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Conserved domains on  [gi|446305325|ref|WP_000383180|]
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MULTISPECIES: 5-oxoprolinase subunit PxpB [Staphylococcus]

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]; ...
1-227 1.14e-105

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


:

Pssm-ID: 441652  Cd Length: 229  Bit Score: 304.76  E-value: 1.14e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325   1 MDVRFINEQTIMIYFENKISEETYRNVTAMVRWIREKEILEIQDIVPSYRAVLIYFDEQAITSSKLIENLElnKFNEKNV 80
Cdd:COG2049    5 MRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAAPLPGVVEVVPAYRSLLVHFDPLVIDPAALAARLR--ALLAELD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325  81 HAVNQTNRIIKIPVQYGGTYGPDIEEVAKHNRITVEQVIEKHTSKPYLIYMLGFMPGFPYLGGLDEQLHTPRRNQPRLKI 160
Cdd:COG2049   83 AAAEVPSRLVEIPVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTRV 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446305325 161 HAGSVGIANNQTGLYPSDSPGGWQIIGRTPLKVFSSEREPMSMYEAGEWIQFYAIDEQKFIQIERDI 227
Cdd:COG2049  163 PAGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPPALLRPGDRVRFVPISEEEFDALRGEV 229
 
Name Accession Description Interval E-value
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
1-227 1.14e-105

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


Pssm-ID: 441652  Cd Length: 229  Bit Score: 304.76  E-value: 1.14e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325   1 MDVRFINEQTIMIYFENKISEETYRNVTAMVRWIREKEILEIQDIVPSYRAVLIYFDEQAITSSKLIENLElnKFNEKNV 80
Cdd:COG2049    5 MRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAAPLPGVVEVVPAYRSLLVHFDPLVIDPAALAARLR--ALLAELD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325  81 HAVNQTNRIIKIPVQYGGTYGPDIEEVAKHNRITVEQVIEKHTSKPYLIYMLGFMPGFPYLGGLDEQLHTPRRNQPRLKI 160
Cdd:COG2049   83 AAAEVPSRLVEIPVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTRV 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446305325 161 HAGSVGIANNQTGLYPSDSPGGWQIIGRTPLKVFSSEREPMSMYEAGEWIQFYAIDEQKFIQIERDI 227
Cdd:COG2049  163 PAGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPPALLRPGDRVRFVPISEEEFDALRGEV 229
AHS1 smart00796
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase ...
1-202 8.06e-99

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


Pssm-ID: 214820  Cd Length: 201  Bit Score: 286.34  E-value: 8.06e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325     1 MDVRFINEQTIMIYFENKISEETYRNVTAMVRWIREKEILEIQDIVPSYRAVLIYFDEQAITSSKLIENLElNKFNEKNV 80
Cdd:smart00796   1 MRIRPAGDRALLVEFGDEIDLALNRRVLALARALRAAPLPGVVELVPGYRSLLVHFDPLVIDPAALLARLR-ALEALPLA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325    81 HAVNQTNRIIKIPVQYGGTYGPDIEEVAKHNRITVEQVIEKHTSKPYLIYMLGFMPGFPYLGGLDEQLHTPRRNQPRLKI 160
Cdd:smart00796  80 EALEVPGRIIEIPVCYGGEFGPDLEFVARHNGLSVDEVIRLHSAAEYRVYMLGFAPGFPYLGGLDPRLATPRRSTPRTRV 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 446305325   161 HAGSVGIANNQTGLYPSDSPGGWQIIGRTPLKVFSSEREPMS 202
Cdd:smart00796 160 PAGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPPA 201
CT_C_D pfam02682
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ...
3-202 9.72e-88

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: 258.25  E-value: 9.72e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325    3 VRFINEQTIMIYFENKISEETYRNVTAMVRWIREKEILEIQDIVPSYRAVLIYFDEQAITSSKLIENLElnKFNEKNVHA 82
Cdd:pfam02682   2 IRPAGDRALLVEFGDEIDLALNRRVLALAAALRAAPLPGVVEVVPGYRSLLVHYDPLVTDLAALEARLR--ALLAALEAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325   83 VNQTNRIIKIPVQYGGTYGPDIEEVAKHNRITVEQVIEKHTSKPYLIYMLGFMPGFPYLGGLDEQLHTPRRNQPRLKIHA 162
Cdd:pfam02682  80 AAPGGRLIEIPVCYDGEFGPDLAEVAAHNGLSVEEVIRLHSAAEYRVYFLGFAPGFPYLGGLDPRLAVPRRATPRTRVPA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 446305325  163 GSVGIANNQTGLYPSDSPGGWQIIGRTPLKVFSSEREPMS 202
Cdd:pfam02682 160 GSVGIAGRQTGIYPLESPGGWQLIGRTPLPLFDPDRDPPA 199
TIGR00370 TIGR00370
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
6-212 7.34e-60

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


Pssm-ID: 129467  Cd Length: 202  Bit Score: 187.75  E-value: 7.34e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325    6 INEQTIMIYFENKISEETYRNVTAMVRWIREKEilEIQDIVPSYRAVLIYFDEQAItSSKLIENLElNKFNEKNVHAVNq 85
Cdd:TIGR00370   1 IGESAVVIRLGPPINEQVQGIVWAAAAYLEEQP--GFVECIPGMNNLTVFYDMYEV-YKHLPQRLS-SPWEEVKDYEVN- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325   86 tNRIIKIPVQYGGTYGPDIEEVAKHNRITVEQVIEKHTSKPYLIYMLGFMPGFPYLGGLDEQLHTPRRNQPRLKIHAGSV 165
Cdd:TIGR00370  76 -RRIIEIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPSVPAGSV 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 446305325  166 GIANNQTGLYPSDSPGGWQIIGRTPLKVFSSEREPMSMYEAGEWIQF 212
Cdd:TIGR00370 155 GIGGLQTGVYPISTPGGWQLIGKTPLALFDPQENPPTLLRAGDIVKF 201
 
Name Accession Description Interval E-value
PxpB COG2049
5-oxoprolinase subunit B/Allophanate hydrolase subunit 1 [Amino acid transport and metabolism]; ...
1-227 1.14e-105

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


Pssm-ID: 441652  Cd Length: 229  Bit Score: 304.76  E-value: 1.14e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325   1 MDVRFINEQTIMIYFENKISEETYRNVTAMVRWIREKEILEIQDIVPSYRAVLIYFDEQAITSSKLIENLElnKFNEKNV 80
Cdd:COG2049    5 MRILPAGDRALLVEFGDEIDLELNRRVLALAAALRAAPLPGVVEVVPAYRSLLVHFDPLVIDPAALAARLR--ALLAELD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325  81 HAVNQTNRIIKIPVQYGGTYGPDIEEVAKHNRITVEQVIEKHTSKPYLIYMLGFMPGFPYLGGLDEQLHTPRRNQPRLKI 160
Cdd:COG2049   83 AAAEVPSRLVEIPVCYDGEFGPDLEEVARHNGLSVEEVIALHTAAEYRVYMLGFAPGFPYLGGLDPRLATPRRATPRTRV 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446305325 161 HAGSVGIANNQTGLYPSDSPGGWQIIGRTPLKVFSSEREPMSMYEAGEWIQFYAIDEQKFIQIERDI 227
Cdd:COG2049  163 PAGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPPALLRPGDRVRFVPISEEEFDALRGEV 229
AHS1 smart00796
Allophanate hydrolase subunit 1; This domain represents subunit 1 of allophanate hydrolase ...
1-202 8.06e-99

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


Pssm-ID: 214820  Cd Length: 201  Bit Score: 286.34  E-value: 8.06e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325     1 MDVRFINEQTIMIYFENKISEETYRNVTAMVRWIREKEILEIQDIVPSYRAVLIYFDEQAITSSKLIENLElNKFNEKNV 80
Cdd:smart00796   1 MRIRPAGDRALLVEFGDEIDLALNRRVLALARALRAAPLPGVVELVPGYRSLLVHFDPLVIDPAALLARLR-ALEALPLA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325    81 HAVNQTNRIIKIPVQYGGTYGPDIEEVAKHNRITVEQVIEKHTSKPYLIYMLGFMPGFPYLGGLDEQLHTPRRNQPRLKI 160
Cdd:smart00796  80 EALEVPGRIIEIPVCYGGEFGPDLEFVARHNGLSVDEVIRLHSAAEYRVYMLGFAPGFPYLGGLDPRLATPRRSTPRTRV 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 446305325   161 HAGSVGIANNQTGLYPSDSPGGWQIIGRTPLKVFSSEREPMS 202
Cdd:smart00796 160 PAGSVGIAGAQTGIYPLESPGGWQLIGRTPLPLFDPDREPPA 201
CT_C_D pfam02682
Carboxyltransferase domain, subdomain C and D; Urea carboxylase (UC) catalyzes a two-step, ...
3-202 9.72e-88

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: 258.25  E-value: 9.72e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325    3 VRFINEQTIMIYFENKISEETYRNVTAMVRWIREKEILEIQDIVPSYRAVLIYFDEQAITSSKLIENLElnKFNEKNVHA 82
Cdd:pfam02682   2 IRPAGDRALLVEFGDEIDLALNRRVLALAAALRAAPLPGVVEVVPGYRSLLVHYDPLVTDLAALEARLR--ALLAALEAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325   83 VNQTNRIIKIPVQYGGTYGPDIEEVAKHNRITVEQVIEKHTSKPYLIYMLGFMPGFPYLGGLDEQLHTPRRNQPRLKIHA 162
Cdd:pfam02682  80 AAPGGRLIEIPVCYDGEFGPDLAEVAAHNGLSVEEVIRLHSAAEYRVYFLGFAPGFPYLGGLDPRLAVPRRATPRTRVPA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 446305325  163 GSVGIANNQTGLYPSDSPGGWQIIGRTPLKVFSSEREPMS 202
Cdd:pfam02682 160 GSVGIAGRQTGIYPLESPGGWQLIGRTPLPLFDPDRDPPA 199
TIGR00370 TIGR00370
sensor histidine kinase inhibitor, KipI family; [Hypothetical proteins, Conserved]
6-212 7.34e-60

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


Pssm-ID: 129467  Cd Length: 202  Bit Score: 187.75  E-value: 7.34e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325    6 INEQTIMIYFENKISEETYRNVTAMVRWIREKEilEIQDIVPSYRAVLIYFDEQAItSSKLIENLElNKFNEKNVHAVNq 85
Cdd:TIGR00370   1 IGESAVVIRLGPPINEQVQGIVWAAAAYLEEQP--GFVECIPGMNNLTVFYDMYEV-YKHLPQRLS-SPWEEVKDYEVN- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446305325   86 tNRIIKIPVQYGGTYGPDIEEVAKHNRITVEQVIEKHTSKPYLIYMLGFMPGFPYLGGLDEQLHTPRRNQPRLKIHAGSV 165
Cdd:TIGR00370  76 -RRIIEIPVCYGGEFGPDLEEVAKINQLSPEEVIDIHSNGEYVVYMLGFQPGFPYLGGLPERLHTPRRASPRPSVPAGSV 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 446305325  166 GIANNQTGLYPSDSPGGWQIIGRTPLKVFSSEREPMSMYEAGEWIQF 212
Cdd:TIGR00370 155 GIGGLQTGVYPISTPGGWQLIGKTPLALFDPQENPPTLLRAGDIVKF 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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