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Conserved domains on  [gi|502304082|ref|WP_012757486|]
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allophanate hydrolase subunit 1 [Rhizobium leguminosarum]

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]; ...
13-231 8.05e-85

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


:

Pssm-ID: 441652  Cd Length: 229  Bit Score: 251.60  E-value: 8.05e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082  13 PNYRPVGGHALLVEFGATIDKRIHDQVVKLDAALKAAPFEGFVEAVPAYASILVCFDPLMADHRTTEVAIAELLGAEVPE 92
Cdd:COG2049    5 MRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAAPLPGVVEVVPAYRSLLVHFDPLVIDPAALAARLRALLAELDAA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082  93 TIGAMREVE--VCYDPDLAPDLASIAEASGLSPEDVISAHLSGDYSVFMYGFAPGYAYLAGVPKAIQQPRKPAPIRGIAA 170
Cdd:COG2049   85 AEVPSRLVEipVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTRVPA 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502304082 171 GSVLIAGPQCLVSTLTMPTGWWIIGRSPTKILDAASnDRPFLFDVGDTVRFRRISRTEFDA 231
Cdd:COG2049  165 GSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDR-EPPALLRPGDRVRFVPISEEEFDA 224
 
Name Accession Description Interval E-value
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
13-231 8.05e-85

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


Pssm-ID: 441652  Cd Length: 229  Bit Score: 251.60  E-value: 8.05e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082  13 PNYRPVGGHALLVEFGATIDKRIHDQVVKLDAALKAAPFEGFVEAVPAYASILVCFDPLMADHRTTEVAIAELLGAEVPE 92
Cdd:COG2049    5 MRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAAPLPGVVEVVPAYRSLLVHFDPLVIDPAALAARLRALLAELDAA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082  93 TIGAMREVE--VCYDPDLAPDLASIAEASGLSPEDVISAHLSGDYSVFMYGFAPGYAYLAGVPKAIQQPRKPAPIRGIAA 170
Cdd:COG2049   85 AEVPSRLVEipVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTRVPA 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502304082 171 GSVLIAGPQCLVSTLTMPTGWWIIGRSPTKILDAASnDRPFLFDVGDTVRFRRISRTEFDA 231
Cdd:COG2049  165 GSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDR-EPPALLRPGDRVRFVPISEEEFDA 224
CT_C_D pfam02682
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ...
14-213 5.84e-70

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: 212.80  E-value: 5.84e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082   14 NYRPVGGHALLVEFGATIDKRIHDQVVKLDAALKAAPFEGFVEAVPAYASILVCFDPLMADHRTTEVAIAELLGAEVPET 93
Cdd:pfam02682   1 RIRPAGDRALLVEFGDEIDLALNRRVLALAAALRAAPLPGVVEVVPGYRSLLVHYDPLVTDLAALEARLRALLAALEAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082   94 IGAMREVE--VCYDPDLAPDLASIAEASGLSPEDVISAHLSGDYSVFMYGFAPGYAYLAGVPKAIQQPRKPAPIRGIAAG 171
Cdd:pfam02682  81 APGGRLIEipVCYDGEFGPDLAEVAAHNGLSVEEVIRLHSAAEYRVYFLGFAPGFPYLGGLDPRLAVPRRATPRTRVPAG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 502304082  172 SVLIAGPQCLVSTLTMPTGWWIIGRSPTKILDAASnDRPFLF 213
Cdd:pfam02682 161 SVGIAGRQTGIYPLESPGGWQLIGRTPLPLFDPDR-DPPALL 201
AHS1 smart00796
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase ...
13-203 5.17e-62

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


Pssm-ID: 214820  Cd Length: 201  Bit Score: 192.74  E-value: 5.17e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082    13 PNYRPVGGHALLVEFGATIDKRIHDQVVKLDAALKAAPFEGFVEAVPAYASILVCFDPLMADHRTTEVAIAELLG-AEVP 91
Cdd:smart00796   1 MRIRPAGDRALLVEFGDEIDLALNRRVLALARALRAAPLPGVVELVPGYRSLLVHFDPLVIDPAALLARLRALEAlPLAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082    92 ETIGAMREVE--VCYDPDLAPDLASIAEASGLSPEDVISAHLSGDYSVFMYGFAPGYAYLAGVPKAIQQPRKPAPIRGIA 169
Cdd:smart00796  81 ALEVPGRIIEipVCYGGEFGPDLEFVARHNGLSVDEVIRLHSAAEYRVYMLGFAPGFPYLGGLDPRLATPRRSTPRTRVP 160
                          170       180       190
                   ....*....|....*....|....*....|....
gi 502304082   170 AGSVLIAGPQCLVSTLTMPTGWWIIGRSPTKILD 203
Cdd:smart00796 161 AGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFD 194
TIGR00370 TIGR00370
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
18-221 2.27e-37

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


Pssm-ID: 129467  Cd Length: 202  Bit Score: 129.59  E-value: 2.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082   18 VGGHALLVEFGATIDKRIHDQVVKLDAALKAAPfeGFVEAVPAYASILVCFDPLMADHRTTEVAIAELLGAEVPETIGAM 97
Cdd:TIGR00370   1 IGESAVVIRLGPPINEQVQGIVWAAAAYLEEQP--GFVECIPGMNNLTVFYDMYEVYKHLPQRLSSPWEEVKDYEVNRRI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082   98 REVEVCYDPDLAPDLASIAEASGLSPEDVISAHLSGDYSVFMYGFAPGYAYLAGVPKAIQQPRKPAPIRGIAAGSVLIAG 177
Cdd:TIGR00370  79 IEIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPSVPAGSVGIGG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 502304082  178 PQCLVSTLTMPTGWWIIGRSPTKILDAASNDrPFLFDVGDTVRF 221
Cdd:TIGR00370 159 LQTGVYPISTPGGWQLIGKTPLALFDPQENP-PTLLRAGDIVKF 201
 
Name Accession Description Interval E-value
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
13-231 8.05e-85

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


Pssm-ID: 441652  Cd Length: 229  Bit Score: 251.60  E-value: 8.05e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082  13 PNYRPVGGHALLVEFGATIDKRIHDQVVKLDAALKAAPFEGFVEAVPAYASILVCFDPLMADHRTTEVAIAELLGAEVPE 92
Cdd:COG2049    5 MRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAAPLPGVVEVVPAYRSLLVHFDPLVIDPAALAARLRALLAELDAA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082  93 TIGAMREVE--VCYDPDLAPDLASIAEASGLSPEDVISAHLSGDYSVFMYGFAPGYAYLAGVPKAIQQPRKPAPIRGIAA 170
Cdd:COG2049   85 AEVPSRLVEipVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTRVPA 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502304082 171 GSVLIAGPQCLVSTLTMPTGWWIIGRSPTKILDAASnDRPFLFDVGDTVRFRRISRTEFDA 231
Cdd:COG2049  165 GSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDR-EPPALLRPGDRVRFVPISEEEFDA 224
CT_C_D pfam02682
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ...
14-213 5.84e-70

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: 212.80  E-value: 5.84e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082   14 NYRPVGGHALLVEFGATIDKRIHDQVVKLDAALKAAPFEGFVEAVPAYASILVCFDPLMADHRTTEVAIAELLGAEVPET 93
Cdd:pfam02682   1 RIRPAGDRALLVEFGDEIDLALNRRVLALAAALRAAPLPGVVEVVPGYRSLLVHYDPLVTDLAALEARLRALLAALEAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082   94 IGAMREVE--VCYDPDLAPDLASIAEASGLSPEDVISAHLSGDYSVFMYGFAPGYAYLAGVPKAIQQPRKPAPIRGIAAG 171
Cdd:pfam02682  81 APGGRLIEipVCYDGEFGPDLAEVAAHNGLSVEEVIRLHSAAEYRVYFLGFAPGFPYLGGLDPRLAVPRRATPRTRVPAG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 502304082  172 SVLIAGPQCLVSTLTMPTGWWIIGRSPTKILDAASnDRPFLF 213
Cdd:pfam02682 161 SVGIAGRQTGIYPLESPGGWQLIGRTPLPLFDPDR-DPPALL 201
AHS1 smart00796
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase ...
13-203 5.17e-62

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


Pssm-ID: 214820  Cd Length: 201  Bit Score: 192.74  E-value: 5.17e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082    13 PNYRPVGGHALLVEFGATIDKRIHDQVVKLDAALKAAPFEGFVEAVPAYASILVCFDPLMADHRTTEVAIAELLG-AEVP 91
Cdd:smart00796   1 MRIRPAGDRALLVEFGDEIDLALNRRVLALARALRAAPLPGVVELVPGYRSLLVHFDPLVIDPAALLARLRALEAlPLAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082    92 ETIGAMREVE--VCYDPDLAPDLASIAEASGLSPEDVISAHLSGDYSVFMYGFAPGYAYLAGVPKAIQQPRKPAPIRGIA 169
Cdd:smart00796  81 ALEVPGRIIEipVCYGGEFGPDLEFVARHNGLSVDEVIRLHSAAEYRVYMLGFAPGFPYLGGLDPRLATPRRSTPRTRVP 160
                          170       180       190
                   ....*....|....*....|....*....|....
gi 502304082   170 AGSVLIAGPQCLVSTLTMPTGWWIIGRSPTKILD 203
Cdd:smart00796 161 AGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFD 194
TIGR00370 TIGR00370
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
18-221 2.27e-37

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


Pssm-ID: 129467  Cd Length: 202  Bit Score: 129.59  E-value: 2.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082   18 VGGHALLVEFGATIDKRIHDQVVKLDAALKAAPfeGFVEAVPAYASILVCFDPLMADHRTTEVAIAELLGAEVPETIGAM 97
Cdd:TIGR00370   1 IGESAVVIRLGPPINEQVQGIVWAAAAYLEEQP--GFVECIPGMNNLTVFYDMYEVYKHLPQRLSSPWEEVKDYEVNRRI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502304082   98 REVEVCYDPDLAPDLASIAEASGLSPEDVISAHLSGDYSVFMYGFAPGYAYLAGVPKAIQQPRKPAPIRGIAAGSVLIAG 177
Cdd:TIGR00370  79 IEIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPSVPAGSVGIGG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 502304082  178 PQCLVSTLTMPTGWWIIGRSPTKILDAASNDrPFLFDVGDTVRF 221
Cdd:TIGR00370 159 LQTGVYPISTPGGWQLIGKTPLALFDPQENP-PTLLRAGDIVKF 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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