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Conserved domains on  [gi|1039794594|ref|XP_017169172|]
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putative protein-lysine deacylase ABHD14B isoform X1 [Mus musculus]

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, ...
 7-209 1.31e-25

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: 98.92  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594   7 HEGTIKVQGQNLFFRETRPgSGQPVrfsvLLLHGIRFSSETWQNLgtLQRLAEaGYRAVAIDLPGLGRSKEAAAPAPIGE 86
Cdd:COG0596     3 TPRFVTVDGVRLHYREAGP-DGPPV----VLLHGLPGSSYEWRPL--IPALAA-GYRVIAPDLRGHGRSDKPAGGYTLDD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  87 PApgSFLAAVVDTLELGPPVVISPSLSGMYSLPF------------------------LVAPGSQLRGFVPVAPICTDKI 142
Cdd:COG0596    75 LA--DDLAALLDALGLERVVLVGHSMGGMVALELaarhpervaglvlvdevlaalaepLRRPGLAPEALAALLRALARTD 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039794594 143 NAVDYASVKTPALIVYGDQDPMGSSSFQH--LKQLPNHRVLVMEGAGHPCYLDKPDEWHKGLLDFLQGL 209
Cdd:COG0596   153 LRERLARITVPTLVIWGEKDPIVPPALARrlAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 7-209 1.31e-25

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: 98.92  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594   7 HEGTIKVQGQNLFFRETRPgSGQPVrfsvLLLHGIRFSSETWQNLgtLQRLAEaGYRAVAIDLPGLGRSKEAAAPAPIGE 86
Cdd:COG0596     3 TPRFVTVDGVRLHYREAGP-DGPPV----VLLHGLPGSSYEWRPL--IPALAA-GYRVIAPDLRGHGRSDKPAGGYTLDD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  87 PApgSFLAAVVDTLELGPPVVISPSLSGMYSLPF------------------------LVAPGSQLRGFVPVAPICTDKI 142
Cdd:COG0596    75 LA--DDLAALLDALGLERVVLVGHSMGGMVALELaarhpervaglvlvdevlaalaepLRRPGLAPEALAALLRALARTD 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039794594 143 NAVDYASVKTPALIVYGDQDPMGSSSFQH--LKQLPNHRVLVMEGAGHPCYLDKPDEWHKGLLDFLQGL 209
Cdd:COG0596   153 LRERLARITVPTLVIWGEKDPIVPPALARrlAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 10-208 5.43e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 49.17  E-value: 5.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  10 TIKVQGQNLFFRETRPGSGQPVrfsvLLLHGirFSSE--TWqnLGTLQRLAeAGYRAVAIDLPGLGRSKEAAAPAPIGEP 87
Cdd:PRK14875  113 KARIGGRTVRYLRLGEGDGTPV----VLIHG--FGGDlnNW--LFNHAALA-AGRPVIALDLPGHGASSKAVGAGSLDEL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  88 ApgSFLAAVVDTLELGPPVVISPSLSGMYSLPF------------LVAP---GSQ-----LRGFV---------PV---- 134
Cdd:PRK14875  184 A--AAVLAFLDALGIERAHLVGHSMGGAVALRLaarapqrvasltLIAPaglGPEingdyIDGFVaaesrrelkPVlell 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594 135 --------------------------------APICTDKINAVDY----ASVKTPALIVYGDQD---PmgsssFQHLKQL 175
Cdd:PRK14875  262 fadpalvtrqmvedllkykrldgvddalralaDALFAGGRQRVDLrdrlASLAIPVLVIWGEQDriiP-----AAHAQGL 336

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039794594 176 PNH-RVLVMEGAGHPCYLDKPDEWHKGLLDFLQG 208
Cdd:PRK14875  337 PDGvAVHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 35-197 6.74e-05

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 42.46  E-value: 6.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  35 VLLLHGirfsseTWQNLGTLQRLAEAGYRAVAIDLPGLGRSkeaaAPAPIGEPAPGSFLAAVVDTLELGPPVVISPSLSG 114
Cdd:pfam12697   1 VVLVHG------AGLSAAPLAALLAAGVAVLAPDLPGHGSS----SPPPLDLADLADLAALLDELGAARPVVLVGHSLGG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594 115 MYSLPF---------LVAPGSQLRGFVPVAPICTDKINAV---------------------------------------- 145
Cdd:pfam12697  71 AVALAAaaaalvvgvLVAPLAAPPGLLAALLALLARLGAAlaapawlaaeslargflddlpadaewaaalarlaallaal 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039794594 146 ------DYASVKTPALIVYGDQDPMGSSSFQHLKQLPNHRVLVMEGAGHpCYLDKPDE 197
Cdd:pfam12697 151 allplaAWRDLPVPVLVLAEEDRLVPELAQRLLAALAGARLVVLPGAGH-LPLDDPEE 207
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 35-100 8.07e-05

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: 42.20  E-value: 8.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039794594  35 VLLLHGIRFSSETWQNlgtLQRLAEAGYRAVAIDLPGLGRSKEaaapapIGEPAPGSFLAAVVDTL 100
Cdd:TIGR03695   5 LVFLHGFLGSGADWQA---LIEALGPHFRCLAIDLPGHGSSQS------PSDIERYDFEEAAQLLL 61
Esterase_713_like cd12806
Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family ...
 32-160 1.74e-04

Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown. This enzyme is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized.


Pssm-ID: 214005  Cd Length: 261  Bit Score: 41.36  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  32 RFSVLLLHGIRFSSETWQN-----LGTLQRLAEAGYRAVAIDLPGLGRS-------KEAAAPAPI-GEPAPGSF------ 92
Cdd:cd12806    48 RYPLLLIHGCGLTGMTWETtpdgrMGWDNYFLRKGYSVYVVDQPGRGRSgwdtqfpVQGQAELWQqMVPDWLGAmptpnp 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039794594  93 ----LAAVVDTleLGPPVVISPSLSGMYSLPFLVAPGSQLRGFVPVAPICTDKINAVDYASvKTPALIVYGD 160
Cdd:cd12806   128 tvaaLSKLADK--LDPTVLLTHSQSGIFGFQTAAMRPKGIKAIVAVEPGGCPKPEDVKPLT-SIPVLVVYGD 196
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 7-209 1.31e-25

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: 98.92  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594   7 HEGTIKVQGQNLFFRETRPgSGQPVrfsvLLLHGIRFSSETWQNLgtLQRLAEaGYRAVAIDLPGLGRSKEAAAPAPIGE 86
Cdd:COG0596     3 TPRFVTVDGVRLHYREAGP-DGPPV----VLLHGLPGSSYEWRPL--IPALAA-GYRVIAPDLRGHGRSDKPAGGYTLDD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  87 PApgSFLAAVVDTLELGPPVVISPSLSGMYSLPF------------------------LVAPGSQLRGFVPVAPICTDKI 142
Cdd:COG0596    75 LA--DDLAALLDALGLERVVLVGHSMGGMVALELaarhpervaglvlvdevlaalaepLRRPGLAPEALAALLRALARTD 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039794594 143 NAVDYASVKTPALIVYGDQDPMGSSSFQH--LKQLPNHRVLVMEGAGHPCYLDKPDEWHKGLLDFLQGL 209
Cdd:COG0596   153 LRERLARITVPTLVIWGEKDPIVPPALARrlAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
15-207 1.06e-16

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 75.42  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  15 GQNLFFRETRPGsgQPVRFSVLLLHGIRFSSETWQNLGtlQRLAEAGYRAVAIDLPGLGRSkEAAAPAPIGEPAPGSFLA 94
Cdd:COG2267    13 GLRLRGRRWRPA--GSPRGTVVLVHGLGEHSGRYAELA--EALAAAGYAVLAFDLRGHGRS-DGPRGHVDSFDDYVDDLR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  95 AVVDTLEL---GPPVVISPSLSGMYSLPFLVAPGSQLRGFVPVAP-ICTDKINAV------------DYASVKTPALIVY 158
Cdd:COG2267    88 AALDALRArpgLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPaYRADPLLGPsarwlralrlaeALARIDVPVLVLH 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039794594 159 GDQDPMGSSS-----FQHLkqLPNHRVLVMEGAGHPCYLDKP-DEWHKGLLDFLQ 207
Cdd:COG2267   168 GGADRVVPPEaarrlAARL--SPDVELVLLPGARHELLNEPArEEVLAAILAWLE 220
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
35-188 1.99e-10

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 58.05  E-value: 1.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  35 VLLLHGIRFSSEtwQNLGTLQRLAEAGYRAVAIDL--PGLGRSKEAAAPAPIGEPAPGSFLA---AVVDTLELGPPVVIS 109
Cdd:COG0412    32 VVVLHEIFGLNP--HIRDVARRLAAAGYVVLAPDLygRGGPGDDPDEARALMGALDPELLAAdlrAALDWLKAQPEVDAG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594 110 P------SLSGMYSLpFLVAPGSQLRGFVPVAPICTDKINAVDYASVKTPALIVYGDQDPMGSSS-----FQHLKQL-PN 177
Cdd:COG0412   110 RvgvvgfCFGGGLAL-LAAARGPDLAAAVSFYGGLPADDLLDLAARIKAPVLLLYGEKDPLVPPEqvaalEAALAAAgVD 188

                         170
                  ....*....|.
gi 1039794594 178 HRVLVMEGAGH 188
Cdd:COG0412   189 VELHVYPGAGH 199
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 25-207 3.26e-08

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 52.22  E-value: 3.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  25 PGSGQPVRFSVLLLHGIRFSSETWQNLGtlQRLAEAGYRAVAIDLPGLGRSkeAAAPAPIGEPAPGSFLAAV--VDTLEL 102
Cdd:COG1073    30 PAGASKKYPAVVVAHGNGGVKEQRALYA--QRLAELGFNVLAFDYRGYGES--EGEPREEGSPERRDARAAVdyLRTLPG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594 103 GPP---VVISPSLSGMYSL----------------PF----------------LVAPGSQLRGFVPVAPICTDKINAVDY 147
Cdd:COG1073   106 VDPeriGLLGISLGGGYALnaaatdprvkavildsPFtsledlaaqrakeargAYLPGVPYLPNVRLASLLNDEFDPLAK 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039794594 148 AS-VKTPALIVYGDQDPMGssSFQHLKQL-----PNHRVLVMEGAGH-PCYLDKPDEWHKGLLDFLQ 207
Cdd:COG1073   186 IEkISRPLLFIHGEKDEAV--PFYMSEDLyeaaaEPKELLIVPGAGHvDLYDRPEEEYFDKLAEFFK 250
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
32-210 3.40e-07

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 49.17  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  32 RFSVLLLHGIRFSSETWQNLGtlQRLAEAGYRAVAIDLPGLGRSKEAAAPAPIGEpapgsFLAAVVDTLELG-----PPV 106
Cdd:COG1647    15 RKGVLLLHGFTGSPAEMRPLA--EALAKAGYTVYAPRLPGHGTSPEDLLKTTWED-----WLEDVEEAYEILkagydKVI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594 107 VISPSLSGMYSL------P-----FLVAPGSQLRG----FVPVAPICTDKINAV-------------------------- 145
Cdd:COG1647    88 VIGLSMGGLLALllaaryPdvaglVLLSPALKIDDpsapLLPLLKYLARSLRGIgsdiedpevaeyaydrtplralaelq 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039794594 146 --------DYASVKTPALIVYGDQDPMGSSS-----FQHLKQlPNHRVLVMEGAGHPCYLDK-PDEWHKGLLDFLQGLA 210
Cdd:COG1647   168 rlirevrrDLPKITAPTLIIQSRKDEVVPPEsaryiYERLGS-PDKELVWLEDSGHVITLDKdREEVAEEILDFLERLA 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 10-208 5.43e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 49.17  E-value: 5.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  10 TIKVQGQNLFFRETRPGSGQPVrfsvLLLHGirFSSE--TWqnLGTLQRLAeAGYRAVAIDLPGLGRSKEAAAPAPIGEP 87
Cdd:PRK14875  113 KARIGGRTVRYLRLGEGDGTPV----VLIHG--FGGDlnNW--LFNHAALA-AGRPVIALDLPGHGASSKAVGAGSLDEL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  88 ApgSFLAAVVDTLELGPPVVISPSLSGMYSLPF------------LVAP---GSQ-----LRGFV---------PV---- 134
Cdd:PRK14875  184 A--AAVLAFLDALGIERAHLVGHSMGGAVALRLaarapqrvasltLIAPaglGPEingdyIDGFVaaesrrelkPVlell 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594 135 --------------------------------APICTDKINAVDY----ASVKTPALIVYGDQD---PmgsssFQHLKQL 175
Cdd:PRK14875  262 fadpalvtrqmvedllkykrldgvddalralaDALFAGGRQRVDLrdrlASLAIPVLVIWGEQDriiP-----AAHAQGL 336

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039794594 176 PNH-RVLVMEGAGHPCYLDKPDEWHKGLLDFLQG 208
Cdd:PRK14875  337 PDGvAVHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 6-142 3.47e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 46.69  E-value: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594   6 QHEGTIKVQGQNLFFRETRPGSGQPVRFSVLLLHGI-RFSSETWQNLGTLqrLAEAGYRAVAIDLPGLGRSKEAAAPAPI 84
Cdd:PLN02298   33 SKSFFTSPRGLSLFTRSWLPSSSSPPRALIFMVHGYgNDISWTFQSTAIF--LAQMGFACFALDLEGHGRSEGLRAYVPN 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039794594  85 GEPAPG---SFLAAVVDTLELG--PPVVISPSLSGMYSLPFLVAPGSQLRGFVPVAPIC--TDKI 142
Cdd:PLN02298  111 VDLVVEdclSFFNSVKQREEFQglPRFLYGESMGGAICLLIHLANPEGFDGAVLVAPMCkiSDKI 175
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 35-197 6.74e-05

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 42.46  E-value: 6.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  35 VLLLHGirfsseTWQNLGTLQRLAEAGYRAVAIDLPGLGRSkeaaAPAPIGEPAPGSFLAAVVDTLELGPPVVISPSLSG 114
Cdd:pfam12697   1 VVLVHG------AGLSAAPLAALLAAGVAVLAPDLPGHGSS----SPPPLDLADLADLAALLDELGAARPVVLVGHSLGG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594 115 MYSLPF---------LVAPGSQLRGFVPVAPICTDKINAV---------------------------------------- 145
Cdd:pfam12697  71 AVALAAaaaalvvgvLVAPLAAPPGLLAALLALLARLGAAlaapawlaaeslargflddlpadaewaaalarlaallaal 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039794594 146 ------DYASVKTPALIVYGDQDPMGSSSFQHLKQLPNHRVLVMEGAGHpCYLDKPDE 197
Cdd:pfam12697 151 allplaAWRDLPVPVLVLAEEDRLVPELAQRLLAALAGARLVVLPGAGH-LPLDDPEE 207
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 25-75 6.97e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 42.65  E-value: 6.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039794594  25 PGSGQPVrfsvLLLHGirfsSETWQNL--GTLQRLAEAGYRAVAIDLPGLGRS 75
Cdd:PRK00870   43 PADGPPV----LLLHG----EPSWSYLyrKMIPILAAAGHRVIAPDLIGFGRS 87
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 35-100 8.07e-05

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: 42.20  E-value: 8.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039794594  35 VLLLHGIRFSSETWQNlgtLQRLAEAGYRAVAIDLPGLGRSKEaaapapIGEPAPGSFLAAVVDTL 100
Cdd:TIGR03695   5 LVFLHGFLGSGADWQA---LIEALGPHFRCLAIDLPGHGSSQS------PSDIERYDFEEAAQLLL 61
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
23-206 9.66e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 41.93  E-value: 9.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  23 TRPGSGQPVRFsVLLLHGIRFSSEtWQNLGTLQRLAEAGYRAVAIDLPGLGRSKEAAAPAPIGEpapgsfLAAVVDTLEL 102
Cdd:COG1506    15 YLPADGKKYPV-VVYVHGGPGSRD-DSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDD------VLAAIDYLAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594 103 GPPV------------------------------VIspSLSGMYSLPFLVAPGSQLRGFVPVAPICT----DKINAVDYA 148
Cdd:COG1506    87 RPYVdpdrigiyghsyggymallaaarhpdrfkaAV--ALAGVSDLRSYYGTTREYTERLMGGPWEDpeayAARSPLAYA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039794594 149 -SVKTPALIVYGDQD---PMGSSS--FQHLKQL-PNHRVLVMEGAGHPCYLDKPDEWHKGLLDFL 206
Cdd:COG1506   165 dKLKTPLLLIHGEADdrvPPEQAErlYEALKKAgKPVELLVYPGEGHGFSGAGAPDYLERILDFL 229
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 35-80 1.03e-04

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 40.20  E-value: 1.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1039794594  35 VLLLHGIRFSSETWQNLGtlQRLAEAGYRAVAIDLPGLGRSKEAAA 80
Cdd:COG1075     8 VVLVHGLGGSAASWAPLA--PRLRAAGYPVYALNYPSTNGSIEDSA 51
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 10-102 1.46e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 41.52  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  10 TIKVQGQNLFFRETrpGSGQPVRFsvllLHGIRFSSETWQNLgtLQRLAEAGyRAVAIDLPGLGRSkeaaapapiGEPAP 89
Cdd:PRK03592   11 RVEVLGSRMAYIET--GEGDPIVF----LHGNPTSSYLWRNI--IPHLAGLG-RCLAPDLIGMGAS---------DKPDI 72

                          90       100
                  ....*....|....*....|
gi 1039794594  90 G-------SFLAAVVDTLEL 102
Cdd:PRK03592   73 DytfadhaRYLDAWFDALGL 92
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 150-210 1.60e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 41.75  E-value: 1.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039794594 150 VKTPALIVYGDQD-------PMGSSSFQHLKQLPNHRVLVMEGAGHPCYLDKPDEWHKGLLDFLQGLA 210
Cdd:PLN02679  291 ISLPILVLWGDQDpftpldgPVGKYFSSLPSQLPNVTLYVLEGVGHCPHDDRPDLVHEKLLPWLAQLP 358
Esterase_713_like cd12806
Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family ...
 32-160 1.74e-04

Novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown. This enzyme is possibly exported from the cytosol to the periplasmic space. A large majority of sequences in this family have yet to be characterized.


Pssm-ID: 214005  Cd Length: 261  Bit Score: 41.36  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  32 RFSVLLLHGIRFSSETWQN-----LGTLQRLAEAGYRAVAIDLPGLGRS-------KEAAAPAPI-GEPAPGSF------ 92
Cdd:cd12806    48 RYPLLLIHGCGLTGMTWETtpdgrMGWDNYFLRKGYSVYVVDQPGRGRSgwdtqfpVQGQAELWQqMVPDWLGAmptpnp 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039794594  93 ----LAAVVDTleLGPPVVISPSLSGMYSLPFLVAPGSQLRGFVPVAPICTDKINAVDYASvKTPALIVYGD 160
Cdd:cd12806   128 tvaaLSKLADK--LDPTVLLTHSQSGIFGFQTAAMRPKGIKAIVAVEPGGCPKPEDVKPLT-SIPVLVVYGD 196
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 35-115 3.86e-04

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: 40.18  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794594  35 VLLLHGIRFSSETWQNLGTLqrLAEAGYRAVAIDLPGLGRSKEAAAPAPIGEPAPGSFLAAVVDTLELGPPVVISPSLSG 114
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPA--LARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80


                  .
gi 1039794594 115 M 115
Cdd:pfam00561  81 L 81
 
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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