|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-354 |
0e+00 |
|
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440106 Cd Length: 355 Bit Score: 564.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 1 MKTLEVDLGNRSYPIYIGTDLIDQPN-LFSACEKATSIYIVSNTTVAPLYAERLTKTLNTFGKPVKTIVLPDGESYKDWK 79
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDELGeLLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGEASKTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 80 NLQLIFDDLLKFGADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVGGKTGINHPLGKNMIGAFHQ 159
Cdd:COG0337 81 TLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 160 PAAVIADLNTLKTLPPRELSAGLAEVVKHGAIADAQFLDWIEANAIPLLACDTEAMGHAVLRSCEIKSAVVSADEREGGI 239
Cdd:COG0337 161 PRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 240 RATLNFGHTFGHAIEAGMGYgEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLPITPPKFGAERYMELMQ 319
Cdd:COG0337 241 RALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPALDPEALLAAMK 319
|
330 340 350
....*....|....*....|....*....|....*.
gi 2278648365 320 VDKKTEGGQIRYVVLEKIGKAQI-KSVADAQVIETL 354
Cdd:COG0337 320 RDKKVRGGKLRFVLLRGIGKAVIvDDVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-354 |
0e+00 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.
Pssm-ID: 341474 Cd Length: 343 Bit Score: 507.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 12 SYPIYIGTDLIDQPNLFSACEKATSIYIVSNTTVAPLYAERLTKTLNTFGKPVKTIVLPDGESYKDWKNLQLIFDDLLKF 91
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGEKSKSLETVERIYDFLLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 92 GADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVGGKTGINHPLGKNMIGAFHQPAAVIADLNTLK 171
Cdd:cd08195 81 GLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 172 TLPPRELSAGLAEVVKHGAIADAQFLDWIEANAIPLLACDTEAMGHAVLRSCEIKSAVVSADEREGGIRATLNFGHTFGH 251
Cdd:cd08195 161 TLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 252 AIEAGMGYgEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLPITPPKFGAERYMELMQVDKKTEGGQIRY 331
Cdd:cd08195 241 AIESASGY-KLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKDLDPEELLEAMKRDKKNRGGKIRF 319
|
330 340
....*....|....*....|....
gi 2278648365 332 VVLEKIGKAQI-KSVADAQVIETL 354
Cdd:cd08195 320 VLLKGIGKAVIvDDVSEEEIREAL 343
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
1-334 |
1.72e-162 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 461.55 E-value: 1.72e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 1 MKTLEVDLGNRSYPIYIGTDLIDQPNLFSACEKATSIYIVSNTTVAPLYAERLTKTLNTFGK--PVKTIVLPDGESYKDW 78
Cdd:PLN02834 67 TTVVKVDLGDRSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGPelTVESVILPDGEKYKDM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 79 KNLQLIFDDLLKFGADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVGGKTGINHPLGKNMIGAFH 158
Cdd:PLN02834 147 ETLMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 159 QPAAVIADLNTLKTLPPRELSAGLAEVVKHGAIADAQFLDWIEANAIPLLACDTEAMGHAVLRSCEIKSAVVSADEREGG 238
Cdd:PLN02834 227 QPQCVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 239 IRATLNFGHTFGHAIEAGMGYGEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLPITPP-KFGAERYMEL 317
Cdd:PLN02834 307 LRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPeKMTVEMFKSL 386
|
330
....*....|....*..
gi 2278648365 318 MQVDKKTEGGQIRYVVL 334
Cdd:PLN02834 387 MAVDKKVADGLLRLILL 403
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
66-325 |
9.03e-156 |
|
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide. 3-dehydroquinate (DHQ) synthase catalyzes the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.
Pssm-ID: 426414 Cd Length: 260 Bit Score: 437.70 E-value: 9.03e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 66 TIVLPDGESYKDWKNLQLIFDDLLKFGADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVGGKTGI 145
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 146 NHPLGKNMIGAFHQPAAVIADLNTLKTLPPRELSAGLAEVVKHGAIADAQFLDWIEANAIPLLACDTEAMGHAVLRSCEI 225
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 226 KSAVVSADEREGGIRATLNFGHTFGHAIEAGMGYGEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLPIT 305
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPTS 240
|
250 260
....*....|....*....|
gi 2278648365 306 PPKFGAERYMELMQVDKKTE 325
Cdd:pfam01761 241 LPDLDVEQLLAAMARDKKVR 260
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-351 |
2.23e-147 |
|
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme catalyzing the second of seven steps in the shikimate pathway of chorismate biosynthesis. Chorismate is the last common intermediate in the biosynthesis of all three aromatic amino acids. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273575 Cd Length: 344 Bit Score: 419.73 E-value: 2.23e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 13 YPIYIGTDLIDQpnLFSACEKATSIYIVSNTTVAPLYAERLTKTLNTFGKPVKTIVLPDGESYKDWKNLQLIFDDLLKFG 92
Cdd:TIGR01357 1 YPVHVGEGLLDQ--LVEELAEPSKLVIITDETVADLYGDKLLEALQALGYNVLKLTVPDGEESKSLETVQRLYDQLLEAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 93 ADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVGGKTGINHPLGKNMIGAFHQPAAVIADLNTLKT 172
Cdd:TIGR01357 79 LDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 173 LPPRELSAGLAEVVKHGAIADAQFLDWIEAN-AIPLLACDTEAMGHAVLRSCEIKSAVVSADEREGGIRATLNFGHTFGH 251
Cdd:TIGR01357 159 LPDRELRSGMAEVIKHGLIADAELFDELESNdKLRLNLQELEHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTIGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 252 AIEAGMGYGEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLPITPPK-FGAERYMELMQVDKKTEGGQIR 330
Cdd:TIGR01357 239 AIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKdLDVDELLNAMLNDKKNSGGKIR 318
|
330 340
....*....|....*....|.
gi 2278648365 331 YVVLEKIGKAQIKSVADAQVI 351
Cdd:TIGR01357 319 FVLLEEIGKAALAREVPDEMV 339
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-354 |
0e+00 |
|
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440106 Cd Length: 355 Bit Score: 564.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 1 MKTLEVDLGNRSYPIYIGTDLIDQPN-LFSACEKATSIYIVSNTTVAPLYAERLTKTLNTFGKPVKTIVLPDGESYKDWK 79
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDELGeLLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGEASKTLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 80 NLQLIFDDLLKFGADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVGGKTGINHPLGKNMIGAFHQ 159
Cdd:COG0337 81 TLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 160 PAAVIADLNTLKTLPPRELSAGLAEVVKHGAIADAQFLDWIEANAIPLLACDTEAMGHAVLRSCEIKSAVVSADEREGGI 239
Cdd:COG0337 161 PRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 240 RATLNFGHTFGHAIEAGMGYgEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLPITPPKFGAERYMELMQ 319
Cdd:COG0337 241 RALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPALDPEALLAAMK 319
|
330 340 350
....*....|....*....|....*....|....*.
gi 2278648365 320 VDKKTEGGQIRYVVLEKIGKAQI-KSVADAQVIETL 354
Cdd:COG0337 320 RDKKVRGGKLRFVLLRGIGKAVIvDDVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-354 |
0e+00 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.
Pssm-ID: 341474 Cd Length: 343 Bit Score: 507.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 12 SYPIYIGTDLIDQPNLFSACEKATSIYIVSNTTVAPLYAERLTKTLNTFGKPVKTIVLPDGESYKDWKNLQLIFDDLLKF 91
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGEKSKSLETVERIYDFLLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 92 GADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVGGKTGINHPLGKNMIGAFHQPAAVIADLNTLK 171
Cdd:cd08195 81 GLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 172 TLPPRELSAGLAEVVKHGAIADAQFLDWIEANAIPLLACDTEAMGHAVLRSCEIKSAVVSADEREGGIRATLNFGHTFGH 251
Cdd:cd08195 161 TLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 252 AIEAGMGYgEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLPITPPKFGAERYMELMQVDKKTEGGQIRY 331
Cdd:cd08195 241 AIESASGY-KLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKDLDPEELLEAMKRDKKNRGGKIRF 319
|
330 340
....*....|....*....|....
gi 2278648365 332 VVLEKIGKAQI-KSVADAQVIETL 354
Cdd:cd08195 320 VLLKGIGKAVIvDDVSEEEIREAL 343
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
1-334 |
1.72e-162 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 461.55 E-value: 1.72e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 1 MKTLEVDLGNRSYPIYIGTDLIDQPNLFSACEKATSIYIVSNTTVAPLYAERLTKTLNTFGK--PVKTIVLPDGESYKDW 78
Cdd:PLN02834 67 TTVVKVDLGDRSYPIYIGSGLLDHGELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGPelTVESVILPDGEKYKDM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 79 KNLQLIFDDLLKFGADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVGGKTGINHPLGKNMIGAFH 158
Cdd:PLN02834 147 ETLMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 159 QPAAVIADLNTLKTLPPRELSAGLAEVVKHGAIADAQFLDWIEANAIPLLACDTEAMGHAVLRSCEIKSAVVSADEREGG 238
Cdd:PLN02834 227 QPQCVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 239 IRATLNFGHTFGHAIEAGMGYGEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLPITPP-KFGAERYMEL 317
Cdd:PLN02834 307 LRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPeKMTVEMFKSL 386
|
330
....*....|....*..
gi 2278648365 318 MQVDKKTEGGQIRYVVL 334
Cdd:PLN02834 387 MAVDKKVADGLLRLILL 403
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
66-325 |
9.03e-156 |
|
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide. 3-dehydroquinate (DHQ) synthase catalyzes the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.
Pssm-ID: 426414 Cd Length: 260 Bit Score: 437.70 E-value: 9.03e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 66 TIVLPDGESYKDWKNLQLIFDDLLKFGADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVGGKTGI 145
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 146 NHPLGKNMIGAFHQPAAVIADLNTLKTLPPRELSAGLAEVVKHGAIADAQFLDWIEANAIPLLACDTEAMGHAVLRSCEI 225
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 226 KSAVVSADEREGGIRATLNFGHTFGHAIEAGMGYGEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLPIT 305
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPTS 240
|
250 260
....*....|....*....|
gi 2278648365 306 PPKFGAERYMELMQVDKKTE 325
Cdd:pfam01761 241 LPDLDVEQLLAAMARDKKVR 260
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-351 |
2.23e-147 |
|
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme catalyzing the second of seven steps in the shikimate pathway of chorismate biosynthesis. Chorismate is the last common intermediate in the biosynthesis of all three aromatic amino acids. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273575 Cd Length: 344 Bit Score: 419.73 E-value: 2.23e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 13 YPIYIGTDLIDQpnLFSACEKATSIYIVSNTTVAPLYAERLTKTLNTFGKPVKTIVLPDGESYKDWKNLQLIFDDLLKFG 92
Cdd:TIGR01357 1 YPVHVGEGLLDQ--LVEELAEPSKLVIITDETVADLYGDKLLEALQALGYNVLKLTVPDGEESKSLETVQRLYDQLLEAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 93 ADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVGGKTGINHPLGKNMIGAFHQPAAVIADLNTLKT 172
Cdd:TIGR01357 79 LDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 173 LPPRELSAGLAEVVKHGAIADAQFLDWIEAN-AIPLLACDTEAMGHAVLRSCEIKSAVVSADEREGGIRATLNFGHTFGH 251
Cdd:TIGR01357 159 LPDRELRSGMAEVIKHGLIADAELFDELESNdKLRLNLQELEHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTIGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 252 AIEAGMGYGEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLPITPPK-FGAERYMELMQVDKKTEGGQIR 330
Cdd:TIGR01357 239 AIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKdLDVDELLNAMLNDKKNSGGKIR 318
|
330 340
....*....|....*....|.
gi 2278648365 331 YVVLEKIGKAQIKSVADAQVI 351
Cdd:TIGR01357 319 FVLLEEIGKAALAREVPDEMV 339
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
12-339 |
6.60e-101 |
|
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose; 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multistep reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. They are important antibacterial agents. DOIS is a homolog of the dehydroquinate synthase which catalyzes the cyclization of 3-deoxy-D-arabino-heputulosonate-7-phosphate to dehydroquinate (DHQ) in the shikimate pathway.
Pssm-ID: 341476 Cd Length: 355 Bit Score: 302.20 E-value: 6.60e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 12 SYPIYIGTDLIDQPNLFSACEKATSIYIVSNTTVAPLYAERLTKTLNTFGKPVKTIVLPDGESYKDWKNLQLIFDDLLKF 91
Cdd:cd08197 1 LTDIYLGRGILESLLSILEELKADRHFLVTDSNVNDLYGDRLLEGLKKAGIPVELLVVPAGESNKTLSTLTELAERLIAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 92 GADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVGGKTGINHPLGKNMIGAFHQPAAVIADLNTLK 171
Cdd:cd08197 81 GITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 172 TLPPRELSAGLAEVVKHGAIADAQFLDWIEANAIPLLACDTEAMGHAVLRSCEIKSAVVSADEREGGIRATLNFGHTFGH 251
Cdd:cd08197 161 TLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFLEKVIDLSIEAKLEVLSNDPYEKKEGLILEYGHTVGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 252 AIEAGMGyGEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLP-ITPPKFGAERYMELMQVDKK-----TE 325
Cdd:cd08197 241 AIELLSG-GELSHGEAVAIGMCVAAEISHLLGLLSEEDVDKHYELLEKIGLPtIIPDGISVEAILEVIRYDNKrgyikAD 319
|
330
....*....|....
gi 2278648365 326 GGQIRYVVLEKIGK 339
Cdd:cd08197 320 ADTIRMVLLEKLGK 333
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
12-339 |
1.30e-90 |
|
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase; This group contains dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. These proteins exhibit the dehydroquinate synthase structural fold. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multi-step reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. 2-epi-5-epi-valiolone synthases catalyze the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications.
Pssm-ID: 341448 [Multi-domain] Cd Length: 328 Bit Score: 274.67 E-value: 1.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 12 SYPIYIGTDLIDQPNLFSACEKATSIYIVSNTTVAPLYAERLTKTLNTFgKPVKTIVLPDGESYKDWKNLQLIFDDLLKF 91
Cdd:cd08169 1 EYPVFFGEGVFESVNSYIPRDAFDQCLIIVDSGVPDLIVNYLAEYFGYY-LEVHVFIIQGGEAYKTFQTVVEELERAAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 92 GADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVGGKTGINHPLGKNMIGAFHQPAAVIADLNTLK 171
Cdd:cd08169 80 HLNRHSAVVAVGGGATGDVVGFAAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 172 TLPPRELSAGLAEVVKHGAIADAQFLDWIEANAIPLLACDTEAMGHAVLRSCEIKSAVVSADEREGGIRATLNFGHTFGH 251
Cdd:cd08169 160 TLPFRQVRAGMAELVKMALIADNDFFEFLEDKANSATVYSPEQLEKLINKCISLKLDVVVADEDEQGKRRGLNYGHTFGH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 252 AIEAGMGYgEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLPI-TPPKFGAERYMELMQVDKKTEGGQIR 330
Cdd:cd08169 240 ALELASGY-KIPHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWLLNKLGLPLdHPLALDPDSLYEYLESDKKSLYGNLG 318
|
....*....
gi 2278648365 331 YVVLEKIGK 339
Cdd:cd08169 319 MILLSGVGD 327
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
12-340 |
9.90e-77 |
|
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications. Validamycin A is an antifungal antibiotic which has a strong trehalase inhibitory activity and has been used to control sheath blight disease in rice caused by Rhizoctonia solani. Acarbose is an alpha-glucosidase inhibitor used for the treatment of type II insulin-independent diabetes. Salbostatin produced by Streptomyces albus also belongs to this family. It exhibits strong trehalase inhibitory activity.
Pssm-ID: 341478 Cd Length: 349 Bit Score: 240.12 E-value: 9.90e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 12 SYPIYIGTDLID--QPNLFSACEKATS-IYIVSNTTVAPLYAERLTKTLNTFGKPVKTIVLPDGESYKDWKNLQLIFDDL 88
Cdd:cd08199 1 SYDVVLVDDLFDpeNPTLADAYGRPGRrRLVVVDENVDRLYGARIRAYFAAHGIEATILVLPGGEANKTMETVLRIVDAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 89 LKFGADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVGGKTGINHPLGKNMIGAFHQPAAVIADLN 168
Cdd:cd08199 81 DDFGLDRREPVIAIGGGVLLDVVGFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAYYPPVATLLDRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 169 TLKTLPPRELSAGLAEVVKHGAIADAQFLDWIEANAIPLLA---CDTEAmGHAVLRsceiKSAVVSADE-----REGGIR 240
Cdd:cd08199 161 FLKTLPRRHIRNGLAEIIKMALVKDAELFELLEEHGAALVEtrfFQDEV-ADEIIR----RAIQGMLEElapnlWEHDLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 241 ATLNFGHTFGHAIEAGMGYgEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLPITPPKFGAERYMELMQV 320
Cdd:cd08199 236 RLVDFGHTFSPILEMAAAP-ELLHGEAVAIDMALSAVLAYRRGLLSEEELDRILRLMRRLGLPVWHPLCTPDLLWRALED 314
|
330 340
....*....|....*....|
gi 2278648365 321 DKKTEGGQIRYVVLEKIGKA 340
Cdd:cd08199 315 IVKHRDGLQRLPLPKGIGEC 334
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
49-338 |
2.71e-69 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 226.28 E-value: 2.71e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 49 YAERLTKTLNTFGKPVKTIVLPDGESYKDWKNLQLIFDDLLKFGADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVP 128
Cdd:PRK14021 223 HSDRARTLLRQGGYEVSDIVIPDAEAGKTIEVANGIWQRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCP 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 129 TTLLAQVDSSVGGKTGINHPLGKNMIGAFHQPAAVIADLNTLKTLPPRELSAGLAEVVKHGAIADAQFLDWIEANAIPLL 208
Cdd:PRK14021 303 TSLLAMVDASTGGKTGINTPQGKNLVGSFYTPAGVLADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAELR 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 209 ACDTEAMGHAVL---------RSCEIKSAVVSADEREGGIRATLNFGHTFGHAIEAgMGYGEWLHGEAVGCGMVLGADLS 279
Cdd:PRK14021 383 AFDGSTFLGSPLedvvaelieRTVKVKAYHVSSDLKEAGLREFLNYGHTLGHAIEK-LEHFRWRHGNAVAVGMVYAAELA 461
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2278648365 280 RRLNYISEADVQRLTKIIQSMNLPITPPKFGAERYMELMQVDKKTEGGQIRYVVLEKIG 338
Cdd:PRK14021 462 HLLGYIDQDLVDYHRSLLASLGLPTSWNGGSFDDVLALMHRDKKARGNELRFVVLDEIG 520
|
|
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
67-340 |
2.51e-60 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 198.97 E-value: 2.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 67 IVLPDGESYK-DWKNLQLIFDDLLKFGADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVGGKTGI 145
Cdd:PRK06203 82 LVVPGGEAAKnDPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKNGI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 146 NHPLGKNMIGAFHQPAAVIADLNTLKTLPPRELSAGLAEVVKHGAIADAQFLDWIEANAIPLLACDTEAMGHAVLRSCEI 225
Cdd:PRK06203 162 NAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAARDPEAMEELIYRCAEL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 226 KSAVV--SADEREGGIRATLNFGHTFGHAIEAGMGYgEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLP 303
Cdd:PRK06203 242 HLEHIagGGDPFEFGSSRPLDFGHWSAHKLEQLTNY-ALRHGEAVAIGIALDSLYSYLLGLLSEAEAQRILALLRALGFP 320
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2278648365 304 ITPPKFGA--ERYMELMQ-VDKKTE--GGQIRYVVLEKIGKA 340
Cdd:PRK06203 321 LYHPALATrdSKGRELLKgLEEFREhlGGRLTITLLTGIGRG 362
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
65-319 |
3.44e-59 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; This family contains dehydroquinate synthase-like proteins. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. The activity of DHQS requires NAD as cofactor. Proteins of this family share sequence similarity and functional motifs with that of dehydroquinate synthase, but the specific function has not been characterized.
Pssm-ID: 341477 Cd Length: 366 Bit Score: 195.10 E-value: 3.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 65 KTIVLPDGESYKdwkNLQLIFDDLLK----FGADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVG 140
Cdd:cd08198 68 PPLIVPGGEAVK---NDPALVEEILSaihdHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 141 GKTGINHPLGKNMIGAFHQPAAVIADLNTLKTLPPRELSAGLAEVVKHGAIADAQFLDWIEANAIPLLACDTEAMGHAVL 220
Cdd:cd08198 145 VKNGINFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLERNAAALRQRDPDAMEKLIR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 221 RSCE--IKSAVVSADEREGGIRATLNFGHTFGHAIEAGMGYgEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQ 298
Cdd:cd08198 225 RCAElhLDHIAASGDPFETGSARPLDFGHWSAHKLEQLSGY-ALRHGEAVAIGIALDSLYARLLGLLSREDFDRILALLQ 303
|
250 260
....*....|....*....|.
gi 2278648365 299 SMNLPITPPKFGAERYMELMQ 319
Cdd:cd08198 304 NLGLPLWHPLLERDGVLELLD 324
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
63-351 |
1.20e-39 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 146.59 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 63 PVKTIVLPDGESYKDWKNLQLIFDDLLKFGADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAQVDSSVGGK 142
Cdd:PRK13951 205 PENRLLFPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQVDASVGGK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 143 TGINHPLGKNMIGAFHQPAAVIADLNTLKTLPPRELSAGLAEVVKHGAIADAQFLDWIEANAIplLACDTEAMGHAVLRS 222
Cdd:PRK13951 285 NAIDFAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSGRGVELFDEPEKI--EKRNLRVLSEMVKIS 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 223 CEIKSAVVSADEREGGIRATLNFGHTFGHAIEAGMGYGewlHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMnL 302
Cdd:PRK13951 363 VEEKARIVMEDPYDMGLRHALNLGHTLGHVYEMLEGVP---HGIAVAWGIEKETMYLYRKGIVPKETMRWIVEKVKQI-V 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2278648365 303 PITPPKFGAERYMELMQVDKKTEGGQ-IRYVVLEKIGKAQIKSVADAQVI 351
Cdd:PRK13951 439 PIPVPSVDVEKARNLILNDKKILKGSrVRLPYVKEIGKIEFLEVDPLELL 488
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
90-305 |
4.52e-23 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 97.05 E-value: 4.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 90 KFGADRQTMLVALGGGVIGDMTGFAAASFMRGIRFIQVPTTLLAqvDSSVGGKTGINHPLGKN-MIGAFHQPAAVIADLN 168
Cdd:cd07766 72 RARAAEADAVIAVGGGSTLDTAKAVAALLNRGIPFIIVPTTAST--DSEVSPKSVITDKGGKNkQVGPHYNPDVVFVDTD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 169 TLKTLPPRELSAGLAEVVKHgaiadaqfldWIEanaipllacdteaMGHAVLRSCEIKSAvvsadereGGIRATLNFGHT 248
Cdd:cd07766 150 ITKGLPPRQVASGGVDALAH----------AVE-------------LEKVVEAATLAGMG--------LFESPGLGLAHA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2278648365 249 FGHAIEAGMGYgewLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLPIT 305
Cdd:cd07766 199 IGHALTAFEGI---PHGEAVAVGLPYVLKVANDMNPEPEAAIEAVFKFLEDLGLPTH 252
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
33-310 |
1.07e-14 |
|
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids.
Pssm-ID: 341479 [Multi-domain] Cd Length: 331 Bit Score: 74.14 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 33 KATSIYIVSNTTVAplYAERLTKTLNTfgkpvktivLPDGESYKdwkNLQLIFDDLLKFGAdrQTMLVALGGGVIGDMTG 112
Cdd:cd08549 24 KRVLIITGKNTKAK--YCRFFYDQLKT---------VCDIVYYD---NIDNLEDELKKYTF--YDCVIGIGGGRSIDTGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 113 FAaaSFMRGIRFIQVPTTllAQVD--SSVGGKTGINHPLGKNMIGAfhqPAAVIADLNTLKTLPPRELSAGLAEVV-KHG 189
Cdd:cd08549 88 YL--AYKLKIPFISVPTS--ASNDgiASPIVSLRIPGVKKTFMADA---PIAIIADTEIIKKSPRRLLSAGIGDLVsNIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 190 AIADAQFLDWIEANAIPLLAcdteamghAVLRSCEIKSAVVSADE---REGGIR----ATLNFG---------------- 246
Cdd:cd08549 161 AVLDWKLAHKEKGEKYSEFA--------AILSKTSAKELVSYVLKasdLEEYHRvlvkALVGSGiamaiagssrpasgse 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2278648365 247 HTFGHAIEA---GMGYGEWLHGEAVGCGMVLGADLSRRLNYISEADVQRLTKIIQSMNLPITPPKFG 310
Cdd:cd08549 233 HLFSHALDKlkeEYLNINVLHGEQVGVGTIIMSYLHEKENKKLSGLHERIKMILKKVGAPTTAKQLG 299
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
15-306 |
3.14e-14 |
|
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer.
Pssm-ID: 341454 Cd Length: 340 Bit Score: 72.54 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 15 IYIGTDLIDQ-PNLFSACEKATSIYIVSNTTVAPLYAERLTKTLNTFGKPVKTIVLPDGES-YKDWKNLQLIFDDLlKFG 92
Cdd:cd08175 4 IVIGEGALKKlPEYLKELFGGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGEGDlIADEAAVGKVLLEL-EKD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 93 ADrqtMLVALGGGVIGDMTGFAaaSFMRGIRFIQVPTTllaqvdSSVGGKTGINHPLgknMIGAF------HQPAAVIAD 166
Cdd:cd08175 83 TD---LIIAVGSGTINDLTKYA--AYKLGIPYISVPTA------PSMDGYTSSGAPI---IVDGVkktfpaHAPKAIFAD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 167 LNTLKTLPPRELSAGLAEVV-KHGAIAdaqflDWIEANAI------PLLACDTEAMGHAVLRSCE-IKSAVVSADER--- 235
Cdd:cd08175 149 LDVLANAPQRMIAAGFGDLLgKYTALA-----DWKLSHLLggeyycPEVADLVQEALEKCLDNAEgIAARDPEAIEAlme 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 236 ---EGGIrATLNFG---------HTFGHAIE---AGMGYGEWLHGEAVGCGMVLGADLsrrlnYISEA--DVQRLTKIIQ 298
Cdd:cd08175 224 aliLSGL-AMQLVGnsrpasgaeHHLSHYWEmefLRLGKPPVLHGEKVGVGTLLIAAL-----YILEQlpPPEELRELLR 297
|
....*...
gi 2278648365 299 SMNLPITP 306
Cdd:cd08175 298 KAGAPTTP 305
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
15-305 |
6.77e-11 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 62.57 E-value: 6.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 15 IYIGTDLIDQ-PNLFSACEKATSIYIVSNTTVAPLYAERLTKTLNTFGKPVKTIvlpDGESYKDWKNLQLIFDDLLKFGA 93
Cdd:cd08173 5 VVVGHGAINKiGEVLKKLLLGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIV---DIATIEEAAEVEKVKKLIKESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 94 DrqtMLVALGGGVIGDMTgfAAASFMRGIRFIQVPTTllAQVDssvggktGINHPL------GKNM-IGAfHQPAAVIAD 166
Cdd:cd08173 82 D---FIIGVGGGKVIDVA--KYAAYKLNLPFISIPTS--ASHD-------GIASPFasikggDKPYsIKA-KAPIAIIAD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 167 LNTLKTLPPRELSAGLAEVV-KHGAIADAQFLDWI------EANAIplLAcDTEAMgHAVLRSCEIKsavvsaDEREGGI 239
Cdd:cd08173 147 TEIISKAPKRLLAAGCGDLIsNITAVKDWRLAHRLkgeyysEYAAS--LA-LMSAK-LIIENADLIK------PGLEEGV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 240 R----ATLNFG----------------HTFGHAIEAgMGYGEWLHGEAVGCGMVLGAdlsrrlnYISEADVQRLTKIIQS 299
Cdd:cd08173 217 RtvvkALISSGvamsiagssrpasgseHLFSHALDK-LAPGPALHGEQCGVGTIMMA-------YLHGGDWKEIREALKK 288
|
....*.
gi 2278648365 300 MNLPIT 305
Cdd:cd08173 289 IGAPTT 294
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
16-269 |
1.50e-10 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 60.78 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 16 YIGTDLIDQPNLFSACEKATSIYIVSNTTVAPLYAERLTKTLNTFGKPVKTIVLPDGESykDWKNLQLIFDdllKFGADR 95
Cdd:pfam13685 1 VIGPGALGRLGEYLAELGFRRVALVADANTYAAAGRKVAESLKRAGIEVETRLEVAGNA--DMETAEKLVG---ALRERD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 96 QTMLVALGGGVIGDMTGFAAasFMRGIRFIQVPTTLlaqvdsSVGGKTGINHPL----GKNMIGAfHQPAAVIADLNTLK 171
Cdd:pfam13685 76 ADAVVGVGGGTVIDLAKYAA--FKLGKPFISVPTAA------SNDGFASPGASLtvdgKKRSIPA-AAPFGVIADTDVIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 172 TLPPRELSAGLAEVV-KHGAIADAQFLDWIEANAIPLLACDTEAMGHAVLRSCEIKSAVVSADEREGGIRATLNFG---- 246
Cdd:pfam13685 147 AAPRRLLASGVGDLLaKITAVADWELAHAEEVAAPLALLSAAMVMNFADRPLRDPGDIEALAELLSALAMGGAGSSrpas 226
|
250 260
....*....|....*....|....*.
gi 2278648365 247 ---HTFGHAIEAgMGYGEWLHGEAVG 269
Cdd:pfam13685 227 gseHLISHALDM-IAPKQALHGEQVG 251
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
15-310 |
3.62e-10 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 60.68 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 15 IYIGTDLIDQ-PNLFSACEKATSIYIVSNTTVAPLYAERLTKTLNTFGKPvkTIVLPDGESYKdwkNLQLIFDDLLKFGA 93
Cdd:PRK00843 14 VVVGHGVLDDiGDVCSDLKLTGRALIVTGPTTKKIAGDRVEENLEDAGDV--EVVIVDEATME---EVEKVEEKAKDVNA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 94 DrqtMLVALGGGVIGDMTGFAaaSFMRGIRFIQVPTTllAQVDSSVGGKTGINHpLGKNMIGAFHQPAAVIADLNTLKTL 173
Cdd:PRK00843 89 G---FLIGVGGGKVIDVAKLA--AYRLGIPFISVPTA--ASHDGIASPRASIKG-GGKPVSVKAKPPLAVIADTEIIAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 174 PPRELSAGLAEVV-KHGAIadaqfLDWIEANAIpllacDTEAMGH--AVLRSCEIKSAVVSAD----EREGGIR----AT 242
Cdd:PRK00843 161 PYRLLAAGCGDIIsNYTAV-----KDWRLAHRL-----RGEYYSEyaAALSLMTAKMLIENADiikpGLEESARlvvkAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 243 LNFG----------------HTFGHAIEAgMGYGEWLHGEAVGCGMVLGAdlsrrlnYISEADVQRLTKIIQSMNLPITP 306
Cdd:PRK00843 231 ISSGvamsiagssrpasgseHLFSHALDR-LAPGPALHGEQCGVGTIIMM-------YLHGGDWRKIRDALKKIGAPTTA 302
|
....
gi 2278648365 307 PKFG 310
Cdd:PRK00843 303 KELG 306
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
37-305 |
3.14e-06 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 48.30 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 37 IYIVSNTTVAPLYAERLTKTLNTFGKPVKTIVLPdGESykDWKNLQLIFDDLLKFGADrqtMLVALGGGVIGDmTGFAAA 116
Cdd:cd08550 25 ALIIGGKTALEAVGEKLEKSLEEAGIDYEVEVFG-GEC--TEENIERLAEKAKEEGAD---VIIGIGGGKVLD-TAKAVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 117 SFMrGIRFIQVPT--------TLLAQVDSSVGGKTGiNHPLGKNmigafhqPAAVIADLNTLKTLPPRELSAGlaevvkh 188
Cdd:cd08550 98 DRL-GLPVVTVPTiaatcaawSALSVLYDEEGEFLG-YSLLKRS-------PDLVLVDTDIIAAAPVRYLAAG------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 189 gaIADAqFLDWIEANAIpLLACDTEAMGHAVLRSCEI---------KSAVVSADERE-------------------GGIR 240
Cdd:cd08550 162 --IGDT-LAKWYEARPS-SRGGPDDLALQAAVQLAKLaydllleygVQAVEDVRQGKvtpaledvvdaiillaglvGSLG 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 241 AtlNFGHT-FGHAIEAGM----GYGEWLHGEAVGCGMVLGAdlsrRLNYISEADVQRLTKIIQSMNLPIT 305
Cdd:cd08550 238 G--GGCRTaAAHAIHNGLtklpETHGTLHGEKVAFGLLVQL----ALEGRSEEEIEELIEFLRRLGLPVT 301
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
99-337 |
3.98e-06 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 47.90 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 99 LVALGGGVIGDMTGFAAasFMRGIRFIQVPTTLlaqvdSSvggkTGINHPL------GKNM-IGAfHQPAAVIADLNTLK 171
Cdd:cd08174 81 IVGIGGGKVLDVAKYAA--FLSKLPFISVPTSL-----SN----DGIASPVavlkvdGKRKsLGA-KMPYGVIVDLDVIK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 172 TLPPRELSAGLAEVV-KHGAIAdaqflDWIeanaiplLACDT--EAM-GHAVLRSceiKSAVVSADEREGGIRATLNF-- 245
Cdd:cd08174 149 SAPRRLILAGIGDLIsNITALY-----DWK-------LAEEKggEPVdDFAYLLS---RTAADSLLNTPGKDIKDDEFlk 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278648365 246 ---------G----------------HTFGHAIEAgMGYGEWLHGEAVGCGMVLGAdlsrrlnYISEADVQRLTKIIQSM 300
Cdd:cd08174 214 elaeslvlsGiameiagssrpasgseHLISHALDK-LFPGPALHGIQVGLGTYFMS-------FLQGQRYEEIRDVLKRT 285
|
250 260 270
....*....|....*....|....*....|....*....
gi 2278648365 301 NLPITPPKFG--AERYMELMQVDKKTEGGqiRYVVLEKI 337
Cdd:cd08174 286 GFPLNPSDLGltKEEFIEAVKLAPSTRPG--RYTILEEL 322
|
|
| |
