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Conserved domains on  [gi|1635471494|ref|WP_137187932|]
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HpcH/HpaI aldolase/citrate lyase family protein [Pseudomonas asiatica]

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 ...
3-297 9.22e-122

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: 351.86  E-value: 9.22e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494   3 RISPWALGATLYMPATRADIVEVICADKQPGLRSLVICLEDAVAATDVEHALQSLRAILTAIGPRASRSPRS-PLVFVRP 81
Cdd:pfam15617   1 ELLAYALGATLYMPATRPDIADDILRQKIPGLRSLVICLEDAVSDQDVPLAEENLVAQLRTLAEAVKTNKDDlPLLFVRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494  82 RDSKMAAQLNEWPE--ITAAHGFVVPKLSLATLGEWVRAVTNPD------LLLMPTLETSDVYN----PGAMGELGCALr 149
Cdd:pfam15617  81 RNPEQLRRLLERLGpgISLLDGFVLPKFTSANGEAYLEALAKTNlragrrLYAMPTLETPEVFYretrVEELLALRRLL- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494 150 AELGDRILALRIGGNDLMSCLGLRRNPATTLYQ-TPMGYVIPMLCGVLGAQ--GFALTAPVFEQLATPQ--------LLA 218
Cdd:pfam15617 160 DKHRDRILALRIGGTDLSSLYGLRRPRDLTIYDvTPVGDVIADIVNVFGRAgtGFVISGPVWEYFDDPErdrqelvsGLI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494 219 EELDLDIAHGLVGKTAIHPTQISQIHDGFRVPLEDYNCAKLIVDGSAPAVFKHN--DAMVEPATHYNWAINIIERVKWHG 296
Cdd:pfam15617 240 REVALDKANGLVGKTVIHPSQIAVVQALYVVTHEEYEDALDILNSAPGGVFKSNygNKMNEPAPHRAWAEKILLRAKIYG 319

                  .
gi 1635471494 297 V 297
Cdd:pfam15617 320 V 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 ...
3-297 9.22e-122

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: 351.86  E-value: 9.22e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494   3 RISPWALGATLYMPATRADIVEVICADKQPGLRSLVICLEDAVAATDVEHALQSLRAILTAIGPRASRSPRS-PLVFVRP 81
Cdd:pfam15617   1 ELLAYALGATLYMPATRPDIADDILRQKIPGLRSLVICLEDAVSDQDVPLAEENLVAQLRTLAEAVKTNKDDlPLLFVRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494  82 RDSKMAAQLNEWPE--ITAAHGFVVPKLSLATLGEWVRAVTNPD------LLLMPTLETSDVYN----PGAMGELGCALr 149
Cdd:pfam15617  81 RNPEQLRRLLERLGpgISLLDGFVLPKFTSANGEAYLEALAKTNlragrrLYAMPTLETPEVFYretrVEELLALRRLL- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494 150 AELGDRILALRIGGNDLMSCLGLRRNPATTLYQ-TPMGYVIPMLCGVLGAQ--GFALTAPVFEQLATPQ--------LLA 218
Cdd:pfam15617 160 DKHRDRILALRIGGTDLSSLYGLRRPRDLTIYDvTPVGDVIADIVNVFGRAgtGFVISGPVWEYFDDPErdrqelvsGLI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494 219 EELDLDIAHGLVGKTAIHPTQISQIHDGFRVPLEDYNCAKLIVDGSAPAVFKHN--DAMVEPATHYNWAINIIERVKWHG 296
Cdd:pfam15617 240 REVALDKANGLVGKTVIHPSQIAVVQALYVVTHEEYEDALDILNSAPGGVFKSNygNKMNEPAPHRAWAEKILLRAKIYG 319

                  .
gi 1635471494 297 V 297
Cdd:pfam15617 320 V 320
CitE COG2301
Citrate lyase beta subunit [Carbohydrate transport and metabolism];
9-300 4.31e-46

Citrate lyase beta subunit [Carbohydrate transport and metabolism];


Pssm-ID: 441876  Cd Length: 288  Bit Score: 157.24  E-value: 4.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494   9 LGATLYMPATRADIVEVIcadKQPGLRSLVICLEDAVAATDVEHALQSLRAILTAIGPRAsrsprsPLVFVR--PRDSKM 86
Cdd:COG2301     6 RRSLLFVPGDRPRRLAKA---LASGADAVILDLEDAVAPDEKDAARENVAEALAELDFGG------PEVFVRinALDTPW 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494  87 AAQLNEWPEITAAHGFVVPKLS----LATLGEWVRAV--TNPDLLLMPTLETsdvynpgAMGELGCALRAELGDRILALR 160
Cdd:COG2301    77 GLDDLAALVGAGLDGIVLPKVEsaedVRALAALLTELeaEGGSIPLMALIET-------ARGLLNAAEIAAASPRVEALV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494 161 IGGNDLMSCLGLRRNPAttlyQTPMGYVIPMLCGVLGAQGFALTAPVFEQLATPQLLAEELDLDIAHGLVGKTAIHPTQI 240
Cdd:COG2301   150 FGAEDLAADLGARRTRD----GDELLYARSRIVLAARAAGLAAIDGVYTDFRDLEGLRAEARRARALGFDGKTAIHPSQI 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1635471494 241 SQIHDGFRVPLEDYNCAKLIVD----GSAPAVFKHNDAMVEPAtHYNWAINIIERVKWHGVKPA 300
Cdd:COG2301   226 AVINEAFAPSEEEVAWARRILAafeeAEAKGVVSLDGKMVDRP-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 ...
3-297 9.22e-122

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: 351.86  E-value: 9.22e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494   3 RISPWALGATLYMPATRADIVEVICADKQPGLRSLVICLEDAVAATDVEHALQSLRAILTAIGPRASRSPRS-PLVFVRP 81
Cdd:pfam15617   1 ELLAYALGATLYMPATRPDIADDILRQKIPGLRSLVICLEDAVSDQDVPLAEENLVAQLRTLAEAVKTNKDDlPLLFVRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494  82 RDSKMAAQLNEWPE--ITAAHGFVVPKLSLATLGEWVRAVTNPD------LLLMPTLETSDVYN----PGAMGELGCALr 149
Cdd:pfam15617  81 RNPEQLRRLLERLGpgISLLDGFVLPKFTSANGEAYLEALAKTNlragrrLYAMPTLETPEVFYretrVEELLALRRLL- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494 150 AELGDRILALRIGGNDLMSCLGLRRNPATTLYQ-TPMGYVIPMLCGVLGAQ--GFALTAPVFEQLATPQ--------LLA 218
Cdd:pfam15617 160 DKHRDRILALRIGGTDLSSLYGLRRPRDLTIYDvTPVGDVIADIVNVFGRAgtGFVISGPVWEYFDDPErdrqelvsGLI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494 219 EELDLDIAHGLVGKTAIHPTQISQIHDGFRVPLEDYNCAKLIVDGSAPAVFKHN--DAMVEPATHYNWAINIIERVKWHG 296
Cdd:pfam15617 240 REVALDKANGLVGKTVIHPSQIAVVQALYVVTHEEYEDALDILNSAPGGVFKSNygNKMNEPAPHRAWAEKILLRAKIYG 319

                  .
gi 1635471494 297 V 297
Cdd:pfam15617 320 V 320
CitE COG2301
Citrate lyase beta subunit [Carbohydrate transport and metabolism];
9-300 4.31e-46

Citrate lyase beta subunit [Carbohydrate transport and metabolism];


Pssm-ID: 441876  Cd Length: 288  Bit Score: 157.24  E-value: 4.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494   9 LGATLYMPATRADIVEVIcadKQPGLRSLVICLEDAVAATDVEHALQSLRAILTAIGPRAsrsprsPLVFVR--PRDSKM 86
Cdd:COG2301     6 RRSLLFVPGDRPRRLAKA---LASGADAVILDLEDAVAPDEKDAARENVAEALAELDFGG------PEVFVRinALDTPW 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494  87 AAQLNEWPEITAAHGFVVPKLS----LATLGEWVRAV--TNPDLLLMPTLETsdvynpgAMGELGCALRAELGDRILALR 160
Cdd:COG2301    77 GLDDLAALVGAGLDGIVLPKVEsaedVRALAALLTELeaEGGSIPLMALIET-------ARGLLNAAEIAAASPRVEALV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494 161 IGGNDLMSCLGLRRNPAttlyQTPMGYVIPMLCGVLGAQGFALTAPVFEQLATPQLLAEELDLDIAHGLVGKTAIHPTQI 240
Cdd:COG2301   150 FGAEDLAADLGARRTRD----GDELLYARSRIVLAARAAGLAAIDGVYTDFRDLEGLRAEARRARALGFDGKTAIHPSQI 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1635471494 241 SQIHDGFRVPLEDYNCAKLIVD----GSAPAVFKHNDAMVEPAtHYNWAINIIERVKWHGVKPA 300
Cdd:COG2301   226 AVINEAFAPSEEEVAWARRILAafeeAEAKGVVSLDGKMVDRP-HLRRARRILARARAIGVRPE 288
HpcH_HpaI pfam03328
HpcH/HpaI aldolase/citrate lyase family; This family includes 2,4-dihydroxyhept-2-ene-1, ...
13-237 8.22e-03

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: 36.95  E-value: 8.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494  13 LYMPATRADIVEvICADKQPGlrSLVICLEDAVAAT-------DVEHALQSLRAILTAigprasrsPRSPLVFVRPRDSK 85
Cdd:pfam03328   4 LFLPGANPAMAE-IAAIAGAD--WVVIDLEDAVALAekdaarvLVPTALQQLDALAAA--------PSEVVVRVNSLDSP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494  86 MAAQLNEWPEItAAHGFVVPKLSLAtlgEWVRAV-------------TNPDLLLMPTLETSD-VYNpgaMGELGCAlrae 151
Cdd:pfam03328  73 FGKQDLAVLDL-GAQVVLVPKVETA---EDARAAvsairyppkgirrANGNTCLLAQIESALgVLN---ADEIAAV---- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635471494 152 lgDRILALRIGGNDLMSCLGLRRNPAttlyQTPMGYVIPMLCGVLGAQGFALTAPVFEQLATPQLLAEELDLDIAHGLVG 231
Cdd:pfam03328 142 --EGVDGIFLGAEDLSADLGTLRSPG----GPEVLYARERIVTAARAAGIAAFDTVYSDENDAEGFLAEGALFVALGFDG 215

                  ....*.
gi 1635471494 232 KTAIHP 237
Cdd:pfam03328 216 KLLINP 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.
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