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Conserved domains on  [gi|755288739|gb|AJI86193|]
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pimelyl-[acyl-carrier protein] methyl ester esterase [Yersinia frederiksenii Y225]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 1-255 6.91e-146

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member PRK10349:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 256  Bit Score: 408.25  E-value: 6.91e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   1 MKQLYWNVCGEGDRDLVLLHGWGLNAGVWHCIIDRLAPHFRLHLVDLPGYGRSNEFGAMSLSEMAEIVLQQAPKQAIWLG 80
Cdd:PRK10349   1 MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDKAIWLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  81 WSMGGLVASQIALQHPERVSGLITVASSPCFAAHDEWPGIRPEVLAGFQQQLSEDFQRTVERFLALQTLGTESARQDARL 160
Cdd:PRK10349  81 WSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739 161 LKAVVLQHQMPEVSVLTGGLDILRTADLREALAGCSLPFLRIYGYLDGLVPRNVASLLDSKWPHTQSVVMKGCAHAPFVS 240
Cdd:PRK10349 161 LKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFIS 240

                        250
                 ....*....|....*
gi 755288739 241 HPDEFSKLIIDFAQQ 255
Cdd:PRK10349 241 HPAEFCHLLVALKQR 255
 
Name Accession Description Interval E-value
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
1-255 6.91e-146

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 408.25  E-value: 6.91e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   1 MKQLYWNVCGEGDRDLVLLHGWGLNAGVWHCIIDRLAPHFRLHLVDLPGYGRSNEFGAMSLSEMAEIVLQQAPKQAIWLG 80
Cdd:PRK10349   1 MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDKAIWLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  81 WSMGGLVASQIALQHPERVSGLITVASSPCFAAHDEWPGIRPEVLAGFQQQLSEDFQRTVERFLALQTLGTESARQDARL 160
Cdd:PRK10349  81 WSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739 161 LKAVVLQHQMPEVSVLTGGLDILRTADLREALAGCSLPFLRIYGYLDGLVPRNVASLLDSKWPHTQSVVMKGCAHAPFVS 240
Cdd:PRK10349 161 LKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFIS 240

                        250
                 ....*....|....*
gi 755288739 241 HPDEFSKLIIDFAQQ 255
Cdd:PRK10349 241 HPAEFCHLLVALKQR 255
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 10-253 4.36e-118

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: 337.56  E-value: 4.36e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   10 GEGDRDLVLLHGWGLNAGVWHCIIDRLAPHFRLHLVDLPGYGRSNEFGAMSLSEMAEIVLQQAPKQAIWLGWSMGGLVAS 89
Cdd:TIGR01738   1 GQGNVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPLSLADMAEAIAAQAPDPAIWLGWSLGGLVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   90 QIALQHPERVSGLITVASSPCFAAHDEWP-GIRPEVLAGFQQQLSEDFQRTVERFLALQTLGTESARQDARLLKAVVLQH 168
Cdd:TIGR01738  81 HIAATHPDRVRALVTVASSPCFSAREDWPeGIKPDVLTGFQQQLSDDYQRTIERFLALQTLGTPTARQDARALKQTLLAR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  169 QMPEVSVLTGGLDILRTADLREALAGCSLPFLRIYGYLDGLVPRNVASLLDSKWPHTQSVVMKGCAHAPFVSHPDEFSKL 248
Cdd:TIGR01738 161 PTPNVQVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSHAEAFCAL 240


                  ....*
gi 755288739  249 IIDFA 253
Cdd:TIGR01738 241 LVAFK 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 3-256 4.24e-41

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: 140.52  E-value: 4.24e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   3 QLYWNVCGEGDRDLVLLHGWGLNAGVWHCIIDRLAPHFRLHLVDLPGYGRSNEF-GAMSLSEMAEIVL----QQAPKQAI 77
Cdd:COG0596   13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPaGGYTLDDLADDLAalldALGLERVV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  78 WLGWSMGGLVASQIALQHPERVSGLITVAsspcfaahdewpgirpEVLAGFQQQLSEDfQRTVERFLALqtlgtesarqd 157
Cdd:COG0596   93 LVGHSMGGMVALELAARHPERVAGLVLVD----------------EVLAALAEPLRRP-GLAPEALAAL----------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739 158 arllkavvlqhqmpevsvltggLDILRTADLREALAGCSLPFLRIYGYLDGLVPRNVASLLDSKWPHTQSVVMKGCAHAP 237
Cdd:COG0596  145 ----------------------LRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFP 202

                        250
                 ....*....|....*....
gi 755288739 238 FVSHPDEFSKLIIDFAQQN 256
Cdd:COG0596  203 PLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 16-242 6.19e-33

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: 120.30  E-value: 6.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   16 LVLLHGWGLNAGVWHCIIDRLAP-HFRLHLVDLPGYGRS------NEFGAMSLSEMAEIVLQQAP-KQAIWLGWSMGGLV 87
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARdGFRVIALDLRGFGKSsrpkaqDDYRTDDLAEDLEYILEALGlEKVNLVGHSMGGLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   88 ASQIALQHPERVSGLITVASSPCFAAHDEWPGIRPEVLAGFQQQLSEDFQRTVERFLALQTLGTESARQDA-RLLKAVVL 166
Cdd:pfam00561  83 ALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLlKALPLLNK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  167 QH----QMPEVSVLTGGL---DILRTADLREALAGCSLPFLRIYGYLDGLVPRNVASLLDSKWPHTQSVVMKGCAHAPFV 239
Cdd:pfam00561 163 RFpsgdYALAKSLVTGALlfiETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAFL 242


                  ...
gi 755288739  240 SHP 242
Cdd:pfam00561 243 EGP 245
 
Name Accession Description Interval E-value
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
1-255 6.91e-146

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 408.25  E-value: 6.91e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   1 MKQLYWNVCGEGDRDLVLLHGWGLNAGVWHCIIDRLAPHFRLHLVDLPGYGRSNEFGAMSLSEMAEIVLQQAPKQAIWLG 80
Cdd:PRK10349   1 MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDKAIWLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  81 WSMGGLVASQIALQHPERVSGLITVASSPCFAAHDEWPGIRPEVLAGFQQQLSEDFQRTVERFLALQTLGTESARQDARL 160
Cdd:PRK10349  81 WSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739 161 LKAVVLQHQMPEVSVLTGGLDILRTADLREALAGCSLPFLRIYGYLDGLVPRNVASLLDSKWPHTQSVVMKGCAHAPFVS 240
Cdd:PRK10349 161 LKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFIS 240

                        250
                 ....*....|....*
gi 755288739 241 HPDEFSKLIIDFAQQ 255
Cdd:PRK10349 241 HPAEFCHLLVALKQR 255
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 10-253 4.36e-118

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: 337.56  E-value: 4.36e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   10 GEGDRDLVLLHGWGLNAGVWHCIIDRLAPHFRLHLVDLPGYGRSNEFGAMSLSEMAEIVLQQAPKQAIWLGWSMGGLVAS 89
Cdd:TIGR01738   1 GQGNVHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPLSLADMAEAIAAQAPDPAIWLGWSLGGLVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   90 QIALQHPERVSGLITVASSPCFAAHDEWP-GIRPEVLAGFQQQLSEDFQRTVERFLALQTLGTESARQDARLLKAVVLQH 168
Cdd:TIGR01738  81 HIAATHPDRVRALVTVASSPCFSAREDWPeGIKPDVLTGFQQQLSDDYQRTIERFLALQTLGTPTARQDARALKQTLLAR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  169 QMPEVSVLTGGLDILRTADLREALAGCSLPFLRIYGYLDGLVPRNVASLLDSKWPHTQSVVMKGCAHAPFVSHPDEFSKL 248
Cdd:TIGR01738 161 PTPNVQVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSHAEAFCAL 240


                  ....*
gi 755288739  249 IIDFA 253
Cdd:TIGR01738 241 LVAFK 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 3-256 4.24e-41

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: 140.52  E-value: 4.24e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   3 QLYWNVCGEGDRDLVLLHGWGLNAGVWHCIIDRLAPHFRLHLVDLPGYGRSNEF-GAMSLSEMAEIVL----QQAPKQAI 77
Cdd:COG0596   13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPaGGYTLDDLADDLAalldALGLERVV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  78 WLGWSMGGLVASQIALQHPERVSGLITVAsspcfaahdewpgirpEVLAGFQQQLSEDfQRTVERFLALqtlgtesarqd 157
Cdd:COG0596   93 LVGHSMGGMVALELAARHPERVAGLVLVD----------------EVLAALAEPLRRP-GLAPEALAAL----------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739 158 arllkavvlqhqmpevsvltggLDILRTADLREALAGCSLPFLRIYGYLDGLVPRNVASLLDSKWPHTQSVVMKGCAHAP 237
Cdd:COG0596  145 ----------------------LRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFP 202

                        250
                 ....*....|....*....
gi 755288739 238 FVSHPDEFSKLIIDFAQQN 256
Cdd:COG0596  203 PLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 16-242 6.19e-33

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: 120.30  E-value: 6.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   16 LVLLHGWGLNAGVWHCIIDRLAP-HFRLHLVDLPGYGRS------NEFGAMSLSEMAEIVLQQAP-KQAIWLGWSMGGLV 87
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARdGFRVIALDLRGFGKSsrpkaqDDYRTDDLAEDLEYILEALGlEKVNLVGHSMGGLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   88 ASQIALQHPERVSGLITVASSPCFAAHDEWPGIRPEVLAGFQQQLSEDFQRTVERFLALQTLGTESARQDA-RLLKAVVL 166
Cdd:pfam00561  83 ALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLlKALPLLNK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  167 QH----QMPEVSVLTGGL---DILRTADLREALAGCSLPFLRIYGYLDGLVPRNVASLLDSKWPHTQSVVMKGCAHAPFV 239
Cdd:pfam00561 163 RFpsgdYALAKSLVTGALlfiETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAFL 242


                  ...
gi 755288739  240 SHP 242
Cdd:pfam00561 243 EGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 10-255 4.03e-20

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 88.08  E-value: 4.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  10 GEGDRD-LVLLHGWGLNAGVWHCIIDRLAPHFRLHLVDLPGYGRSN-EFGAMSLSEMAEIVL----QQAPKQAIWLGWSM 83
Cdd:PRK14875 127 GEGDGTpVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSkAVGAGSLDELAAAVLafldALGIERAHLVGHSM 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  84 GGLVASQIALQHPERVSGLITVASSpcfaahdewpGIRPEVLAGFQQQLSE-DFQRTVERFLALqtLGTESARQDARLLK 162
Cdd:PRK14875 207 GGAVALRLAARAPQRVASLTLIAPA----------GLGPEINGDYIDGFVAaESRRELKPVLEL--LFADPALVTRQMVE 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739 163 AVVLQHQMPEV----SVLTGGL--DILRTADLREALAGCSLPFLRIYGYLDGLVPRNVASLLDSKWPHTqsvVMKGCAHA 236
Cdd:PRK14875 275 DLLKYKRLDGVddalRALADALfaGGRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQGLPDGVAVH---VLPGAGHM 351

                        250
                 ....*....|....*....
gi 755288739 237 PFVSHPDEFSKLIIDFAQQ 255
Cdd:PRK14875 352 PQMEAAADVNRLLAEFLGK 370
menH_SHCHC TIGR03695
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ...
 16-252 3.60e-19

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: 83.80  E-value: 3.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   16 LVLLHGWGLNAGVWHCIIDRLAPHFRLHLVDLPGYGRSNEFGAMSLSEMAEIV-------LQQAPKQAIWL-GWSMGGLV 87
Cdd:TIGR03695   5 LVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERYDFEEAAqlllatlLDQLGIEPFFLvGYSMGGRI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   88 ASQIALQHPERVSGLITVASSPCFAAHDEwpgiRPEVLAGfQQQLSEDF-QRTVERFLAL---------QTLGTESARQD 157
Cdd:TIGR03695  85 ALYYALQYPERVQGLILESGSPGLQTEEE----RAARRQN-DEQLAQRFeQEGLEAFLDDwyqqplfasQKNLPPEQRQA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  158 ARLLKAvvlqHQMPEvsVLTGGLDILRTA---DLREALAGCSLPFLRIYGYLD----GLVPRNVASLLDSKWphtqsVVM 230
Cdd:TIGR03695 160 LRAERL----ANNPE--GLAKMLRATGLGkqpSLWPKLQALKIPVLYLCGERDekfvQIAKEMQKLIPNLTL-----HII 228

                         250       260
                  ....*....|....*....|..
gi 755288739  231 KGCAHAPFVSHPDEFSKLIIDF 252
Cdd:TIGR03695 229 PNAGHNIHLENPEAFAKILLAF 250
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
6-129 2.98e-16

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 75.04  E-value: 2.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   6 WNVCGEGDRDLVLLHGWGLNAGVWHCIIDRLAPH-FRLHLVDLPGYGRS-------NEFGAM--SLSEMAEIVLQQAPKQ 75
Cdd:COG2267   21 WRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSdgprghvDSFDDYvdDLRAALDALRARPGLP 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755288739  76 AIWLGWSMGGLVASQIALQHPERVSGLitVASSPCFAAhDEWPGIRPEVLAGFQ 129
Cdd:COG2267  101 VVLLGHSMGGLIALLYAARYPDRVAGL--VLLAPAYRA-DPLLGPSARWLRALR 151
PLN02578 PLN02578
hydrolase
 3-253 1.64e-12

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 66.40  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   3 QLYWNVCGEGdRDLVLLHGWGLNAGVWHCIIDRLAPHFRLHLVDLPGYGRSN----EFGAMSLSE-MAEIVLQQAPKQAI 77
Cdd:PLN02578  77 KIHYVVQGEG-LPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDkaliEYDAMVWRDqVADFVKEVVKEPAV 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  78 WLGWSMGGLVASQIALQHPERVSGLITVASSPCFAAHDE--------------WPGIRPevlagfqqqLSEDFQRTVERF 143
Cdd:PLN02578 156 LVGNSLGGFTALSTAVGYPELVAGVALLNSAGQFGSESRekeeaivveetvltRFVVKP---------LKEWFQRVVLGF 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739 144 L------------ALQTLGTESARQDARLLKAVVLQHQMP---EV--SVLTGGLDILRTADLREALAGCSLPFLRIYGYL 206
Cdd:PLN02578 227 LfwqakqpsriesVLKSVYKDKSNVDDYLVESITEPAADPnagEVyyRLMSRFLFNQSRYTLDSLLSKLSCPLLLLWGDL 306

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 755288739 207 DGLVPRNVASLLDSKWPHTqSVVMKGCAHAPFVSHPDEFSKLIIDFA 253
Cdd:PLN02578 307 DPWVGPAKAEKIKAFYPDT-TLVNLQAGHCPHDEVPEQVNKALLEWL 352
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 16-245 5.51e-11

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 60.57  E-value: 5.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   16 LVLLHGWGLNAGVWHciiDRLAPHFRLHLVDLPGYGRSN--EFGAMSLSEMAEIVLQ-QAPKQAIWLGWSMGGLVASQIA 92
Cdd:pfam12697   1 VVLVHGAGLSAAPLA---ALLAAGVAVLAPDLPGHGSSSppPLDLADLADLAALLDElGAARPVVLVGHSLGGAVALAAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   93 lqhpeRVSGLITVASSPCFAAHDEWPGIRPEVLAgfqqqlsEDFQRTVERFLALQTLGTESARQDARLLKAVVLQHQMPE 172
Cdd:pfam12697  78 -----AAALVVGVLVAPLAAPPGLLAALLALLAR-------LGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAA 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755288739  173 vsvLTGGLDILRTADLREALAgcslPFLRIYGyLDGLVPRNVASLLDsKWPHTQSVVMKGCAHAPFvSHPDEF 245
Cdd:pfam12697 146 ---LLAALALLPLAAWRDLPV----PVLVLAE-EDRLVPELAQRLLA-ALAGARLVVLPGAGHLPL-DDPEEV 208
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 16-107 4.13e-10

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 55.61  E-value: 4.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  16 LVLLHGWGLNAGVWHCIIDRL-APHFRLHLVDLPGYGRSNEFGAMSLSEMAEIVLQQAPKQAIWL-GWSMGGLVAsQIAL 93
Cdd:COG1075    8 VVLVHGLGGSAASWAPLAPRLrAAGYPVYALNYPSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLvGHSMGGLVA-RYYL 86

                         90
                 ....*....|....*..
gi 755288739  94 QH---PERVSGLITVAS 107
Cdd:COG1075   87 KRlggAAKVARVVTLGT 103
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 16-212 6.51e-10

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: 57.61  E-value: 6.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   16 LVLLHGWGLNAGVWHCIIDRLAPH-FRLHLVDLPGYGRS-------NEFGAM--SLSEMAEIVLQQAPKQ-AIWLGWSMG 84
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHGRSdgkrghvPSFDDYvdDLDTFVDKIREEHPGLpLFLLGHSMG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   85 GLVASQIALQHPERVSGLItvASSPCFaahdewpGIRPEVLAGFQQQLSEDFQRTVERFLALQTLGTESARQDARLLKAV 164
Cdd:pfam12146  87 GLIAALYALRYPDKVDGLI--LSAPAL-------KIKPYLAPPILKLLAKLLGKLFPRLRVPNNLLPDSLSRDPEVVAAY 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755288739  165 V---LQHQMPEVSVLTGGLDIlrTADLREALAGCSLPFLRIYGYLDGLVPR 212
Cdd:pfam12146 158 AadpLVHGGISARTLYELLDA--GERLLRRAAAITVPLLLLHGGADRVVDP 206
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 11-129 7.14e-10

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 58.77  E-value: 7.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  11 EGDRDLVLLHGWGLNAGVWHCIIDRLAPHFRLHLVDLPGYGRSN--EFGAMSLSE--------MAEIVLQQAPKQAIWLG 80
Cdd:PLN02894 103 EDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSrpDFTCKSTEEteawfidsFEEWRKAKNLSNFILLG 182

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 755288739  81 WSMGGLVASQIALQHPERVSGLITVASSPCFAAHDEWpgirPEVLAGFQ 129
Cdd:PLN02894 183 HSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESDDK----SEWLTKFR 227
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 17-208 3.26e-09

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 57.17  E-value: 3.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   17 VLLHGWGLNAGVWHCIIDRLAPHFRLHLVDLPGYGRS---------NEFGAMSLSEMAEIVL----QQAPKQAIWLGWSM 83
Cdd:PLN02980 1375 LFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSkiqnhaketQTEPTLSVELVADLLYklieHITPGKVTLVGYSM 1454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   84 GGLVASQIALQHPERVSGLITVASSpcfaahdewPGIRPEVLAGFqqQLSEDFQRT-------VERFLALQTLGT--ESA 154
Cdd:PLN02980 1455 GARIALYMALRFSDKIEGAVIISGS---------PGLKDEVARKI--RSAKDDSRArmlidhgLEIFLENWYSGElwKSL 1523

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755288739  155 RQDARLLKAVV--LQHQ-MPEVSVLTGGLDILRTADLREALAGCSLPFLRIYGYLDG 208
Cdd:PLN02980 1524 RNHPHFNKIVAsrLLHKdVPSLAKLLSDLSIGRQPSLWEDLKQCDTPLLLVVGEKDV 1580
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 16-103 1.25e-07

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 50.99  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  16 LVLLHGWGLNAGVWHCIIDRLaPHFRLHLVDLPGYGRSNEFGAMSLSEMAEIV---LQQAPKQAIWL-GWSMGGLVASQI 91
Cdd:PRK11126   5 LVFLHGLLGSGQDWQPVGEAL-PDYPRLYIDLPGHGGSAAISVDGFADVSRLLsqtLQSYNILPYWLvGYSLGGRIAMYY 83

                         90
                 ....*....|...
gi 755288739  92 ALQ-HPERVSGLI 103
Cdd:PRK11126  84 ACQgLAGGLCGLI 96
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
16-138 1.92e-06

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 47.70  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  16 LVLLHGWGLNA-GVWHCIIDRLAPH-FRLHLVDLPGYGRSneFGAMSLSEMAEIV-----LQQAP-----KQAIWlGWSM 83
Cdd:COG1506   26 VVYVHGGPGSRdDSFLPLAQALASRgYAVLAPDYRGYGES--AGDWGGDEVDDVLaaidyLAARPyvdpdRIGIY-GHSY 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755288739  84 GGLVASQIALQHPERVSGLITVASSPCFAAHDEWPGIRPEVLAGFQQQLSEDFQR 138
Cdd:COG1506  103 GGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTERLMGGPWEDPEAYAA 157
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
17-255 5.10e-06

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 46.47  E-value: 5.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  17 VLLHGWGLNAGVWHCIIDRLAPH-FRLHLVDLPGYGRS----NEFGA----MSLSEMAEIVLQQAPKQAIwLGWSMGGLV 87
Cdd:COG1647   19 LLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTSpedlLKTTWedwlEDVEEAYEILKAGYDKVIV-IGLSMGGLL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  88 ASQIALQHPErVSGLITVasSPCFAAHDEWPGIRPeVLAGFQQQL---SEDFQRTVERFLALQTLGTESARQDARLLKAV 164
Cdd:COG1647   98 ALLLAARYPD-VAGLVLL--SPALKIDDPSAPLLP-LLKYLARSLrgiGSDIEDPEVAEYAYDRTPLRALAELQRLIREV 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739 165 vlQHQMPEVSVltggldilrtadlrealagcslPFLRIYGYLDGLVPRNVASLLDSKWPHTQS--VVMKGCAHAPFVSH- 241
Cdd:COG1647  174 --RRDLPKITA----------------------PTLIIQSRKDEVVPPESARYIYERLGSPDKelVWLEDSGHVITLDKd 229

                        250
                 ....*....|....
gi 755288739 242 PDEFSKLIIDFAQQ 255
Cdd:COG1647  230 REEVAEEILDFLER 243
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 16-103 2.78e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 44.34  E-value: 2.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  16 LVLLHGWGLNAGVWHCIIDRLAPHFRLHLVDLPGYGRSN-----EFGAMSL-------SEMAEIVLQQAPKQAIWLGWSM 83
Cdd:PLN02824  32 LVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDkpnprSAPPNSFytfetwgEQLNDFCSDVVGDPAFVICNSV 111

                         90       100
                 ....*....|....*....|
gi 755288739  84 GGLVASQIALQHPERVSGLI 103
Cdd:PLN02824 112 GGVVGLQAAVDAPELVRGVM 131
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
 36-117 4.42e-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: 43.88  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   36 LAPHFRLHLVDLPGYgrsnEFGAMS------------LSEMAEIVLQQ-APKQAIWLGWSMGGLVASQIALQHPERVSGL 102
Cdd:pfam03096  52 ILENFCIYHVDAPGQ----EDGAASfpggypypsmddLADMLPVVLDHfRLKSVIGMGVGAGAYILARFALKHPERVEGL 127

                          90
                  ....*....|....*
gi 755288739  103 ITVASSPCFAAHDEW 117
Cdd:pfam03096 128 VLINPTPKAAGWIEW 142
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
16-179 9.42e-05

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 42.92  E-value: 9.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  16 LVLLHGWGLNAGVW------HCIIDRL-----APHFRLHLVDLPGYGRSNEFGAMS---LSEMAEIVLQQAPKQ------ 75
Cdd:COG2382  115 LYLLDGGGGDEQDWfdqgrlPTILDNLiaagkIPPMIVVMPDGGDGGDRGTEGPGNdafERFLAEELIPFVEKNyrvsad 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  76 ----AIwLGWSMGGLVASQIALQHPERVSGLITVASSPcfaahdeWPGIRPEVLAGFQQQLSEDFQRTVERFLaLQTlGT 151
Cdd:COG2382  195 pehrAI-AGLSMGGLAALYAALRHPDLFGYVGSFSGSF-------WWPPGDADRGGWAELLAAGAPKKPLRFY-LDV-GT 264

                        170       180       190
                 ....*....|....*....|....*....|
gi 755288739 152 -ESARQDARLLKAVVLQHQMP-EVSVLTGG 179
Cdd:COG2382  265 eDDLLEANRALAAALKAKGYDvEYREFPGG 294
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 14-252 1.77e-04

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 41.61  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   14 RDLVLLHGWGLNAGVWHCIIDRLAPHFRLHLVDLPGYGRS----NEFGAMsLSEMAEIVLQQAPKQAIWL-GWSMGGLVA 88
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGepplNSIEAL-ADEYAEALRQIQPEGPYALfGHSMGGMLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   89 SQIALQHPER---VSGLITVASSPCFAAHDEWPgiRPEVLAGFQQQLSeDFQRTVERFLALQ---TLGTESARQDARLLK 162
Cdd:pfam00975  80 FEVARRLERQgeaVRSLFLSDASAPHTVRYEAS--RAPDDDEVVAEFT-DEGGTPEELLEDEellSMLLPALRADYRALE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  163 -AVVLQHQMPEVSVLTGGLDILRTADLRealagcslpflriygyldglvprnvASLLDSKWPHTQSVVMKGCAHAPFVSH 241
Cdd:pfam00975 157 sYSCPPLDAQSATLFYGSDDPLHDADDL-------------------------AEWVRDHTPGEFDVHVFDGDHFYLIEH 211

                         250
                  ....*....|.
gi 755288739  242 PDEFSKLIIDF 252
Cdd:pfam00975 212 LEAVLEIIEAK 222
PRK10673 PRK10673
esterase;
45-109 2.01e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 38.56  E-value: 2.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755288739  45 VDLPGYGRSNEFGAMSLSEMAEIVLQ----QAPKQAIWLGWSMGGLVASQIALQHPERVSGLITVASSP 109
Cdd:PRK10673  48 VDMRNHGLSPRDPVMNYPAMAQDLLDtldaLQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAP 116
PRK05855 PRK05855
SDR family oxidoreductase;
11-66 2.75e-03

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 38.81  E-value: 2.75e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755288739  11 EGDRD---LVLLHGWGLNAGVWHCIIDRLAPHFRLHLVDLPGYGRSN---EFGAMSLSEMAE 66
Cdd:PRK05855  20 WGDPDrptVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSapkRTAAYTLARLAD 81
YpfH COG0400
Predicted esterase [General function prediction only];
16-122 3.34e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 37.58  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739  16 LVLLHGWGLNAGVWHCIIDRLA-PHFRL------HLVDLPGY---------GRSNEFGAM-SLSEMAEIVLQQA------ 72
Cdd:COG0400    8 VVLLHGYGGDEEDLLPLAPELAlPGAAVlaprapVPEGPGGRawfdlsfleGREDEEGLAaAAEALAAFIDELEarygid 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 755288739  73 PKQAIWLGWSMGGLVASQIALQHPERVSGLitVASSPCFAAHDEWPGIRP 122
Cdd:COG0400   88 PERIVLAGFSQGAAMALSLALRRPELLAGV--VALSGYLPGEEALPAPEA 135
metX PRK00175
homoserine O-acetyltransferase; Provisional
 79-109 3.57e-03

homoserine O-acetyltransferase; Provisional


Pssm-ID: 234678 [Multi-domain]  Cd Length: 379  Bit Score: 38.25  E-value: 3.57e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 755288739  79 LGWSMGGLVASQIALQHPERVSGLITVASSP 109
Cdd:PRK00175 152 VGGSMGGMQALEWAIDYPDRVRSALVIASSA 182
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
60-147 4.33e-03

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 38.49  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755288739   60 SLSEMAE----IVLQQAPKQAIWL-GWSMGGLVASQIALQHPER---VSGLITVASSPCfaAHDEW-----PGIRPEVLA 126
Cdd:PRK10252 1114 SLDEVCEahlaTLLEQQPHGPYHLlGYSLGGTLAQGIAARLRARgeeVAFLGLLDTWPP--ETQNWrekeaNGLDPEVLA 1191

                          90       100
                  ....*....|....*....|.
gi 755288739  127 gfqqqlseDFQRTVERFLALQ 147
Cdd:PRK10252 1192 --------EIDREREAFLAAQ 1204
MET2 COG2021
Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine ...
 79-109 4.94e-03

Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine O-acetyltransferase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 441624 [Multi-domain]  Cd Length: 355  Bit Score: 37.76  E-value: 4.94e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 755288739  79 LGWSMGGLVASQIALQHPERVSGLITVASSP 109
Cdd:COG2021  133 IGGSMGGMQALEWAVSYPDRVRRAIVIATAA 163
 
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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