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Conserved domains on  [gi|504199442|ref|WP_014386544|]
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MULTISPECIES: HpcH/HpaI aldolase/citrate lyase family protein [Enterobacteriaceae]

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 ...
7-300 4.11e-150

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: 423.90  E-value: 4.11e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442    7 PWELGATLYMPATRKDIAEVVLEGKIPGLRSLVVCLEDAVSEHDIPLAIQNLSLFLKQLRHARAVNDDEkYPLVFIRPRH 86
Cdd:pfam15617   4 AYALGATLYMPATRPDIADDILRQKIPGLRSLVICLEDAVSDQDVPLAEENLVAQLRTLAEAVKTNKDD-LPLLFVRVRN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442   87 TDMGGWLTTNL--DLSAVDGFVLPKFTLSTLPVWWDIMAGTS------LMMMPTLETEEVY----DVIKMQALANELSSH 154
Cdd:pfam15617  83 PEQLRRLLERLgpGISLLDGFVLPKFTSANGEAYLEALAKTNlragrrLYAMPTLETPEVFyretRVEELLALRRLLDKH 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442  155 dcRDRIIALRIGGNDLMNVVSLRRPRDLTLYD-TPMGYVIKMLVSVFAPR--DFALTAPVCEHIDDH--------GVLGR 223
Cdd:pfam15617 163 --RDRILALRIGGTDLSSLYGLRRPRDLTIYDvTPVGDVIADIVNVFGRAgtGFVISGPVWEYFDDPerdrqelvSGLIR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442  224 ELSMDIAHGLVGKTAIHPDQISVIEEALKVSPGEHSDALRILNSTQ-AVFKSQ--GAMCEPATHRRWAQGILGRGQVYGL 300
Cdd:pfam15617 241 EVALDKANGLVGKTVIHPSQIAVVQALYVVTHEEYEDALDILNSAPgGVFKSNygNKMNEPAPHRAWAEKILLRAKIYGV 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 ...
7-300 4.11e-150

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: 423.90  E-value: 4.11e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442    7 PWELGATLYMPATRKDIAEVVLEGKIPGLRSLVVCLEDAVSEHDIPLAIQNLSLFLKQLRHARAVNDDEkYPLVFIRPRH 86
Cdd:pfam15617   4 AYALGATLYMPATRPDIADDILRQKIPGLRSLVICLEDAVSDQDVPLAEENLVAQLRTLAEAVKTNKDD-LPLLFVRVRN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442   87 TDMGGWLTTNL--DLSAVDGFVLPKFTLSTLPVWWDIMAGTS------LMMMPTLETEEVY----DVIKMQALANELSSH 154
Cdd:pfam15617  83 PEQLRRLLERLgpGISLLDGFVLPKFTSANGEAYLEALAKTNlragrrLYAMPTLETPEVFyretRVEELLALRRLLDKH 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442  155 dcRDRIIALRIGGNDLMNVVSLRRPRDLTLYD-TPMGYVIKMLVSVFAPR--DFALTAPVCEHIDDH--------GVLGR 223
Cdd:pfam15617 163 --RDRILALRIGGTDLSSLYGLRRPRDLTIYDvTPVGDVIADIVNVFGRAgtGFVISGPVWEYFDDPerdrqelvSGLIR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442  224 ELSMDIAHGLVGKTAIHPDQISVIEEALKVSPGEHSDALRILNSTQ-AVFKSQ--GAMCEPATHRRWAQGILGRGQVYGL 300
Cdd:pfam15617 241 EVALDKANGLVGKTVIHPSQIAVVQALYVVTHEEYEDALDILNSAPgGVFKSNygNKMNEPAPHRAWAEKILLRAKIYGV 320
CitE COG2301
Citrate lyase beta subunit [Carbohydrate transport and metabolism];
10-301 1.71e-57

Citrate lyase beta subunit [Carbohydrate transport and metabolism];


Pssm-ID: 441876  Cd Length: 288  Bit Score: 186.90  E-value: 1.71e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442  10 LGATLYMPATRKDIAEVVLEgkiPGLRSLVVCLEDAVSEHDIPLAIQNLSLFLKQLRHARavnddekyPLVFIRPRHTDM 89
Cdd:COG2301    6 RRSLLFVPGDRPRRLAKALA---SGADAVILDLEDAVAPDEKDAARENVAEALAELDFGG--------PEVFVRINALDT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442  90 GGWLttnLDLSAV-----DGFVLPKF-TLSTLPVWWDIMA-----GTSLMMMPTLETEEVydVIKMQALAnelsshDCRD 158
Cdd:COG2301   75 PWGL---DDLAALvgaglDGIVLPKVeSAEDVRALAALLTeleaeGGSIPLMALIETARG--LLNAAEIA------AASP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442 159 RIIALRIGGNDLMNVVSLRRPRDltlyDTPMGYVIKMLVSVFAPRDFALTAPVCEHIDDHGVLGRELSMDIAHGLVGKTA 238
Cdd:COG2301  144 RVEALVFGAEDLAADLGARRTRD----GDELLYARSRIVLAARAAGLAAIDGVYTDFRDLEGLRAEARRARALGFDGKTA 219
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504199442 239 IHPDQISVIEEALKVSPGEHSDALRILNSTQA-----VFKSQGAMCEPAtHRRWAQGILGRGQVYGLT 301
Cdd:COG2301  220 IHPSQIAVINEAFAPSEEEVAWARRILAAFEEaeakgVVSLDGKMVDRP-HLRRARRILARARAIGVR 286
 
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 ...
7-300 4.11e-150

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: 423.90  E-value: 4.11e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442    7 PWELGATLYMPATRKDIAEVVLEGKIPGLRSLVVCLEDAVSEHDIPLAIQNLSLFLKQLRHARAVNDDEkYPLVFIRPRH 86
Cdd:pfam15617   4 AYALGATLYMPATRPDIADDILRQKIPGLRSLVICLEDAVSDQDVPLAEENLVAQLRTLAEAVKTNKDD-LPLLFVRVRN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442   87 TDMGGWLTTNL--DLSAVDGFVLPKFTLSTLPVWWDIMAGTS------LMMMPTLETEEVY----DVIKMQALANELSSH 154
Cdd:pfam15617  83 PEQLRRLLERLgpGISLLDGFVLPKFTSANGEAYLEALAKTNlragrrLYAMPTLETPEVFyretRVEELLALRRLLDKH 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442  155 dcRDRIIALRIGGNDLMNVVSLRRPRDLTLYD-TPMGYVIKMLVSVFAPR--DFALTAPVCEHIDDH--------GVLGR 223
Cdd:pfam15617 163 --RDRILALRIGGTDLSSLYGLRRPRDLTIYDvTPVGDVIADIVNVFGRAgtGFVISGPVWEYFDDPerdrqelvSGLIR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442  224 ELSMDIAHGLVGKTAIHPDQISVIEEALKVSPGEHSDALRILNSTQ-AVFKSQ--GAMCEPATHRRWAQGILGRGQVYGL 300
Cdd:pfam15617 241 EVALDKANGLVGKTVIHPSQIAVVQALYVVTHEEYEDALDILNSAPgGVFKSNygNKMNEPAPHRAWAEKILLRAKIYGV 320
CitE COG2301
Citrate lyase beta subunit [Carbohydrate transport and metabolism];
10-301 1.71e-57

Citrate lyase beta subunit [Carbohydrate transport and metabolism];


Pssm-ID: 441876  Cd Length: 288  Bit Score: 186.90  E-value: 1.71e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442  10 LGATLYMPATRKDIAEVVLEgkiPGLRSLVVCLEDAVSEHDIPLAIQNLSLFLKQLRHARavnddekyPLVFIRPRHTDM 89
Cdd:COG2301    6 RRSLLFVPGDRPRRLAKALA---SGADAVILDLEDAVAPDEKDAARENVAEALAELDFGG--------PEVFVRINALDT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442  90 GGWLttnLDLSAV-----DGFVLPKF-TLSTLPVWWDIMA-----GTSLMMMPTLETEEVydVIKMQALAnelsshDCRD 158
Cdd:COG2301   75 PWGL---DDLAALvgaglDGIVLPKVeSAEDVRALAALLTeleaeGGSIPLMALIETARG--LLNAAEIA------AASP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504199442 159 RIIALRIGGNDLMNVVSLRRPRDltlyDTPMGYVIKMLVSVFAPRDFALTAPVCEHIDDHGVLGRELSMDIAHGLVGKTA 238
Cdd:COG2301  144 RVEALVFGAEDLAADLGARRTRD----GDELLYARSRIVLAARAAGLAAIDGVYTDFRDLEGLRAEARRARALGFDGKTA 219
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504199442 239 IHPDQISVIEEALKVSPGEHSDALRILNSTQA-----VFKSQGAMCEPAtHRRWAQGILGRGQVYGLT 301
Cdd:COG2301  220 IHPSQIAVINEAFAPSEEEVAWARRILAAFEEaeakgVVSLDGKMVDRP-HLRRARRILARARAIGVR 286
 
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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