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Conserved domains on  [gi|1994618587|ref|WP_205306410|]
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alpha/beta fold hydrolase [Oerskovia jenensis]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 2-240 1.46e-22

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


:

Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 91.99  E-value: 1.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   2 GLPVLFVHGSRTSRTMWRAQLEAMdRAGLAAAAVDLPGHG--ARTGEAFTLDGAVATVAGAVDDLG-GRALVVGLSLGGY 78
Cdd:COG0596    23 GPPVVLLHGLPGSSYEWRPLIPAL-AAGYRVIAPDLRGHGrsDKPAGGYTLDDLADDLAALLDALGlERVVLVGHSMGGM 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587  79 VGIEHRARFPEQVAGLVaascctvpasrlrgawrVAADRIEKLPDNgaalnqalvnrtlpgagiedIGAGGFALTAMTAI 158
Cdd:COG0596   102 VALELAARHPERVAGLV-----------------LVDEVLAALAEP--------------------LRRPGLAPEALAAL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587 159 LDEVGRTDPLAALSTTDSPVWFLNGRWDhfRFGERAYLAAARAGGARAELVVVPGAKHLVSLDRPVAFNRAVLgahTFLA 238
Cdd:COG0596   145 LRALARTDLRERLARITVPTLVIWGEKD--PIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALR---DFLA 219


                  ..
gi 1994618587 239 EA 240
Cdd:COG0596   220 RL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 2-240 1.46e-22

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 91.99  E-value: 1.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   2 GLPVLFVHGSRTSRTMWRAQLEAMdRAGLAAAAVDLPGHG--ARTGEAFTLDGAVATVAGAVDDLG-GRALVVGLSLGGY 78
Cdd:COG0596    23 GPPVVLLHGLPGSSYEWRPLIPAL-AAGYRVIAPDLRGHGrsDKPAGGYTLDDLADDLAALLDALGlERVVLVGHSMGGM 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587  79 VGIEHRARFPEQVAGLVaascctvpasrlrgawrVAADRIEKLPDNgaalnqalvnrtlpgagiedIGAGGFALTAMTAI 158
Cdd:COG0596   102 VALELAARHPERVAGLV-----------------LVDEVLAALAEP--------------------LRRPGLAPEALAAL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587 159 LDEVGRTDPLAALSTTDSPVWFLNGRWDhfRFGERAYLAAARAGGARAELVVVPGAKHLVSLDRPVAFNRAVLgahTFLA 238
Cdd:COG0596   145 LRALARTDLRERLARITVPTLVIWGEKD--PIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALR---DFLA 219


                  ..
gi 1994618587 239 EA 240
Cdd:COG0596   220 RL 221
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 2-231 2.29e-10

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 59.57  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   2 GLPVLFVHGSRTSRTMWRAQLEAMdRAGLAAAAVDLPGHGARTG--EAFTLDGAVATVAGAVDDLG-GRALVVGLSLGGY 78
Cdd:PRK14875  131 GTPVVLIHGFGGDLNNWLFNHAAL-AAGRPVIALDLPGHGASSKavGAGSLDELAAAVLAFLDALGiERAHLVGHSMGGA 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587  79 VGIEHRARFPEQVA--GLVAASCC--TVPASRLRGAwrVAADR-------IEKLPDNGAALNQALVNRTLPGAGIEDIGA 147
Cdd:PRK14875  210 VALRLAARAPQRVAslTLIAPAGLgpEINGDYIDGF--VAAESrrelkpvLELLFADPALVTRQMVEDLLKYKRLDGVDD 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587 148 ggfALTAMTAIL--DEVGRTDPLAALSTTDSPVWFLNGRWDhfRFGERAYlaaARAGGARAELVVVPGAKHLVSLDRPVA 225
Cdd:PRK14875  288 ---ALRALADALfaGGRQRVDLRDRLASLAIPVLVIWGEQD--RIIPAAH---AQGLPDGVAVHVLPGAGHMPQMEAAAD 359


                  ....*.
gi 1994618587 226 FNRAVL 231
Cdd:PRK14875  360 VNRLLA 365
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 5-226 7.51e-09

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 54.44  E-value: 7.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   5 VLFVHGSRTSRTMWRAQLEAMdRAGLAAAAVDLPGHG-ARTGEAFTLDGAVATVAGAVDDlggRALVVGLSLGGYVGIEH 83
Cdd:TIGR01738   7 LVLIHGWGMNAEVFRCLDEEL-SAHFTLHLVDLPGHGrSRGFGPLSLADMAEAIAAQAPD---PAIWLGWSLGGLVALHI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587  84 RARFPEQVAGLV--AASCCTVPasrlRGAWR--VAADRIEKLPDNGAALNQALVNRTLP-------------GAGIEDIG 146
Cdd:TIGR01738  83 AATHPDRVRALVtvASSPCFSA----REDWPegIKPDVLTGFQQQLSDDYQRTIERFLAlqtlgtptarqdaRALKQTLL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587 147 AGGFALT-AMTAILDEVGRTDPLAALSTTDSPVWFLNGRWDhfRFGERAYLAAARAGGARAELVVVPGAKHLVSLDRPVA 225
Cdd:TIGR01738 159 ARPTPNVqVLQAGLEILATVDLRQPLQNISVPFLRLYGYLD--GLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSHAEA 236


                  .
gi 1994618587 226 F 226
Cdd:TIGR01738 237 F 237
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 5-229 9.43e-07

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 48.24  E-value: 9.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   5 VLFVHGSRTSRtmwrAQLEAMDRAGLAAAAVDLPGHGARTGEAFTLDgAVATVAGAVDDLGG--RALVVGLSLGGYVGIE 82
Cdd:pfam12697   1 VVLVHGAGLSA----APLAALLAAGVAVLAPDLPGHGSSSPPPLDLA-DLADLAALLDELGAarPVVLVGHSLGGAVALA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587  83 HRARFPEQVAGLVAASCCTVPASRLRGAWRVAADRIEKLP-DNGAALNQALVNRTLPGAGIEDIGAGGFALTAMTAilde 161
Cdd:pfam12697  76 AAAAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAwLAAESLARGFLDDLPADAEWAAALARLAALLAALA---- 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1994618587 162 vgrTDPLAALSTTDSPVWFLNGRwDHFrfgERAYLAAARAGGARAELVVVPGAKHLVsLDRPVAFNRA 229
Cdd:pfam12697 152 ---LLPLAAWRDLPVPVLVLAEE-DRL---VPELAQRLLAALAGARLVVLPGAGHLP-LDDPEEVAEA 211
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 2-240 1.46e-22

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 91.99  E-value: 1.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   2 GLPVLFVHGSRTSRTMWRAQLEAMdRAGLAAAAVDLPGHG--ARTGEAFTLDGAVATVAGAVDDLG-GRALVVGLSLGGY 78
Cdd:COG0596    23 GPPVVLLHGLPGSSYEWRPLIPAL-AAGYRVIAPDLRGHGrsDKPAGGYTLDDLADDLAALLDALGlERVVLVGHSMGGM 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587  79 VGIEHRARFPEQVAGLVaascctvpasrlrgawrVAADRIEKLPDNgaalnqalvnrtlpgagiedIGAGGFALTAMTAI 158
Cdd:COG0596   102 VALELAARHPERVAGLV-----------------LVDEVLAALAEP--------------------LRRPGLAPEALAAL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587 159 LDEVGRTDPLAALSTTDSPVWFLNGRWDhfRFGERAYLAAARAGGARAELVVVPGAKHLVSLDRPVAFNRAVLgahTFLA 238
Cdd:COG0596   145 LRALARTDLRERLARITVPTLVIWGEKD--PIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALR---DFLA 219


                  ..
gi 1994618587 239 EA 240
Cdd:COG0596   220 RL 221
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
4-98 3.58e-11

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 60.79  E-value: 3.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   4 PVLFVHGSRTSRTMWRAQLEAMDRAGLAAAAVDLPGHG---ARTGEAFTLDGAVATVAGAVDDL----GGRALVVGLSLG 76
Cdd:COG2267    30 TVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGrsdGPRGHVDSFDDYVDDLRAALDALrarpGLPVVLLGHSMG 109

                          90       100
                  ....*....|....*....|..
gi 1994618587  77 GYVGIEHRARFPEQVAGLVAAS 98
Cdd:COG2267   110 GLIALLYAARYPDRVAGLVLLA 131
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 2-231 2.29e-10

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 59.57  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   2 GLPVLFVHGSRTSRTMWRAQLEAMdRAGLAAAAVDLPGHGARTG--EAFTLDGAVATVAGAVDDLG-GRALVVGLSLGGY 78
Cdd:PRK14875  131 GTPVVLIHGFGGDLNNWLFNHAAL-AAGRPVIALDLPGHGASSKavGAGSLDELAAAVLAFLDALGiERAHLVGHSMGGA 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587  79 VGIEHRARFPEQVA--GLVAASCC--TVPASRLRGAwrVAADR-------IEKLPDNGAALNQALVNRTLPGAGIEDIGA 147
Cdd:PRK14875  210 VALRLAARAPQRVAslTLIAPAGLgpEINGDYIDGF--VAAESrrelkpvLELLFADPALVTRQMVEDLLKYKRLDGVDD 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587 148 ggfALTAMTAIL--DEVGRTDPLAALSTTDSPVWFLNGRWDhfRFGERAYlaaARAGGARAELVVVPGAKHLVSLDRPVA 225
Cdd:PRK14875  288 ---ALRALADALfaGGRQRVDLRDRLASLAIPVLVIWGEQD--RIIPAAH---AQGLPDGVAVHVLPGAGHMPQMEAAAD 359


                  ....*.
gi 1994618587 226 FNRAVL 231
Cdd:PRK14875  360 VNRLLA 365
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 5-226 7.51e-09

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 54.44  E-value: 7.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   5 VLFVHGSRTSRTMWRAQLEAMdRAGLAAAAVDLPGHG-ARTGEAFTLDGAVATVAGAVDDlggRALVVGLSLGGYVGIEH 83
Cdd:TIGR01738   7 LVLIHGWGMNAEVFRCLDEEL-SAHFTLHLVDLPGHGrSRGFGPLSLADMAEAIAAQAPD---PAIWLGWSLGGLVALHI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587  84 RARFPEQVAGLV--AASCCTVPasrlRGAWR--VAADRIEKLPDNGAALNQALVNRTLP-------------GAGIEDIG 146
Cdd:TIGR01738  83 AATHPDRVRALVtvASSPCFSA----REDWPegIKPDVLTGFQQQLSDDYQRTIERFLAlqtlgtptarqdaRALKQTLL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587 147 AGGFALT-AMTAILDEVGRTDPLAALSTTDSPVWFLNGRWDhfRFGERAYLAAARAGGARAELVVVPGAKHLVSLDRPVA 225
Cdd:TIGR01738 159 ARPTPNVqVLQAGLEILATVDLRQPLQNISVPFLRLYGYLD--GLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSHAEA 236


                  .
gi 1994618587 226 F 226
Cdd:TIGR01738 237 F 237
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
5-98 5.54e-08

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 51.87  E-value: 5.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   5 VLFVHG---SRTSRTMWRAQLEamdRAGLAAAAVDLPGHGARTGE--AFTLDGAVATVAGAVDDL---GGRALVVGLSLG 76
Cdd:COG1647    18 VLLLHGftgSPAEMRPLAEALA---KAGYTVYAPRLPGHGTSPEDllKTTWEDWLEDVEEAYEILkagYDKVIVIGLSMG 94

                          90       100
                  ....*....|....*....|..
gi 1994618587  77 GYVGIEHRARFPEqVAGLVAAS 98
Cdd:COG1647    95 GLLALLLAARYPD-VAGLVLLS 115
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
5-130 1.24e-07

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 50.79  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   5 VLFVHGSRTSRT-MWRAQLEAMDRAGLAAAAVDLPGHGARTGEAFTLDgaVATVAGAVDDL-------GGRALVVGLSLG 76
Cdd:COG1506    26 VVYVHGGPGSRDdSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDE--VDDVLAAIDYLaarpyvdPDRIGIYGHSYG 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1994618587  77 GYVGIEHRARFPEQVAGLVAASCCTVPASRLRGAWRVAADRIEKLPDNGAALNQ 130
Cdd:COG1506   104 GYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTERLMGGPWEDPEAYAA 157
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 5-223 4.93e-07

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 49.14  E-value: 4.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   5 VLFVHGSRTSRTMWRAQLEAMDRAGLAAAAVDLPGHGARTGEAfTLDGAVAT--VAGAVDDLGGRALV-------VGLSL 75
Cdd:COG1073    40 VVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEP-REEGSPERrdARAAVDYLRTLPGVdperiglLGISL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587  76 GGYVGIEHRARFPeQVAGLVAAScctvPASRLrgaWRVAADRIEKlpDNGAALNQALVnrtLPGAGIEDIGAGGFaltam 155
Cdd:COG1073   119 GGGYALNAAATDP-RVKAVILDS----PFTSL---EDLAAQRAKE--ARGAYLPGVPY---LPNVRLASLLNDEF----- 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994618587 156 taildevgrtDPLAALSTTDSPVWFLNGRWDH---FRFGERAYlaaaRAGGARAELVVVPGAKHLVSLDRP 223
Cdd:COG1073   181 ----------DPLAKIEKISRPLLFIHGEKDEavpFYMSEDLY----EAAAEPKELLIVPGAGHVDLYDRP 237
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 4-232 7.24e-07

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274729 [Multi-domain]  Cd Length: 252  Bit Score: 48.75  E-value: 7.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   4 PVLFVHGSRTSRTMWRAQLEAMDRaGLAAAAVDLPGHGArtgEAFTLDGAVATVAGAVDDL---------GGRALVVGLS 74
Cdd:TIGR03695   4 VLVFLHGFLGSGADWQALIEALGP-HFRCLAIDLPGHGS---SQSPSDIERYDFEEAAQLLlatlldqlgIEPFFLVGYS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587  75 LGGYVGIEHRARFPEQVAGLVAASC---CTVPASRlrgAWRVA-----ADRIEKLP--------------DNGAALN--- 129
Cdd:TIGR03695  80 MGGRIALYYALQYPERVQGLILESGspgLQTEEER---AARRQndeqlAQRFEQEGleaflddwyqqplfASQKNLPpeq 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587 130 -QALVNRTLPGAGIEdIGAggfALTAMTaildeVGRT-DPLAALSTTDSPVWFLNGRWDHfRFgeRAYLAAARAGGARAE 207
Cdd:TIGR03695 157 rQALRAERLANNPEG-LAK---MLRATG-----LGKQpSLWPKLQALKIPVLYLCGERDE-KF--VQIAKEMQKLIPNLT 224

                         250       260
                  ....*....|....*....|....*
gi 1994618587 208 LVVVPGAKHLVSLDRPVAFNRAVLG 232
Cdd:TIGR03695 225 LHIIPNAGHNIHLENPEAFAKILLA 249
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 5-229 9.43e-07

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 48.24  E-value: 9.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   5 VLFVHGSRTSRtmwrAQLEAMDRAGLAAAAVDLPGHGARTGEAFTLDgAVATVAGAVDDLGG--RALVVGLSLGGYVGIE 82
Cdd:pfam12697   1 VVLVHGAGLSA----APLAALLAAGVAVLAPDLPGHGSSSPPPLDLA-DLADLAALLDELGAarPVVLVGHSLGGAVALA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587  83 HRARFPEQVAGLVAASCCTVPASRLRGAWRVAADRIEKLP-DNGAALNQALVNRTLPGAGIEDIGAGGFALTAMTAilde 161
Cdd:pfam12697  76 AAAAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAwLAAESLARGFLDDLPADAEWAAALARLAALLAALA---- 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1994618587 162 vgrTDPLAALSTTDSPVWFLNGRwDHFrfgERAYLAAARAGGARAELVVVPGAKHLVsLDRPVAFNRA 229
Cdd:pfam12697 152 ---LLPLAAWRDLPVPVLVLAEE-DRL---VPELAQRLLAALAGARLVVLPGAGHLP-LDDPEEVAEA 211
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 4-95 2.06e-05

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 44.42  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   4 PVLFVHGSRTSRTMWRAQLEAMDRAGLAAAAVDLPGHG----ARTGEAFTLDGAVATVAGAVDDLG-GRALVVGLSLGGY 78
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGkssrPKAQDDYRTDDLAEDLEYILEALGlEKVNLVGHSMGGL 81

                          90
                  ....*....|....*..
gi 1994618587  79 VGIEHRARFPEQVAGLV 95
Cdd:pfam00561  82 IALAYAAKYPDRVKALV 98
PLN02578 PLN02578
hydrolase
 2-95 2.16e-04

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 41.75  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   2 GLPVLFVHGSRTSRTMWRAQLEAMDRAgLAAAAVDLPGHGARTGEAFTLDGAVAT--VAGAVDDLGGR-ALVVGLSLGGY 78
Cdd:PLN02578   86 GLPIVLIHGFGASAFHWRYNIPELAKK-YKVYALDLLGFGWSDKALIEYDAMVWRdqVADFVKEVVKEpAVLVGNSLGGF 164

                          90
                  ....*....|....*..
gi 1994618587  79 VGIEHRARFPEQVAGLV 95
Cdd:PLN02578  165 TALSTAVGYPELVAGVA 181
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
5-111 3.40e-04

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 40.77  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   5 VLFVHGSRTSRTMWRAQLEAMDrAGLAAAAVDLPGHGARTG-EAFTLDGAVATVAGAVDDlggRALVVGLSLGGYVGIEH 83
Cdd:PRK10349   16 LVLLHGWGLNAEVWRCIDEELS-SHFTLHLVDLPGFGRSRGfGALSLADMAEAVLQQAPD---KAIWLGWSLGGLVASQI 91

                          90       100
                  ....*....|....*....|....*...
gi 1994618587  84 RARFPEQVAGLVAASccTVPASRLRGAW 111
Cdd:PRK10349   92 ALTHPERVQALVTVA--SSPCFSARDEW 117
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 1-141 5.79e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 40.36  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994618587   1 MGLPVLFVHGSRTSRTMWRAQLEAMDRAGlAAAAVDLPGHGA--RTGEAFTLDGAVATVAGAVDDLGGRALV-VGLSLGG 77
Cdd:PRK03592   26 EGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGAsdKPDIDYTFADHARYLDAWFDALGLDDVVlVGHDWGS 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1994618587  78 YVGIEHRARFPEQVAGLVAASCCTVPASrlrgaWrvaadriEKLPDNGAALNQALvnRTlPGAG 141
Cdd:PRK03592  105 ALGFDWAARHPDRVRGIAFMEAIVRPMT-----W-------DDFPPAVRELFQAL--RS-PGEG 153
 
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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