NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|491230468|ref|WP_005088713|]
View 

alpha/beta fold hydrolase [Mycobacteroides abscessus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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, ...
 8-286 1.96e-33

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: 122.03  E-value: 1.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468   8 HRRSVDIERGRISYLDIGAGSPT-VFVHGVLTNSLLWRDVVTAVAAtGRRCIALDLPGHGHSPVPADDidVTLSGLAQLI 86
Cdd:COG0596    3 TPRFVTVDGVRLHYREAGPDGPPvVLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGG--YTLDDLADDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  87 AEFLDSIGIDEFDLVANDTGGAVAQIMVARQPDRIRTLALTNcdteghvppklfkpvvalarpplmaligprlfarrkVL 166
Cdd:COG0596   80 AALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------EV 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468 167 RALLGAGYRKPGRLPDSIVEsygqpvfgtaessrflskMLRAMHTRDLeaaRAGLVTFTKPTLIAWGLGDYFFPLRYGQR 246
Cdd:COG0596  124 LAALAEPLRRPGLAPEALAA------------------LLRALARTDL---RERLARITVPTLVIWGEKDPIVPPALARR 182

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 491230468 247 LAELFGGpVTVETVPDGRLYFPDEDADRLLPLLYRHWHSA 286
Cdd:COG0596  183 LAELLPN-AELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 8-286 1.96e-33

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: 122.03  E-value: 1.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468   8 HRRSVDIERGRISYLDIGAGSPT-VFVHGVLTNSLLWRDVVTAVAAtGRRCIALDLPGHGHSPVPADDidVTLSGLAQLI 86
Cdd:COG0596    3 TPRFVTVDGVRLHYREAGPDGPPvVLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGG--YTLDDLADDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  87 AEFLDSIGIDEFDLVANDTGGAVAQIMVARQPDRIRTLALTNcdteghvppklfkpvvalarpplmaligprlfarrkVL 166
Cdd:COG0596   80 AALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------EV 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468 167 RALLGAGYRKPGRLPDSIVEsygqpvfgtaessrflskMLRAMHTRDLeaaRAGLVTFTKPTLIAWGLGDYFFPLRYGQR 246
Cdd:COG0596  124 LAALAEPLRRPGLAPEALAA------------------LLRALARTDL---RERLARITVPTLVIWGEKDPIVPPALARR 182

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 491230468 247 LAELFGGpVTVETVPDGRLYFPDEDADRLLPLLYRHWHSA 286
Cdd:COG0596  183 LAELLPN-AELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 31-271 4.39e-24

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: 97.96  E-value: 4.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468   31 VFVHGVLTNSLLWRDVVTAVAATGRRCIALDLPGHGHSPVPADDIDVTLSGLAQLIAEFLDSIGIDEFDLVANDTGGAVA 110
Cdd:pfam00561   4 LLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLIA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  111 QIMVARQPDRIRTLALTNCDTEGHV-----------PPKLFKPVVALARPPLMALIGPRLFARrkvLRALLGAGYRKPGR 179
Cdd:pfam00561  84 LAYAAKYPDRVKALVLLGALDPPHEldeadrfilalFPGFFDGFVADFAPNPLGRLVAKLLAL---LLLRLRLLKALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  180 LPDSIVESYGQPVFGTAESSRFLSkmlramhTRDLEAARAGLVTFTKPTLIAWGLGDYFFPLRYGQRLAELFGGPVTVET 259
Cdd:pfam00561 161 NKRFPSGDYALAKSLVTGALLFIE-------TWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI 233

                         250
                  ....*....|..
gi 491230468  260 VPDGRLYFPDED 271
Cdd:pfam00561 234 PDAGHFAFLEGP 245
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 9-137 3.23e-21

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 91.21  E-value: 3.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468   9 RRSVDIERGRISYLDIGAGSPTVFVHGVLTNSLLWRDVVTAVAATGrRCIALDLPGHGHSPVPadDIDVTLSGLAQLIAE 88
Cdd:PRK03592   9 MRRVEVLGSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKP--DIDYTFADHARYLDA 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 491230468  89 FLDSIGIDEFDLVANDTGGAVAQIMVARQPDRIRTLALtncdTEGHVPP 137
Cdd:PRK03592  86 WFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAF----MEAIVRP 130
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 26-129 1.73e-10

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: 59.92  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468   26 AGSPTVFVHGVLTNSLLWRDVVTAVAAtGRRCIALDLPGHGHSPVPAD----DIDVTLSglaQLIAEFLDSIGIDEFDLV 101
Cdd:TIGR03695   1 AKPVLVFLHGFLGSGADWQALIEALGP-HFRCLAIDLPGHGSSQSPSDieryDFEEAAQ---LLLATLLDQLGIEPFFLV 76

                          90       100
                  ....*....|....*....|....*...
gi 491230468  102 ANDTGGAVAQIMVARQPDRIRTLALTNC 129
Cdd:TIGR03695  77 GYSMGGRIALYYALQYPERVQGLILESG 104
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 8-286 1.96e-33

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: 122.03  E-value: 1.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468   8 HRRSVDIERGRISYLDIGAGSPT-VFVHGVLTNSLLWRDVVTAVAAtGRRCIALDLPGHGHSPVPADDidVTLSGLAQLI 86
Cdd:COG0596    3 TPRFVTVDGVRLHYREAGPDGPPvVLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGG--YTLDDLADDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  87 AEFLDSIGIDEFDLVANDTGGAVAQIMVARQPDRIRTLALTNcdteghvppklfkpvvalarpplmaligprlfarrkVL 166
Cdd:COG0596   80 AALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------EV 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468 167 RALLGAGYRKPGRLPDSIVEsygqpvfgtaessrflskMLRAMHTRDLeaaRAGLVTFTKPTLIAWGLGDYFFPLRYGQR 246
Cdd:COG0596  124 LAALAEPLRRPGLAPEALAA------------------LLRALARTDL---RERLARITVPTLVIWGEKDPIVPPALARR 182

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 491230468 247 LAELFGGpVTVETVPDGRLYFPDEDADRLLPLLYRHWHSA 286
Cdd:COG0596  183 LAELLPN-AELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 31-271 4.39e-24

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: 97.96  E-value: 4.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468   31 VFVHGVLTNSLLWRDVVTAVAATGRRCIALDLPGHGHSPVPADDIDVTLSGLAQLIAEFLDSIGIDEFDLVANDTGGAVA 110
Cdd:pfam00561   4 LLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLIA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  111 QIMVARQPDRIRTLALTNCDTEGHV-----------PPKLFKPVVALARPPLMALIGPRLFARrkvLRALLGAGYRKPGR 179
Cdd:pfam00561  84 LAYAAKYPDRVKALVLLGALDPPHEldeadrfilalFPGFFDGFVADFAPNPLGRLVAKLLAL---LLLRLRLLKALPLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  180 LPDSIVESYGQPVFGTAESSRFLSkmlramhTRDLEAARAGLVTFTKPTLIAWGLGDYFFPLRYGQRLAELFGGPVTVET 259
Cdd:pfam00561 161 NKRFPSGDYALAKSLVTGALLFIE-------TWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVI 233

                         250
                  ....*....|..
gi 491230468  260 VPDGRLYFPDED 271
Cdd:pfam00561 234 PDAGHFAFLEGP 245
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 9-137 3.23e-21

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 91.21  E-value: 3.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468   9 RRSVDIERGRISYLDIGAGSPTVFVHGVLTNSLLWRDVVTAVAATGrRCIALDLPGHGHSPVPadDIDVTLSGLAQLIAE 88
Cdd:PRK03592   9 MRRVEVLGSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKP--DIDYTFADHARYLDA 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 491230468  89 FLDSIGIDEFDLVANDTGGAVAQIMVARQPDRIRTLALtncdTEGHVPP 137
Cdd:PRK03592  86 WFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAF----MEAIVRP 130
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 10-126 5.85e-20

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 88.46  E-value: 5.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  10 RSVDIERGRISYLDIGAGSPT--VFVHGV---LTNsllWRDVVTAVAAtGRRCIALDLPGHGHSP--VPADDIDvtlsGL 82
Cdd:PRK14875 112 RKARIGGRTVRYLRLGEGDGTpvVLIHGFggdLNN---WLFNHAALAA-GRPVIALDLPGHGASSkaVGAGSLD----EL 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 491230468  83 AQLIAEFLDSIGIDEFDLVANDTGGAVAQIMVARQPDRIRTLAL 126
Cdd:PRK14875 184 AAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTL 227
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 10-272 1.15e-19

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 86.83  E-value: 1.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  10 RSVDIERGRISYLDIGAGSPTVFVHGVLTNSLLWRDVVTAVAATgRRCIALDLPGHGHSPVPaDDIDVTLSGLAQLIAEF 89
Cdd:PRK03204  17 RWFDSSRGRIHYIDEGTGPPILLCHGNPTWSFLYRDIIVALRDR-FRCVAPDYLGFGLSERP-SGFGYQIDEHARVIGEF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  90 LDSIGIDEFDLVANDTGGAVAQIMVARQPDRIRTLALTNcdteghvppKLFKPVVALARPPLMALIGPRLFARRKVLR-- 167
Cdd:PRK03204  95 VDHLGLDRYLSMGQDWGGPISMAVAVERADRVRGVVLGN---------TWFWPADTLAMKAFSRVMSSPPVQYAILRRnf 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468 168 ---ALLGAGYRkpGRLPDSIVESYgQPVFGTAESSRFLSKMLRAMH-TRDLEAARAGLVTF---TKPTLIAWGLGDYFF- 239
Cdd:PRK03204 166 fveRLIPAGTE--HRPSSAVMAHY-RAVQPNAAARRGVAEMPKQILaARPLLARLAREVPAtlgTKPTLLVWGMKDVAFr 242

                        250       260       270
                 ....*....|....*....|....*....|...
gi 491230468 240 PLRYGQRLAELFGGPVTVEtVPDGRlYFPDEDA 272
Cdd:PRK03204 243 PKTILPRLRATFPDHVLVE-LPNAK-HFIQEDA 273
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 18-148 1.02e-11

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 64.22  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  18 RISYLDIG--AGSPTVFVHGVLTNSLLWRDVVTAVAATGRRCIALDLPGHGHSPVPADDIDVTLSGLAQLIAEFLDSIGI 95
Cdd:PRK00870  35 RMHYVDEGpaDGPPVLLLHGEPSWSYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPTRREDYTYARHVEWMRSWFEQLDL 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491230468  96 DEFDLVANDTGGAVAQIMVARQPDRIRTLALTNC--DTEGHVPPKLFKPVVALAR 148
Cdd:PRK00870 115 TDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANTglPTGDGPMPDAFWAWRAFSQ 169
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 26-129 1.73e-10

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: 59.92  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468   26 AGSPTVFVHGVLTNSLLWRDVVTAVAAtGRRCIALDLPGHGHSPVPAD----DIDVTLSglaQLIAEFLDSIGIDEFDLV 101
Cdd:TIGR03695   1 AKPVLVFLHGFLGSGADWQALIEALGP-HFRCLAIDLPGHGSSQSPSDieryDFEEAAQ---LLLATLLDQLGIEPFFLV 76

                          90       100
                  ....*....|....*....|....*...
gi 491230468  102 ANDTGGAVAQIMVARQPDRIRTLALTNC 129
Cdd:TIGR03695  77 GYSMGGRIALYYALQYPERVQGLILESG 104
bchO_mg_che_rel TIGR03056
putative magnesium chelatase accessory protein; Members of this family belong to the alpha ...
 26-279 5.64e-10

putative magnesium chelatase accessory protein; Members of this family belong to the alpha/beta fold family hydrolases (pfam00561). Members are found in bacterial genomes if and only if they encoded for anoxygenic photosynthetic systems similar to that of Rhodobacter capsulatus and other alpha-Proteobacteria. Members often are encoded in the same operon as subunits of the protoporphyrin IX magnesium chelatase, and were once designated BchO. No literature supports a role as an actual subunit of magnesium chelatase, but an accessory role is possible, as suggested by placement by its probable hydrolase activity. [Energy metabolism, Photosynthesis]


Pssm-ID: 132100  Cd Length: 278  Bit Score: 58.75  E-value: 5.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468   26 AGSPTVFVHGVLTNSLLWRDVVTAVAATgRRCIALDLPGHGHSPVPADDiDVTLSGLAQLIAEFLDSIGIDEFDLVANDT 105
Cdd:TIGR03056  27 AGPLLLLLHGTGASTHSWRDLMPPLARS-FRVVAPDLPGHGFTRAPFRF-RFTLPSMAEDLSALCAAEGLSPDGVIGHSA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  106 GGAVAQIMVARQPDRIRTLALTNC------DTEGHVPPKLFKpvvALARPPLMALIGPRLFARRKVLRALLGAgyrkPGR 179
Cdd:TIGR03056 105 GAAIALRLALDGPVTPRMVVGINAalmpfeGMAGTLFPYMAR---VLACNPFTPPMMSRGAADQQRVERLIRD----TGS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  180 LPDSIVESYGQPVFGTAESsrfLSKMLRAMHTRDLEAARAGLVTFTKPTLIAWGLGDYFFPLRYGQRLAElFGGPVTVET 259
Cdd:TIGR03056 178 LLDKAGMTYYGRLIRSPAH---VDGALSMMAQWDLAPLNRDLPRITIPLHLIAGEEDKAVPPDESKRAAT-RVPTATLHV 253

                         250       260
                  ....*....|....*....|
gi 491230468  260 VPDGRLYFPDEDADRLLPLL 279
Cdd:TIGR03056 254 VPGGGHLVHEEQADGVVGLI 273
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
31-128 1.85e-09

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 56.55  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  31 VFVHGVLTNSLLWRDVVTAVAATGRRCIALDLPGHGHSPVPADDIDvTLSGLAQLIAEFLDSIGIDEFD---LVANDTGG 107
Cdd:COG2267   32 VLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVD-SFDDYVDDLRAALDALRARPGLpvvLLGHSMGG 110

                         90       100
                 ....*....|....*....|.
gi 491230468 108 AVAQIMVARQPDRIRTLALTN 128
Cdd:COG2267  111 LIALLYAARYPDRVAGLVLLA 131
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 25-250 9.14e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 52.43  E-value: 9.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  25 GAGSPTVFVHGVLTNSLLWRDVVTAVAATGrRCIALDLPGHGHSPVP-----ADDIDVTLSGLAQLIAEFLDSIGIDEFD 99
Cdd:PLN02824  27 TSGPALVLVHGFGGNADHWRKNTPVLAKSH-RVYAIDLLGYGYSDKPnprsaPPNSFYTFETWGEQLNDFCSDVVGDPAF 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468 100 LVANDTGGAVAQIMVARQPDRIRTLALTNCDTEG-HVP--PKLFKPVVALARPPLMALIGPRLF----ARRKVLRALLGA 172
Cdd:PLN02824 106 VICNSVGGVVGLQAAVDAPELVRGVMLINISLRGlHIKkqPWLGRPFIKAFQNLLRETAVGKAFfksvATPETVKNILCQ 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468 173 GYRKPGRLPDSIVESYGQPVFGTAESSRFLskmlramhtrDLEAARAG------LVTFTKPTLIAWGLGDYFFPLRYGQR 246
Cdd:PLN02824 186 CYHDDSAVTDELVEAILRPGLEPGAVDVFL----------DFISYSGGplpeelLPAVKCPVLIAWGEKDPWEPVELGRA 255


                 ....
gi 491230468 247 LAEL 250
Cdd:PLN02824 256 YANF 259
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 29-124 9.68e-08

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 49.44  E-value: 9.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  29 PTVFVHGVLTNSLLWRDVVTAVAATGRRCIALDLPGHGHSpvpaddIDVTLSGLAQLIAEFLDSIGIDEFDLVANDTGGA 108
Cdd:COG1075    7 PVVLVHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGS------IEDSAEQLAAFVDAVLAATGAEKVDLVGHSMGGL 80

                         90
                 ....*....|....*...
gi 491230468 109 VAQIMVARQ--PDRIRTL 124
Cdd:COG1075   81 VARYYLKRLggAAKVARV 98
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 23-126 1.34e-07

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 52.50  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  23 DIGAGSPTVFVHGVLTNSLLWRDVV----TAVAATGRRCIALDLPGHGHSPVPADDIdVTLSGLAQLIAE-FLDSIGIDE 97
Cdd:PLN03087 197 DNKAKEDVLFIHGFISSSAFWTETLfpnfSDAAKSTYRLFAVDLLGFGRSPKPADSL-YTLREHLEMIERsVLERYKVKS 275

                         90       100
                 ....*....|....*....|....*....
gi 491230468  98 FDLVANDTGGAVAQIMVARQPDRIRTLAL 126
Cdd:PLN03087 276 FHIVAHSLGCILALALAVKHPGAVKSLTL 304
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 27-110 2.46e-07

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 50.61  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  27 GSPT-VFVHGVLTNSLLWRDVVTAvaATGRRCIALDLPGHGHSPvpaddiDVTLSGLA---QLIAEFLDSIGIDEFDLVA 102
Cdd:PRK11126   1 GLPWlVFLHGLLGSGQDWQPVGEA--LPDYPRLYIDLPGHGGSA------AISVDGFAdvsRLLSQTLQSYNILPYWLVG 72


                 ....*...
gi 491230468 103 NDTGGAVA 110
Cdd:PRK11126  73 YSLGGRIA 80
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 31-127 1.12e-06

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: 48.66  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468   31 VFVHGVLTNSLLWRDVVTAVAATgRRCIALDLPGHGHSPV--PADdidvtLSGLAQLIAEFLDsigiDEFDLVANDTGGA 108
Cdd:TIGR01738   8 VLIHGWGMNAEVFRCLDEELSAH-FTLHLVDLPGHGRSRGfgPLS-----LADMAEAIAAQAP----DPAIWLGWSLGGL 77

                          90
                  ....*....|....*....
gi 491230468  109 VAQIMVARQPDRIRTLALT 127
Cdd:TIGR01738  78 VALHIAATHPDRVRALVTV 96
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 23-122 1.55e-06

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 49.47  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468   23 DIGA---GSPTVFVHGVLTNSLLWRDVVTAVAATGRrCIALDLPGHGHSPVPA----DDIDVTLSglAQLIAEFL----D 91
Cdd:PLN02980 1364 EVGQnaeGSVVLFLHGFLGTGEDWIPIMKAISGSAR-CISIDLPGHGGSKIQNhakeTQTEPTLS--VELVADLLykliE 1440

                          90       100       110
                  ....*....|....*....|....*....|.
gi 491230468   92 SIGIDEFDLVANDTGGAVAQIMVARQPDRIR 122
Cdd:PLN02980 1441 HITPGKVTLVGYSMGARIALYMALRFSDKIE 1471
PLN02578 PLN02578
hydrolase
 18-236 8.29e-06

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 46.76  E-value: 8.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  18 RISYLDIGAGSPTVFVHGVLTNSLLWRDVVTAVAATgRRCIALDLPGHGHSPVPADDIDVTLsgLAQLIAEFLDSIGIDE 97
Cdd:PLN02578  77 KIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKK-YKVYALDLLGFGWSDKALIEYDAMV--WRDQVADFVKEVVKEP 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  98 FDLVANDTGGAVAQIMVARQPDRIRTLALTNC-----DTEGHVPPKLFKPVVALARPPLMALigpRLFARRKVL------ 166
Cdd:PLN02578 154 AVLVGNSLGGFTALSTAVGYPELVAGVALLNSagqfgSESREKEEAIVVEETVLTRFVVKPL---KEWFQRVVLgflfwq 230

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491230468 167 -------RALLGAGYRKPGRLPDSIVESYGQPVFGTAESSRFLSKMLRAMHTRDLEAARAGLVTFTKPTLIAWGLGD 236
Cdd:PLN02578 231 akqpsriESVLKSVYKDKSNVDDYLVESITEPAADPNAGEVYYRLMSRFLFNQSRYTLDSLLSKLSCPLLLLWGDLD 307
PRK10673 PRK10673
esterase;
28-124 1.10e-05

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 45.88  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  28 SPTVFVHGVLTN----SLLWRDVVTAvaatgRRCIALDLPGHGHSPvpaDDIDVTLSGLAQLIAEFLDSIGIDEFDLVAN 103
Cdd:PRK10673  17 SPIVLVHGLFGSldnlGVLARDLVND-----HDIIQVDMRNHGLSP---RDPVMNYPAMAQDLLDTLDALQIEKATFIGH 88

                         90       100
                 ....*....|....*....|.
gi 491230468 104 DTGGAVAQIMVARQPDRIRTL 124
Cdd:PRK10673  89 SMGGKAVMALTALAPDRIDKL 109
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 31-171 2.79e-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: 44.39  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468   31 VFVHGvltnSLLWRDVVTAVAATGRRCIALDLPGHGHSPVPADDIDvTLSGLAQLIAEFldsIGIDEFDLVANDTGGAVA 110
Cdd:pfam12697   2 VLVHG----AGLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLA-DLADLAALLDEL---GAARPVVLVGHSLGGAVA 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491230468  111 QIMVARQPDRIRTLALTNcdteghVPPKLFKPVVALARPPLMALIGPRLFARRKVLRALLG 171
Cdd:pfam12697  74 LAAAAAALVVGVLVAPLA------APPGLLAALLALLARLGAALAAPAWLAAESLARGFLD 128
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 18-129 3.84e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 41.36  E-value: 3.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  18 RISYLDIGAGS------PTVFVHGVLTNSLLWRDVVtAVAATGRRCIALDLPGHGHSPVPADdIDVTLSGLAQLIAEFLD 91
Cdd:PLN02679  73 SINYLVKGSPEvtssgpPVLLVHGFGASIPHWRRNI-GVLAKNYTVYAIDLLGFGASDKPPG-FSYTMETWAELILDFLE 150

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 491230468  92 SIGIDEFDLVANDTGGAVAQIMVAR-QPDRIRTLALTNC 129
Cdd:PLN02679 151 EVVQKPTVLIGNSVGSLACVIAASEsTRDLVRGLVLLNC 189
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 31-236 1.05e-03

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 39.89  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468   31 VFVHGVLTNSLLWRDVVTAVAATGRRCIALDLPGHGHSP-----VPADDIDVT-LSGLAQLIAEflDSIGIDEFdLVAND 104
Cdd:pfam12146   8 VLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDgkrghVPSFDDYVDdLDTFVDKIRE--EHPGLPLF-LLGHS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  105 TGGAVAQIMVARQPDRIRTLALTN--CDteghVPPKLFKPVVALARpPLMALIGPRLFARRKVLRALLgagYRKPgrlpd 182
Cdd:pfam12146  85 MGGLIAALYALRYPDKVDGLILSApaLK----IKPYLAPPILKLLA-KLLGKLFPRLRVPNNLLPDSL---SRDP----- 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 491230468  183 SIVESYGQ-PVFGTAESSRFLSKMLRAMhtRDLEaARAGLVTFtkPTLIAWGLGD 236
Cdd:pfam12146 152 EVVAAYAAdPLVHGGISARTLYELLDAG--ERLL-RRAAAITV--PLLLLHGGAD 201
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 29-236 3.26e-03

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 38.71  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468  29 PTVFVHGVLTNSLLWRDVVTaVAATGRRCIALDLPGHGHS--PVPADDIDVTLSGLAQLIAEFLDSIGIDEFDLVANDTG 106
Cdd:PLN03084 129 PVLLIHGFPSQAYSYRKVLP-VLSKNYHAIAFDWLGFGFSdkPQPGYGFNYTLDEYVSSLESLIDELKSDKVSLVVQGYF 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491230468 107 GAVAQIMVARQPDRIRTLALTNcdteghvpPKLFKPVVALarPPLMA-----LIGpRLFAR---RKVLRALLGAGYRKPg 178
Cdd:PLN03084 208 SPPVVKYASAHPDKIKKLILLN--------PPLTKEHAKL--PSTLSefsnfLLG-EIFSQdplRASDKALTSCGPYAM- 275

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491230468 179 RLPDSIVesYGQPVFGTAESSRFLSKMLRAMhTRDL----EAARAGLV--TFTKPTLIAWGLGD 236
Cdd:PLN03084 276 KEDDAMV--YRRPYLTSGSSGFALNAISRSM-KKELkkyiEEMRSILTdkNWKTPITVCWGLRD 336
 
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