|
Name |
Accession |
Description |
Interval |
E-value |
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
8-326 |
1.92e-156 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 441.50 E-value: 1.92e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 8 GLSEEDLKVIYKWMDLGRKIDERLWLLNRAGKIPFVVSGQGQEATQIGMAYALEEGDITAPYYRDLAFVTYMGISAYDTF 87
Cdd:COG1071 16 DLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALARGVDPKELM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 88 LSAFGKKDDvNSGGKQMPSHFSSRSKNILSQSSPVATQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAG 167
Cdd:COG1071 96 AELFGKATG-PSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 168 VHKLPFVCVIINNKYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARERAISGQGSTLIEAVTSRMT 247
Cdd:COG1071 175 VWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRLG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 248 AHSSDDDDQ-YRTKEEREALKKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDIINKATKAAEDAPYPSVEEAYAFVYEE 326
Cdd:COG1071 255 GHSTSDDPTrYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYAE 334
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
17-308 |
4.56e-135 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 385.31 E-value: 4.56e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 17 IYKWMDLGRKIDERLWLLNRAGKIPFVV-SGQGQEATQIGMAYALEEGDITAPYYRDLAFVTYMGISAYDTFLSAFGKKD 95
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGGFYhLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 96 DvNSGGKQMPSHFSSRSKNILSQSSPVATQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGVHKLPFVC 175
Cdd:cd02000 81 G-PCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 176 VIINNKYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARERAISGQGSTLIEAVTSRMTAHSSDDDD 255
Cdd:cd02000 160 VCENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446490507 256 Q-YRTKEEREALKKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDIINKATKAA 308
Cdd:cd02000 240 SrYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| PDH_E1_alph_x |
TIGR03181 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
9-326 |
1.49e-116 |
|
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 213783 [Multi-domain] Cd Length: 341 Bit Score: 340.28 E-value: 1.49e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 9 LSEEDLKVIYKWMDLGRKIDERLWLLNRAGKIPFVVSGQGQEATQIGMAYALEEGDITAPYYRDLAFVTYMGISAYDTFL 88
Cdd:TIGR03181 21 LSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFPSYRDHAAMLARGVPLVEILL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 89 SAFGkkddvNSGGKQMPshfssRSKNILSQSSPVATQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGV 168
Cdd:TIGR03181 101 YWRG-----DERGSWDP-----EGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTSEGDFYEALNFAGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 169 HKLPFVCVIINNKYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARERAISGQGSTLIEAVTSRMTA 248
Cdd:TIGR03181 171 FKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGGGPTLIEAVTYRLGP 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446490507 249 H-SSDDDDQYRTKEEREALKKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDIINKATKAAEDAPYPSVEEAYAFVYEE 326
Cdd:TIGR03181 251 HtTADDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPPPVDDIFDHVYAE 329
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
18-317 |
8.08e-97 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 288.45 E-value: 8.08e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 18 YKWMDLGRKIDERLWLLNRAGKIPFVVSGQGQEATQIGMAYALEEGDITAPYYRDLAFVTYMGISAYDTFLSAFGKKDDV 97
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 98 NSGGKQMpsHFSSRSKNILSQSSPVATQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGVHKLPFVCVI 177
Cdd:pfam00676 81 KGGSMHG--YYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 178 INNKYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARERAISGQGSTLIEAVTSRMTAHSSDDDDQ- 256
Cdd:pfam00676 159 ENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPSt 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446490507 257 YRTKEEREAL-KKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDIINKATKAAEDAPYPSVE 317
Cdd:pfam00676 239 YRTRDEYEEVrKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
4-324 |
4.92e-46 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 159.26 E-value: 4.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 4 YKSLGLSEEDLKVIYKWMDLGRKIDERLWLLNRAGKI-PFVVSGQGQEATQIGMAYALEEGDITAPYYRDLAFVTYMGIS 82
Cdd:CHL00149 12 SNENNINSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMfGFVHLYNGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 83 AYDTFLSAFGKKDDVNSG-GKQMpsHFSSRSKNILSQSSPVATQIPHAVGAALA-------LKMDGKKKIATATVGEGSS 154
Cdd:CHL00149 92 PKNVMAELFGKETGCSRGrGGSM--HIFSAPHNFLGGFAFIGEGIPIALGAAFQsiyrqqvLKEVQPLRVTACFFGDGTT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 155 NQGDFHEGLNFAGVHKLPFVCVIINNKYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARERAISGQ 234
Cdd:CHL00149 170 NNGQFFECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 235 GSTLIEAVTSRMTAHSSDDDDQYRTKEEREALKKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDIINKATKAAEDAPYP 314
Cdd:CHL00149 250 GPTLIEALTYRFRGHSLADPDELRSKQEKEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEP 329
|
330
....*....|
gi 446490507 315 SVEEAYAFVY 324
Cdd:CHL00149 330 NISDLKKYLF 339
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
8-326 |
1.92e-156 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 441.50 E-value: 1.92e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 8 GLSEEDLKVIYKWMDLGRKIDERLWLLNRAGKIPFVVSGQGQEATQIGMAYALEEGDITAPYYRDLAFVTYMGISAYDTF 87
Cdd:COG1071 16 DLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWIFPTYRDHGHALARGVDPKELM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 88 LSAFGKKDDvNSGGKQMPSHFSSRSKNILSQSSPVATQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAG 167
Cdd:COG1071 96 AELFGKATG-PSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 168 VHKLPFVCVIINNKYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARERAISGQGSTLIEAVTSRMT 247
Cdd:COG1071 175 VWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRLG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 248 AHSSDDDDQ-YRTKEEREALKKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDIINKATKAAEDAPYPSVEEAYAFVYEE 326
Cdd:COG1071 255 GHSTSDDPTrYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYAE 334
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
17-308 |
4.56e-135 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 385.31 E-value: 4.56e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 17 IYKWMDLGRKIDERLWLLNRAGKIPFVV-SGQGQEATQIGMAYALEEGDITAPYYRDLAFVTYMGISAYDTFLSAFGKKD 95
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGGFYhLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 96 DvNSGGKQMPSHFSSRSKNILSQSSPVATQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGVHKLPFVC 175
Cdd:cd02000 81 G-PCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 176 VIINNKYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARERAISGQGSTLIEAVTSRMTAHSSDDDD 255
Cdd:cd02000 160 VCENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446490507 256 Q-YRTKEEREALKKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDIINKATKAA 308
Cdd:cd02000 240 SrYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| PDH_E1_alph_x |
TIGR03181 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
9-326 |
1.49e-116 |
|
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 213783 [Multi-domain] Cd Length: 341 Bit Score: 340.28 E-value: 1.49e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 9 LSEEDLKVIYKWMDLGRKIDERLWLLNRAGKIPFVVSGQGQEATQIGMAYALEEGDITAPYYRDLAFVTYMGISAYDTFL 88
Cdd:TIGR03181 21 LSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWVFPSYRDHAAMLARGVPLVEILL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 89 SAFGkkddvNSGGKQMPshfssRSKNILSQSSPVATQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGV 168
Cdd:TIGR03181 101 YWRG-----DERGSWDP-----EGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTSEGDFYEALNFAGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 169 HKLPFVCVIINNKYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARERAISGQGSTLIEAVTSRMTA 248
Cdd:TIGR03181 171 FKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGGGPTLIEAVTYRLGP 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446490507 249 H-SSDDDDQYRTKEEREALKKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDIINKATKAAEDAPYPSVEEAYAFVYEE 326
Cdd:TIGR03181 251 HtTADDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPPPVDDIFDHVYAE 329
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
18-317 |
8.08e-97 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 288.45 E-value: 8.08e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 18 YKWMDLGRKIDERLWLLNRAGKIPFVVSGQGQEATQIGMAYALEEGDITAPYYRDLAFVTYMGISAYDTFLSAFGKKDDV 97
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 98 NSGGKQMpsHFSSRSKNILSQSSPVATQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGVHKLPFVCVI 177
Cdd:pfam00676 81 KGGSMHG--YYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 178 INNKYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARERAISGQGSTLIEAVTSRMTAHSSDDDDQ- 256
Cdd:pfam00676 159 ENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPSt 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446490507 257 YRTKEEREAL-KKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDIINKATKAAEDAPYPSVE 317
Cdd:pfam00676 239 YRTRDEYEEVrKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
4-324 |
4.92e-46 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 159.26 E-value: 4.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 4 YKSLGLSEEDLKVIYKWMDLGRKIDERLWLLNRAGKI-PFVVSGQGQEATQIGMAYALEEGDITAPYYRDLAFVTYMGIS 82
Cdd:CHL00149 12 SNENNINSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMfGFVHLYNGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 83 AYDTFLSAFGKKDDVNSG-GKQMpsHFSSRSKNILSQSSPVATQIPHAVGAALA-------LKMDGKKKIATATVGEGSS 154
Cdd:CHL00149 92 PKNVMAELFGKETGCSRGrGGSM--HIFSAPHNFLGGFAFIGEGIPIALGAAFQsiyrqqvLKEVQPLRVTACFFGDGTT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 155 NQGDFHEGLNFAGVHKLPFVCVIINNKYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARERAISGQ 234
Cdd:CHL00149 170 NNGQFFECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 235 GSTLIEAVTSRMTAHSSDDDDQYRTKEEREALKKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDIINKATKAAEDAPYP 314
Cdd:CHL00149 250 GPTLIEALTYRFRGHSLADPDELRSKQEKEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEP 329
|
330
....*....|
gi 446490507 315 SVEEAYAFVY 324
Cdd:CHL00149 330 NISDLKKYLF 339
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
6-315 |
2.34e-37 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 138.54 E-value: 2.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 6 SLGLSEEDLKVIYKWMDLGRKIDERLWLLNRAGKI-PFVVSGQGQEATQIGMAYALEEGDITAPYYRDLAFVTYMGISAY 84
Cdd:PLN02374 80 DLLVTREEGLELYEDMVLGRSFEDMCAQMYYRGKMfGFVHLYNGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVPAR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 85 DTFLSAFGKKDDVNSG-GKQMpsHFSSRSKNILSQSSPVATQIPHAVGAALA-------LKMDGKKKIATATVGEGSSNQ 156
Cdd:PLN02374 160 AVMSELFGKATGCCRGqGGSM--HMFSKEHNLLGGFAFIGEGIPVATGAAFSskyrrevLKEESCDDVTLAFFGDGTCNN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 157 GDFHEGLNFAGVHKLPFVCVIINNKYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARERAISGQGS 236
Cdd:PLN02374 238 GQFFECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEGP 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446490507 237 TLIEAVTSRMTAHSSDDDDQYRTKEEREALKKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDIINKATKAAEDAPYPS 315
Cdd:PLN02374 318 TLVECETYRFRGHSLADPDELRDPAEKAHYAARDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFADASPLPP 396
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
48-327 |
3.51e-36 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 133.69 E-value: 3.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 48 GQEATQIGMAYALEEGD--ITApyYRDLAFVTYMGISAYDTFLSAFGKKDDVNSG-GKQMpsHFSSRSKNILSQSSPVAT 124
Cdd:PLN02269 67 GQEAVAVGMEAAITKEDaiITA--YRDHCTHLGRGGTVLEVFAELMGRKDGCSRGkGGSM--HFYKKDANFYGGHGIVGA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 125 QIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGVHKLPFVCVIINNKYAISVpdSLQYAAEKLSDRALGY 204
Cdd:PLN02269 143 QVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMGT--AEWRAAKSPAYYKRGD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 205 GIHGEQVDGNDPLAMYKAMKEARERAISgQGSTLIEAVTSRMTAHS-SDDDDQYRTKEEREALKKA-DCNEKFKKELLSA 282
Cdd:PLN02269 221 YVPGLKVDGMDVLAVKQACKFAKEHALS-NGPIVLEMDTYRYHGHSmSDPGSTYRTRDEISGVRQErDPIERVRKLLLAH 299
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446490507 283 GIIDDAWLAEIEAEHKDIINKATKAAEDAPYPSVEEAYAFVYEEG 327
Cdd:PLN02269 300 ELATEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELFTNVYVKG 344
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
126-258 |
1.23e-11 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 63.68 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 126 IPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGVHKLPFVCVII-NNKYAISVPDSLQYAAEKLSDRALGY 204
Cdd:cd02012 111 LSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNLIAIVdSNRIQIDGPTDDILFTEDLAKKFEAF 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446490507 205 GIHGEQVDGNDPLAMYKAMKEARE----------RAISGQGSTLIEAVTSrmTAHSSDDDDQYR 258
Cdd:cd02012 191 GWNVIEVDGHDVEEILAALEEAKKskgkptliiaKTIKGKGVPFMENTAK--WHGKPLGEEEVE 252
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
126-243 |
2.06e-08 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 52.98 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 126 IPHAVGAALALkmDGKKKIATatVGEGSSNQGDfhEGLNFAGVHKLPFVCVIINNK-YAISVPDSLQYAAEKLSDR---- 200
Cdd:cd02002 55 LPAAVGAALAN--PDRKVVAI--IGDGSFMYTI--QALWTAARYGLPVTVVILNNRgYGALRSFLKRVGPEGPGENapdg 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446490507 201 -------------ALGYGIHGEQVDGNDplamykAMKEARERAISGQGSTLIEAVT 243
Cdd:cd02002 129 ldlldpgidfaaiAKAFGVEAERVETPE------ELDEALREALAEGGPALIEVVV 178
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
124-243 |
2.65e-08 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 53.32 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 124 TQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGVHKLPFVcVIIN-NKYAIS----VPDSLQyaaekls 198
Cdd:cd02007 79 TSISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMI-VILNdNEMSISpnvgTPGNLF------- 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446490507 199 dRALGYGIHGEqVDGNDPLAMYKAMKEAREraisGQGSTLIEAVT 243
Cdd:cd02007 151 -EELGFRYIGP-VDGHNIEALIKVLKEVKD----LKGPVLLHVVT 189
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
127-243 |
1.41e-06 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 49.57 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 127 PHAVGAALALkmDGKKKIATatVGEGSSNQGDfhEGLNFAGVHKLPFVCVIINN-KYAisvpdSLQYAAEKLSDR----- 200
Cdd:PRK07092 414 PAAVGVALAQ--PGRRVIGL--IGDGSAMYSI--QALWSAAQLKLPVTFVILNNgRYG-----ALRWFAPVFGVRdvpgl 482
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446490507 201 ----------ALGYGIHGEQVDGNDPLAmykamkEARERAISGQGSTLIEAVT 243
Cdd:PRK07092 483 dlpgldfvalARGYGCEAVRVSDAAELA------DALARALAADGPVLVEVEV 529
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
126-243 |
2.87e-06 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 48.59 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 126 IPHAVGAALALKMDGKK--KIATATVG-------------EGSSnqgdfHEGLNFAGVHKLPFVCVII-NNKYAIS--VP 187
Cdd:PRK05899 124 LANAVGMALAEKYLAALfnRPGLDIVDhytyvlcgdgdlmEGIS-----HEACSLAGHLKLGNLIVIYdDNRISIDgpTE 198
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446490507 188 DSLqyaAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEAReraiSGQGSTLIEAVT 243
Cdd:PRK05899 199 GWF---TEDVKKRFEAYGWHVIEVDGHDVEAIDAAIEEAK----ASTKPTLIIAKT 247
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
126-243 |
1.64e-05 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 44.55 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 126 IPHAVGAALALKmdgKKKIAtATVGEGSsnqgdFHEG---LNFAGVHKLPFVCVIINNKYAISVPDS------LQYAAEK 196
Cdd:cd00568 52 LPAAIGAALAAP---DRPVV-CIAGDGG-----FMMTgqeLATAVRYGLPVIVVVFNNGGYGTIRMHqeafygGRVSGTD 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446490507 197 LS-----DRALGYGIHGEQVDGNDplamykAMKEARERAISGQGSTLIEAVT 243
Cdd:cd00568 123 LSnpdfaALAEAYGAKGVRVEDPE------DLEAALAEALAAGGPALIEVKT 168
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
129-246 |
3.97e-05 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 44.99 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 129 AVGAALALKMDGKKKIATATVGEGS---SNQGDFHEglnFAGVHKLPFVCVIINNKYAISVPDSLQ------YAAEK--- 196
Cdd:PRK08327 435 ALGAALGAKLATPDRLVIATVGDGSfifGVPEAAHW---VAERYGLPVLVVVFNNGGWLAVKEAVLevypegYAARKgtf 511
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 197 ----LSDR------ALGYGIHGEQVDgnDPLAMYKAMKEARERAISGQGSTLIEAVTSRM 246
Cdd:PRK08327 512 pgtdFDPRpdfakiAEAFGGYGERVE--DPEELKGALRRALAAVRKGRRSAVLDVIVDRV 569
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
71-247 |
6.33e-05 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 43.42 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 71 RDLAFVTYMGIS--AYDTFLSAFGKKDDVNSGgkqmpshfssrsknilsQSSPVATQIPHAVGAALAlkmDGKKKIATAt 148
Cdd:cd02006 23 RDVRYVTTIGLSqiAGAQMLHVYKPRHWINCG-----------------QAGPLGWTVPAALGVAAA---DPDRQVVAL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 149 vgegsSNQGDFH---EGLNFAGVHKLPFVCVIINNKY---------AISVPDSLQYAAEKLSDRAL-GYGI-HGEQVDG- 213
Cdd:cd02006 82 -----SGDYDFQfmiEELAVGAQHRIPYIHVLVNNAYlglirqaqrAFDMDYQVNLAFENINSSELgGYGVdHVKVAEGl 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446490507 214 -------NDPLAMYKAMKEARERAISGQGSTLIEAVTSRMT 247
Cdd:cd02006 157 gckairvTKPEELAAAFEQAKKLMAEHRVPVVVEAILERVT 197
|
|
| TPP_PK |
cd02011 |
Thiamine pyrophosphate (TPP) family, Phosphoketolase (PK) subfamily, TPP-binding module; PK ... |
126-232 |
8.85e-05 |
|
Thiamine pyrophosphate (TPP) family, Phosphoketolase (PK) subfamily, TPP-binding module; PK catalyzes the conversion of D-xylulose 5-phosphate and phosphate to acetyl phosphate, D-glyceraldehyde-3-phosphate and H2O. This enzyme requires divalent magnesium ions and TPP for activity.
Pssm-ID: 238969 [Multi-domain] Cd Length: 227 Bit Score: 43.09 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 126 IPHAVGAAlalkMDGKKKIATATVGEGSSNQGDF------HEGLNFA---GVhkLPFVCViinNKYAISVPDSL-QYAAE 195
Cdd:cd02011 68 LSHAYGAV----FDNPDLIVACVVGDGEAETGPLatswhsNKFLNPAtdgAV--LPILHL---NGYKISNPTILaRISHE 138
|
90 100 110
....*....|....*....|....*....|....*..
gi 446490507 196 KLSDRALGYGIHGEQVDGNDPLAMYKAMKEARERAIS 232
Cdd:cd02011 139 ELEALFRGYGYEPYFVEGDDPETMHQAMAATLDWAIE 175
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
124-184 |
3.16e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 39.22 E-value: 3.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446490507 124 TQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGVHKLPFVCVIINNKYAI 184
Cdd:PRK12315 117 TSIALATGLAKARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAAELKSNLIIIVNDNQMSI 177
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
258-307 |
5.82e-03 |
|
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.
Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 37.28 E-value: 5.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446490507 258 RTKEEREALKKADCNEKFKKELLSAGIIDDAWLAEIEAEHKdiINKATKA 307
Cdd:cd00862 120 RALEFRDATRIVDTWEEFKEALNEKGIVLAPWCGEEECEEE--IKEETAA 167
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
123-240 |
8.90e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 37.96 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490507 123 ATQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGVHKLPFVcVIINNKYAISVPD-----------SLQ 191
Cdd:PLN02582 147 STTISAGLGMAVGRDLKGKKNNVVAVIGDGAMTAGQAYEAMNNAGYLDSDMI-VILNDNKQVSLPTatldgpappvgALS 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446490507 192 YAAEKL-SDRAL------GYGIhGEQVDGNDPLAMYKAMKEARErAISGQGSTLIE 240
Cdd:PLN02582 226 SALSRLqSSRPLrelrevAKGV-TKQIGGPMHELAAKVDEYARG-MISGSGSTLFE 279
|
|
| |
