NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|772702522|ref|WP_045295132|]
View 

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
4-299 1.59e-144

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: 410.03  E-value: 1.59e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522    4 RLSPWNLGATLYMPATRYDIEGAILDGKIPGLRSLVICLEDAVSETDIPRALENLRQLLQRLSQEKLRAGnQDWPLVFIR 83
Cdd:pfam15617   1 ELLAYALGATLYMPATRPDIADDILRQKIPGLRSLVICLEDAVSDQDVPLAEENLVAQLRTLAEAVKTNK-DDLPLLFVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522   84 PRHTEMGQWLVQNV--DLSAVDGFVLPKFTLASLPEWWAAMADTH------LCLMPTLETDDVF----DVLRMRELAEKL 151
Cdd:pfam15617  80 VRNPEQLRRLLERLgpGISLLDGFVLPKFTSANGEAYLEALAKTNlragrrLYAMPTLETPEVFyretRVEELLALRRLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522  152 LSHPclDRLIALRIGGNDLMNVVSLRRPRNLTLYD-GPMGYVIKMLVSVFGPR--DFALTAPVCEHIDDH--------DI 220
Cdd:pfam15617 160 DKHR--DRILALRIGGTDLSSLYGLRRPRDLTIYDvTPVGDVIADIVNVFGRAgtGFVISGPVWEYFDDPerdrqelvSG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522  221 MARELALDMAHGLVGKTAIHPAQIDVIENALKVSAGEHSDALRILNSTQ-AVFKSQ--GAMCEPATHRRWAASILERARI 297
Cdd:pfam15617 238 LIREVALDKANGLVGKTVIHPSQIAVVQALYVVTHEEYEDALDILNSAPgGVFKSNygNKMNEPAPHRAWAEKILLRAKI 317

                  ..
gi 772702522  298 YG 299
Cdd:pfam15617 318 YG 319
 
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 ...
4-299 1.59e-144

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: 410.03  E-value: 1.59e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522    4 RLSPWNLGATLYMPATRYDIEGAILDGKIPGLRSLVICLEDAVSETDIPRALENLRQLLQRLSQEKLRAGnQDWPLVFIR 83
Cdd:pfam15617   1 ELLAYALGATLYMPATRPDIADDILRQKIPGLRSLVICLEDAVSDQDVPLAEENLVAQLRTLAEAVKTNK-DDLPLLFVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522   84 PRHTEMGQWLVQNV--DLSAVDGFVLPKFTLASLPEWWAAMADTH------LCLMPTLETDDVF----DVLRMRELAEKL 151
Cdd:pfam15617  80 VRNPEQLRRLLERLgpGISLLDGFVLPKFTSANGEAYLEALAKTNlragrrLYAMPTLETPEVFyretRVEELLALRRLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522  152 LSHPclDRLIALRIGGNDLMNVVSLRRPRNLTLYD-GPMGYVIKMLVSVFGPR--DFALTAPVCEHIDDH--------DI 220
Cdd:pfam15617 160 DKHR--DRILALRIGGTDLSSLYGLRRPRDLTIYDvTPVGDVIADIVNVFGRAgtGFVISGPVWEYFDDPerdrqelvSG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522  221 MARELALDMAHGLVGKTAIHPAQIDVIENALKVSAGEHSDALRILNSTQ-AVFKSQ--GAMCEPATHRRWAASILERARI 297
Cdd:pfam15617 238 LIREVALDKANGLVGKTVIHPSQIAVVQALYVVTHEEYEDALDILNSAPgGVFKSNygNKMNEPAPHRAWAEKILLRAKI 317

                  ..
gi 772702522  298 YG 299
Cdd:pfam15617 318 YG 319
CitE COG2301
Citrate lyase beta subunit [Carbohydrate transport and metabolism];
10-303 8.68e-59

Citrate lyase beta subunit [Carbohydrate transport and metabolism];


Pssm-ID: 441876  Cd Length: 288  Bit Score: 190.36  E-value: 8.68e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522  10 LGATLYMPATRYDiegAILDGKIPGLRSLVICLEDAVSETDIPRALENLRQLLQRLSQEKlragnqdwPLVFIRPRHTEM 89
Cdd:COG2301    6 RRSLLFVPGDRPR---RLAKALASGADAVILDLEDAVAPDEKDAARENVAEALAELDFGG--------PEVFVRINALDT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522  90 GQWLVqnvDLSAV-----DGFVLPKFTLASLPEWWAAM------ADTHLCLMPTLETDDVfdVLRMRELAEkllshpCLD 158
Cdd:COG2301   75 PWGLD---DLAALvgaglDGIVLPKVESAEDVRALAALlteleaEGGSIPLMALIETARG--LLNAAEIAA------ASP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522 159 RLIALRIGGNDLMNVVSLRRPRNltlyDGPMGYVIKMLVSVFGPRDFALTAPVCEHIDDHDIMARELALDMAHGLVGKTA 238
Cdd:COG2301  144 RVEALVFGAEDLAADLGARRTRD----GDELLYARSRIVLAARAAGLAAIDGVYTDFRDLEGLRAEARRARALGFDGKTA 219
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522 239 IHPAQIDVIENALKVSAGEHSDALRILNSTQA-----VFKSQGAMCEPAtHRRWAASILERARIYGMIPE 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 ...
4-299 1.59e-144

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: 410.03  E-value: 1.59e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522    4 RLSPWNLGATLYMPATRYDIEGAILDGKIPGLRSLVICLEDAVSETDIPRALENLRQLLQRLSQEKLRAGnQDWPLVFIR 83
Cdd:pfam15617   1 ELLAYALGATLYMPATRPDIADDILRQKIPGLRSLVICLEDAVSDQDVPLAEENLVAQLRTLAEAVKTNK-DDLPLLFVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522   84 PRHTEMGQWLVQNV--DLSAVDGFVLPKFTLASLPEWWAAMADTH------LCLMPTLETDDVF----DVLRMRELAEKL 151
Cdd:pfam15617  80 VRNPEQLRRLLERLgpGISLLDGFVLPKFTSANGEAYLEALAKTNlragrrLYAMPTLETPEVFyretRVEELLALRRLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522  152 LSHPclDRLIALRIGGNDLMNVVSLRRPRNLTLYD-GPMGYVIKMLVSVFGPR--DFALTAPVCEHIDDH--------DI 220
Cdd:pfam15617 160 DKHR--DRILALRIGGTDLSSLYGLRRPRDLTIYDvTPVGDVIADIVNVFGRAgtGFVISGPVWEYFDDPerdrqelvSG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522  221 MARELALDMAHGLVGKTAIHPAQIDVIENALKVSAGEHSDALRILNSTQ-AVFKSQ--GAMCEPATHRRWAASILERARI 297
Cdd:pfam15617 238 LIREVALDKANGLVGKTVIHPSQIAVVQALYVVTHEEYEDALDILNSAPgGVFKSNygNKMNEPAPHRAWAEKILLRAKI 317

                  ..
gi 772702522  298 YG 299
Cdd:pfam15617 318 YG 319
CitE COG2301
Citrate lyase beta subunit [Carbohydrate transport and metabolism];
10-303 8.68e-59

Citrate lyase beta subunit [Carbohydrate transport and metabolism];


Pssm-ID: 441876  Cd Length: 288  Bit Score: 190.36  E-value: 8.68e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522  10 LGATLYMPATRYDiegAILDGKIPGLRSLVICLEDAVSETDIPRALENLRQLLQRLSQEKlragnqdwPLVFIRPRHTEM 89
Cdd:COG2301    6 RRSLLFVPGDRPR---RLAKALASGADAVILDLEDAVAPDEKDAARENVAEALAELDFGG--------PEVFVRINALDT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522  90 GQWLVqnvDLSAV-----DGFVLPKFTLASLPEWWAAM------ADTHLCLMPTLETDDVfdVLRMRELAEkllshpCLD 158
Cdd:COG2301   75 PWGLD---DLAALvgaglDGIVLPKVESAEDVRALAALlteleaEGGSIPLMALIETARG--LLNAAEIAA------ASP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522 159 RLIALRIGGNDLMNVVSLRRPRNltlyDGPMGYVIKMLVSVFGPRDFALTAPVCEHIDDHDIMARELALDMAHGLVGKTA 238
Cdd:COG2301  144 RVEALVFGAEDLAADLGARRTRD----GDELLYARSRIVLAARAAGLAAIDGVYTDFRDLEGLRAEARRARALGFDGKTA 219
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522 239 IHPAQIDVIENALKVSAGEHSDALRILNSTQA-----VFKSQGAMCEPAtHRRWAASILERARIYGMIPE 303
Cdd:COG2301  220 IHPSQIAVINEAFAPSEEEVAWARRILAAFEEaeakgVVSLDGKMVDRP-HLRRARRILARARAIGVRPE 288
HpcH_HpaI pfam03328
HpcH/HpaI aldolase/citrate lyase family; This family includes 2,4-dihydroxyhept-2-ene-1, ...
37-241 7.18e-04

HpcH/HpaI aldolase/citrate lyase family; This family includes 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase and 4-hydroxy-2-oxovalerate aldolase.


Pssm-ID: 427247 [Multi-domain]  Cd Length: 221  Bit Score: 40.42  E-value: 7.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522   37 SLVICLEDAVSETDIPRALENLRQLLQRLsqEKLRAGNQDwPLVFIRPRHTEMGQWLVQNVDLSAvDGFVLPKF------ 110
Cdd:pfam03328  24 WVVIDLEDAVALAEKDAARVLVPTALQQL--DALAAAPSE-VVVRVNSLDSPFGKQDLAVLDLGA-QVVLVPKVetaeda 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 772702522  111 -TLASL---PEWWAAMADTHLCLMPTLETDDvfDVLRMRELAekllshpCLDRLIALRIGGNDLmnVVSLRRPRNltlYD 186
Cdd:pfam03328 100 rAAVSAiryPPKGIRRANGNTCLLAQIESAL--GVLNADEIA-------AVEGVDGIFLGAEDL--SADLGTLRS---PG 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 772702522  187 GP-MGYVIKMLVSVFGPRDFALTAPVCEHIDDHDIMARELALDMAHGLVGKTAIHP 241
Cdd:pfam03328 166 GPeVLYARERIVTAARAAGIAAFDTVYSDENDAEGFLAEGALFVALGFDGKLLINP 221
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH