|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
51-327 |
4.18e-40 |
|
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: 4.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 51 RYVRHEDYQFCYSFRGRPGnkPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQ 130
Cdd:COG0596 5 RFVTVDGVRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 131 FVEclKLNKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVcpaglqystdNQFVQRLKElqesaavekiplipstpeem 210
Cdd:COG0596 82 LLD--ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV----------DEVLAALAE-------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 211 semlqlcsyvrfrvpqqilqglvdvRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLA 290
Cdd:COG0596 130 -------------------------PLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLA 184
|
250 260 270
....*....|....*....|....*....|....*..
gi 821389629 291 KSIANCQVELLENCGHSVVMERPRKTAKLIVDFLASV 327
Cdd:COG0596 185 ELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
62-327 |
5.18e-30 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 117.35 E-value: 5.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 62 YSFRGrPGNKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKp 141
Cdd:PRK14875 123 YLRLG-EGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGH-GASSKAVGAGSLDELAAAVLAFLDALGIERA- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 142 fHLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPAGLQYSTDNQFVQRLKELQESAAVEkiPLIpstpeemsEMLqlcsyvr 221
Cdd:PRK14875 200 -HLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLGPEINGDYIDGFVAAESRRELK--PVL--------ELL------- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 222 FRVPQQILQGLVD--VRiphnnfYRKL-----FLEIVSE------KSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADM 288
Cdd:PRK14875 262 FADPALVTRQMVEdlLK------YKRLdgvddALRALADalfaggRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQG 335
|
250 260 270
....*....|....*....|....*....|....*....
gi 821389629 289 LAksiANCQVELLENCGHSVVMERPRKTAKLIVDFLASV 327
Cdd:PRK14875 336 LP---DGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
72-313 |
2.01e-27 |
|
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: 107.59 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 72 PSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH-EGTTRSSLDDLSIDGQVKRIHQFVEclKLNKKPFHLIGTSM 149
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFgKSSRPKAQDDYRTDDLAEDLEYILE--ALGLEKVNLVGHSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 150 GGHVAGVYAAHYPSDVCSLSLVCPAGLQYSTDNQFVQRLKELQES-----AAVEKIPLIPSTPEEMSEmLQLCSYVRFRV 224
Cdd:pfam00561 79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFfdgfvADFAPNPLGRLVAKLLAL-LLLRLRLLKAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 225 PQQILQGLVDVRIPHNN--FYRKLFLEIVSEKSRYSLHQNmdkIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVELLE 302
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSlvTGALLFIETWSTELRAKFLGR---LDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234
|
250
....*....|.
gi 821389629 303 NCGHSVVMERP 313
Cdd:pfam00561 235 DAGHFAFLEGP 245
|
|
| menH_SHCHC |
TIGR03695 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ... |
70-324 |
5.82e-21 |
|
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: 90.35 E-value: 5.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 70 NKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDL--SIDGQVKRI-HQFVEclKLNKKPFHLIG 146
Cdd:TIGR03695 1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGH-GSSQSPSDIEryDFEEAAQLLlATLLD--QLGIEPFFLVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 147 TSMGGHVAGVYAAHYPSDVCSLSLV-CPAGLQ--------YSTDNQFVQRLkeLQESAAV-----EKIPLIpSTPEEMse 212
Cdd:TIGR03695 78 YSMGGRIALYYALQYPERVQGLILEsGSPGLQteeeraarRQNDEQLAQRF--EQEGLEAflddwYQQPLF-ASQKNL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 213 mlqlcsyvrfrvPQQILQGLVDVRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMlAKS 292
Cdd:TIGR03695 153 ------------PPEQRQALRAERLANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQIAKEM-QKL 219
|
250 260 270
....*....|....*....|....*....|..
gi 821389629 293 IANCQVELLENCGHSVVMERPRKTAKLIVDFL 324
Cdd:TIGR03695 220 IPNLTLHIIPNAGHNIHLENPEAFAKILLAFL 251
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
51-327 |
4.18e-40 |
|
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: 4.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 51 RYVRHEDYQFCYSFRGRPGnkPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQ 130
Cdd:COG0596 5 RFVTVDGVRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 131 FVEclKLNKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVcpaglqystdNQFVQRLKElqesaavekiplipstpeem 210
Cdd:COG0596 82 LLD--ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV----------DEVLAALAE-------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 211 semlqlcsyvrfrvpqqilqglvdvRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLA 290
Cdd:COG0596 130 -------------------------PLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRLA 184
|
250 260 270
....*....|....*....|....*....|....*..
gi 821389629 291 KSIANCQVELLENCGHSVVMERPRKTAKLIVDFLASV 327
Cdd:COG0596 185 ELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
62-327 |
5.18e-30 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 117.35 E-value: 5.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 62 YSFRGrPGNKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKp 141
Cdd:PRK14875 123 YLRLG-EGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGH-GASSKAVGAGSLDELAAAVLAFLDALGIERA- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 142 fHLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPAGLQYSTDNQFVQRLKELQESAAVEkiPLIpstpeemsEMLqlcsyvr 221
Cdd:PRK14875 200 -HLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLGPEINGDYIDGFVAAESRRELK--PVL--------ELL------- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 222 FRVPQQILQGLVD--VRiphnnfYRKL-----FLEIVSE------KSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADM 288
Cdd:PRK14875 262 FADPALVTRQMVEdlLK------YKRLdgvddALRALADalfaggRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQG 335
|
250 260 270
....*....|....*....|....*....|....*....
gi 821389629 289 LAksiANCQVELLENCGHSVVMERPRKTAKLIVDFLASV 327
Cdd:PRK14875 336 LP---DGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGKA 371
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
72-313 |
2.01e-27 |
|
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: 107.59 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 72 PSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH-EGTTRSSLDDLSIDGQVKRIHQFVEclKLNKKPFHLIGTSM 149
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFgKSSRPKAQDDYRTDDLAEDLEYILE--ALGLEKVNLVGHSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 150 GGHVAGVYAAHYPSDVCSLSLVCPAGLQYSTDNQFVQRLKELQES-----AAVEKIPLIPSTPEEMSEmLQLCSYVRFRV 224
Cdd:pfam00561 79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFfdgfvADFAPNPLGRLVAKLLAL-LLLRLRLLKAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 225 PQQILQGLVDVRIPHNN--FYRKLFLEIVSEKSRYSLHQNmdkIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVELLE 302
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSlvTGALLFIETWSTELRAKFLGR---LDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIP 234
|
250
....*....|.
gi 821389629 303 NCGHSVVMERP 313
Cdd:pfam00561 235 DAGHFAFLEGP 245
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
60-326 |
1.24e-24 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 99.69 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 60 FCYSFRGRPGNKPSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGHEGTTRSSLDDLSIDGQVKRIHQFVECLK-L 137
Cdd:COG2267 17 RGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALRaR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 138 NKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPAglqYSTDnqfvqrlkelqesaavekiPLIPSTPEEMSEMLqlc 217
Cdd:COG2267 97 PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA---YRAD-------------------PLLGPSARWLRALR--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 218 syvrfrvpqqilqglvdvriphnnfyrklfleivseksrysLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIA-NC 296
Cdd:COG2267 152 -----------------------------------------LAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSpDV 190
|
250 260 270
....*....|....*....|....*....|.
gi 821389629 297 QVELLENCGHSVVMERPRKTA-KLIVDFLAS 326
Cdd:COG2267 191 ELVLLPGARHELLNEPAREEVlAAILAWLER 221
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
68-329 |
8.27e-22 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 92.31 E-value: 8.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 68 PGNKPSILMLHGFSAHKdmwlSVVKFLPKNLH-----LVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPF 142
Cdd:COG1647 12 EGGRKGVLLLHGFTGSP----AEMRPLAEALAkagytVYAPRLPGH-GTSPEDLLKTTWEDWLEDVEEAYEILKAGYDKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 143 HLIGTSMGGHVAGVYAAHYPsDVCSLSLVCPAgLQYSTDNQFVQRLKELqesaAVEKIPLIPSTPEEmsemLQLCSYVRF 222
Cdd:COG1647 87 IVIGLSMGGLLALLLAARYP-DVAGLVLLSPA-LKIDDPSAPLLPLLKY----LARSLRGIGSDIED----PEVAEYAYD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 223 RVPQQILQglvdvriphnNFYRklFLEIVSEksryslhqNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVEL-- 300
Cdd:COG1647 157 RTPLRALA----------ELQR--LIREVRR--------DLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELvw 216
|
250 260 270
....*....|....*....|....*....|
gi 821389629 301 LENCGHSVVMERPRKT-AKLIVDFLASVHS 329
Cdd:COG1647 217 LEDSGHVITLDKDREEvAEEILDFLERLAA 246
|
|
| menH_SHCHC |
TIGR03695 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ... |
70-324 |
5.82e-21 |
|
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: 90.35 E-value: 5.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 70 NKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDL--SIDGQVKRI-HQFVEclKLNKKPFHLIG 146
Cdd:TIGR03695 1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGH-GSSQSPSDIEryDFEEAAQLLlATLLD--QLGIEPFFLVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 147 TSMGGHVAGVYAAHYPSDVCSLSLV-CPAGLQ--------YSTDNQFVQRLkeLQESAAV-----EKIPLIpSTPEEMse 212
Cdd:TIGR03695 78 YSMGGRIALYYALQYPERVQGLILEsGSPGLQteeeraarRQNDEQLAQRF--EQEGLEAflddwYQQPLF-ASQKNL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 213 mlqlcsyvrfrvPQQILQGLVDVRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMlAKS 292
Cdd:TIGR03695 153 ------------PPEQRQALRAERLANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQIAKEM-QKL 219
|
250 260 270
....*....|....*....|....*....|..
gi 821389629 293 IANCQVELLENCGHSVVMERPRKTAKLIVDFL 324
Cdd:TIGR03695 220 IPNLTLHIIPNAGHNIHLENPEAFAKILLAFL 251
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
74-319 |
3.10e-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: 62.11 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 74 ILMLHGFSAHKDmwlSVVKFLPKNLHLVCVDMPGHeGTTRSSLDDLSidgQVKRIHQFVECLKlNKKPFHLIGTSMGGHV 153
Cdd:pfam12697 1 VVLVHGAGLSAA---PLAALLAAGVAVLAPDLPGH-GSSSPPPLDLA---DLADLAALLDELG-AARPVVLVGHSLGGAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 154 AGVYAAHYPSDVCslsLVCPAGLQYSTDNQFVQRLKELQESAAVEKIPLIPSTPEEMSEMLQLCSYVRFRVPQQILQGLV 233
Cdd:pfam12697 73 ALAAAAAALVVGV---LVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 234 DVRIPHNNFyrklfleivseksryslhqnmDKIKVPTQIIWGkQDQVLDvSGADMLAKSIANCQVELLENCGHSvVMERP 313
Cdd:pfam12697 150 LALLPLAAW---------------------RDLPVPVLVLAE-EDRLVP-ELAQRLLAALAGARLVVLPGAGHL-PLDDP 205
|
....*.
gi 821389629 314 RKTAKL 319
Cdd:pfam12697 206 EEVAEA 211
|
|
| PLN02578 |
PLN02578 |
hydrolase |
9-326 |
1.15e-10 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 61.78 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 9 FVIAGGTLAIPILAFVASFLLWP-SALIRI-------YYWYWRralGMQVRYVRHedyqfcysfrgrpGNKPSILMLHGF 80
Cdd:PLN02578 32 IFIFGGIVASGVSVMGSSSASQSvQGLERLpfkkegyNFWTWR---GHKIHYVVQ-------------GEGLPIVLIHGF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 81 SAHKDMWLSVVKFLPKNLHLVCVDMPGHeGTTRSSLddLSIDGQVKRiHQFVECLK-LNKKPFHLIGTSMGGHVAGVYAA 159
Cdd:PLN02578 96 GASAFHWRYNIPELAKKYKVYALDLLGF-GWSDKAL--IEYDAMVWR-DQVADFVKeVVKEPAVLVGNSLGGFTALSTAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 160 HYPSDVCSLSLVCPAGlqystdnQFVQRLKELQESAAVEKIPLIPSTPEEMSEMLQ----LCSYVRFRVPQQILQGLVDV 235
Cdd:PLN02578 172 GYPELVAGVALLNSAG-------QFGSESREKEEAIVVEETVLTRFVVKPLKEWFQrvvlGFLFWQAKQPSRIESVLKSV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 236 RIPHNN---------------------FYRkLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIA 294
Cdd:PLN02578 245 YKDKSNvddylvesitepaadpnagevYYR-LMSRFLFNQSRYTLDSLLSKLSCPLLLLWGDLDPWVGPAKAEKIKAFYP 323
|
330 340 350
....*....|....*....|....*....|..
gi 821389629 295 NCQVELLEnCGHSVVMERPRKTAKLIVDFLAS 326
Cdd:PLN02578 324 DTTLVNLQ-AGHCPHDEVPEQVNKALLEWLSS 354
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
71-312 |
1.21e-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: 60.69 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 71 KPSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH---EGTTR--SSLDDLsidgqVKRIHQFVECLKLN--KKPF 142
Cdd:pfam12146 4 RAVVVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHgrsDGKRGhvPSFDDY-----VDDLDTFVDKIREEhpGLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 143 HLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPA-GLQYSTDNQFVQRLKELQESAAVEKIPLIPSTPEEMS---EMLQLC- 217
Cdd:pfam12146 79 FLLGHSMGGLIAALYALRYPDKVDGLILSAPAlKIKPYLAPPILKLLAKLLGKLFPRLRVPNNLLPDSLSrdpEVVAAYa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 218 --SYVRFRVPQQILQGLVDVRIphnnfyrklfleivseksrySLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSI-- 293
Cdd:pfam12146 159 adPLVHGGISARTLYELLDAGE--------------------RLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAgs 218
|
250
....*....|....*....
gi 821389629 294 ANCQVELLENCGHSVVMER 312
Cdd:pfam12146 219 TDKTLKLYPGLYHELLNEP 237
|
|
| protocat_pcaD |
TIGR02427 |
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that ... |
62-325 |
2.33e-10 |
|
3-oxoadipate enol-lactonase; Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]
Pssm-ID: 131480 [Multi-domain] Cd Length: 251 Bit Score: 60.06 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 62 YSFRGRPGNKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGH----EGTTRSSLDDLSIDgqvkrihqfVECL-- 135
Cdd:TIGR02427 4 YRLDGAADGAPVLVFINSLGTDLRMWDPVLPALTPDFRVLRYDKRGHglsdAPEGPYSIEDLADD---------VLALld 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 136 KLNKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPAGlQYSTDNQFVQRLkelqesAAVEKiplipstpEEMSEMLQ 215
Cdd:TIGR02427 75 HLGIERAVFCGLSLGGLIAQGLAARRPDRVRALVLSNTAA-KIGTPESWNARI------AAVRA--------EGLAALAD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 216 lCSYVRFRVPqqilqglvDVRIPHN---NFYRKLFLEivSEKSRYSLH----QNMD------KIKVPTQIIWGKQDQVLD 282
Cdd:TIGR02427 140 -AVLERWFTP--------GFREAHParlDLYRNMLVR--QPPDGYAGCcaaiRDADfrdrlgAIAVPTLCIAGDQDGSTP 208
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 821389629 283 VSGADMLAKSIANCQVELLENCGHSVVMERPRKTAKLIVDFLA 325
Cdd:TIGR02427 209 PELVREIADLVPGARFAEIRGAGHIPCVEQPEAFNAALRDFLR 251
|
|
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
47-313 |
1.11e-08 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 56.07 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 47 GMQVRYVRHEDYQFCY----SFRGRPgNKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTRSSLDDLSID 122
Cdd:PLN02894 78 GSKVRWFRSASNEPRFintvTFDSKE-DAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCKSTE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 123 -GQVKRIHQFVECLKL-NKKPFHLIGTSMGGHVAGVYAAHYPSDVCSLSLVCPAGlqystdnqfvqrlkelqesaaveki 200
Cdd:PLN02894 157 eTEAWFIDSFEEWRKAkNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAG------------------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 201 plIPSTPEEMSEMLqlcsyVRFR----------------VPQQILQGL-----------VDVRIPHNN------------ 241
Cdd:PLN02894 212 --FSSESDDKSEWL-----TKFRatwkgavlnhlwesnfTPQKIIRGLgpwgpnlvrryTTARFGAHStgdilseeeskl 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 242 ----FYRKLFLEIVSEK-----------SRYSLHQNMDKIKVPTQIIWGKQDQvLDVSGADMLAKSI-ANCQVELLENCG 305
Cdd:PLN02894 285 ltdyVYHTLAAKASGELclkyifsfgafARKPLLESASEWKVPTTFIYGRHDW-MNYEGAVEARKRMkVPCEIIRVPQGG 363
|
....*...
gi 821389629 306 HSVVMERP 313
Cdd:PLN02894 364 HFVFLDNP 371
|
|
| bioH |
TIGR01738 |
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ... |
72-323 |
1.26e-08 |
|
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: 54.82 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 72 PSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTrsSLDDLSIDGQVKRIHQFVEclklnkKPFHLIGTSMGG 151
Cdd:TIGR01738 5 VHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSR--GFGPLSLADMAEAIAAQAP------DPAIWLGWSLGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 152 HVAGVYAAHYPSDVCSLSLVC-----------PAGLQYSTDNQFVQRLK-ELQESaaVEKIPLIPS--TPEEMSEMLQLC 217
Cdd:TIGR01738 77 LVALHIAATHPDRVRALVTVAsspcfsaredwPEGIKPDVLTGFQQQLSdDYQRT--IERFLALQTlgTPTARQDARALK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 218 SYVRFR-VPQ-QILQGLVDVriphnnfyrklfleivseKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIAN 295
Cdd:TIGR01738 155 QTLLARpTPNvQVLQAGLEI------------------LATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPH 216
|
250 260
....*....|....*....|....*...
gi 821389629 296 CQVELLENCGHSVVMERPRKTAKLIVDF 323
Cdd:TIGR01738 217 SELYIFAKAAHAPFLSHAEAFCALLVAF 244
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
68-325 |
2.60e-08 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 53.87 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 68 PGNKPSILMLHGFSAHKD-MWLSVVKFLPKN-LHLVCVDMPGHeGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPFHLI 145
Cdd:COG1506 20 GKKYPVVVYVHGGPGSRDdSFLPLAQALASRgYAVLAPDYRGY-GESAGDWGGDEVDDVLAAIDYLAARPYVDPDRIGIY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 146 GTSMGGHVAGVYAAHYPSDVCSLSLVCPA---GLQYSTDNQFVQRLKElqesaavekiplipsTPEEMSEMLQlcsyvrf 222
Cdd:COG1506 99 GHSYGGYMALLAAARHPDRFKAAVALAGVsdlRSYYGTTREYTERLMG---------------GPWEDPEAYA------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 223 rvpqqilqglvdvriphnnfyrklfleivseksRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSI--ANCQVEL 300
Cdd:COG1506 157 ---------------------------------ARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEALkkAGKPVEL 203
|
250 260
....*....|....*....|....*..
gi 821389629 301 L--ENCGHSVVMERPRKTAKLIVDFLA 325
Cdd:COG1506 204 LvyPGEGHGFSGAGAPDYLERILDFLD 230
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
70-160 |
4.19e-08 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 53.30 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 70 NKPSILMLHGFSAHKDMWLSVVKFLPKNlHLVCVDMPGHeGTTRssldDLSIDGQVKRIHQFVECLK-LNKKPFHLIGTS 148
Cdd:PRK11126 1 GLPWLVFLHGLLGSGQDWQPVGEALPDY-PRLYIDLPGH-GGSA----AISVDGFADVSRLLSQTLQsYNILPYWLVGYS 74
|
90
....*....|..
gi 821389629 149 MGGHVAGVYAAH 160
Cdd:PRK11126 75 LGGRIAMYYACQ 86
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
62-324 |
8.67e-07 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 49.53 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 62 YSFRGRPGNKPSILMLHGFSAHKDMWLSVVKFLPKN-LHLVCVDMPGH---EGTTRSSLDDLSIDgqvkrIHQFVEclKL 137
Cdd:COG1073 28 YLPAGASKKYPAVVVAHGNGGVKEQRALYAQRLAELgFNVLAFDYRGYgesEGEPREEGSPERRD-----ARAAVD--YL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 138 NKKPFH------LIGTSMGGHVAGVYAAHYPsDVCSLSLVCPAglqystdNQFVQRLKELQESAAVEKIPLIPSTPeems 211
Cdd:COG1073 101 RTLPGVdperigLLGISLGGGYALNAAATDP-RVKAVILDSPF-------TSLEDLAAQRAKEARGAYLPGVPYLP---- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 212 emlqlcsyvrfrvpqqilqglvdvRIPHNNFYRKLFleivseksrYSLHQnMDKIKVPTQIIWGKQDQVldVS---GADM 288
Cdd:COG1073 169 ------------------------NVRLASLLNDEF---------DPLAK-IEKISRPLLFIHGEKDEA--VPfymSEDL 212
|
250 260 270
....*....|....*....|....*....|....*..
gi 821389629 289 LAKSIANCQVELLENCGHSVVMERPRKTA-KLIVDFL 324
Cdd:COG1073 213 YEAAAEPKELLIVPGAGHVDLYDRPEEEYfDKLAEFF 249
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
67-161 |
1.81e-04 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 40.20 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821389629 67 RPGNKPsILMLHGFSAHKDMWLSVVKFLPKNLHLVC-VDMPGHEGTTRSSLDDLsiDGQVKRIHQfveclKLNKKPFHLI 145
Cdd:COG1075 2 AATRYP-VVLVHGLGGSAASWAPLAPRLRAAGYPVYaLNYPSTNGSIEDSAEQL--AAFVDAVLA-----ATGAEKVDLV 73
|
90
....*....|....*.
gi 821389629 146 GTSMGGHVAGVYAAHY 161
Cdd:COG1075 74 GHSMGGLVARYYLKRL 89
|
|
|