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Conserved domains on  [gi|914605143|ref|WP_050599570|]
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MULTISPECIES: alpha/beta fold hydrolase [Alphaproteobacteria]

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, ...
 37-319 6.05e-25

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


:

Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 100.08  E-value: 6.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  37 REEGFVEVGGARVHYLRWGRRDRPkLLMTHGFLAHARCFAFIAPYLAEDYDVVAFDLAGMGDSEM-RGVADIAARGKEFV 115
Cdd:COG0596    2 STPRFVTVDGVRLHYREAGPDGPP-VVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKpAGGYTLDDLADDLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143 116 EISEALDLfadgSRPTIIAHSFGSGAALTAVSQSPDAFAGVIVCDlmvmrpeklekywtmgrsspgsgnpdkpvrrypty 195
Cdd:COG0596   81 ALLDALGL----ERVVLVGHSMGGMVALELAARHPERVAGLVLVD----------------------------------- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143 196 eAARERYIlsppqavgEPFLMDYMAYHSLRRdgeewtwkfspeVFRRSNKPDEWLTVGQrlVDAPgrKAIVYGEKSQLFD 275
Cdd:COG0596  122 -EVLAALA--------EPLRRPGLAPEALAA------------LLRALARTDLRERLAR--ITVP--TLVIWGEKDPIVP 176

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 914605143 276 RDSARYIRELGGGkIPIVAVPDARHHLMLDQPLAFVAALRAVLA 319
Cdd:COG0596  177 PALARRLAELLPN-AELVVLPGAGHFPPLEQPEAFAAALRDFLA 219
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 37-319 6.05e-25

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


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 100.08  E-value: 6.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  37 REEGFVEVGGARVHYLRWGRRDRPkLLMTHGFLAHARCFAFIAPYLAEDYDVVAFDLAGMGDSEM-RGVADIAARGKEFV 115
Cdd:COG0596    2 STPRFVTVDGVRLHYREAGPDGPP-VVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKpAGGYTLDDLADDLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143 116 EISEALDLfadgSRPTIIAHSFGSGAALTAVSQSPDAFAGVIVCDlmvmrpeklekywtmgrsspgsgnpdkpvrrypty 195
Cdd:COG0596   81 ALLDALGL----ERVVLVGHSMGGMVALELAARHPERVAGLVLVD----------------------------------- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143 196 eAARERYIlsppqavgEPFLMDYMAYHSLRRdgeewtwkfspeVFRRSNKPDEWLTVGQrlVDAPgrKAIVYGEKSQLFD 275
Cdd:COG0596  122 -EVLAALA--------EPLRRPGLAPEALAA------------LLRALARTDLRERLAR--ITVP--TLVIWGEKDPIVP 176

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 914605143 276 RDSARYIRELGGGkIPIVAVPDARHHLMLDQPLAFVAALRAVLA 319
Cdd:COG0596  177 PALARRLAELLPN-AELVVLPGAGHFPPLEQPEAFAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 62-307 2.41e-12

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: 65.60  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143   62 LLMTHGFLAHARCFAFIAPYLAED-YDVVAFDLAGMGDSEMR------GVADIAargKEFVEISEALDLfadgSRPTIIA 134
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPkaqddyRTDDLA---EDLEYILEALGL----EKVNLVG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  135 HSFGSGAALTAVSQSPDAFAGVIvcdlmvmrpeklekywTMGRSSPGSGNPDKPVRRYPTYEAARERYILSPPQAVGEPF 214
Cdd:pfam00561  76 HSMGGLIALAYAAKYPDRVKALV----------------LLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRL 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  215 LMDYMA----YHSLRRDGEEWTWKFSPEVFRRSNKPD----------EWLTVGQRLVDAPGRKAIVYGEKSQLFDRDSAR 280
Cdd:pfam00561 140 VAKLLAllllRLRLLKALPLLNKRFPSGDYALAKSLVtgallfietwSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALE 219

                         250       260
                  ....*....|....*....|....*..
gi 914605143  281 YIRELGGGKIPIVaVPDARHHLMLDQP 307
Cdd:pfam00561 220 KLAQLFPNARLVV-IPDAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 41-151 6.31e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 53.41  E-value: 6.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  41 FVEVGGARVHYLRWGRRDRPKLLMTHGFLAHARCFAFIAPYLAEDYDVVAFDLAGMGDSEMR-GVADIAARGKEFVEISE 119
Cdd:PRK14875 113 KARIGGRTVRYLRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAvGAGSLDELAAAVLAFLD 192

                         90       100       110
                 ....*....|....*....|....*....|..
gi 914605143 120 ALDLfadgSRPTIIAHSFGSGAALTAVSQSPD 151
Cdd:PRK14875 193 ALGI----ERAHLVGHSMGGAVALRLAARAPQ 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 37-319 6.05e-25

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


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 100.08  E-value: 6.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  37 REEGFVEVGGARVHYLRWGRRDRPkLLMTHGFLAHARCFAFIAPYLAEDYDVVAFDLAGMGDSEM-RGVADIAARGKEFV 115
Cdd:COG0596    2 STPRFVTVDGVRLHYREAGPDGPP-VVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKpAGGYTLDDLADDLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143 116 EISEALDLfadgSRPTIIAHSFGSGAALTAVSQSPDAFAGVIVCDlmvmrpeklekywtmgrsspgsgnpdkpvrrypty 195
Cdd:COG0596   81 ALLDALGL----ERVVLVGHSMGGMVALELAARHPERVAGLVLVD----------------------------------- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143 196 eAARERYIlsppqavgEPFLMDYMAYHSLRRdgeewtwkfspeVFRRSNKPDEWLTVGQrlVDAPgrKAIVYGEKSQLFD 275
Cdd:COG0596  122 -EVLAALA--------EPLRRPGLAPEALAA------------LLRALARTDLRERLAR--ITVP--TLVIWGEKDPIVP 176

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 914605143 276 RDSARYIRELGGGkIPIVAVPDARHHLMLDQPLAFVAALRAVLA 319
Cdd:COG0596  177 PALARRLAELLPN-AELVVLPGAGHFPPLEQPEAFAAALRDFLA 219
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
36-159 3.78e-16

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 76.19  E-value: 3.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  36 PREEGFVEVGGARVHYLRWGRRDRPK--LLMTHGFLAHARCFAFIAPYLAE-DYDVVAFDLAGMGDSE-MRGVADIAArg 111
Cdd:COG2267    3 RRLVTLPTRDGLRLRGRRWRPAGSPRgtVVLVHGLGEHSGRYAELAEALAAaGYAVLAFDLRGHGRSDgPRGHVDSFD-- 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 914605143 112 kEFVE-ISEALDLFA--DGSRPTIIAHSFGSGAALTAVSQSPDAFAGVIVC 159
Cdd:COG2267   81 -DYVDdLRAALDALRarPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLL 130
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 62-307 2.41e-12

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: 65.60  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143   62 LLMTHGFLAHARCFAFIAPYLAED-YDVVAFDLAGMGDSEMR------GVADIAargKEFVEISEALDLfadgSRPTIIA 134
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPkaqddyRTDDLA---EDLEYILEALGL----EKVNLVG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  135 HSFGSGAALTAVSQSPDAFAGVIvcdlmvmrpeklekywTMGRSSPGSGNPDKPVRRYPTYEAARERYILSPPQAVGEPF 214
Cdd:pfam00561  76 HSMGGLIALAYAAKYPDRVKALV----------------LLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRL 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  215 LMDYMA----YHSLRRDGEEWTWKFSPEVFRRSNKPD----------EWLTVGQRLVDAPGRKAIVYGEKSQLFDRDSAR 280
Cdd:pfam00561 140 VAKLLAllllRLRLLKALPLLNKRFPSGDYALAKSLVtgallfietwSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALE 219

                         250       260
                  ....*....|....*....|....*..
gi 914605143  281 YIRELGGGKIPIVaVPDARHHLMLDQP 307
Cdd:pfam00561 220 KLAQLFPNARLVV-IPDAGHFAFLEGP 245
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 62-313 2.62e-08

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 53.25  E-value: 2.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143   62 LLMTHGFLAHarcFAFIAPYLAEDYDVVAFDLAGMGDSEmRGVADIAArgkeFVEISEALDLFADGSRPTIIAHSFGSGA 141
Cdd:pfam12697   1 VVLVHGAGLS---AAPLAALLAAGVAVLAPDLPGHGSSS-PPPLDLAD----LADLAALLDELGAARPVVLVGHSLGGAV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  142 ALTAVSQSPdaFAGVIVCDLMVmrpeklekywtmgrsspGSGNPDKPVRRYPTYEAARERYILSPPQAVGEPFLMDYMAY 221
Cdd:pfam12697  73 ALAAAAAAL--VVGVLVAPLAA-----------------PPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPAD 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  222 hslrrdgEEWTWKFSPEVFRRsnkpDEWLTVGQRLVDAPGRKAIVYGEKSQLFDRDSARYIRELGGGKipIVAVPDARHH 301
Cdd:pfam12697 134 -------AEWAAALARLAALL----AALALLPLAAWRDLPVPVLVLAEEDRLVPELAQRLLAALAGAR--LVVLPGAGHL 200

                         250
                  ....*....|..
gi 914605143  302 LmLDQPLAFVAA 313
Cdd:pfam12697 201 P-LDDPEEVAEA 211
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 41-151 6.31e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 53.41  E-value: 6.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  41 FVEVGGARVHYLRWGRRDRPKLLMTHGFLAHARCFAFIAPYLAEDYDVVAFDLAGMGDSEMR-GVADIAARGKEFVEISE 119
Cdd:PRK14875 113 KARIGGRTVRYLRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAvGAGSLDELAAAVLAFLD 192

                         90       100       110
                 ....*....|....*....|....*....|..
gi 914605143 120 ALDLfadgSRPTIIAHSFGSGAALTAVSQSPD 151
Cdd:PRK14875 193 ALGI----ERAHLVGHSMGGAVALRLAARAPQ 220
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 59-202 4.81e-07

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: 49.91  E-value: 4.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143   59 RPKLLMTHGFLAHARCFAFIAPYLAE-DYDVVAFDLAGMGDSE-MRG--------VADIAARGKEFVEISEALDLFadgs 128
Cdd:pfam12146   4 RAVVVLVHGLGEHSGRYAHLADALAAqGFAVYAYDHRGHGRSDgKRGhvpsfddyVDDLDTFVDKIREEHPGLPLF---- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  129 rptIIAHSFGSGAALTAVSQSPDAFAGVIVC------DLMVMRPEKLEKYWTMGRSSPGS--GNPDKPVRRYpTYEAARE 200
Cdd:pfam12146  80 ---LLGHSMGGLIAALYALRYPDKVDGLILSapalkiKPYLAPPILKLLAKLLGKLFPRLrvPNNLLPDSLS-RDPEVVA 155


                  ..
gi 914605143  201 RY 202
Cdd:pfam12146 156 AY 157
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
66-320 1.36e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 45.70  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  66 HGFLAHARCFAFIAPYLAE-DYDVVAFDLAGMGDSEmrgvADIAARG-KEFVE-ISEALD-LFADGSRPTIIAHSFGSGA 141
Cdd:COG1647   22 HGFTGSPAEMRPLAEALAKaGYTVYAPRLPGHGTSP----EDLLKTTwEDWLEdVEEAYEiLKAGYDKVIVIGLSMGGLL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143 142 ALTAVSQSPDAFAGVIVC-----DLMVMRPEKLEKYWTmgRSSPGSGNPDKpvrrypTYEAARERYILSPPQAVGEpfLM 216
Cdd:COG1647   98 ALLLAARYPDVAGLVLLSpalkiDDPSAPLLPLLKYLA--RSLRGIGSDIE------DPEVAEYAYDRTPLRALAE--LQ 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143 217 DYMAYhsLRRDGEEWTwkfSPeVFrrsnkpdewltvgqrlvdapgrkaIVYGEKSQLFDRDSARYI-RELGGGKIPIVAV 295
Cdd:COG1647  168 RLIRE--VRRDLPKIT---AP-TL------------------------IIQSRKDEVVPPESARYIyERLGSPDKELVWL 217

                        250       260
                 ....*....|....*....|....*
gi 914605143 296 PDARHHLMLDQPLAFVAalRAVLAF 320
Cdd:COG1647  218 EDSGHVITLDKDREEVA--EEILDF 240
PRK05855 PRK05855
SDR family oxidoreductase;
38-99 5.72e-05

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 44.59  E-value: 5.72e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914605143  38 EEGFVEVGGARVHYLRWGRRDRPKLLMTHGFLAHARCFAFIAPYLAEDYDVVAFDLAGMGDS 99
Cdd:PRK05855   4 RRTVVSSDGVRLAVYEWGDPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRS 65
PLN02578 PLN02578
hydrolase
 46-158 1.22e-04

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 43.29  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  46 GARVHYLRWGRRdrPKLLMTHGFLAHARCFAFIAPYLAEDYDVVAFDLAGMGDSE-----------MRGVADIAargKEF 114
Cdd:PLN02578  75 GHKIHYVVQGEG--LPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDkalieydamvwRDQVADFV---KEV 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 914605143 115 VEisealdlfadgsRPTIIA-HSFGSGAALTAVSQSPDAFAGVIV 158
Cdd:PLN02578 150 VK------------EPAVLVgNSLGGFTALSTAVGYPELVAGVAL 182
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 53-100 2.96e-04

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 42.18  E-value: 2.96e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 914605143  53 RW-----GRRDRPKLLMTHGFLAHARCFAFIAPYLAEDYDVVAFDLAGMGDSE 100
Cdd:PLN03084 116 RWfcvesGSNNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSD 168
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 29-158 9.46e-04

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 40.28  E-value: 9.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  29 FAWALSVPREEGFVEVGG-----ARVHYLRWGRRDRPKLLMTHGFLAHARCFAFIAPYLAE-DYDVVAFDLAGMGDSE-- 100
Cdd:COG1073    2 FPPSDKVNKEDVTFKSRDgiklaGDLYLPAGASKKYPAVVVAHGNGGVKEQRALYAQRLAElGFNVLAFDYRGYGESEge 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914605143 101 MRGVADIAARGkefveISEALD-----LFADGSRPTIIAHSFGSGAALTAVSQSPDaFAGVIV 158
Cdd:COG1073   82 PREEGSPERRD-----ARAAVDylrtlPGVDPERIGLLGISLGGGYALNAAATDPR-VKAVIL 138
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 265-318 7.92e-03

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 38.30  E-value: 7.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914605143  265 IVYGEKSQLFDRDSARYIRELGGGK----------IPIVAVPDARHHLMLDQPLAFVAALRAVL 318
Cdd:PLN02980 1573 LVVGEKDVKFKQIAQKMYREIGKSKesgndkgkeiIEIVEIPNCGHAVHLENPLPVIRALRKFL 1636
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 60-153 8.88e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 37.51  E-value: 8.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  60 PKLLMTHGFLAHARCFAFIAPYLAEDYDVVAFDLAGMGDSE--------MRGVAD-IAARGKEFVEisealdlfadgsRP 130
Cdd:PLN02679  89 PPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDkppgfsytMETWAElILDFLEEVVQ------------KP 156

                         90       100
                 ....*....|....*....|....
gi 914605143 131 TI-IAHSFGSGAALTAVSQSPDAF 153
Cdd:PLN02679 157 TVlIGNSVGSLACVIAASESTRDL 180
PRK10673 PRK10673
esterase;
58-161 9.03e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 37.02  E-value: 9.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914605143  58 DRPKLLMTHGFLAHARCFAFIAPYLAEDYDVVAFDLAGMGDSEMRGVADIAARGKEFVEISEALDLfadgSRPTIIAHSF 137
Cdd:PRK10673  15 NNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI----EKATFIGHSM 90

                         90       100
                 ....*....|....*....|....
gi 914605143 138 GSGAALTAVSQSPDAFAGVIVCDL 161
Cdd:PRK10673  91 GGKAVMALTALAPDRIDKLVAIDI 114
 
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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