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Conserved domains on  [gi|1160399839|ref|WP_079442944|]
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MULTISPECIES: alpha/beta fold hydrolase [Pseudomonas]

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, ...
 28-320 4.59e-36

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: 130.12  E-value: 4.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839  28 TQTVDLAQVSIAYQSIGRaSDPALLLVMGLGGQLIHWPDevVVALCQQGFRVIRYDNRDVGLSTWRqapasanltfevlr 107
Cdd:COG0596     4 PRFVTVDGVRLHYREAGP-DGPPVVLLHGLPGSSYEWRP--LIPALAAGYRVIAPDLRGHGRSDKP-------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 108 yklglpvAAPYTLTDMADDALGLMDALQVRQFHVLGASMGGMIAQHLAAMAPQRVESLTLImtssgaeglpapnaalvql 187
Cdd:COG0596    67 -------AGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV------------------- 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 188 lsrrsapnravaleqqADLLAALgspyvkddrqvllhqAALSYDRAFNPEGVKRQiMAILAEPSRVPLLNQLRVPTLVVH 267
Cdd:COG0596   121 ----------------DEVLAAL---------------AEPLRRPGLAPEALAAL-LRALARTDLRERLARITVPTLVIW 168

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1160399839 268 GTADPLLPVMHGVHLAAHIQGSQLKLIPGLAHRFQEAFKAPLLAAVLPYLQAH 320
Cdd:COG0596   169 GEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 28-320 4.59e-36

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: 130.12  E-value: 4.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839  28 TQTVDLAQVSIAYQSIGRaSDPALLLVMGLGGQLIHWPDevVVALCQQGFRVIRYDNRDVGLSTWRqapasanltfevlr 107
Cdd:COG0596     4 PRFVTVDGVRLHYREAGP-DGPPVVLLHGLPGSSYEWRP--LIPALAAGYRVIAPDLRGHGRSDKP-------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 108 yklglpvAAPYTLTDMADDALGLMDALQVRQFHVLGASMGGMIAQHLAAMAPQRVESLTLImtssgaeglpapnaalvql 187
Cdd:COG0596    67 -------AGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV------------------- 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 188 lsrrsapnravaleqqADLLAALgspyvkddrqvllhqAALSYDRAFNPEGVKRQiMAILAEPSRVPLLNQLRVPTLVVH 267
Cdd:COG0596   121 ----------------DEVLAAL---------------AEPLRRPGLAPEALAAL-LRALARTDLRERLARITVPTLVIW 168

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1160399839 268 GTADPLLPVMHGVHLAAHIQGSQLKLIPGLAHRFQEAFKAPLLAAVLPYLQAH 320
Cdd:COG0596   169 GEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 49-299 1.81e-20

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: 88.72  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839  49 PALLLVMGLGGQLIHWPdEVVVALCQQGFRVIRYDNRDVGLSTwrqapasanltfevlryklGLPVAAPYTLTDMADDAL 128
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWR-KLAPALARDGFRVIALDLRGFGKSS-------------------RPKAQDDYRTDDLAEDLE 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 129 GLMDALQVRQFHVLGASMGGMIAQHLAAMAPQRVESLTLIMTSSGAEGLPAPNAALVQLLSRRsaPNRAVALEQQADLLA 208
Cdd:pfam00561  61 YILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGF--FDGFVADFAPNPLGR 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 209 ALGSPYVKDDRQVLLHQAALSYDRAFNPEGVKRQIM---------AILAEPSRVPLLNQLRVPTLVVHGTADPLLPVMHG 279
Cdd:pfam00561 139 LVAKLLALLLLRLRLLKALPLLNKRFPSGDYALAKSlvtgallfiETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQAL 218

                         250       260
                  ....*....|....*....|
gi 1160399839 280 VHLAAHIQGSQLKLIPGLAH 299
Cdd:pfam00561 219 EKLAQLFPNARLVVIPDAGH 238
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 29-299 2.35e-16

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 78.83  E-value: 2.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839  29 QTVDLAQVSIAYQSIGRASDPALLLVMGLGGQLIHWpdEVVVALCQQGFRVIRYDNRDVGLSTWRQAPASanltfevlry 108
Cdd:PRK14875  112 RKARIGGRTVRYLRLGEGDGTPVVLIHGFGGDLNNW--LFNHAALAAGRPVIALDLPGHGASSKAVGAGS---------- 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 109 klglpvaapytLTDMADDALGLMDALQVRQFHVLGASMGGMIAQHLAAMAPQRVESLTLImtSSGAEGlPAPNAALVQLL 188
Cdd:PRK14875  180 -----------LDELAAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLI--APAGLG-PEINGDYIDGF 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 189 SRrsAPNRAvaleQQADLLAALGSPYVKDDRQVLlhQAALSYDRAfnpEGVKRQIMAI---LAEPSR-----VPLLNQLR 260
Cdd:PRK14875  246 VA--AESRR----ELKPVLELLFADPALVTRQMV--EDLLKYKRL---DGVDDALRALadaLFAGGRqrvdlRDRLASLA 314

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1160399839 261 VPTLVVHGTADPLLPVMHGVHLAAHIqgsQLKLIPGLAH 299
Cdd:PRK14875  315 IPVLVIWGEQDRIIPAAHAQGLPDGV---AVHVLPGAGH 350
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 28-320 4.59e-36

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: 130.12  E-value: 4.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839  28 TQTVDLAQVSIAYQSIGRaSDPALLLVMGLGGQLIHWPDevVVALCQQGFRVIRYDNRDVGLSTWRqapasanltfevlr 107
Cdd:COG0596     4 PRFVTVDGVRLHYREAGP-DGPPVVLLHGLPGSSYEWRP--LIPALAAGYRVIAPDLRGHGRSDKP-------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 108 yklglpvAAPYTLTDMADDALGLMDALQVRQFHVLGASMGGMIAQHLAAMAPQRVESLTLImtssgaeglpapnaalvql 187
Cdd:COG0596    67 -------AGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV------------------- 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 188 lsrrsapnravaleqqADLLAALgspyvkddrqvllhqAALSYDRAFNPEGVKRQiMAILAEPSRVPLLNQLRVPTLVVH 267
Cdd:COG0596   121 ----------------DEVLAAL---------------AEPLRRPGLAPEALAAL-LRALARTDLRERLARITVPTLVIW 168

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1160399839 268 GTADPLLPVMHGVHLAAHIQGSQLKLIPGLAHRFQEAFKAPLLAAVLPYLQAH 320
Cdd:COG0596   169 GEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 49-299 1.81e-20

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: 88.72  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839  49 PALLLVMGLGGQLIHWPdEVVVALCQQGFRVIRYDNRDVGLSTwrqapasanltfevlryklGLPVAAPYTLTDMADDAL 128
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWR-KLAPALARDGFRVIALDLRGFGKSS-------------------RPKAQDDYRTDDLAEDLE 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 129 GLMDALQVRQFHVLGASMGGMIAQHLAAMAPQRVESLTLIMTSSGAEGLPAPNAALVQLLSRRsaPNRAVALEQQADLLA 208
Cdd:pfam00561  61 YILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGF--FDGFVADFAPNPLGR 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 209 ALGSPYVKDDRQVLLHQAALSYDRAFNPEGVKRQIM---------AILAEPSRVPLLNQLRVPTLVVHGTADPLLPVMHG 279
Cdd:pfam00561 139 LVAKLLALLLLRLRLLKALPLLNKRFPSGDYALAKSlvtgallfiETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQAL 218

                         250       260
                  ....*....|....*....|
gi 1160399839 280 VHLAAHIQGSQLKLIPGLAH 299
Cdd:pfam00561 219 EKLAQLFPNARLVVIPDAGH 238
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 29-299 2.35e-16

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 78.83  E-value: 2.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839  29 QTVDLAQVSIAYQSIGRASDPALLLVMGLGGQLIHWpdEVVVALCQQGFRVIRYDNRDVGLSTWRQAPASanltfevlry 108
Cdd:PRK14875  112 RKARIGGRTVRYLRLGEGDGTPVVLIHGFGGDLNNW--LFNHAALAAGRPVIALDLPGHGASSKAVGAGS---------- 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 109 klglpvaapytLTDMADDALGLMDALQVRQFHVLGASMGGMIAQHLAAMAPQRVESLTLImtSSGAEGlPAPNAALVQLL 188
Cdd:PRK14875  180 -----------LDELAAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLI--APAGLG-PEINGDYIDGF 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 189 SRrsAPNRAvaleQQADLLAALGSPYVKDDRQVLlhQAALSYDRAfnpEGVKRQIMAI---LAEPSR-----VPLLNQLR 260
Cdd:PRK14875  246 VA--AESRR----ELKPVLELLFADPALVTRQMV--EDLLKYKRL---DGVDDALRALadaLFAGGRqrvdlRDRLASLA 314

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1160399839 261 VPTLVVHGTADPLLPVMHGVHLAAHIqgsQLKLIPGLAH 299
Cdd:PRK14875  315 IPVLVIWGEQDRIIPAAHAQGLPDGV---AVHVLPGAGH 350
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
36-319 4.24e-14

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 70.42  E-value: 4.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839  36 VSIAYQSIGRASDP--ALLLVMGLGGQLIHWpDEVVVALCQQGFRVIRYDNRDVGLSTWRQApasanltfevlryklglp 113
Cdd:COG2267    14 LRLRGRRWRPAGSPrgTVVLVHGLGEHSGRY-AELAEALAAAGYAVLAFDLRGHGRSDGPRG------------------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 114 vaAPYTLTDMADDALGLMDALQVR---QFHVLGASMGGMIAQHLAAMAPQRVESLTLIMTSSGAEGLPAPNAALVqllsr 190
Cdd:COG2267    75 --HVDSFDDYVDDLRAALDALRARpglPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWL----- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 191 rsapnravaleqqadllaalgspyvkddRQVLLHQAalsydrafnpegvkrqimailaepsrvplLNQLRVPTLVVHGTA 270
Cdd:COG2267   148 ----------------------------RALRLAEA-----------------------------LARIDVPVLVLHGGA 170

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1160399839 271 DPLLPVMHGVHLAAHI-QGSQLKLIPGLAH-RFQEAFKAPLLAAVLPYLQA 319
Cdd:COG2267   171 DRVVPPEAARRLAARLsPDVELVLLPGARHeLLNEPAREEVLAAILAWLER 221
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 66-299 2.85e-11

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: 62.62  E-value: 2.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839  66 DEVVVALCQQGFRVIRYDNRDVGLSTwrqapasanltfevlryklGLPVAAPyTLTDMADDALGLMDALQVRQFH----V 141
Cdd:pfam12146  21 AHLADALAAQGFAVYAYDHRGHGRSD-------------------GKRGHVP-SFDDYVDDLDTFVDKIREEHPGlplfL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 142 LGASMGGMIAQHLAAMAPQRVESLTLimtSSGAEGLPAPNAALVQLLSRRSAPNRAVALEQQADLLAALGSpyvkDDRQV 221
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLIL---SAPALKIKPYLAPPILKLLAKLLGKLFPRLRVPNNLLPDSLS----RDPEV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 222 llhQAALSYD-------RAFNPEGVKRQIMAILAepsrvpLLNQLRVPTLVVHGTADPLLPVMHGVHLAAHIQGS--QLK 292
Cdd:pfam12146 154 ---VAAYAADplvhggiSARTLYELLDAGERLLR------RAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTdkTLK 224


                  ....*..
gi 1160399839 293 LIPGLAH 299
Cdd:pfam12146 225 LYPGLYH 231
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
49-320 1.08e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 55.02  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839  49 PALLLVMGLGGQLIHWPDEVVVALCQQGFRVIRYDNRDVGLS--TWRqapasanltfevlryklglpvaapytlTDMADD 126
Cdd:COG1506    24 PVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESagDWG---------------------------GDEVDD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 127 ALGLMDALQVRQF------HVLGASMGGMIAQHLAAMAPQRVesltlimtssgaeglpapnAALVqllSRRSAPNraval 200
Cdd:COG1506    77 VLAAIDYLAARPYvdpdriGIYGHSYGGYMALLAAARHPDRF-------------------KAAV---ALAGVSD----- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 201 eqqadllaalgspyvkddrqvLLHQAALSYDRAFNPEGVKRQIMAILAEPSRVPLLNQLRVPTLVVHGTADPLLPVMHGV 280
Cdd:COG1506   130 ---------------------LRSYYGTTREYTERLMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRVPPEQAE 188

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1160399839 281 HLAAHIQG----SQLKLIPGLAHRFQEAFKAPLLAAVLPYLQAH 320
Cdd:COG1506   189 RLYEALKKagkpVELLVYPGEGHGFSGAGAPDYLERILDFLDRH 232
PRK10673 PRK10673
esterase;
74-168 6.61e-08

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 52.81  E-value: 6.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839  74 QQGFRVIRYDNRDVGLStwrqaPASANLTFEvlryklglpvaapytltDMADDALGLMDALQVRQFHVLGASMGGMIAQH 153
Cdd:PRK10673   40 VNDHDIIQVDMRNHGLS-----PRDPVMNYP-----------------AMAQDLLDTLDALQIEKATFIGHSMGGKAVMA 97

                          90
                  ....*....|....*
gi 1160399839 154 LAAMAPQRVESLTLI 168
Cdd:PRK10673   98 LTALAPDRIDKLVAI 112
PRK05855 PRK05855
SDR family oxidoreductase;
36-143 3.78e-07

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 51.52  E-value: 3.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839  36 VSIAYQSIGRASDPALLLVMGlggqlihWPD--EV---VVALCQQGFRVIRYDNRDVGLSTwrqAPASanltfevlrykl 110
Cdd:PRK05855   13 VRLAVYEWGDPDRPTVVLVHG-------YPDnhEVwdgVAPLLADRFRVVAYDVRGAGRSS---APKR------------ 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1160399839 111 glpvAAPYTLTDMADDALGLMDALQV-RQFHVLG 143
Cdd:PRK05855   71 ----TAAYTLARLADDFAAVIDAVSPdRPVHLLA 100
PRK06765 PRK06765
homoserine O-acetyltransferase; Provisional
 107-172 3.68e-06

homoserine O-acetyltransferase; Provisional


Pssm-ID: 235859 [Multi-domain]  Cd Length: 389  Bit Score: 48.16  E-value: 3.68e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1160399839 107 RYKLGLPVaapYTLTDMADDALGLMDALQVRQFH-VLGASMGGMIAQHLAAMAPQRVESLTLIMTSS 172
Cdd:PRK06765  133 PYGMDFPV---VTILDFVRVQKELIKSLGIARLHaVMGPSMGGMQAQEWAVHYPHMVERMIGVIGNP 196
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
118-294 1.96e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 45.32  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 118 YTLTDMADDALGLMDALQ--VRQFHVLGASMGGMIAQHLAAMAPQrVESLTLImtsSGAEGLPAPNAALVQLLSRRSAPN 195
Cdd:COG1647    63 TTWEDWLEDVEEAYEILKagYDKVIVIGLSMGGLLALLLAARYPD-VAGLVLL---SPALKIDDPSAPLLPLLKYLARSL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 196 RAVALEQQADLLAALGSPYVkddrqvllHQAALsydrafnpegvkRQIMAILAEPSRvpLLNQLRVPTLVVHGTADPLLP 275
Cdd:COG1647   139 RGIGSDIEDPEVAEYAYDRT--------PLRAL------------AELQRLIREVRR--DLPKITAPTLIIQSRKDEVVP 196

                         170
                  ....*....|....*....
gi 1160399839 276 VMHGVHLAAHIQGSQLKLI 294
Cdd:COG1647   197 PESARYIYERLGSPDKELV 215
metX PRK00175
homoserine O-acetyltransferase; Provisional
 119-171 6.03e-05

homoserine O-acetyltransferase; Provisional


Pssm-ID: 234678 [Multi-domain]  Cd Length: 379  Bit Score: 44.41  E-value: 6.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1160399839 119 TLTDMADDALGLMDALQVRQFH-VLGASMGGMIAQHLAAMAPQRVESLTLIMTS 171
Cdd:PRK00175  128 TIRDWVRAQARLLDALGITRLAaVVGGSMGGMQALEWAIDYPDRVRSALVIASS 181
PRK08775 PRK08775
homoserine O-succinyltransferase;
116-204 5.21e-03

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 38.23  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1160399839 116 APYTLTDMADDALGLMDALQVRQFH-VLGASMGGMIAQHLAAMAPQRVESLTLImtsSGAEgLPAPNAAlvqllSRRSAP 194
Cdd:PRK08775  116 VPIDTADQADAIALLLDALGIARLHaFVGYSYGALVGLQFASRHPARVRTLVVV---SGAH-RAHPYAA-----AWRALQ 186

                          90
                  ....*....|
gi 1160399839 195 NRAVALEQQA 204
Cdd:PRK08775  187 RRAVALGQLQ 196
 
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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