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Conserved domains on  [gi|15829990|ref|NP_308763|]
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allophanate hydrolase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

5-oxoprolinase subunit PxpB( domain architecture ID 10015631)

5-oxoprolinase subunit PxpB is part of an ATP-dependent oxoprolinase, an enzyme that disposes of 5-oxoproline, a damage product formed spontaneously from glutamine and other sources

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TIGR00370 TIGR00370
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
9-211 2.72e-123

sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]


:

Pssm-ID: 129467  Cd Length: 202  Bit Score: 347.23  E-value: 2.72e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990     9 IGETAVVLELEPPVTLASQKRIWRLAQRLVDMPNVVEAIPGMNNITVILrNPESLALDAIERLQRWWEESEALEPESRFI 88
Cdd:TIGR00370   1 IGESAVVIRLGPPINEQVQGIVWAAAAYLEEQPGFVECIPGMNNLTVFY-DMYEVYKHLPQRLSSPWEEVKDYEVNRRII 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990    89 EIPVVYGGAGGPDLAVVAAHCGLSEKQVVELHSSVEYVVWFLGFQPGFPYLGSLPEQLHTPRRAEPRLLVPAGSVGIGGP 168
Cdd:TIGR00370  80 EIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPSVPAGSVGIGGL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 15829990   169 QTGVYPLATPGGWQLIGHTSLSLFDPARDEPILLRPGDSVRFV 211
Cdd:TIGR00370 160 QTGVYPISTPGGWQLIGKTPLALFDPQENPPTLLRAGDIVKFV 202
 
Name Accession Description Interval E-value
TIGR00370 TIGR00370
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
9-211 2.72e-123

sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]


Pssm-ID: 129467  Cd Length: 202  Bit Score: 347.23  E-value: 2.72e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990     9 IGETAVVLELEPPVTLASQKRIWRLAQRLVDMPNVVEAIPGMNNITVILrNPESLALDAIERLQRWWEESEALEPESRFI 88
Cdd:TIGR00370   1 IGESAVVIRLGPPINEQVQGIVWAAAAYLEEQPGFVECIPGMNNLTVFY-DMYEVYKHLPQRLSSPWEEVKDYEVNRRII 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990    89 EIPVVYGGAGGPDLAVVAAHCGLSEKQVVELHSSVEYVVWFLGFQPGFPYLGSLPEQLHTPRRAEPRLLVPAGSVGIGGP 168
Cdd:TIGR00370  80 EIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPSVPAGSVGIGGL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 15829990   169 QTGVYPLATPGGWQLIGHTSLSLFDPARDEPILLRPGDSVRFV 211
Cdd:TIGR00370 160 QTGVYPISTPGGWQLIGKTPLALFDPQENPPTLLRAGDIVKFV 202
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
1-215 3.93e-102

5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism];


Pssm-ID: 441652  Cd Length: 229  Bit Score: 294.74  E-value: 3.93e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990   1 MQRARCYLIGETAVVLELEPPVTLASQKRIWRLAQRLVDM--PNVVEAIPGMNNITVILrNPESLALDA-IERLQRWWEE 77
Cdd:COG2049   2 RMAMRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAAplPGVVEVVPAYRSLLVHF-DPLVIDPAAlAARLRALLAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990  78 -SEALEPESRFIEIPVVYGGAGGPDLAVVAAHCGLSEKQVVELHSSVEYVVWFLGFQPGFPYLGSLPEQLHTPRRAEPRL 156
Cdd:COG2049  81 lDAAAEVPSRLVEIPVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRT 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15829990 157 LVPAGSVGIGGPQTGVYPLATPGGWQLIGHTSLSLFDPARDEPILLRPGDSVRFVPQKE 215
Cdd:COG2049 161 RVPAGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPPALLRPGDRVRFVPISE 219
CT_C_D pfam02682
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ...
5-202 2.64e-93

Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ATP- and biotin-dependent carboxylation reaction of urea. It is composed of biotin carboxylase (BC), carboxyltransferase (CT), and biotin carboxyl carrier protein (BCCP) domains. The CT domain of UC consists of four subdomains, named A, B, C and D. This domain covers the C and D subdomains of the CT domain. This domain covers the whole length of kipI (kinase A inhibitor) from Bacillus subtilis. It can also be found in S. cerevisiae urea amidolyase Dur1,2, which is a multifunctional biotin-dependent enzyme with domains for urea carboxylase and allophanate (urea carboxylate) hydrolase activity.


Pssm-ID: 426925  Cd Length: 201  Bit Score: 271.35  E-value: 2.64e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990     5 RCYLIGETAVVLELEPPVTLASQKRIWRLAQRLVDM--PNVVEAIPGMNNITVILRnPESLALDA-IERLQRWWEE-SEA 80
Cdd:pfam02682   1 RIRPAGDRALLVEFGDEIDLALNRRVLALAAALRAAplPGVVEVVPGYRSLLVHYD-PLVTDLAAlEARLRALLAAlEAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990    81 LEPESRFIEIPVVYGGAGGPDLAVVAAHCGLSEKQVVELHSSVEYVVWFLGFQPGFPYLGSLPEQLHTPRRAEPRLLVPA 160
Cdd:pfam02682  80 AAPGGRLIEIPVCYDGEFGPDLAEVAAHNGLSVEEVIRLHSAAEYRVYFLGFAPGFPYLGGLDPRLAVPRRATPRTRVPA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 15829990   161 GSVGIGGPQTGVYPLATPGGWQLIGHTSLSLFDPARDEPILL 202
Cdd:pfam02682 160 GSVGIAGRQTGIYPLESPGGWQLIGRTPLPLFDPDRDPPALL 201
AHS1 smart00796
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase ...
5-199 4.97e-88

Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase (AHS1).


Pssm-ID: 214820  Cd Length: 201  Bit Score: 257.84  E-value: 4.97e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990      5 RCYLIGETAVVLELEPPVTLASQKRIWRLAQRLV--DMPNVVEAIPGMNNITVILRNPESLALDAIERLQRWWEE--SEA 80
Cdd:smart00796   2 RIRPAGDRALLVEFGDEIDLALNRRVLALARALRaaPLPGVVELVPGYRSLLVHFDPLVIDPAALLARLRALEALplAEA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990     81 LEPESRFIEIPVVYGGAGGPDLAVVAAHCGLSEKQVVELHSSVEYVVWFLGFQPGFPYLGSLPEQLHTPRRAEPRLLVPA 160
Cdd:smart00796  82 LEVPGRIIEIPVCYGGEFGPDLEFVARHNGLSVDEVIRLHSAAEYRVYMLGFAPGFPYLGGLDPRLATPRRSTPRTRVPA 161
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 15829990    161 GSVGIGGPQTGVYPLATPGGWQLIGHTSLSLFDPARDEP 199
Cdd:smart00796 162 GSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPP 200
 
Name Accession Description Interval E-value
TIGR00370 TIGR00370
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
9-211 2.72e-123

sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]


Pssm-ID: 129467  Cd Length: 202  Bit Score: 347.23  E-value: 2.72e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990     9 IGETAVVLELEPPVTLASQKRIWRLAQRLVDMPNVVEAIPGMNNITVILrNPESLALDAIERLQRWWEESEALEPESRFI 88
Cdd:TIGR00370   1 IGESAVVIRLGPPINEQVQGIVWAAAAYLEEQPGFVECIPGMNNLTVFY-DMYEVYKHLPQRLSSPWEEVKDYEVNRRII 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990    89 EIPVVYGGAGGPDLAVVAAHCGLSEKQVVELHSSVEYVVWFLGFQPGFPYLGSLPEQLHTPRRAEPRLLVPAGSVGIGGP 168
Cdd:TIGR00370  80 EIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPSVPAGSVGIGGL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 15829990   169 QTGVYPLATPGGWQLIGHTSLSLFDPARDEPILLRPGDSVRFV 211
Cdd:TIGR00370 160 QTGVYPISTPGGWQLIGKTPLALFDPQENPPTLLRAGDIVKFV 202
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
1-215 3.93e-102

5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism];


Pssm-ID: 441652  Cd Length: 229  Bit Score: 294.74  E-value: 3.93e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990   1 MQRARCYLIGETAVVLELEPPVTLASQKRIWRLAQRLVDM--PNVVEAIPGMNNITVILrNPESLALDA-IERLQRWWEE 77
Cdd:COG2049   2 RMAMRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAAplPGVVEVVPAYRSLLVHF-DPLVIDPAAlAARLRALLAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990  78 -SEALEPESRFIEIPVVYGGAGGPDLAVVAAHCGLSEKQVVELHSSVEYVVWFLGFQPGFPYLGSLPEQLHTPRRAEPRL 156
Cdd:COG2049  81 lDAAAEVPSRLVEIPVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRT 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15829990 157 LVPAGSVGIGGPQTGVYPLATPGGWQLIGHTSLSLFDPARDEPILLRPGDSVRFVPQKE 215
Cdd:COG2049 161 RVPAGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPPALLRPGDRVRFVPISE 219
CT_C_D pfam02682
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ...
5-202 2.64e-93

Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ATP- and biotin-dependent carboxylation reaction of urea. It is composed of biotin carboxylase (BC), carboxyltransferase (CT), and biotin carboxyl carrier protein (BCCP) domains. The CT domain of UC consists of four subdomains, named A, B, C and D. This domain covers the C and D subdomains of the CT domain. This domain covers the whole length of kipI (kinase A inhibitor) from Bacillus subtilis. It can also be found in S. cerevisiae urea amidolyase Dur1,2, which is a multifunctional biotin-dependent enzyme with domains for urea carboxylase and allophanate (urea carboxylate) hydrolase activity.


Pssm-ID: 426925  Cd Length: 201  Bit Score: 271.35  E-value: 2.64e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990     5 RCYLIGETAVVLELEPPVTLASQKRIWRLAQRLVDM--PNVVEAIPGMNNITVILRnPESLALDA-IERLQRWWEE-SEA 80
Cdd:pfam02682   1 RIRPAGDRALLVEFGDEIDLALNRRVLALAAALRAAplPGVVEVVPGYRSLLVHYD-PLVTDLAAlEARLRALLAAlEAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990    81 LEPESRFIEIPVVYGGAGGPDLAVVAAHCGLSEKQVVELHSSVEYVVWFLGFQPGFPYLGSLPEQLHTPRRAEPRLLVPA 160
Cdd:pfam02682  80 AAPGGRLIEIPVCYDGEFGPDLAEVAAHNGLSVEEVIRLHSAAEYRVYFLGFAPGFPYLGGLDPRLAVPRRATPRTRVPA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 15829990   161 GSVGIGGPQTGVYPLATPGGWQLIGHTSLSLFDPARDEPILL 202
Cdd:pfam02682 160 GSVGIAGRQTGIYPLESPGGWQLIGRTPLPLFDPDRDPPALL 201
AHS1 smart00796
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase ...
5-199 4.97e-88

Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase (AHS1).


Pssm-ID: 214820  Cd Length: 201  Bit Score: 257.84  E-value: 4.97e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990      5 RCYLIGETAVVLELEPPVTLASQKRIWRLAQRLV--DMPNVVEAIPGMNNITVILRNPESLALDAIERLQRWWEE--SEA 80
Cdd:smart00796   2 RIRPAGDRALLVEFGDEIDLALNRRVLALARALRaaPLPGVVELVPGYRSLLVHFDPLVIDPAALLARLRALEALplAEA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829990     81 LEPESRFIEIPVVYGGAGGPDLAVVAAHCGLSEKQVVELHSSVEYVVWFLGFQPGFPYLGSLPEQLHTPRRAEPRLLVPA 160
Cdd:smart00796  82 LEVPGRIIEIPVCYGGEFGPDLEFVARHNGLSVDEVIRLHSAAEYRVYMLGFAPGFPYLGGLDPRLATPRRSTPRTRVPA 161
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 15829990    161 GSVGIGGPQTGVYPLATPGGWQLIGHTSLSLFDPARDEP 199
Cdd:smart00796 162 GSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPP 200
 
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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