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Conserved domains on  [gi|1053731771|ref|WP_066045133|]
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allophanate hydrolase subunit 1 [Francisella hispaniensis]

Protein Classification

5-oxoprolinase subunit B family protein( domain architecture ID 10005226)

5-oxoprolinase subunit B family protein similar to 5-oxoprolinase, which hydrolizes 5-oxoproline to glutamate in an ATP-dependent step, and to allophanate hydrolase subunit 1 (AHS1), which converts allophanate to ammonium and carbon dioxide, and is essential for utilization of urea as a nitrogen source in bacteria

EC:  3.5.-.-
SCOP:  4001873

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
4-204 4.06e-62

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


:

Pssm-ID: 441652  Cd Length: 229  Bit Score: 192.66  E-value: 4.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771   4 YFLNESCFIYSVSDKLSLEDNLKILNIYQYfIKDSSFcrkYAIYDIVPAYNSIAFHFSYQYI--YDLERAILAKIRNINL 81
Cdd:COG2049     8 LPAGDRALLVEFGDEIDLELNRRVLALAAA-LRAAPL---PGVVEVVPAYRSLLVHFDPLVIdpAALAARLRALLAELDA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771  82 SASIKAKTHYIDVSY---TGIDLQNAAEILGLDVTEIIKRHTQVEYHIAMLGFKPYFPYLLGLDPSLSLPRLATPRNRIA 158
Cdd:COG2049    84 AAEVPSRLVEIPVCYdgeFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTRVP 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1053731771 159 AGSVAIGGSQTTIFPEQSPSGWNIIGISDFKDF-------AKFSPGDKIIFRE 204
Cdd:COG2049   164 AGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFdpdreppALLRPGDRVRFVP 216
 
Name Accession Description Interval E-value
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
4-204 4.06e-62

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


Pssm-ID: 441652  Cd Length: 229  Bit Score: 192.66  E-value: 4.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771   4 YFLNESCFIYSVSDKLSLEDNLKILNIYQYfIKDSSFcrkYAIYDIVPAYNSIAFHFSYQYI--YDLERAILAKIRNINL 81
Cdd:COG2049     8 LPAGDRALLVEFGDEIDLELNRRVLALAAA-LRAAPL---PGVVEVVPAYRSLLVHFDPLVIdpAALAARLRALLAELDA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771  82 SASIKAKTHYIDVSY---TGIDLQNAAEILGLDVTEIIKRHTQVEYHIAMLGFKPYFPYLLGLDPSLSLPRLATPRNRIA 158
Cdd:COG2049    84 AAEVPSRLVEIPVCYdgeFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTRVP 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1053731771 159 AGSVAIGGSQTTIFPEQSPSGWNIIGISDFKDF-------AKFSPGDKIIFRE 204
Cdd:COG2049   164 AGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFdpdreppALLRPGDRVRFVP 216
CT_C_D pfam02682
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ...
4-184 1.14e-53

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: 170.04  E-value: 1.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771   4 YFLNESCFIYSVSDKLSLEDNLKILNIYQYfIKDSSFcrkYAIYDIVPAYNSIAFHFS-YQYIYD-LERAILAKIRNINL 81
Cdd:pfam02682   3 RPAGDRALLVEFGDEIDLALNRRVLALAAA-LRAAPL---PGVVEVVPGYRSLLVHYDpLVTDLAaLEARLRALLAALEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771  82 SASIKAKTHYIDVSY---TGIDLQNAAEILGLDVTEIIKRHTQVEYHIAMLGFKPYFPYLLGLDPSLSLPRLATPRNRIA 158
Cdd:pfam02682  79 AAAPGGRLIEIPVCYdgeFGPDLAEVAAHNGLSVEEVIRLHSAAEYRVYFLGFAPGFPYLGGLDPRLAVPRRATPRTRVP 158
                         170       180
                  ....*....|....*....|....*.
gi 1053731771 159 AGSVAIGGSQTTIFPEQSPSGWNIIG 184
Cdd:pfam02682 159 AGSVGIAGRQTGIYPLESPGGWQLIG 184
AHS1 smart00796
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase ...
1-184 3.12e-51

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


Pssm-ID: 214820  Cd Length: 201  Bit Score: 163.85  E-value: 3.12e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771    1 MNHYFLNESCFIYSVSDKLSLEDNLKILNIYQYfIKDSSFcrkYAIYDIVPAYNSIAFHF-----SYQYIYDLERAILAk 75
Cdd:smart00796   1 MRIRPAGDRALLVEFGDEIDLALNRRVLALARA-LRAAPL---PGVVELVPGYRSLLVHFdplviDPAALLARLRALEA- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771   76 iRNINLSASIKAKTHYIDVSY---TGIDLQNAAEILGLDVTEIIKRHTQVEYHIAMLGFKPYFPYLLGLDPSLSLPRLAT 152
Cdd:smart00796  76 -LPLAEALEVPGRIIEIPVCYggeFGPDLEFVARHNGLSVDEVIRLHSAAEYRVYMLGFAPGFPYLGGLDPRLATPRRST 154
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1053731771  153 PRNRIAAGSVAIGGSQTTIFPEQSPSGWNIIG 184
Cdd:smart00796 155 PRTRVPAGSVGIAGAQTGIYPLESPGGWQLIG 186
TIGR00370 TIGR00370
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
6-202 4.29e-27

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


Pssm-ID: 129467  Cd Length: 202  Bit Score: 102.24  E-value: 4.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771   6 LNESCFIYSVSDKLSLEDNLKILNIYQYFIKDSSFCrkyaiyDIVPAYNSIAFhfsyqyIYDLERAILAKIRNIN-LSAS 84
Cdd:TIGR00370   1 IGESAVVIRLGPPINEQVQGIVWAAAAYLEEQPGFV------ECIPGMNNLTV------FYDMYEVYKHLPQRLSsPWEE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771  85 IKA-----KTHYIDVSYTGI---DLQNAAEILGLDVTEIIKRHTQVEYHIAMLGFKPYFPYLLGLDPSLSLPRLATPRNR 156
Cdd:TIGR00370  69 VKDyevnrRIIEIPVCYGGEfgpDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPS 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1053731771 157 IAAGSVAIGGSQTTIFPEQSPSGWNIIGISDFKDFAK-------FSPGDKIIF 202
Cdd:TIGR00370 149 VPAGSVGIGGLQTGVYPISTPGGWQLIGKTPLALFDPqenpptlLRAGDIVKF 201
 
Name Accession Description Interval E-value
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
4-204 4.06e-62

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


Pssm-ID: 441652  Cd Length: 229  Bit Score: 192.66  E-value: 4.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771   4 YFLNESCFIYSVSDKLSLEDNLKILNIYQYfIKDSSFcrkYAIYDIVPAYNSIAFHFSYQYI--YDLERAILAKIRNINL 81
Cdd:COG2049     8 LPAGDRALLVEFGDEIDLELNRRVLALAAA-LRAAPL---PGVVEVVPAYRSLLVHFDPLVIdpAALAARLRALLAELDA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771  82 SASIKAKTHYIDVSY---TGIDLQNAAEILGLDVTEIIKRHTQVEYHIAMLGFKPYFPYLLGLDPSLSLPRLATPRNRIA 158
Cdd:COG2049    84 AAEVPSRLVEIPVCYdgeFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTRVP 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1053731771 159 AGSVAIGGSQTTIFPEQSPSGWNIIGISDFKDF-------AKFSPGDKIIFRE 204
Cdd:COG2049   164 AGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFdpdreppALLRPGDRVRFVP 216
CT_C_D pfam02682
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ...
4-184 1.14e-53

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: 170.04  E-value: 1.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771   4 YFLNESCFIYSVSDKLSLEDNLKILNIYQYfIKDSSFcrkYAIYDIVPAYNSIAFHFS-YQYIYD-LERAILAKIRNINL 81
Cdd:pfam02682   3 RPAGDRALLVEFGDEIDLALNRRVLALAAA-LRAAPL---PGVVEVVPGYRSLLVHYDpLVTDLAaLEARLRALLAALEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771  82 SASIKAKTHYIDVSY---TGIDLQNAAEILGLDVTEIIKRHTQVEYHIAMLGFKPYFPYLLGLDPSLSLPRLATPRNRIA 158
Cdd:pfam02682  79 AAAPGGRLIEIPVCYdgeFGPDLAEVAAHNGLSVEEVIRLHSAAEYRVYFLGFAPGFPYLGGLDPRLAVPRRATPRTRVP 158
                         170       180
                  ....*....|....*....|....*.
gi 1053731771 159 AGSVAIGGSQTTIFPEQSPSGWNIIG 184
Cdd:pfam02682 159 AGSVGIAGRQTGIYPLESPGGWQLIG 184
AHS1 smart00796
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase ...
1-184 3.12e-51

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


Pssm-ID: 214820  Cd Length: 201  Bit Score: 163.85  E-value: 3.12e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771    1 MNHYFLNESCFIYSVSDKLSLEDNLKILNIYQYfIKDSSFcrkYAIYDIVPAYNSIAFHF-----SYQYIYDLERAILAk 75
Cdd:smart00796   1 MRIRPAGDRALLVEFGDEIDLALNRRVLALARA-LRAAPL---PGVVELVPGYRSLLVHFdplviDPAALLARLRALEA- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771   76 iRNINLSASIKAKTHYIDVSY---TGIDLQNAAEILGLDVTEIIKRHTQVEYHIAMLGFKPYFPYLLGLDPSLSLPRLAT 152
Cdd:smart00796  76 -LPLAEALEVPGRIIEIPVCYggeFGPDLEFVARHNGLSVDEVIRLHSAAEYRVYMLGFAPGFPYLGGLDPRLATPRRST 154
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1053731771  153 PRNRIAAGSVAIGGSQTTIFPEQSPSGWNIIG 184
Cdd:smart00796 155 PRTRVPAGSVGIAGAQTGIYPLESPGGWQLIG 186
TIGR00370 TIGR00370
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
6-202 4.29e-27

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


Pssm-ID: 129467  Cd Length: 202  Bit Score: 102.24  E-value: 4.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771   6 LNESCFIYSVSDKLSLEDNLKILNIYQYFIKDSSFCrkyaiyDIVPAYNSIAFhfsyqyIYDLERAILAKIRNIN-LSAS 84
Cdd:TIGR00370   1 IGESAVVIRLGPPINEQVQGIVWAAAAYLEEQPGFV------ECIPGMNNLTV------FYDMYEVYKHLPQRLSsPWEE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053731771  85 IKA-----KTHYIDVSYTGI---DLQNAAEILGLDVTEIIKRHTQVEYHIAMLGFKPYFPYLLGLDPSLSLPRLATPRNR 156
Cdd:TIGR00370  69 VKDyevnrRIIEIPVCYGGEfgpDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPS 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1053731771 157 IAAGSVAIGGSQTTIFPEQSPSGWNIIGISDFKDFAK-------FSPGDKIIF 202
Cdd:TIGR00370 149 VPAGSVGIGGLQTGVYPISTPGGWQLIGKTPLALFDPqenpptlLRAGDIVKF 201
 
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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