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Conserved domains on  [gi|446720053|ref|WP_000797366|]
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MULTISPECIES: HpcH/HpaI aldolase/citrate lyase family protein [Enterobacterales]

Protein Classification

HpcH/HpaI aldolase/citrate lyase family protein( domain architecture ID 10634866)

HpcH/HpaI aldolase/citrate lyase family protein with similarity to citrate lyase subunit beta (CitE)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
C-C_Bond_Lyase pfam15617
C-C_Bond_Lyase of the TIM-Barrel fold; This family of TIM-Barrel fold C-C bond lyase is ...
4-300 2.05e-151

C-C_Bond_Lyase of the TIM-Barrel fold; This family of TIM-Barrel fold C-C bond lyase is related to citrate-lyase. These genes are found in the biosynthetic operon, with other enzymatic domains, associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


:

Pssm-ID: 406131  Cd Length: 320  Bit Score: 427.36  E-value: 2.05e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053    4 RLSPWNLGATLYMPATREDIADAVLHGKIPGLRSLVICLEDAVSEADIPVALKNLEHLLHELSNSMHSlGKNDWPLVFIR 83
Cdd:pfam15617   1 ELLAYALGATLYMPATRPDIADDILRQKIPGLRSLVICLEDAVSDQDVPLAEENLVAQLRTLAEAVKT-NKDDLPLLFVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053   84 PRHAEMGRWLKAHY--DLSAVDGFVLPKFTLSSLAEWWDIM------GGTHLCMMPTLETEDVF----DVVQMRELATRL 151
Cdd:pfam15617  80 VRNPEQLRRLLERLgpGISLLDGFVLPKFTSANGEAYLEALaktnlrAGRRLYAMPTLETPEVFyretRVEELLALRRLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053  152 VEHpcHDRIIALRIGGNDLMNVVSLRRPRDLTLYD-SPMGYVIKMLVSVFGPR--DFALTAPVCEHIDDHA--------V 220
Cdd:pfam15617 160 DKH--RDRILALRIGGTDLSSLYGLRRPRDLTIYDvTPVGDVIADIVNVFGRAgtGFVISGPVWEYFDDPErdrqelvsG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053  221 MARELALDMAHGLVGKTAIHPGQIEVIQNALMVTQGEHSDALRILNSTQ-AVFKSQ--GAMCEPATHRRWAAGILDRARF 297
Cdd:pfam15617 238 LIREVALDKANGLVGKTVIHPSQIAVVQALYVVTHEEYEDALDILNSAPgGVFKSNygNKMNEPAPHRAWAEKILLRAKI 317

                  ...
gi 446720053  298 YGL 300
Cdd:pfam15617 318 YGV 320
 
Name Accession Description Interval E-value
C-C_Bond_Lyase pfam15617
C-C_Bond_Lyase of the TIM-Barrel fold; This family of TIM-Barrel fold C-C bond lyase is ...
4-300 2.05e-151

C-C_Bond_Lyase of the TIM-Barrel fold; This family of TIM-Barrel fold C-C bond lyase is related to citrate-lyase. These genes are found in the biosynthetic operon, with other enzymatic domains, associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 406131  Cd Length: 320  Bit Score: 427.36  E-value: 2.05e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053    4 RLSPWNLGATLYMPATREDIADAVLHGKIPGLRSLVICLEDAVSEADIPVALKNLEHLLHELSNSMHSlGKNDWPLVFIR 83
Cdd:pfam15617   1 ELLAYALGATLYMPATRPDIADDILRQKIPGLRSLVICLEDAVSDQDVPLAEENLVAQLRTLAEAVKT-NKDDLPLLFVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053   84 PRHAEMGRWLKAHY--DLSAVDGFVLPKFTLSSLAEWWDIM------GGTHLCMMPTLETEDVF----DVVQMRELATRL 151
Cdd:pfam15617  80 VRNPEQLRRLLERLgpGISLLDGFVLPKFTSANGEAYLEALaktnlrAGRRLYAMPTLETPEVFyretRVEELLALRRLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053  152 VEHpcHDRIIALRIGGNDLMNVVSLRRPRDLTLYD-SPMGYVIKMLVSVFGPR--DFALTAPVCEHIDDHA--------V 220
Cdd:pfam15617 160 DKH--RDRILALRIGGTDLSSLYGLRRPRDLTIYDvTPVGDVIADIVNVFGRAgtGFVISGPVWEYFDDPErdrqelvsG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053  221 MARELALDMAHGLVGKTAIHPGQIEVIQNALMVTQGEHSDALRILNSTQ-AVFKSQ--GAMCEPATHRRWAAGILDRARF 297
Cdd:pfam15617 238 LIREVALDKANGLVGKTVIHPSQIAVVQALYVVTHEEYEDALDILNSAPgGVFKSNygNKMNEPAPHRAWAEKILLRAKI 317

                  ...
gi 446720053  298 YGL 300
Cdd:pfam15617 318 YGV 320
CitE COG2301
Citrate lyase beta subunit [Carbohydrate transport and metabolism];
10-303 1.74e-59

Citrate lyase beta subunit [Carbohydrate transport and metabolism];


Pssm-ID: 441876  Cd Length: 288  Bit Score: 192.29  E-value: 1.74e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053  10 LGATLYMPATREDIADAVLhgkIPGLRSLVICLEDAVSEADIPVALKNLEHLLHELsnsmhslGKNDwPLVFIRPRHAEM 89
Cdd:COG2301    6 RRSLLFVPGDRPRRLAKAL---ASGADAVILDLEDAVAPDEKDAARENVAEALAEL-------DFGG-PEVFVRINALDT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053  90 GRWLKahyDLSAV-----DGFVLPKFT----LSSLAEWWDIMG--GTHLCMMPTLETEDVfdVVQMRELATrlvehpCHD 158
Cdd:COG2301   75 PWGLD---DLAALvgaglDGIVLPKVEsaedVRALAALLTELEaeGGSIPLMALIETARG--LLNAAEIAA------ASP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053 159 RIIALRIGGNDLMNVVSLRRPRDltlyDSPMGYVIKMLVSVFGPRDFALTAPVCEHIDDHAVMARELALDMAHGLVGKTA 238
Cdd:COG2301  144 RVEALVFGAEDLAADLGARRTRD----GDELLYARSRIVLAARAAGLAAIDGVYTDFRDLEGLRAEARRARALGFDGKTA 219
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053 239 IHPGQIEVIQNALMVTQGEHSDALRILNSTQA-----VFKSQGAMCEPAtHRRWAAGILDRARFYGLQNE 303
Cdd:COG2301  220 IHPSQIAVINEAFAPSEEEVAWARRILAAFEEaeakgVVSLDGKMVDRP-HLRRARRILARARAIGVRPE 288
 
Name Accession Description Interval E-value
C-C_Bond_Lyase pfam15617
C-C_Bond_Lyase of the TIM-Barrel fold; This family of TIM-Barrel fold C-C bond lyase is ...
4-300 2.05e-151

C-C_Bond_Lyase of the TIM-Barrel fold; This family of TIM-Barrel fold C-C bond lyase is related to citrate-lyase. These genes are found in the biosynthetic operon, with other enzymatic domains, associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 406131  Cd Length: 320  Bit Score: 427.36  E-value: 2.05e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053    4 RLSPWNLGATLYMPATREDIADAVLHGKIPGLRSLVICLEDAVSEADIPVALKNLEHLLHELSNSMHSlGKNDWPLVFIR 83
Cdd:pfam15617   1 ELLAYALGATLYMPATRPDIADDILRQKIPGLRSLVICLEDAVSDQDVPLAEENLVAQLRTLAEAVKT-NKDDLPLLFVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053   84 PRHAEMGRWLKAHY--DLSAVDGFVLPKFTLSSLAEWWDIM------GGTHLCMMPTLETEDVF----DVVQMRELATRL 151
Cdd:pfam15617  80 VRNPEQLRRLLERLgpGISLLDGFVLPKFTSANGEAYLEALaktnlrAGRRLYAMPTLETPEVFyretRVEELLALRRLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053  152 VEHpcHDRIIALRIGGNDLMNVVSLRRPRDLTLYD-SPMGYVIKMLVSVFGPR--DFALTAPVCEHIDDHA--------V 220
Cdd:pfam15617 160 DKH--RDRILALRIGGTDLSSLYGLRRPRDLTIYDvTPVGDVIADIVNVFGRAgtGFVISGPVWEYFDDPErdrqelvsG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053  221 MARELALDMAHGLVGKTAIHPGQIEVIQNALMVTQGEHSDALRILNSTQ-AVFKSQ--GAMCEPATHRRWAAGILDRARF 297
Cdd:pfam15617 238 LIREVALDKANGLVGKTVIHPSQIAVVQALYVVTHEEYEDALDILNSAPgGVFKSNygNKMNEPAPHRAWAEKILLRAKI 317

                  ...
gi 446720053  298 YGL 300
Cdd:pfam15617 318 YGV 320
CitE COG2301
Citrate lyase beta subunit [Carbohydrate transport and metabolism];
10-303 1.74e-59

Citrate lyase beta subunit [Carbohydrate transport and metabolism];


Pssm-ID: 441876  Cd Length: 288  Bit Score: 192.29  E-value: 1.74e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053  10 LGATLYMPATREDIADAVLhgkIPGLRSLVICLEDAVSEADIPVALKNLEHLLHELsnsmhslGKNDwPLVFIRPRHAEM 89
Cdd:COG2301    6 RRSLLFVPGDRPRRLAKAL---ASGADAVILDLEDAVAPDEKDAARENVAEALAEL-------DFGG-PEVFVRINALDT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053  90 GRWLKahyDLSAV-----DGFVLPKFT----LSSLAEWWDIMG--GTHLCMMPTLETEDVfdVVQMRELATrlvehpCHD 158
Cdd:COG2301   75 PWGLD---DLAALvgaglDGIVLPKVEsaedVRALAALLTELEaeGGSIPLMALIETARG--LLNAAEIAA------ASP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053 159 RIIALRIGGNDLMNVVSLRRPRDltlyDSPMGYVIKMLVSVFGPRDFALTAPVCEHIDDHAVMARELALDMAHGLVGKTA 238
Cdd:COG2301  144 RVEALVFGAEDLAADLGARRTRD----GDELLYARSRIVLAARAAGLAAIDGVYTDFRDLEGLRAEARRARALGFDGKTA 219
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446720053 239 IHPGQIEVIQNALMVTQGEHSDALRILNSTQA-----VFKSQGAMCEPAtHRRWAAGILDRARFYGLQNE 303
Cdd:COG2301  220 IHPSQIAVINEAFAPSEEEVAWARRILAAFEEaeakgVVSLDGKMVDRP-HLRRARRILARARAIGVRPE 288
 
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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