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Conserved domains on  [gi|499775190|ref|WP_011455924|]
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allophanate hydrolase subunit 1 [Jannaschia sp. CCS1]

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]; ...
1-212 2.52e-86

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


:

Pssm-ID: 441652  Cd Length: 229  Bit Score: 254.68  E-value: 2.52e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190   1 MLSFKPAGDTGLLVTVAETASDAANDRVIALDHAVTAAQIDGVLETIPALVNLMVHFDPLVTDHAALEAATRALFP-LPE 79
Cdd:COG2049    4 AMRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAAPLPGVVEVVPAYRSLLVHFDPLVIDPAALAARLRALLAeLDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190  80 MAAQDTRTHVIPVCYDAELCPDLLATAKATGLSIDAVIDAHSSARLRVSMYGFAPGYAYLSGLPPNLHVPRKTTALRDVP 159
Cdd:COG2049   84 AAEVPSRLVEIPVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTRVP 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499775190 160 KGSVLIAGGQSILTPLTMPTGWNIIGRSPAEVI---QDDKFLFNVGDTVTFTRVAR 212
Cdd:COG2049  164 AGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFdpdREPPALLRPGDRVRFVPISE 219
 
Name Accession Description Interval E-value
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
1-212 2.52e-86

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


Pssm-ID: 441652  Cd Length: 229  Bit Score: 254.68  E-value: 2.52e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190   1 MLSFKPAGDTGLLVTVAETASDAANDRVIALDHAVTAAQIDGVLETIPALVNLMVHFDPLVTDHAALEAATRALFP-LPE 79
Cdd:COG2049    4 AMRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAAPLPGVVEVVPAYRSLLVHFDPLVIDPAALAARLRALLAeLDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190  80 MAAQDTRTHVIPVCYDAELCPDLLATAKATGLSIDAVIDAHSSARLRVSMYGFAPGYAYLSGLPPNLHVPRKTTALRDVP 159
Cdd:COG2049   84 AAEVPSRLVEIPVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTRVP 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499775190 160 KGSVLIAGGQSILTPLTMPTGWNIIGRSPAEVI---QDDKFLFNVGDTVTFTRVAR 212
Cdd:COG2049  164 AGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFdpdREPPALLRPGDRVRFVPISE 219
CT_C_D pfam02682
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ...
4-196 1.00e-83

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: 247.08  E-value: 1.00e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190    4 FKPAGDTGLLVTVAETASDAANDRVIALDHAVTAAQIDGVLETIPALVNLMVHFDPLVTDHAALEAATRALFPLPEMAAQ 83
Cdd:pfam02682   2 IRPAGDRALLVEFGDEIDLALNRRVLALAAALRAAPLPGVVEVVPGYRSLLVHYDPLVTDLAALEARLRALLAALEAAAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190   84 DT-RTHVIPVCYDAELCPDLLATAKATGLSIDAVIDAHSSARLRVSMYGFAPGYAYLSGLPPNLHVPRKTTALRDVPKGS 162
Cdd:pfam02682  82 PGgRLIEIPVCYDGEFGPDLAEVAAHNGLSVEEVIRLHSAAEYRVYFLGFAPGFPYLGGLDPRLAVPRRATPRTRVPAGS 161
                         170       180       190
                  ....*....|....*....|....*....|....
gi 499775190  163 VLIAGGQSILTPLTMPTGWNIIGRSPAEVIQDDK 196
Cdd:pfam02682 162 VGIAGRQTGIYPLESPGGWQLIGRTPLPLFDPDR 195
AHS1 smart00796
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase ...
4-196 2.85e-79

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


Pssm-ID: 214820  Cd Length: 201  Bit Score: 235.88  E-value: 2.85e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190     4 FKPAGDTGLLVTVAETASDAANDRVIALDHAVTAAQIDGVLETIPALVNLMVHFDPLVTDHAALEAATRAL--FPLPEMA 81
Cdd:smart00796   3 IRPAGDRALLVEFGDEIDLALNRRVLALARALRAAPLPGVVELVPGYRSLLVHFDPLVIDPAALLARLRALeaLPLAEAL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190    82 AQDTRTHVIPVCYDAELCPDLLATAKATGLSIDAVIDAHSSARLRVSMYGFAPGYAYLSGLPPNLHVPRKTTALRDVPKG 161
Cdd:smart00796  83 EVPGRIIEIPVCYGGEFGPDLEFVARHNGLSVDEVIRLHSAAEYRVYMLGFAPGFPYLGGLDPRLATPRRSTPRTRVPAG 162
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 499775190   162 SVLIAGGQSILTPLTMPTGWNIIGRSPAEVIQDDK 196
Cdd:smart00796 163 SVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDR 197
TIGR00370 TIGR00370
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
8-207 2.05e-36

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


Pssm-ID: 129467  Cd Length: 202  Bit Score: 126.89  E-value: 2.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190    8 GDTGLLVTVAETASDAANDRVIALdhavtAAQID---GVLETIPALVNLMVHFDPLVTdhaALEAATRALFPLPEMAAQD 84
Cdd:TIGR00370   2 GESAVVIRLGPPINEQVQGIVWAA-----AAYLEeqpGFVECIPGMNNLTVFYDMYEV---YKHLPQRLSSPWEEVKDYE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190   85 -TRTHV-IPVCYDAELCPDLLATAKATGLSIDAVIDAHSSARLRVSMYGFAPGYAYLSGLPPNLHVPRKTTALRDVPKGS 162
Cdd:TIGR00370  74 vNRRIIeIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPSVPAGS 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 499775190  163 VLIAGGQSILTPLTMPTGWNIIGRSPAEVI---QDDKFLFNVGDTVTF 207
Cdd:TIGR00370 154 VGIGGLQTGVYPISTPGGWQLIGKTPLALFdpqENPPTLLRAGDIVKF 201
 
Name Accession Description Interval E-value
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
1-212 2.52e-86

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


Pssm-ID: 441652  Cd Length: 229  Bit Score: 254.68  E-value: 2.52e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190   1 MLSFKPAGDTGLLVTVAETASDAANDRVIALDHAVTAAQIDGVLETIPALVNLMVHFDPLVTDHAALEAATRALFP-LPE 79
Cdd:COG2049    4 AMRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAAPLPGVVEVVPAYRSLLVHFDPLVIDPAALAARLRALLAeLDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190  80 MAAQDTRTHVIPVCYDAELCPDLLATAKATGLSIDAVIDAHSSARLRVSMYGFAPGYAYLSGLPPNLHVPRKTTALRDVP 159
Cdd:COG2049   84 AAEVPSRLVEIPVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTRVP 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499775190 160 KGSVLIAGGQSILTPLTMPTGWNIIGRSPAEVI---QDDKFLFNVGDTVTFTRVAR 212
Cdd:COG2049  164 AGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFdpdREPPALLRPGDRVRFVPISE 219
CT_C_D pfam02682
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ...
4-196 1.00e-83

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: 247.08  E-value: 1.00e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190    4 FKPAGDTGLLVTVAETASDAANDRVIALDHAVTAAQIDGVLETIPALVNLMVHFDPLVTDHAALEAATRALFPLPEMAAQ 83
Cdd:pfam02682   2 IRPAGDRALLVEFGDEIDLALNRRVLALAAALRAAPLPGVVEVVPGYRSLLVHYDPLVTDLAALEARLRALLAALEAAAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190   84 DT-RTHVIPVCYDAELCPDLLATAKATGLSIDAVIDAHSSARLRVSMYGFAPGYAYLSGLPPNLHVPRKTTALRDVPKGS 162
Cdd:pfam02682  82 PGgRLIEIPVCYDGEFGPDLAEVAAHNGLSVEEVIRLHSAAEYRVYFLGFAPGFPYLGGLDPRLAVPRRATPRTRVPAGS 161
                         170       180       190
                  ....*....|....*....|....*....|....
gi 499775190  163 VLIAGGQSILTPLTMPTGWNIIGRSPAEVIQDDK 196
Cdd:pfam02682 162 VGIAGRQTGIYPLESPGGWQLIGRTPLPLFDPDR 195
AHS1 smart00796
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase ...
4-196 2.85e-79

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


Pssm-ID: 214820  Cd Length: 201  Bit Score: 235.88  E-value: 2.85e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190     4 FKPAGDTGLLVTVAETASDAANDRVIALDHAVTAAQIDGVLETIPALVNLMVHFDPLVTDHAALEAATRAL--FPLPEMA 81
Cdd:smart00796   3 IRPAGDRALLVEFGDEIDLALNRRVLALARALRAAPLPGVVELVPGYRSLLVHFDPLVIDPAALLARLRALeaLPLAEAL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190    82 AQDTRTHVIPVCYDAELCPDLLATAKATGLSIDAVIDAHSSARLRVSMYGFAPGYAYLSGLPPNLHVPRKTTALRDVPKG 161
Cdd:smart00796  83 EVPGRIIEIPVCYGGEFGPDLEFVARHNGLSVDEVIRLHSAAEYRVYMLGFAPGFPYLGGLDPRLATPRRSTPRTRVPAG 162
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 499775190   162 SVLIAGGQSILTPLTMPTGWNIIGRSPAEVIQDDK 196
Cdd:smart00796 163 SVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDR 197
TIGR00370 TIGR00370
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
8-207 2.05e-36

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


Pssm-ID: 129467  Cd Length: 202  Bit Score: 126.89  E-value: 2.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190    8 GDTGLLVTVAETASDAANDRVIALdhavtAAQID---GVLETIPALVNLMVHFDPLVTdhaALEAATRALFPLPEMAAQD 84
Cdd:TIGR00370   2 GESAVVIRLGPPINEQVQGIVWAA-----AAYLEeqpGFVECIPGMNNLTVFYDMYEV---YKHLPQRLSSPWEEVKDYE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499775190   85 -TRTHV-IPVCYDAELCPDLLATAKATGLSIDAVIDAHSSARLRVSMYGFAPGYAYLSGLPPNLHVPRKTTALRDVPKGS 162
Cdd:TIGR00370  74 vNRRIIeIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPSVPAGS 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 499775190  163 VLIAGGQSILTPLTMPTGWNIIGRSPAEVI---QDDKFLFNVGDTVTF 207
Cdd:TIGR00370 154 VGIGGLQTGVYPISTPGGWQLIGKTPLALFdpqENPPTLLRAGDIVKF 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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