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Conserved domains on  [gi|981680011|ref|WP_059876670|]
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alpha/beta fold hydrolase [Burkholderia ubonensis]

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, ...
 4-266 3.17e-48

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: 159.78  E-value: 3.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   4 LSFNDHDLYYADIG-SGLPIMLIHDLGSCGLAWARQVPFLRhAGYRVIVPDLPGHGASSYPSRTLAMGELAADLEGLLDH 82
Cdd:COG0596    7 VTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  83 LGLDSAALVGLSLGGAIALTVAIDAPSRVGKLVVCNGCSNLVAdDHMRRVAQWKAGFqrgdgpvrwfeemwpslvsaefa 162
Cdd:COG0596   86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALA-EPLRRPGLAPEAL----------------------- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011 163 qsergeiayqigharaaatdaahlARICDSIASYDVRRRLNLVRSETLVLHSEDDGVYPPVEGRRLAAMIPGAQFGSLPG 242
Cdd:COG0596  142 ------------------------AALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPG 197

                        250       260
                 ....*....|....*....|....
gi 981680011 243 SGHHPNLDRADTFNWTLLHFLSGH 266
Cdd:COG0596  198 AGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 4-266 3.17e-48

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: 159.78  E-value: 3.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   4 LSFNDHDLYYADIG-SGLPIMLIHDLGSCGLAWARQVPFLRhAGYRVIVPDLPGHGASSYPSRTLAMGELAADLEGLLDH 82
Cdd:COG0596    7 VTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  83 LGLDSAALVGLSLGGAIALTVAIDAPSRVGKLVVCNGCSNLVAdDHMRRVAQWKAGFqrgdgpvrwfeemwpslvsaefa 162
Cdd:COG0596   86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALA-EPLRRPGLAPEAL----------------------- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011 163 qsergeiayqigharaaatdaahlARICDSIASYDVRRRLNLVRSETLVLHSEDDGVYPPVEGRRLAAMIPGAQFGSLPG 242
Cdd:COG0596  142 ------------------------AALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPG 197

                        250       260
                 ....*....|....*....|....
gi 981680011 243 SGHHPNLDRADTFNWTLLHFLSGH 266
Cdd:COG0596  198 AGHFPPLEQPEAFAAALRDFLARL 221
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 21-264 1.21e-35

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 128.24  E-value: 1.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   21 PIMLIHDLGSCGLAWARQVPFLrHAGYRVIVPDLPGHGASSYPSRTLAMGELAADLEGLLDHLGLDSAALVGLSLGGAIA 100
Cdd:TIGR02427  15 VLVFINSLGTDLRMWDPVLPAL-TPDFRVLRYDKRGHGLSDAPEGPYSIEDLADDVLALLDHLGIERAVFCGLSLGGLIA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  101 LTVAIDAPSRVGKLVVCNGCSNL-VADDHMRRVAQWKA-GFQRGDGPV--RWFEEMWPSLVSAEF--------AQSERGE 168
Cdd:TIGR02427  94 QGLAARRPDRVRALVLSNTAAKIgTPESWNARIAAVRAeGLAALADAVleRWFTPGFREAHPARLdlyrnmlvRQPPDGY 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  169 IAyqigharaaatdaahlarICDSIASYDVRRRLNLVRSETLVLHSEDDGVYPPVEGRRLAAMIPGAQFGSLPGSGHHPN 248
Cdd:TIGR02427 174 AG------------------CCAAIRDADFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPC 235

                         250
                  ....*....|....*.
gi 981680011  249 LDRADTFNWTLLHFLS 264
Cdd:TIGR02427 236 VEQPEAFNAALRDFLR 251
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 21-252 2.45e-26

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: 103.35  E-value: 2.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   21 PIMLIHDLGSCGLAWARQVPFLRHAGYRVIVPDLPGHGASSYPSR--TLAMGELAADLEGLLDHLGLDSAALVGLSLGGA 98
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAqdDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   99 IALTVAIDAPSRVGKLVVCNGCSN-LVADDHMRRVAQWKAGFQRGD--GPVRWFEEMWPSLVSAE--------------F 161
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPpHELDEADRFILALFPGFFDGFvaDFAPNPLGRLVAKLLALlllrlrllkalpllN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  162 AQSERGEIAYQIGHARAAATDaahlariCDSIASYDVRRRLNLVRSETLVLHSEDDGVYPPVEGRRLAAMIPGAQFGSLP 241
Cdd:pfam00561 162 KRFPSGDYALAKSLVTGALLF-------IETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234

                         250
                  ....*....|.
gi 981680011  242 GSGHHPNLDRA 252
Cdd:pfam00561 235 DAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 9-266 1.52e-24

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 101.17  E-value: 1.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   9 HDLYYADIG--SGLPIMLIHDLGSCGLAWARQVPFLRhAGYRVIVPDLPGHGASSYPSRTLAMGELAADLEGLLDHLGLD 86
Cdd:PRK14875 119 RTVRYLRLGegDGTPVVLIHGFGGDLNNWLFNHAALA-AGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDALGIE 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  87 SAALVGLSLGGAIALTVAIDAPSRVGK--LVVCNGCSNLVADDHMRrvaqwkaGFQRGDG-----PV--RWFEEmwPSLV 157
Cdd:PRK14875 198 RAHLVGHSMGGAVALRLAARAPQRVASltLIAPAGLGPEINGDYID-------GFVAAESrrelkPVleLLFAD--PALV 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011 158 SAEFAQS--------ERGEIAYQIGHARAAatdaahlaricDSIASYDVRRRLNLVRSETLVLHSEDDGVYPPVEGRRLA 229
Cdd:PRK14875 269 TRQMVEDllkykrldGVDDALRALADALFA-----------GGRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQGLP 337

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 981680011 230 amiPGAQFGSLPGSGHHPNLDRADTFNWTLLHFLSGH 266
Cdd:PRK14875 338 ---DGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 4-266 3.17e-48

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: 159.78  E-value: 3.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   4 LSFNDHDLYYADIG-SGLPIMLIHDLGSCGLAWARQVPFLRhAGYRVIVPDLPGHGASSYPSRTLAMGELAADLEGLLDH 82
Cdd:COG0596    7 VTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  83 LGLDSAALVGLSLGGAIALTVAIDAPSRVGKLVVCNGCSNLVAdDHMRRVAQWKAGFqrgdgpvrwfeemwpslvsaefa 162
Cdd:COG0596   86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALA-EPLRRPGLAPEAL----------------------- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011 163 qsergeiayqigharaaatdaahlARICDSIASYDVRRRLNLVRSETLVLHSEDDGVYPPVEGRRLAAMIPGAQFGSLPG 242
Cdd:COG0596  142 ------------------------AALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPG 197

                        250       260
                 ....*....|....*....|....
gi 981680011 243 SGHHPNLDRADTFNWTLLHFLSGH 266
Cdd:COG0596  198 AGHFPPLEQPEAFAAALRDFLARL 221
protocat_pcaD TIGR02427
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ...
 21-264 1.21e-35

3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]


Pssm-ID: 131480 [Multi-domain]  Cd Length: 251  Bit Score: 128.24  E-value: 1.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   21 PIMLIHDLGSCGLAWARQVPFLrHAGYRVIVPDLPGHGASSYPSRTLAMGELAADLEGLLDHLGLDSAALVGLSLGGAIA 100
Cdd:TIGR02427  15 VLVFINSLGTDLRMWDPVLPAL-TPDFRVLRYDKRGHGLSDAPEGPYSIEDLADDVLALLDHLGIERAVFCGLSLGGLIA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  101 LTVAIDAPSRVGKLVVCNGCSNL-VADDHMRRVAQWKA-GFQRGDGPV--RWFEEMWPSLVSAEF--------AQSERGE 168
Cdd:TIGR02427  94 QGLAARRPDRVRALVLSNTAAKIgTPESWNARIAAVRAeGLAALADAVleRWFTPGFREAHPARLdlyrnmlvRQPPDGY 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  169 IAyqigharaaatdaahlarICDSIASYDVRRRLNLVRSETLVLHSEDDGVYPPVEGRRLAAMIPGAQFGSLPGSGHHPN 248
Cdd:TIGR02427 174 AG------------------CCAAIRDADFRDRLGAIAVPTLCIAGDQDGSTPPELVREIADLVPGARFAEIRGAGHIPC 235

                         250
                  ....*....|....*.
gi 981680011  249 LDRADTFNWTLLHFLS 264
Cdd:TIGR02427 236 VEQPEAFNAALRDFLR 251
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 21-252 2.45e-26

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: 103.35  E-value: 2.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   21 PIMLIHDLGSCGLAWARQVPFLRHAGYRVIVPDLPGHGASSYPSR--TLAMGELAADLEGLLDHLGLDSAALVGLSLGGA 98
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAqdDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   99 IALTVAIDAPSRVGKLVVCNGCSN-LVADDHMRRVAQWKAGFQRGD--GPVRWFEEMWPSLVSAE--------------F 161
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPpHELDEADRFILALFPGFFDGFvaDFAPNPLGRLVAKLLALlllrlrllkalpllN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  162 AQSERGEIAYQIGHARAAATDaahlariCDSIASYDVRRRLNLVRSETLVLHSEDDGVYPPVEGRRLAAMIPGAQFGSLP 241
Cdd:pfam00561 162 KRFPSGDYALAKSLVTGALLF-------IETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234

                         250
                  ....*....|.
gi 981680011  242 GSGHHPNLDRA 252
Cdd:pfam00561 235 DAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 9-266 1.52e-24

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 101.17  E-value: 1.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   9 HDLYYADIG--SGLPIMLIHDLGSCGLAWARQVPFLRhAGYRVIVPDLPGHGASSYPSRTLAMGELAADLEGLLDHLGLD 86
Cdd:PRK14875 119 RTVRYLRLGegDGTPVVLIHGFGGDLNNWLFNHAALA-AGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDALGIE 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  87 SAALVGLSLGGAIALTVAIDAPSRVGK--LVVCNGCSNLVADDHMRrvaqwkaGFQRGDG-----PV--RWFEEmwPSLV 157
Cdd:PRK14875 198 RAHLVGHSMGGAVALRLAARAPQRVASltLIAPAGLGPEINGDYID-------GFVAAESrrelkPVleLLFAD--PALV 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011 158 SAEFAQS--------ERGEIAYQIGHARAAatdaahlaricDSIASYDVRRRLNLVRSETLVLHSEDDGVYPPVEGRRLA 229
Cdd:PRK14875 269 TRQMVEDllkykrldGVDDALRALADALFA-----------GGRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQGLP 337

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 981680011 230 amiPGAQFGSLPGSGHHPNLDRADTFNWTLLHFLSGH 266
Cdd:PRK14875 338 ---DGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
21-252 3.06e-17

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 78.51  E-value: 3.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  21 PIMLIHDLGSCGLAWARQVPFLRHAGYRVIVPDLPGHGASSYPSRTLA-MGELAADLEGLLDHLGLDSAA---LVGLSLG 96
Cdd:COG2267   30 TVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDsFDDYVDDLRAALDALRARPGLpvvLLGHSMG 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  97 GAIALTVAIDAPSRVGKLVVCNgcSNLVADDHMRrvaqwkagfqrgdGPVRWFEEMWpslvsaefaqsergeiayqigha 176
Cdd:COG2267  110 GLIALLYAARYPDRVAGLVLLA--PAYRADPLLG-------------PSARWLRALR----------------------- 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981680011 177 raaatdaahlaricdsiasydVRRRLNLVRSETLVLHSEDDGVYPPVEGRRLA-AMIPGAQFGSLPGSGHHPNLDRA 252
Cdd:COG2267  152 ---------------------LAEALARIDVPVLVLHGGADRVVPPEAARRLAaRLSPDVELVLLPGARHELLNEPA 207
bchO_mg_che_rel TIGR03056
putative magnesium chelatase accessory protein; Members of this family belong to the alpha ...
 1-263 4.15e-17

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: 79.16  E-value: 4.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011    1 MAKLSFNDHDLYYADIG--SGLPIMLIHDLGSCGLAWARQVPFLRhAGYRVIVPDLPGHGASSYPSRT-LAMGELAADLE 77
Cdd:TIGR03056   8 SRRVTVGPFHWHVQDMGptAGPLLLLLHGTGASTHSWRDLMPPLA-RSFRVVAPDLPGHGFTRAPFRFrFTLPSMAEDLS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   78 GLLDHLGLDSAALVGLSLGGAIALTVAIDAPSRVGKLVVCNGcsnlvADDHMRRVAQWKAGFQrgdGPVRWFEEMWPSLV 157
Cdd:TIGR03056  87 ALCAAEGLSPDGVIGHSAGAAIALRLALDGPVTPRMVVGINA-----ALMPFEGMAGTLFPYM---ARVLACNPFTPPMM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  158 SAEFAQSER-GEIAYQIGHARAAATDAAHLARICDS---------IASYD---VRRRLNLVRSETLVLHSEDDGVYPPVE 224
Cdd:TIGR03056 159 SRGAADQQRvERLIRDTGSLLDKAGMTYYGRLIRSPahvdgalsmMAQWDlapLNRDLPRITIPLHLIAGEEDKAVPPDE 238

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 981680011  225 GRRLAAMIPGAQFGSLPGSGHHPNLDRADTFNWTLLHFL 263
Cdd:TIGR03056 239 SKRAATRVPTATLHVVPGGGHLVHEEQADGVVGLILQAA 277
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
22-268 6.07e-17

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 78.06  E-value: 6.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  22 IMLIHDLGSC---GLAWARqvpFLRHAGYRVIVPDLPGHGASSYPSRTLAMGELAADLEGLLDHL--GLDSAALVGLSLG 96
Cdd:COG1647   18 VLLLHGFTGSpaeMRPLAE---ALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILkaGYDKVIVIGLSMG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  97 GAIALTVAIDAPsRVGKLVVCNgcSNLVADDHMRRVAQWkagfqrgdgpVRWFEEMWPSlVSAEFAQSERGEIAYQIGHA 176
Cdd:COG1647   95 GLLALLLAARYP-DVAGLVLLS--PALKIDDPSAPLLPL----------LKYLARSLRG-IGSDIEDPEVAEYAYDRTPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011 177 raaatdaahlaricDSIAS-----YDVRRRLNLVRSETLVLHSEDDGVYPPVEGRRLAAMIPGA--QFGSLPGSGH--HP 247
Cdd:COG1647  161 --------------RALAElqrliREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPdkELVWLEDSGHviTL 226

                        250       260
                 ....*....|....*....|.
gi 981680011 248 NLDRADTFNWTlLHFLSGHDP 268
Cdd:COG1647  227 DKDREEVAEEI-LDFLERLAA 246
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 22-254 3.15e-13

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 67.11  E-value: 3.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   22 IMLIHDLGSCglawARQVPFLRHAGYRVIVPDLPGHGASSYPSRTLAmgeLAADLEGLLDHLGLDSAA-LVGLSLGGAIA 100
Cdd:pfam12697   1 VVLVHGAGLS----AAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLA---DLADLAALLDELGAARPVvLVGHSLGGAVA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  101 LTVAIDAPsrVGKLVVcngCSNLVADDHMRRVAQWKAGFQRGDGPVRWFEEMWPslvSAEFAQSERGEIAYQIGHARAAA 180
Cdd:pfam12697  74 LAAAAAAL--VVGVLV---APLAAPPGLLAALLALLARLGAALAAPAWLAAESL---ARGFLDDLPADAEWAAALARLAA 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 981680011  181 TDAAHlaricdsiaSYDVRRRLNLVRSETLVLHSEDDGVYPPVEgrRLAAMIPGAQFGSLPGSGHHPNLDRADT 254
Cdd:pfam12697 146 LLAAL---------ALLPLAAWRDLPVPVLVLAEEDRLVPELAQ--RLLAALAGARLVVLPGAGHLPLDDPEEV 208
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 17-262 1.30e-12

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: 65.99  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   17 GSGLP-IMLIHDLGSCGLAWARQVPFLRhAGYRVIVPDLPGHGAssypSRTLAMGELAADLEGLLDHLGlDSAALVGLSL 95
Cdd:TIGR01738   1 GQGNVhLVLIHGWGMNAEVFRCLDEELS-AHFTLHLVDLPGHGR----SRGFGPLSLADMAEAIAAQAP-DPAIWLGWSL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   96 GGAIALTVAIDAPSRVGKLVVCNGCSNLVADDHMRR----------VAQWKAGFQRgdgPVRWFeeMWPSLVSAEFAQSE 165
Cdd:TIGR01738  75 GGLVALHIAATHPDRVRALVTVASSPCFSAREDWPEgikpdvltgfQQQLSDDYQR---TIERF--LALQTLGTPTARQD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  166 RGEIAYQIGHARAAATDAAHLAriCDSIASYDVRRRLNLVRSETLVLHSEDDGVYPPVEGRRLAAMIPGAQFGSLPGSGH 245
Cdd:TIGR01738 150 ARALKQTLLARPTPNVQVLQAG--LEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAH 227

                         250
                  ....*....|....*..
gi 981680011  246 HPNLDRADTFNWTLLHF 262
Cdd:TIGR01738 228 APFLSHAEAFCALLVAF 244
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 21-153 4.51e-12

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: 64.54  E-value: 4.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   21 PIMLIHDLGSCGLAWARQVPFLRHaGYRVIVPDLPGHGASSYPS--RTLAMGELAAD-LEGLLDHLGLDSAALVGLSLGG 97
Cdd:TIGR03695   4 VLVFLHGFLGSGADWQALIEALGP-HFRCLAIDLPGHGSSQSPSdiERYDFEEAAQLlLATLLDQLGIEPFFLVGYSMGG 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   98 AIALTVAIDAPSRVGKLVVCNGCSNLVADDhmRRVAQWKAGFQRGD----GPVRWFEEMW 153
Cdd:TIGR03695  83 RIALYYALQYPERVQGLILESGSPGLQTEE--ERAARRQNDEQLAQrfeqEGLEAFLDDW 140
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
11-266 1.13e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 57.33  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  11 LYYADIGSGLP-IMLIHDL-GSCGLAWARQVPFLRHAGYRVIVPDLPGHGASsypSRTLAMGELaADLEGLLDHL----G 84
Cdd:COG1506   14 LYLPADGKKYPvVVYVHGGpGSRDDSFLPLAQALASRGYAVLAPDYRGYGES---AGDWGGDEV-DDVLAAIDYLaarpY 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  85 LDSA--ALVGLSLGGAIALTVAIDAPSRVGKLVVCNGCSNLVADDH-MRRVAQWKAGfqrgdGPVRWFEEMWpslvsaef 161
Cdd:COG1506   90 VDPDriGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGtTREYTERLMG-----GPWEDPEAYA-------- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011 162 aqsergeiayqigharaaatdaahlaricdsiaSYDVRRRLNLVRSETLVLHSEDDGVYPPVEGRRLAAMIPGA----QF 237
Cdd:COG1506  157 ---------------------------------ARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKAgkpvEL 203

                        250       260
                 ....*....|....*....|....*....
gi 981680011 238 GSLPGSGHHPNLDRADTFNWTLLHFLSGH 266
Cdd:COG1506  204 LVYPGEGHGFSGAGAPDYLERILDFLDRH 232
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 1-111 1.27e-09

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 57.70  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   1 MAKLSFNDHDLYYADIGSGLPIMLIHDLGSCGLAWARQVPFLRHAGyRVIVPDLPGHGASSYPSRTLAMGELAADLEGLL 80
Cdd:PRK03592   9 MRRVEVLGSRMAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPDIDYTFADHARYLDAWF 87

                         90       100       110
                 ....*....|....*....|....*....|.
gi 981680011  81 DHLGLDSAALVGLSLGGAIALTVAIDAPSRV 111
Cdd:PRK03592  88 DALGLDDVVLVGHDWGSALGFDWAARHPDRV 118
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 11-119 1.41e-09

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 57.67  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  11 LYYADIGS--GLPIMLIHDLGSCGLAWARQVPFLRHAGYRVIVPDLPGHGASSYPSRTlamgelaAD---------LEGL 79
Cdd:PRK00870  36 MHYVDEGPadGPPVLLLHGEPSWSYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPTRR-------EDytyarhvewMRSW 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 981680011  80 LDHLGLDSAALVGLSLGGAIALTVAIDAPSRVGKLVVCNG 119
Cdd:PRK00870 109 FEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANT 148
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 21-115 2.51e-09

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 53.68  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  21 PIMLIHDLGSCGLAWARQVPFLRHAGYRVIVPDLPGHGASSYPSrtlaMGELAADLEGLLDHLGLDSAALVGLSLGGAIA 100
Cdd:COG1075    7 PVVLVHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDS----AEQLAAFVDAVLAATGAEKVDLVGHSMGGLVA 82

                         90
                 ....*....|....*..
gi 981680011 101 LTVA--IDAPSRVGKLV 115
Cdd:COG1075   83 RYYLkrLGGAAKVARVV 99
PRK10673 PRK10673
esterase;
18-116 8.29e-09

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 55.12  E-value: 8.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  18 SGLPIMLIH----DLGSCGLAwARQVpflrHAGYRVIVPDLPGHGASSYpSRTLAMGELAADLEGLLDHLGLDSAALVGL 93
Cdd:PRK10673  15 NNSPIVLVHglfgSLDNLGVL-ARDL----VNDHDIIQVDMRNHGLSPR-DPVMNYPAMAQDLLDTLDALQIEKATFIGH 88

                         90       100
                 ....*....|....*....|...
gi 981680011  94 SLGGAIALTVAIDAPSRVGKLVV 116
Cdd:PRK10673  89 SMGGKAVMALTALAPDRIDKLVA 111
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 11-118 3.81e-08

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 53.32  E-value: 3.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  11 LYYADIGSGLPIMLIHDLGSCGLAWARQVPFLRHAgYRVIVPDLPGHGASSYPSR-TLAMGELAADLEGLLDHLGLDSAA 89
Cdd:PRK03204  26 IHYIDEGTGPPILLCHGNPTWSFLYRDIIVALRDR-FRCVAPDYLGFGLSERPSGfGYQIDEHARVIGEFVDHLGLDRYL 104

                         90       100
                 ....*....|....*....|....*....
gi 981680011  90 LVGLSLGGAIALTVAIDAPSRVGKLVVCN 118
Cdd:PRK03204 105 SMGQDWGGPISMAVAVERADRVRGVVLGN 133
PLN02578 PLN02578
hydrolase
 8-118 2.43e-07

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 51.38  E-value: 2.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   8 DHDLYYADIGSGLPIMLIHDLGSCGLAWARQVPFLRHAgYRVIVPDLPGHGASSYpsrtlAMGELAADL-----EGLLDH 82
Cdd:PLN02578  75 GHKIHYVVQGEGLPIVLIHGFGASAFHWRYNIPELAKK-YKVYALDLLGFGWSDK-----ALIEYDAMVwrdqvADFVKE 148

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 981680011  83 LGLDSAALVGLSLGGAIALTVAIDAPSRVGKLVVCN 118
Cdd:PLN02578 149 VVKEPAVLVGNSLGGFTALSTAVGYPELVAGVALLN 184
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 22-245 5.62e-06

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: 46.44  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   22 IMLIHDLGSCGLAWARQVPFLRHAGYRVIVPDLPGHGASS-YPSRTLAMGELAADLEGLLDHLGLDSA----ALVGLSLG 96
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDgKRGHVPSFDDYVDDLDTFVDKIREEHPglplFLLGHSMG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   97 GAIALTVAIDAPSRVGKLVVCngCSNL-VADDHMRRVAQWKAGFQRGDGPVRWFE-EMWPSLVS------AEFAQSE--R 166
Cdd:pfam12146  87 GLIAALYALRYPDKVDGLILS--APALkIKPYLAPPILKLLAKLLGKLFPRLRVPnNLLPDSLSrdpevvAAYAADPlvH 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  167 GEIAYQIGHAraaatdaahlarICDSIAsyDVRRRLNLVRSETLVLHSEDDGVYPPVEGRRLAAMIPGA--QFGSLPGSG 244
Cdd:pfam12146 165 GGISARTLYE------------LLDAGE--RLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTdkTLKLYPGLY 230


                  .
gi 981680011  245 H 245
Cdd:pfam12146 231 H 231
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 10-245 9.43e-06

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 46.06  E-value: 9.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  10 DLYY-ADIGSGLPIMLI-HDLGSCGLAWARQVPFLRHAGYRVIVPDLPGHGASSYPSRTLAMGElAADLEGLLDHL---- 83
Cdd:COG1073   26 DLYLpAGASKKYPAVVVaHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPE-RRDARAAVDYLrtlp 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  84 GLDSA--ALVGLSLGGAIALTVAIDAPsRVGKLVVcngcsnLVADDHMRRVAQWKAGFQRGDgPVRWFeEMWPSLVSAEF 161
Cdd:COG1073  105 GVDPEriGLLGISLGGGYALNAAATDP-RVKAVIL------DSPFTSLEDLAAQRAKEARGA-YLPGV-PYLPNVRLASL 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011 162 AQSErgeiayqigharaaatdaahlaricdsiasYDVRRRLNLVRSETLVLHSEDDGVYPPVEGRRLAAMIPGA-QFGSL 240
Cdd:COG1073  176 LNDE------------------------------FDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPkELLIV 225


                 ....*
gi 981680011 241 PGSGH 245
Cdd:COG1073  226 PGAGH 230
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
11-108 1.63e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 44.96  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  11 LYYADIGSGLP-IMLIHD---LGSCGLAWARQvpfLRHAGYRVIVPDLPGHGASSYPS-------RTLAMGELAADLEGL 79
Cdd:COG0412   20 LARPAGGGPRPgVVVLHEifgLNPHIRDVARR---LAAAGYVVLAPDLYGRGGPGDDPdearalmGALDPELLAADLRAA 96

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 981680011  80 LDHL----GLDSA--ALVGLSLGGAIALTVAIDAP 108
Cdd:COG0412   97 LDWLkaqpEVDAGrvGVVGFCFGGGLALLAAARGP 131
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
 53-122 8.54e-05

Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, and Ndr3. Their similarity was previously noted. The precise molecular and cellular function of members of this family is still unknown. Yet, they are known to be involved in cellular differentiation events. The Ndr1 group was the first to be discovered. Their expression is repressed by the proto-oncogenes N-myc and c-myc, and in line with this observation, Ndr1 protein expression is down-regulated in neoplastic cells, and is reactivated when differentiation is induced by chemicals such as retinoic acid. Ndr2 and Ndr3 expression is not under the control of N-myc or c-myc. Ndr1 expression is also activated by several chemicals: tunicamycin and homocysteine induce Ndr1 in human umbilical endothelial cells; nickel induces Ndr1 in several cell types. Members of this family are found in wide variety of multicellular eukaryotes, including an Ndr1 type protein in Helianthus annuus (sunflower), known as Sf21. Interestingly, the highest scoring matches in the noise are all alpha/beta hydrolases pfam00561, suggesting that this family may have an enzymatic function (Bateman A pers. obs.).


Pssm-ID: 397285 [Multi-domain]  Cd Length: 285  Bit Score: 43.11  E-value: 8.54e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 981680011   53 DLPGH--GASSYPS--RTLAMGELAADLEGLLDHLGLDSAALVGLSLGGAIALTVAIDAPSRVGKLVVCNGCSN 122
Cdd:pfam03096  62 DAPGQedGAASFPGgyPYPSMDDLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPK 135
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 12-118 1.75e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 42.42  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  12 YYADIGSGLPIMLIHDLGSCGLAWARQVPFLRHAGyRVIVPDLPGHGASSYPS-RTLAMGEL------AADLEGLLDHLG 84
Cdd:PLN02824  22 YQRAGTSGPALVLVHGFGGNADHWRKNTPVLAKSH-RVYAIDLLGYGYSDKPNpRSAPPNSFytfetwGEQLNDFCSDVV 100

                         90       100       110
                 ....*....|....*....|....*....|....
gi 981680011  85 LDSAALVGLSLGGAIALTVAIDAPSRVGKLVVCN 118
Cdd:PLN02824 101 GDPAFVICNSVGGVVGLQAAVDAPELVRGVMLIN 134
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 48-132 2.42e-04

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 42.54  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011   48 RVIVPDLPGHGAS--------SYPSRTLAMgELAAD-LEGLLDHLGLDSAALVGLSLGGAIALTVAIDAPSRVGKLVVCN 118
Cdd:PLN02980 1399 RCISIDLPGHGGSkiqnhakeTQTEPTLSV-ELVADlLYKLIEHITPGKVTLVGYSMGARIALYMALRFSDKIEGAVIIS 1477

                          90
                  ....*....|....
gi 981680011  119 GCSNLvADDHMRRV 132
Cdd:PLN02980 1478 GSPGL-KDEVARKI 1490
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 21-169 6.93e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 40.66  E-value: 6.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  21 PIMLIHDLGSCGLAWARQVPFLRhAGYRVIVPDLPGHGASSYPSRTLAMGELAAD-----LEGLLDHLGLDSAALVGLSL 95
Cdd:PLN02894 107 TLVMVHGYGASQGFFFRNFDALA-SRFRVIAIDQLGWGGSSRPDFTCKSTEETEAwfidsFEEWRKAKNLSNFILLGHSF 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  96 GGAIALTVAIDAPSRVGKLV-VCNGCSNLVADDHMRRVAQ-------------WKAGFQ-----RGDGPvrWFEEMWPSL 156
Cdd:PLN02894 186 GGYVAAKYALKHPEHVQHLIlVGPAGFSSESDDKSEWLTKfratwkgavlnhlWESNFTpqkiiRGLGP--WGPNLVRRY 263

                        170
                 ....*....|...
gi 981680011 157 VSAEFAQSERGEI 169
Cdd:PLN02894 264 TTARFGAHSTGDI 276
YpfH COG0400
Predicted esterase [General function prediction only];
22-119 7.09e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 36.81  E-value: 7.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981680011  22 IMLIHDLGSCGLAWARQVPFLRHAGYRVIVPD---LPGHGASS-YPSRTL-----------AMGELAADLEGLLDHLGLD 86
Cdd:COG0400    8 VVLLHGYGGDEEDLLPLAPELALPGAAVLAPRapvPEGPGGRAwFDLSFLegredeeglaaAAEALAAFIDELEARYGID 87

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 981680011  87 SA--ALVGLSLGGAIALTVAIDAPSRVGKLVVCNG 119
Cdd:COG0400   88 PEriVLAGFSQGAAMALSLALRRPELLAGVVALSG 122
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 26-101 9.02e-03

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 36.74  E-value: 9.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981680011  26 HDLGSCGLAWARQVPFLRHagYRVIVPDLPGHGAS-SYPSRTLAmgELAADLEGLLDHLGLDSAALVGLSLGGAIAL 101
Cdd:PRK11126   9 HGLLGSGQDWQPVGEALPD--YPRLYIDLPGHGGSaAISVDGFA--DVSRLLSQTLQSYNILPYWLVGYSLGGRIAM 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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