|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
38-312 |
8.15e-28 |
|
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: 107.78 E-value: 8.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 38 FIEIDEVltlrRMIVRAPAPKG-TVLLLHGFPETLTVWNDIATTLAHDYDVHAFDWPGYGQSSRPASerfSYAPMAYAQV 116
Cdd:COG0596 6 FVTVDGV----RLHYREAGPDGpPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAG---GYTLDDLADD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 117 LKAYIERAGIDRskLVIYATDIGALPVLLLALDEPTIARQIIVgdfapfdrphymwenlqnlkaeptasptrayMNKTSD 196
Cdd:COG0596 79 LAALLDALGLER--VVLVGHSMGGMVALELAARHPERVAGLVL-------------------------------VDEVLA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 197 EILQNVHRRGLSPaeqfdlpadvqrdmtrswsldgmtsaDAFAHYYANFTGDQhyLEANLTRLKTPVKVIWGEKDIYIAR 276
Cdd:COG0596 126 ALAEPLRRPGLAP--------------------------EALAALLRALARTD--LRERLARITVPTLVIWGEKDPIVPP 177
|
250 260 270
....*....|....*....|....*....|....*..
gi 517053230 277 EMGIEFAGKI-GAKVDILSGIGHFPHLQNSKQTVEEI 312
Cdd:COG0596 178 ALARRLAELLpNAELVVLPGAGHFPPLEQPEAFAAAL 214
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
59-304 |
7.40e-16 |
|
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: 75.62 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 59 GTVLLLHGFPETLTVWNDIATTLAHD-YDVHAFDWPGYGQSSRPaSERFSYAPMAYAQVLKAYIERAGIDrsKLVIYATD 137
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRP-KAQDDYRTDDLAEDLEYILEALGLE--KVNLVGHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 138 IGALPVLLLALDEPTIARQII----VGDFAPFDRPHYMW-----ENLQNLKAEPTASPTRAYMNKTSDEILQNVHRRGLS 208
Cdd:pfam00561 78 MGGLIALAYAAKYPDRVKALVllgaLDPPHELDEADRFIlalfpGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 209 PaeQFDLPADVQRDMTRswSLDGMTSADAFAHYYANFTGDQhyleanLTRLKTPVKVIWGEKDIYIAREMGIEFAGKI-G 287
Cdd:pfam00561 158 P--LLNKRFPSGDYALA--KSLVTGALLFIETWSTELRAKF------LGRLDEPTLIIWGDQDPLVPPQALEKLAQLFpN 227
|
250
....*....|....*..
gi 517053230 288 AKVDILSGIGHFPHLQN 304
Cdd:pfam00561 228 ARLVVIPDAGHFAFLEG 244
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
25-317 |
2.15e-12 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 66.89 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 25 TSASREAAQDAVD---------FIEIDEvlTLRRMIVRAPAPKGTVLLLHGFPETLTVWNDIATTLAHDYDVHAFDWPGY 95
Cdd:PRK14875 91 APFARRFAPEGIDeedagpaprKARIGG--RTVRYLRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGH 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 96 GQSSrPASERFSYAPMayAQVLKAYIERAGIDRSKLViyATDIGALPVLLLALDEPTIARQI-----------IVGDFap 164
Cdd:PRK14875 169 GASS-KAVGAGSLDEL--AAAVLAFLDALGIERAHLV--GHSMGGAVALRLAARAPQRVASLtliapaglgpeINGDY-- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 165 fdrphymwenLQNLKAEPTasptraymnktsdeilqnvhRRGLSP--AEQFDLPADVQR----DMTRSWSLDGMTSA-DA 237
Cdd:PRK14875 242 ----------IDGFVAAES--------------------RRELKPvlELLFADPALVTRqmveDLLKYKRLDGVDDAlRA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 238 FAHyyANFTGD--QHYLEANLTRLKTPVKVIWGEKDIYIAREMGIEFAGkiGAKVDILSGIGHFPHLQNSKQTVEEINTS 315
Cdd:PRK14875 292 LAD--ALFAGGrqRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQGLPD--GVAVHVLPGAGHMPQMEAAADVNRLLAEF 367
|
..
gi 517053230 316 FR 317
Cdd:PRK14875 368 LG 369
|
|
| bioH |
TIGR01738 |
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ... |
61-167 |
7.27e-03 |
|
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: 37.49 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 61 VLLLHGFPETLTVWNDIATTLAHDYDVHAFDWPGYGQSSrpaserfSYAPMAYAQVLKAYIERAGidrSKLVIYATDIGA 140
Cdd:TIGR01738 7 LVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSR-------GFGPLSLADMAEAIAAQAP---DPAIWLGWSLGG 76
|
90 100
....*....|....*....|....*...
gi 517053230 141 LPVLLLALDEPTIARQII-VGDFAPFDR 167
Cdd:TIGR01738 77 LVALHIAATHPDRVRALVtVASSPCFSA 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
38-312 |
8.15e-28 |
|
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: 107.78 E-value: 8.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 38 FIEIDEVltlrRMIVRAPAPKG-TVLLLHGFPETLTVWNDIATTLAHDYDVHAFDWPGYGQSSRPASerfSYAPMAYAQV 116
Cdd:COG0596 6 FVTVDGV----RLHYREAGPDGpPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAG---GYTLDDLADD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 117 LKAYIERAGIDRskLVIYATDIGALPVLLLALDEPTIARQIIVgdfapfdrphymwenlqnlkaeptasptrayMNKTSD 196
Cdd:COG0596 79 LAALLDALGLER--VVLVGHSMGGMVALELAARHPERVAGLVL-------------------------------VDEVLA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 197 EILQNVHRRGLSPaeqfdlpadvqrdmtrswsldgmtsaDAFAHYYANFTGDQhyLEANLTRLKTPVKVIWGEKDIYIAR 276
Cdd:COG0596 126 ALAEPLRRPGLAP--------------------------EALAALLRALARTD--LRERLARITVPTLVIWGEKDPIVPP 177
|
250 260 270
....*....|....*....|....*....|....*..
gi 517053230 277 EMGIEFAGKI-GAKVDILSGIGHFPHLQNSKQTVEEI 312
Cdd:COG0596 178 ALARRLAELLpNAELVVLPGAGHFPPLEQPEAFAAAL 214
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
59-304 |
7.40e-16 |
|
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: 75.62 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 59 GTVLLLHGFPETLTVWNDIATTLAHD-YDVHAFDWPGYGQSSRPaSERFSYAPMAYAQVLKAYIERAGIDrsKLVIYATD 137
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRP-KAQDDYRTDDLAEDLEYILEALGLE--KVNLVGHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 138 IGALPVLLLALDEPTIARQII----VGDFAPFDRPHYMW-----ENLQNLKAEPTASPTRAYMNKTSDEILQNVHRRGLS 208
Cdd:pfam00561 78 MGGLIALAYAAKYPDRVKALVllgaLDPPHELDEADRFIlalfpGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 209 PaeQFDLPADVQRDMTRswSLDGMTSADAFAHYYANFTGDQhyleanLTRLKTPVKVIWGEKDIYIAREMGIEFAGKI-G 287
Cdd:pfam00561 158 P--LLNKRFPSGDYALA--KSLVTGALLFIETWSTELRAKF------LGRLDEPTLIIWGDQDPLVPPQALEKLAQLFpN 227
|
250
....*....|....*..
gi 517053230 288 AKVDILSGIGHFPHLQN 304
Cdd:pfam00561 228 ARLVVIPDAGHFAFLEG 244
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
25-317 |
2.15e-12 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 66.89 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 25 TSASREAAQDAVD---------FIEIDEvlTLRRMIVRAPAPKGTVLLLHGFPETLTVWNDIATTLAHDYDVHAFDWPGY 95
Cdd:PRK14875 91 APFARRFAPEGIDeedagpaprKARIGG--RTVRYLRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGH 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 96 GQSSrPASERFSYAPMayAQVLKAYIERAGIDRSKLViyATDIGALPVLLLALDEPTIARQI-----------IVGDFap 164
Cdd:PRK14875 169 GASS-KAVGAGSLDEL--AAAVLAFLDALGIERAHLV--GHSMGGAVALRLAARAPQRVASLtliapaglgpeINGDY-- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 165 fdrphymwenLQNLKAEPTasptraymnktsdeilqnvhRRGLSP--AEQFDLPADVQR----DMTRSWSLDGMTSA-DA 237
Cdd:PRK14875 242 ----------IDGFVAAES--------------------RRELKPvlELLFADPALVTRqmveDLLKYKRLDGVDDAlRA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 238 FAHyyANFTGD--QHYLEANLTRLKTPVKVIWGEKDIYIAREMGIEFAGkiGAKVDILSGIGHFPHLQNSKQTVEEINTS 315
Cdd:PRK14875 292 LAD--ALFAGGrqRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQGLPD--GVAVHVLPGAGHMPQMEAAADVNRLLAEF 367
|
..
gi 517053230 316 FR 317
Cdd:PRK14875 368 LG 369
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
54-170 |
2.35e-12 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 65.41 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 54 APAPKGTVLLLHGFPETLTVWNDIATTLA-HDYDVHAFDWPGYGQSSRPASERFSYApmAYAQVLKAYIERAGIDRS-KL 131
Cdd:COG2267 24 AGSPRGTVVLVHGLGEHSGRYAELAEALAaAGYAVLAFDLRGHGRSDGPRGHVDSFD--DYVDDLRAALDALRARPGlPV 101
|
90 100 110
....*....|....*....|....*....|....*....
gi 517053230 132 VIYATDIGALPVLLLALDEPTIARQIIVGDFAPFDRPHY 170
Cdd:COG2267 102 VLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLL 140
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
55-289 |
1.17e-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: 63.39 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 55 PAPKGTVLLLHGFPETLTVWNDIATTLA-HDYDVHAFDWPGYGQSS--RPASERFSyapmAYAQVLKAYIERAGID--RS 129
Cdd:pfam12146 1 GEPRAVVVLVHGLGEHSGRYAHLADALAaQGFAVYAYDHRGHGRSDgkRGHVPSFD----DYVDDLDTFVDKIREEhpGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 130 KLVIYATDIGALPVLLLALDEPTIARQIIVgdFAPFDRPHymwenlqnlkaEPTASPTRAYMNKtsdeILQNVHRRGLSP 209
Cdd:pfam12146 77 PLFLLGHSMGGLIAALYALRYPDKVDGLIL--SAPALKIK-----------PYLAPPILKLLAK----LLGKLFPRLRVP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 210 AEqfDLPADVQRDMTRSWSLD------GMTSADAFAHYYAnfTGDQhyLEANLTRLKTPVKVIWGEKDIYIAREMGIEFA 283
Cdd:pfam12146 140 NN--LLPDSLSRDPEVVAAYAadplvhGGISARTLYELLD--AGER--LLRRAAAITVPLLLLHGGADRVVDPAGSREFY 213
|
....*.
gi 517053230 284 GKIGAK 289
Cdd:pfam12146 214 ERAGST 219
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
54-299 |
9.39e-09 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 55.31 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 54 APAPKGTVLLLHGFPETLTVWNDIATTLA-HDYDVHAFDWPGYGQSSRPASERFSYAPMAYAQVLKAYIERAGIDRSKLV 132
Cdd:COG1073 33 ASKKYPAVVVAHGNGGVKEQRALYAQRLAeLGFNVLAFDYRGYGESEGEPREEGSPERRDARAAVDYLRTLPGVDPERIG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 133 IYATDIGALPVLLLALDEPTIARQIIVgdfAPFDrphymweNLQNLKAEPTASPTRAYMnktsdeilqnvhrrglsPAEQ 212
Cdd:COG1073 113 LLGISLGGGYALNAAATDPRVKAVILD---SPFT-------SLEDLAAQRAKEARGAYL-----------------PGVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 213 FDLPADVQRDMTRSWsldgmtsaDAFAHyyanftgdqhyleanLTRLKTPVKVIWGEKDIYIAREMGIEFAGKIGAKVD- 291
Cdd:COG1073 166 YLPNVRLASLLNDEF--------DPLAK---------------IEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKEl 222
|
....*....
gi 517053230 292 -ILSGIGHF 299
Cdd:COG1073 223 lIVPGAGHV 231
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
61-303 |
2.86e-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: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 61 VLLLHGFPETLTvwnDIATTLAHDYDVHAFDWPGYGQSSRPAserFSYAPMA-YAQVLKAYIERAGIdrsklVIYATDIG 139
Cdd:pfam12697 1 VVLVHGAGLSAA---PLAALLAAGVAVLAPDLPGHGSSSPPP---LDLADLAdLAALLDELGAARPV-----VLVGHSLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 140 ALPVLLLALDEPTIARqIIVGDFAPFDRPHYMWENLQnlkaeptasptraymnktsdeilqnvHRRGLSPAEQFDLPADV 219
Cdd:pfam12697 70 GAVALAAAAAALVVGV-LVAPLAAPPGLLAALLALLA--------------------------RLGAALAAPAWLAAESL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 220 QRDMTRSWSLDGMTsADAFAHYYANFTGDQHYLEANLTRLKTPVKVIWGEKDIyIAREMGIEFAGKIGAKVDILSGIGHF 299
Cdd:pfam12697 123 ARGFLDDLPADAEW-AAALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRL-VPELAQRLLAALAGARLVVLPGAGHL 200
|
....
gi 517053230 300 PHLQ 303
Cdd:pfam12697 201 PLDD 204
|
|
| PLN03084 |
PLN03084 |
alpha/beta hydrolase fold protein; Provisional |
60-133 |
9.01e-08 |
|
alpha/beta hydrolase fold protein; Provisional
Pssm-ID: 178633 Cd Length: 383 Bit Score: 52.96 E-value: 9.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517053230 60 TVLLLHGFPETLTVWNDIATTLAHDYDVHAFDWPGYGQSSRP-ASERFSYAPMAYAQVLKAYIERAGIDRSKLVI 133
Cdd:PLN03084 129 PVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDKPqPGYGFNYTLDEYVSSLESLIDELKSDKVSLVV 203
|
|
| PRK05855 |
PRK05855 |
SDR family oxidoreductase; |
60-149 |
5.83e-07 |
|
SDR family oxidoreductase;
Pssm-ID: 235628 [Multi-domain] Cd Length: 582 Bit Score: 50.75 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 60 TVLLLHGFPETLTVWNDIATTLAHDYDVHAFDWPGYGQSSRPASERfSYAPMAYAQVLKAYIERAGIDRsklviyatdig 139
Cdd:PRK05855 27 TVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPKRTA-AYTLARLADDFAAVIDAVSPDR----------- 94
|
90
....*....|
gi 517053230 140 alPVLLLALD 149
Cdd:PRK05855 95 --PVHLLAHD 102
|
|
| PLN02679 |
PLN02679 |
hydrolase, alpha/beta fold family protein |
60-151 |
1.50e-06 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178283 [Multi-domain] Cd Length: 360 Bit Score: 49.07 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 60 TVLLLHGFPETLTVWNDIATTLAHDYDVHAFDWPGYGQSSRPASerFSYAPMAYAQVLKAYIERagIDRSKLVIYATDIG 139
Cdd:PLN02679 90 PVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGASDKPPG--FSYTMETWAELILDFLEE--VVQKPTVLIGNSVG 165
|
90
....*....|..
gi 517053230 140 ALPVLLLALDEP 151
Cdd:PLN02679 166 SLACVIAASEST 177
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
50-311 |
1.24e-05 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 45.70 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 50 MIVRAPAP---KGT---VLLLHGFPETLTVWNDIATTLA-HDYDVHAFDWPGYGqsSRPASERFSYAPMAYAQVLKAYIE 122
Cdd:COG1647 1 MKILGAEPfflEGGrkgVLLLHGFTGSPAEMRPLAEALAkAGYTVYAPRLPGHG--TSPEDLLKTTWEDWLEDVEEAYEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 123 -RAGIDrsKLVIYATDIGALPVLLLALDEPTIARqIIVgdFAPfdrPHYMWENLQNLKaeptasPTRAYMNKTSDEILQN 201
Cdd:COG1647 79 lKAGYD--KVIVIGLSMGGLLALLLAARYPDVAG-LVL--LSP---ALKIDDPSAPLL------PLLKYLARSLRGIGSD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 202 VHRRGLSPAEQFDLPADVQRDMTRSWsldgmtsadafahyyanftgdqHYLEANLTRLKTPVKVIWGEKDIYIAREMGIE 281
Cdd:COG1647 145 IEDPEVAEYAYDRTPLRALAELQRLI----------------------REVRRDLPKITAPTLIIQSRKDEVVPPESARY 202
|
250 260 270
....*....|....*....|....*....|...
gi 517053230 282 FAGKIGA---KVDILSGIGHFPHLQNSKQTVEE 311
Cdd:COG1647 203 IYERLGSpdkELVWLEDSGHVITLDKDREEVAE 235
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
53-134 |
7.25e-04 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 40.39 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 53 RAPAPKGTVLLLHGFPET-LTVWNDIATTLA-HDYDVHAFDWPGYGQSSRpaseRFSYAPMAYAQ-VLKAYIERAGIDRS 129
Cdd:COG1506 18 ADGKKYPVVVYVHGGPGSrDDSFLPLAQALAsRGYAVLAPDYRGYGESAG----DWGGDEVDDVLaAIDYLAARPYVDPD 93
|
....*
gi 517053230 130 KLVIY 134
Cdd:COG1506 94 RIGIY 98
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
61-124 |
7.75e-04 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 38.27 E-value: 7.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517053230 61 VLLLHGFPETLTVWNDIATTL-AHDYDVHAFDWPGYGQSSRpaserfsyapmAYAQVLKAYIERA 124
Cdd:COG1075 8 VVLVHGLGGSAASWAPLAPRLrAAGYPVYALNYPSTNGSIE-----------DSAEQLAAFVDAV 61
|
|
| PRK03204 |
PRK03204 |
haloalkane dehalogenase; Provisional |
60-166 |
3.38e-03 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 179554 [Multi-domain] Cd Length: 286 Bit Score: 38.68 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 60 TVLLLHGFPETLTVWNDIATTLAHDYDVHAFDWPGYGQSSRPASerFSYAPMAYAQVLKAYIERAGIDRskLVIYATDIG 139
Cdd:PRK03204 36 PILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPSG--FGYQIDEHARVIGEFVDHLGLDR--YLSMGQDWG 111
|
90 100
....*....|....*....|....*....
gi 517053230 140 ALPVLLLALDEPTIARQIIVGD--FAPFD 166
Cdd:PRK03204 112 GPISMAVAVERADRVRGVVLGNtwFWPAD 140
|
|
| bioH |
TIGR01738 |
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ... |
61-167 |
7.27e-03 |
|
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: 37.49 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053230 61 VLLLHGFPETLTVWNDIATTLAHDYDVHAFDWPGYGQSSrpaserfSYAPMAYAQVLKAYIERAGidrSKLVIYATDIGA 140
Cdd:TIGR01738 7 LVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSR-------GFGPLSLADMAEAIAAQAP---DPAIWLGWSLGG 76
|
90 100
....*....|....*....|....*...
gi 517053230 141 LPVLLLALDEPTIARQII-VGDFAPFDR 167
Cdd:TIGR01738 77 LVALHIAATHPDRVRALVtVASSPCFSA 104
|
|
| |
