFTEAYAVIPKGVMRDIVTSFLPFWEGTRAWVLARPLSGFAETFSQYIMEVAPGGGSDRPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  91 LDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTSDQVARFHWIRKAYQRVEGIDLPEPFVTNETDVE 170
Cdd:NF040771   81 PDPGAEGVLFVVEGELTLTIDGEEHELTPGGYAYLPPGADWTLRNGGDAPARFHWIRKAYEPVEGLDAPEAFVTNERDIE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649 171 GGEMPGTDGAWKTQRFVDPDDVRHDMHVNIVSFEPGGAIPFPETHVMEHGLYVLEGKAVYLLNKDWVEVQEGDFMWLRAF 250
Cdd:NF040771  161 PTPMPDTDGAWATTRFVDPADLRHDMHVNIVTFEPGGVIPFAETHVMEHGLYVLEGKAVYRLNQDWVEVEAGDFMWLRAF 240

                         250       260
                  ....*....|....*....|....*..
gi 1906352649 251 CPQACYAGGPGRFRYLLYKDVNRHAVL 277
Cdd:NF040771  241 CPQACYAGGPGPFRYLLYKDVNRHMPL 267
AllE COG3257
Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];
11-277 0e+00

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 442488 [Multi-domain]  Cd Length: 262  Bit Score: 500.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  11 YYAPTGGHPSQRELTTDRAVFTEAYAVLPRgtmRDIVTSKLPFWDETRLWVIARPLSGFaeTFSQYIVEVSPGGGSDKPE 90
Cdd:COG3257     2 YYAPKGGLPPQTDLLTTRAVFTEAYAVIPP---DDIVTSVLPGWENTRVWILARPLSGA--TFSQYIVEVAPGGGSDRPE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  91 LDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTSDQVARFHWIRKAYQRVEGIDLPEPFVTNETDVE 170
Cdd:COG3257    77 PDPGAETFLFVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRNAGDEPARFHWIRKRYEPVEGLEAPEAFVGNEADVE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649 171 GGEMPGTDGAwkTQRFVDPDDVRHDMHVNIVSFEPGGAIPFPETHVMEHGLYVLEGKAVYLLNKDWVEVQEGDFMWLRAF 250
Cdd:COG3257   157 PTPMPGTEGA--TTRFLLPEDLRFDMHVNIVTFEPGGSIPFVETHVMEHGLYVLEGKGVYRLNNDWVEVEAGDFIWMRAY 234

                         250       260
                  ....*....|....*....|....*..
gi 1906352649 251 CPQACYAGGPGRFRYLLYKDVNRHAVL 277
Cdd:COG3257   235 CPQACYAGGPGPFRYLLYKDVNRHPEL 261
PRK11171 PRK11171
(S)-ureidoglycine aminohydrolase;
11-277 1.27e-176

(S)-ureidoglycine aminohydrolase;


Pssm-ID: 183011 [Multi-domain]  Cd Length: 266  Bit Score: 487.48  E-value: 1.27e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  11 YYAPTGGHPSQRELTTDRAVFTEAYAVLPRGtmrDIVTSKLPFWDETRLWVIARPlsGFAETFSQYIVEVSPGGGSDKPE 90
Cdd:PRK11171    4 YYAPVGGLPPQTDLLTTRAVVTEAYAVIPPD---DIVTSVLPGWENTRAWVLARP--GLGATFSQYLVEVEPGGGSDQPE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  91 LDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTSDQVARFHWIRKAYQRVEGIDLPEPFVTNETDVE 170
Cdd:PRK11171   79 PDEGAETFLFVVEGEITLTLEGKTHALSEGGYAYLPPGSDWTLRNAGAEDARFHWIRKRYEPVEGHEAPEAFVGNESDIE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649 171 GGEMPGTDGAWKTQRFVDPDDVRHDMHVNIVSFEPGGAIPFPETHVMEHGLYVLEGKAVYLLNKDWVEVQEGDFMWLRAF 250
Cdd:PRK11171  159 PIPMPGTDGVWATTRLVDPEDLRFDMHVNIVTFEPGASIPFVETHVMEHGLYVLEGKGVYRLNNDWVEVEAGDFIWMRAY 238

                         250       260
                  ....*....|....*....|....*..
gi 1906352649 251 CPQACYAGGPGRFRYLLYKDVNRHAVL 277
Cdd:PRK11171  239 CPQACYAGGPGPFRYLLYKDVNRHPEL 265
ura-cupin TIGR03214
putative allantoin catabolism protein; This model represents a protein containing a tandem ...
 21-277 4.61e-144

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: 404.46  E-value: 4.61e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  21 QRELTTDRAVFTEAYAVL-PRGTMRDIVtsklPFWDETRLWVIARPLSGFAETFSQYIVEVSPGGGSDKPELDAGAEGVL 99
Cdd:TIGR03214   1 QKQLLTTRAIFTGNYAVItPDGLVSNIV----PGFENTDIWILARPKLGFSATFVQYIVEVHPGGGATTGFGGEGIETFL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649 100 FVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTSDQVARFHWIRKAYQRVEGIDLPEPFVTNETDVEGGEMPGTDG 179
Cdd:TIGR03214  77 FVIDGEVNVSLGGETHELEEGGYAYLPPGSKWTLENAQDEDARFFLYKKRYQPVEGLHAPEAVVGNERDIEPEAYEGMDD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649 180 AWKTQRFvdPDDVRHDMHVNIVSFEPGGAIPFPETHVMEHGLYVLEGKAVYLLNKDWVEVQEGDFMWLRAFCPQACYAGG 259
Cdd:TIGR03214 157 VWATTLL--PKELAFDMNVHILSFEPGASHPYIETHVMEHGLYVLEGKGVYNLDNDWVPVEAGDYIWMGAYCPQACYAVG 234

                         250
                  ....*....|....*...
gi 1906352649 260 PGRFRYLLYKDVNRHAVL 277
Cdd:TIGR03214 235 RGPFRYLLYKDVNRHPKL 252
cupin_UGlyAH_N cd02211
(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family ...
 47-165 1.06e-56

(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: 177.71  E-value: 1.06e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  47 VTSKLPFWDETRLWVIARPLSGfaETFSQYIVEVSPGGGSDKPELDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLP 126
Cdd:cd02211     1 VTSVLPGWENTRASVLASPKLG--ATFVQYLVEVEPGGGSTAPEGGEGIERFLYVLEGEVELTVGGETHTLTAGGYAYLP 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1906352649 127 PGCTWTLHNTSDQVARFHWIRKAYQRVEGIDLPEPFVTN 165
Cdd:cd02211    79 PGTKHSLRNAGDEPARLLWYKKRYEPLEGGAAPEVVVGN 117
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 76-146 9.56e-09

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: 51.10  E-value: 9.56e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906352649  76 YIVEVSPGGGSdKPELDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTSDQVARFHWI 146
Cdd:pfam07883   1 GLVTLPPGESS-PPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDV 70
 
Name Accession Description Interval E-value
AAH_UGLYAH2 NF040771
bifunctional allantoicase/(S)-ureidoglycine aminohydrolase, UGLYAH2 family; The UGLYAH2 family ...
 11-277 0e+00

bifunctional allantoicase/(S)-ureidoglycine aminohydrolase, UGLYAH2 family; The UGLYAH2 family acts primarily as allantoicase (allantoate amidinohydrolase, EC 3.5.3.4), while unrelated to the AllC family of allantoicase enzymes. It belongs to a broader family of enzymes with (S)-ureidoglycine aminohydrolase activity (EC 3.5.3.26) carried out at the same active site. However, Puggioni, et al. consider that activity secondary, as (S)-ureidoglycine is an unstable compound expected only as a product of allantoate amidohydrolase (AAH) activity, and AAH is nearly always absent when UGLYAH2 is present. UGLYAH2 is an acronym for (S)-ureidoglycine aminohydrolase type 2.


Pssm-ID: 468730  Cd Length: 267  Bit Score: 596.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  11 YYAPTGGHPSQRELTTDRAVFTEAYAVLPRGTMRDIVTSKLPFWDETRLWVIARPLSGFAETFSQYIVEVSPGGGSDKPE 90
Cdd:NF040771    1 YYAPPGGLPPQTDLLTDRAVFTEAYAVIPKGVMRDIVTSFLPFWEGTRAWVLARPLSGFAETFSQYIMEVAPGGGSDRPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  91 LDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTSDQVARFHWIRKAYQRVEGIDLPEPFVTNETDVE 170
Cdd:NF040771   81 PDPGAEGVLFVVEGELTLTIDGEEHELTPGGYAYLPPGADWTLRNGGDAPARFHWIRKAYEPVEGLDAPEAFVTNERDIE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649 171 GGEMPGTDGAWKTQRFVDPDDVRHDMHVNIVSFEPGGAIPFPETHVMEHGLYVLEGKAVYLLNKDWVEVQEGDFMWLRAF 250
Cdd:NF040771  161 PTPMPDTDGAWATTRFVDPADLRHDMHVNIVTFEPGGVIPFAETHVMEHGLYVLEGKAVYRLNQDWVEVEAGDFMWLRAF 240

                         250       260
                  ....*....|....*....|....*..
gi 1906352649 251 CPQACYAGGPGRFRYLLYKDVNRHAVL 277
Cdd:NF040771  241 CPQACYAGGPGPFRYLLYKDVNRHMPL 267
AllE COG3257
Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];
11-277 0e+00

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 442488 [Multi-domain]  Cd Length: 262  Bit Score: 500.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  11 YYAPTGGHPSQRELTTDRAVFTEAYAVLPRgtmRDIVTSKLPFWDETRLWVIARPLSGFaeTFSQYIVEVSPGGGSDKPE 90
Cdd:COG3257     2 YYAPKGGLPPQTDLLTTRAVFTEAYAVIPP---DDIVTSVLPGWENTRVWILARPLSGA--TFSQYIVEVAPGGGSDRPE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  91 LDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTSDQVARFHWIRKAYQRVEGIDLPEPFVTNETDVE 170
Cdd:COG3257    77 PDPGAETFLFVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRNAGDEPARFHWIRKRYEPVEGLEAPEAFVGNEADVE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649 171 GGEMPGTDGAwkTQRFVDPDDVRHDMHVNIVSFEPGGAIPFPETHVMEHGLYVLEGKAVYLLNKDWVEVQEGDFMWLRAF 250
Cdd:COG3257   157 PTPMPGTEGA--TTRFLLPEDLRFDMHVNIVTFEPGGSIPFVETHVMEHGLYVLEGKGVYRLNNDWVEVEAGDFIWMRAY 234

                         250       260
                  ....*....|....*....|....*..
gi 1906352649 251 CPQACYAGGPGRFRYLLYKDVNRHAVL 277
Cdd:COG3257   235 CPQACYAGGPGPFRYLLYKDVNRHPEL 261
PRK11171 PRK11171
(S)-ureidoglycine aminohydrolase;
11-277 1.27e-176

(S)-ureidoglycine aminohydrolase;


Pssm-ID: 183011 [Multi-domain]  Cd Length: 266  Bit Score: 487.48  E-value: 1.27e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  11 YYAPTGGHPSQRELTTDRAVFTEAYAVLPRGtmrDIVTSKLPFWDETRLWVIARPlsGFAETFSQYIVEVSPGGGSDKPE 90
Cdd:PRK11171    4 YYAPVGGLPPQTDLLTTRAVVTEAYAVIPPD---DIVTSVLPGWENTRAWVLARP--GLGATFSQYLVEVEPGGGSDQPE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  91 LDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTSDQVARFHWIRKAYQRVEGIDLPEPFVTNETDVE 170
Cdd:PRK11171   79 PDEGAETFLFVVEGEITLTLEGKTHALSEGGYAYLPPGSDWTLRNAGAEDARFHWIRKRYEPVEGHEAPEAFVGNESDIE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649 171 GGEMPGTDGAWKTQRFVDPDDVRHDMHVNIVSFEPGGAIPFPETHVMEHGLYVLEGKAVYLLNKDWVEVQEGDFMWLRAF 250
Cdd:PRK11171  159 PIPMPGTDGVWATTRLVDPEDLRFDMHVNIVTFEPGASIPFVETHVMEHGLYVLEGKGVYRLNNDWVEVEAGDFIWMRAY 238

                         250       260
                  ....*....|....*....|....*..
gi 1906352649 251 CPQACYAGGPGRFRYLLYKDVNRHAVL 277
Cdd:PRK11171  239 CPQACYAGGPGPFRYLLYKDVNRHPEL 265
ura-cupin TIGR03214
putative allantoin catabolism protein; This model represents a protein containing a tandem ...
 21-277 4.61e-144

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: 404.46  E-value: 4.61e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  21 QRELTTDRAVFTEAYAVL-PRGTMRDIVtsklPFWDETRLWVIARPLSGFAETFSQYIVEVSPGGGSDKPELDAGAEGVL 99
Cdd:TIGR03214   1 QKQLLTTRAIFTGNYAVItPDGLVSNIV----PGFENTDIWILARPKLGFSATFVQYIVEVHPGGGATTGFGGEGIETFL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649 100 FVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTSDQVARFHWIRKAYQRVEGIDLPEPFVTNETDVEGGEMPGTDG 179
Cdd:TIGR03214  77 FVIDGEVNVSLGGETHELEEGGYAYLPPGSKWTLENAQDEDARFFLYKKRYQPVEGLHAPEAVVGNERDIEPEAYEGMDD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649 180 AWKTQRFvdPDDVRHDMHVNIVSFEPGGAIPFPETHVMEHGLYVLEGKAVYLLNKDWVEVQEGDFMWLRAFCPQACYAGG 259
Cdd:TIGR03214 157 VWATTLL--PKELAFDMNVHILSFEPGASHPYIETHVMEHGLYVLEGKGVYNLDNDWVPVEAGDYIWMGAYCPQACYAVG 234

                         250
                  ....*....|....*...
gi 1906352649 260 PGRFRYLLYKDVNRHAVL 277
Cdd:TIGR03214 235 RGPFRYLLYKDVNRHPKL 252
cupin_UGlyAH_N cd02211
(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family ...
 47-165 1.06e-56

(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: 177.71  E-value: 1.06e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  47 VTSKLPFWDETRLWVIARPLSGfaETFSQYIVEVSPGGGSDKPELDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLP 126
Cdd:cd02211     1 VTSVLPGWENTRASVLASPKLG--ATFVQYLVEVEPGGGSTAPEGGEGIERFLYVLEGEVELTVGGETHTLTAGGYAYLP 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1906352649 127 PGCTWTLHNTSDQVARFHWIRKAYQRVEGIDLPEPFVTN 165
Cdd:cd02211    79 PGTKHSLRNAGDEPARLLWYKKRYEPLEGGAAPEVVVGN 117
cupin_UGlyAH_C cd02212
(S)-ureidoglycine aminohydrolase and related proteins, C-terminal cupin domain; This family ...
 181-273 7.54e-54

(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: 169.59  E-value: 7.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649 181 WKTQRFVdPDDVRHDMHVNIVSFEPGGAIPFPETHVMEHGLYVLEGKAVYLLNKDWVEVQEGDFMWLRAFCPQACYAGGP 260
Cdd:cd02212     1 FELRKLL-PDSDGFDMNVNIMTFEPGASLPFVETHVMEHGLYMLEGQGIYRLGDDWYPVQAGDFIWMAPYCPQWFYALGR 79

                          90
                  ....*....|...
gi 1906352649 261 GRFRYLLYKDVNR 273
Cdd:cd02212    80 EPFRYLLYKDVNR 92
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
58-146 4.32e-11

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 58.88  E-value: 4.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  58 RLWVIARPLSGfaETFSQYIVEVSPGGGSDKPELDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTS 137
Cdd:COG3837    15 RYRRLGDALGL--TRLGVNLITLPPGASSSPYHAHSAEEEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLRNRG 92


                  ....*....
gi 1906352649 138 DQVARFHWI 146
Cdd:COG3837    93 DEPARYLVV 101
cupin_YP766765-like cd20299
Rhizobium leguminosarum YP_766765.1 and related proteins, cupin domain; This family includes ...
 63-142 8.44e-09

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: 51.90  E-value: 8.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  63 ARPLSGFAETFSQ-YIVEVS---PGGGsdkPELDAGA-EGVLFVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTS 137
Cdd:cd20299     3 ALRLQGSEETGTEcAWVGLShflPGGG---AETDASPrEKVYVVLEGELTVTTDGEEVVLGPGDSCYIPPGETRSIDNRT 79


                  ....*
gi 1906352649 138 DQVAR 142
Cdd:cd20299    80 NGPAT 84
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 76-146 9.56e-09

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: 51.10  E-value: 9.56e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906352649  76 YIVEVSPGGGSdKPELDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTSDQVARFHWI 146
Cdd:pfam07883   1 GLVTLPPGESS-PPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDV 70
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 76-146 1.30e-08

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: 51.35  E-value: 1.30e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906352649  76 YIVEVSPGGGSDKPELDAGAEGVlFVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTSDQVARFHWI 146
Cdd:cd02209    19 FLVTLPPGGSGGEPYSHEGEEFG-YVLEGELELTVGGETYVLEAGDSIYFDSDVPHRYRNPGDEPARVLWV 88
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 179-246 2.38e-08

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: 50.53  E-value: 2.38e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906352649 179 GAWKtQRFVDPDDVRHDMHVNIVSFEPGGAIPFpETHVMEHGLYVLEGKAVYLLNKDWVEVQEGDFMW 246
Cdd:cd02222     1 GVTI-RVLIGPEDGAPNFAMRYFEIEPGGHTPL-HTHPWEHEVYVLRGKGVVVIGGEEYPVKPGDVVY 66
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
61-146 4.04e-08

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 50.23  E-value: 4.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  61 VIARPLSGFAETFSQYIVEVSPGGGSdkPELDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTSDQV 140
Cdd:COG1917    11 VSVRVLADGEDELEVVRVTFEPGART--PWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEP 88


                  ....*.
gi 1906352649 141 ARFHWI 146
Cdd:COG1917    89 AVLLVV 94
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
43-146 7.66e-08

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 49.75  E-value: 7.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  43 MRDIVTSKLPfwdeTRLWVIARPLSGFAETFSQYIVEVSPGGGSDKPELDAGAEgVLFVVEGALTLSIEGEKHELAPGGY 122
Cdd:COG0662     1 MQDVNIEELK----AIGWGSYEVLGEGGERLSVKRITVPPGAELSLHVHPHRDE-FFYVLEGTGEVTIGDEEVELKAGDS 75

                          90       100
                  ....*....|....*....|....
gi 1906352649 123 AFLPPGCTWTLHNTSDQVARFHWI 146
Cdd:COG0662    76 VYIPAGVPHRLRNPGDEPLELLEV 99
Cupin_3 pfam05899
EutQ-like cupin domain; This entry represents the cupin domain, with a conserved jelly ...
 68-150 1.41e-07

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: 48.06  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  68 GFAETFSQYIVEVSPGGGSDKPELDAGAegvlFVVEGALTLSIEGEK-HELAPGGYAFLPPG--CTWTLHNTsdqvarfh 144
Cdd:pfam05899   2 SPLGVFSWGIWECTPGKFRWTYEEDETC----YILSGEVTVTPEGGKtVTLRAGDLVVLPKGlsGTWDVLET-------- 69


                  ....*.
gi 1906352649 145 wIRKAY 150
Cdd:pfam05899  70 -VRKHY 74
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
193-266 3.97e-07

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 47.54  E-value: 3.97e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906352649 193 RHDMHVNIVSFEPGGAIPfPETHVMEHGLYVLEGKAVYLLNKDWVEVQEGDFMWLRAFCPQACYAGGPGRFRYL 266
Cdd:COG1917    20 EDELEVVRVTFEPGARTP-WHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLL 92
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 57-143 8.81e-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: 43.21  E-value: 8.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649  57 TRLWVIARPlsGFAETFSQYIVEVSPGGGSDKPELDAgaEGVLFVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNT 136
Cdd:cd02222     3 TIRVLIGPE--DGAPNFAMRYFEIEPGGHTPLHTHPW--EHEVYVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPHQFRNT 78


                  ....*..
gi 1906352649 137 SDQVARF 143
Cdd:cd02222    79 GDEPLGF 85
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 98-147 3.66e-05

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: 40.93  E-value: 3.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1906352649  98 VLFVVEGALTLSIE-GEKHELAPGGYAFLPPGCTWTLHNTSDQVARFHWIR 147
Cdd:cd02208    23 IFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
cupin_SPO2919-like cd02224
Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase ...
 99-143 5.12e-05

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: 41.32  E-value: 5.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1906352649  99 LFVVEGALTLSIEGEKHELAPGGYAFLPPGCTW--TLHNTSDQVARF 143
Cdd:cd02224    43 VYVLSGEGTLRLDGEEVLPRPGDFVGFPAGTGVahQLINRSDEPLVY 89
cupin_RemF-like cd06979
Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is ...
 68-128 7.27e-05

Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is a manganese-containing polyketide cyclase present in bacteria that is involved in the biosynthesis of resistomycin, the aromatic pentacyclic metabolite in Streptomyces resistomycificus. Structure of this enzyme shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold that forms a homodimer. It contains an unusual octahedral zinc-binding site in a large hydrophobic pocket that may represent the active site. The zinc ion, coordinated to four histidine side chains and two water molecules, could act as a Lewis acid in the aldol condensation reaction catalyzed by RemF, reminiscent of class II aldolases.


Pssm-ID: 380384 [Multi-domain]  Cd Length: 93  Bit Score: 40.91  E-value: 7.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906352649  68 GFAETFSQYIVEVSPGGGSDKPELDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLPPG 128
Cdd:cd06979    12 GTADRFDLFEFEVSPNAGMPPPHYHEDWEETIYGLEGSVTLTLPGKTVEVGPGDSIFIPRG 72
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 185-249 1.25e-04

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: 40.18  E-value: 1.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906352649 185 RFVDPDDVRHDMHVNIVSFEPGGAIPFPETHVMEHGLYVLEGKAVYLLNKDWVEVQEGDFMWLRA 249
Cdd:cd02209     5 ELLSPGLPGRKMEPFLVTLPPGGSGGEPYSHEGEEFGYVLEGELELTVGGETYVLEAGDSIYFDS 69
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 200-266 1.86e-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: 1.86e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906352649 200 IVSFEPGGAIPFPETHVMEHGLYVLEGKAVYLLNKDWVEVQEGDFMWLRAFCPQACYAGGPGRFRYL 266
Cdd:pfam07883   2 LVTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLL 68
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
190-266 3.61e-04

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 39.35  E-value: 3.61e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906352649 190 DDVRHDMHVNIVSFEPGGAIPFPETHVMEHGLYVLEGKAVYLLNKDWVEVQEGDFMWLRAFCPQACYAGGPGRFRYL 266
Cdd:COG0662    21 GEGGERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGDEPLELL 97
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 198-266 8.25e-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: 37.46  E-value: 8.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352649 198 VNIVSFEPGGAIPFPETHVMEHGLYVLEGKAVYLLN-KDWVEVQEGDFMWLRAFCPQACYAGGPGRFRYL 266
Cdd:cd02208     1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFL 70
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 98-129 1.22e-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: 37.90  E-value: 1.22e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1906352649  98 VLFVVEGALTLSIEGEKHELAPGGYAFLPPGC 129
Cdd:cd02215    56 TFYVLEGRLQLWLDGESRLLTPGDFASVPPGT 87
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 78-143 1.40e-03

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 37.11  E-value: 1.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906352649  78 VEVSPGGGSdKPELDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLPPGCTWTLHNTSDQVARF 143
Cdd:cd02214    24 ARVPPGEST-LPHRLKGSEEVYYILEGEGTMEIDGEPREVGPGDAVLIPPGAVQRIENTGEEDLVF 88
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
194-249 3.31e-03

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 36.53  E-value: 3.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1906352649 194 HDMHVNIVSFEPGGAIPFPETHVMEH-GLYVLEGKAVYLLNKDWVEVQEGDFMWLRA 249
Cdd:COG3837    26 TRLGVNLITLPPGASSSPYHAHSAEEeFVYVLEGELTLRIGGEEYVLEPGDSVGFPA 82
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 90-128 4.75e-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: 35.91  E-value: 4.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1906352649  90 ELDAGAEGVL---------FVVEGALTLSIEGEKHELAPGGYAFLPPG 128
Cdd:cd02238    33 RFEKGAVVPLhshpheqigYVLSGRFEFTIGGETRILKPGDSYYIPPN 80
cupin_HP0902-like cd02230
Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes ...
 89-128 4.91e-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: 4.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1906352649  89 PELDAGAEGVLFVVEGALTLSIEGEKHELAPGGYAFLPPG 128
Cdd:cd02230    25 SEHTAPGDATVQVLEGEAEFTIGGETVTLKAGELIVMPAN 64
 
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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