|
Name |
Accession |
Description |
Interval |
E-value |
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
14-403 |
0e+00 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 650.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 14 LQPIRQSFSVTFDYGVHFTNAVFDTKNPLLAKVIATDGETKPKKVLAVVDSGLLQSRRMLLKQIATYSDHYADTLKLAAD 93
Cdd:PRK06203 1 MRVIRQSFAVTFEYPVYFTRDLFSPENPLLAEVLAADGEGKPKKVLVVIDSGVLRAHPDLLEQITAYFAAHADVLELVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 94 PIIVLGGEEAKNDPNELLKIHQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNG 173
Cdd:PRK06203 81 PLVVPGGEAAKNDPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 174 INAFGKKNFLGTFAPPYAVLNDFTFLTSLNDRDWRSGIAEAVKVALIKDADFFEYISTYAHALVCRDLNRMQNVIYRCAQ 253
Cdd:PRK06203 161 INAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAARDPEAMEELIYRCAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 254 LHMDHIANNGDSFEKGSSRPLDFGHWAAHKLEQLTNYRLRHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLGFV 333
Cdd:PRK06203 241 LHLEHIAGGGDPFEFGSSRPLDFGHWSAHKLEQLTNYALRHGEAVAIGIALDSLYSYLLGLLSEAEAQRILALLRALGFP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 334 LYLPELSEQMtepEHPRSLFRGLNEFREHLGGELTLTLLQRIGKGVEIHEVDMSLFRQAIWLLGEFYNSS 403
Cdd:PRK06203 321 LYHPALATRD---SKGRELLKGLEEFREHLGGRLTITLLTGIGRGIEVHEIDLDLLRQAIARLAERAKAS 387
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
26-393 |
0e+00 |
|
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: 556.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 26 DYGVHFTNAVFDTKNPLLAKVIATDGETKPKKVLAVVDSGLLQSRRMLLKQIATYSDHYADTLKLAADPIIVLGGEEAKN 105
Cdd:cd08198 1 SYPVCFTHDLFSPDNPLLRALLVRRGPGRRHRVLFVIDSGVAAAHPALVKQIERYFQAHPDRLELVAPPLIVPGGEAVKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 106 DPNELLKIHQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNGINAFGKKNFLGT 185
Cdd:cd08198 81 DPALVEEILSAIHDHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGINFFGKKNFLGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 186 FAPPYAVLNDFTFLTSLNDRDWRSGIAEAVKVALIKDADFFEYISTYAHALVCRDLNRMQNVIYRCAQLHMDHIANNGDS 265
Cdd:cd08198 161 FAPPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLERNAAALRQRDPDAMEKLIRRCAELHLDHIAASGDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 266 FEKGSSRPLDFGHWAAHKLEQLTNYRLRHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLGFVLYLPELseqmtE 345
Cdd:cd08198 241 FETGSARPLDFGHWSAHKLEQLSGYALRHGEAVAIGIALDSLYARLLGLLSREDFDRILALLQNLGLPLWHPLL-----E 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1199832887 346 PEHPRSLFRGLNEFREHLGGELTLTLLQRIGKGVEIHEVDMSLFRQAI 393
Cdd:cd08198 316 RDGVLELLDGLEEFREHLGGRLTITLLRGIGVGVEVHEIDLDLMEEAI 363
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
19-393 |
9.90e-129 |
|
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: 374.81 E-value: 9.90e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 19 QSFSVTFD---YGVHFTNAVFDTKNPLLAKVIatdgetKPKKVLAVVDSGLlqsRRMLLKQIATYSDHYAdtlkLAADPI 95
Cdd:COG0337 2 QTLTVNLGersYDIRIGRGLLDELGELLAELL------KGRRVLVVTDENV---APLYGERLRAALEAAG----FEVHLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 96 IVLGGEEAKNdPNELLKIHQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNGIN 175
Cdd:COG0337 69 VLPDGEASKT-LETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 176 AFGKKNFLGTFAPPYAVLNDFTFLTSLNDRDWRSGIAEAVKVALIKDADFFEYISTYAHALVCRDLNRMQNVIYRCAQLH 255
Cdd:COG0337 148 HPGGKNLIGAFHQPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 256 MDHIAnnGDSFEKGSSRPLDFGHWAAHKLEQLTNYRLRHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLGFVLY 335
Cdd:COG0337 228 AEVVA--ADERESGLRALLNFGHTFGHAIEAATGYRLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTR 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199832887 336 LPELSeqmtepehPRSLFRGLNEFREHLGGELTLTLLQRIGKGVEIHEVDMSLFRQAI 393
Cdd:COG0337 306 LPALD--------PEALLAAMKRDKKVRGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
94-340 |
7.03e-86 |
|
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: 262.05 E-value: 7.03e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 94 PIIVLGGEEAKNdPNELLKIHQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNG 173
Cdd:pfam01761 1 TIVIPDGEKSKT-LETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 174 INAFGKKNFLGTFAPPYAVLNDFTFLTSLNDRDWRSGIAEAVKVALIKDADFFEYISTYAHALVCRDLNRMQNVIYRCAQ 253
Cdd:pfam01761 80 INHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 254 LHMDHIAnnGDSFEKGSSRPLDFGHWAAHKLEQLTNY-RLRHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLGF 332
Cdd:pfam01761 160 VKADVVA--QDEKESGLRALLNLGHTFGHAIEALSGYgALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGL 237
|
....*...
gi 1199832887 333 VLYLPELS 340
Cdd:pfam01761 238 PTSLPDLD 245
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
27-331 |
2.85e-63 |
|
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: 206.71 E-value: 2.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 27 YGVHFTNAVFDTKNPLLAKviatdgetkPKKVLAVVDSgllqsrrmllkqiaTYSDHYADTLKLA-------ADPIIVLG 99
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEELAE---------PSKLVIITDE--------------TVADLYGDKLLEAlqalgynVLKLTVPD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 100 GEEAKNDPNeLLKIHQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNGINAFGK 179
Cdd:TIGR01357 58 GEESKSLET-VQRLYDQLLEAGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 180 KNFLGTFAPPYAVLNDFTFLTSLNDRDWRSGIAEAVKVALIKDADFFEYISTYAHALVCR-DLNRMQNVIYRCAQLHMDH 258
Cdd:TIGR01357 137 KNLIGTFYQPKAVLIDPDFLKTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLqELEHLEELIKRSIEVKASI 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199832887 259 IAnnGDSFEKGSSRPLDFGHWAAHKLEQLTNYR-LRHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLG 331
Cdd:TIGR01357 217 VA--EDEKESGLRAILNFGHTIGHAIEAEAGYGkIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYG 288
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
14-403 |
0e+00 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 650.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 14 LQPIRQSFSVTFDYGVHFTNAVFDTKNPLLAKVIATDGETKPKKVLAVVDSGLLQSRRMLLKQIATYSDHYADTLKLAAD 93
Cdd:PRK06203 1 MRVIRQSFAVTFEYPVYFTRDLFSPENPLLAEVLAADGEGKPKKVLVVIDSGVLRAHPDLLEQITAYFAAHADVLELVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 94 PIIVLGGEEAKNDPNELLKIHQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNG 173
Cdd:PRK06203 81 PLVVPGGEAAKNDPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 174 INAFGKKNFLGTFAPPYAVLNDFTFLTSLNDRDWRSGIAEAVKVALIKDADFFEYISTYAHALVCRDLNRMQNVIYRCAQ 253
Cdd:PRK06203 161 INAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAARDPEAMEELIYRCAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 254 LHMDHIANNGDSFEKGSSRPLDFGHWAAHKLEQLTNYRLRHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLGFV 333
Cdd:PRK06203 241 LHLEHIAGGGDPFEFGSSRPLDFGHWSAHKLEQLTNYALRHGEAVAIGIALDSLYSYLLGLLSEAEAQRILALLRALGFP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 334 LYLPELSEQMtepEHPRSLFRGLNEFREHLGGELTLTLLQRIGKGVEIHEVDMSLFRQAIWLLGEFYNSS 403
Cdd:PRK06203 321 LYHPALATRD---SKGRELLKGLEEFREHLGGRLTITLLTGIGRGIEVHEIDLDLLRQAIARLAERAKAS 387
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
26-393 |
0e+00 |
|
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: 556.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 26 DYGVHFTNAVFDTKNPLLAKVIATDGETKPKKVLAVVDSGLLQSRRMLLKQIATYSDHYADTLKLAADPIIVLGGEEAKN 105
Cdd:cd08198 1 SYPVCFTHDLFSPDNPLLRALLVRRGPGRRHRVLFVIDSGVAAAHPALVKQIERYFQAHPDRLELVAPPLIVPGGEAVKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 106 DPNELLKIHQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNGINAFGKKNFLGT 185
Cdd:cd08198 81 DPALVEEILSAIHDHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGINFFGKKNFLGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 186 FAPPYAVLNDFTFLTSLNDRDWRSGIAEAVKVALIKDADFFEYISTYAHALVCRDLNRMQNVIYRCAQLHMDHIANNGDS 265
Cdd:cd08198 161 FAPPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLERNAAALRQRDPDAMEKLIRRCAELHLDHIAASGDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 266 FEKGSSRPLDFGHWAAHKLEQLTNYRLRHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLGFVLYLPELseqmtE 345
Cdd:cd08198 241 FETGSARPLDFGHWSAHKLEQLSGYALRHGEAVAIGIALDSLYARLLGLLSREDFDRILALLQNLGLPLWHPLL-----E 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1199832887 346 PEHPRSLFRGLNEFREHLGGELTLTLLQRIGKGVEIHEVDMSLFRQAI 393
Cdd:cd08198 316 RDGVLELLDGLEEFREHLGGRLTITLLRGIGVGVEVHEIDLDLMEEAI 363
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
19-393 |
9.90e-129 |
|
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: 374.81 E-value: 9.90e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 19 QSFSVTFD---YGVHFTNAVFDTKNPLLAKVIatdgetKPKKVLAVVDSGLlqsRRMLLKQIATYSDHYAdtlkLAADPI 95
Cdd:COG0337 2 QTLTVNLGersYDIRIGRGLLDELGELLAELL------KGRRVLVVTDENV---APLYGERLRAALEAAG----FEVHLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 96 IVLGGEEAKNdPNELLKIHQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNGIN 175
Cdd:COG0337 69 VLPDGEASKT-LETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 176 AFGKKNFLGTFAPPYAVLNDFTFLTSLNDRDWRSGIAEAVKVALIKDADFFEYISTYAHALVCRDLNRMQNVIYRCAQLH 255
Cdd:COG0337 148 HPGGKNLIGAFHQPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 256 MDHIAnnGDSFEKGSSRPLDFGHWAAHKLEQLTNYRLRHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLGFVLY 335
Cdd:COG0337 228 AEVVA--ADERESGLRALLNFGHTFGHAIEAATGYRLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTR 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199832887 336 LPELSeqmtepehPRSLFRGLNEFREHLGGELTLTLLQRIGKGVEIHEVDMSLFRQAI 393
Cdd:COG0337 306 LPALD--------PEALLAAMKRDKKVRGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
27-378 |
1.98e-98 |
|
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: 296.63 E-value: 1.98e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 27 YGVHFTNAVFDTKNpllakviATDGETKPKKVLAVVDSGLLQSR-RMLLKQIATYsdhyadtlkLAADPIIVLGGEEAKN 105
Cdd:cd08169 2 YPVFFGEGVFESVN-------SYIPRDAFDQCLIIVDSGVPDLIvNYLAEYFGYY---------LEVHVFIIQGGEAYKT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 106 DPnELLKIHQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNGINAFGKKNFLGT 185
Cdd:cd08169 66 FQ-TVVEELERAAALHLNRHSAVVAVGGGATGDVVGFAAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 186 FAPPYAVLNDFTFLTSLNDRDWRSGIAEAVKVALIKDADFFEYISTYAHALVCRDLNRMQNVIYRCAQLHMDHIANNGDs 265
Cdd:cd08169 145 FYPPRAVFADFSFLKTLPFRQVRAGMAELVKMALIADNDFFEFLEDKANSATVYSPEQLEKLINKCISLKLDVVVADED- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 266 fEKGSSRPLDFGHWAAHKLEQLTNYRLRHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLGFVLYLPELSEqmte 345
Cdd:cd08169 224 -EQGKRRGLNYGHTFGHALELASGYKIPHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWLLNKLGLPLDHPLALD---- 298
|
330 340 350
....*....|....*....|....*....|...
gi 1199832887 346 pehPRSLFRGLNEFREHLGGELTLTLLQRIGKG 378
Cdd:cd08169 299 ---PDSLYEYLESDKKSLYGNLGMILLSGVGDG 328
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
94-340 |
7.03e-86 |
|
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: 262.05 E-value: 7.03e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 94 PIIVLGGEEAKNdPNELLKIHQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNG 173
Cdd:pfam01761 1 TIVIPDGEKSKT-LETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 174 INAFGKKNFLGTFAPPYAVLNDFTFLTSLNDRDWRSGIAEAVKVALIKDADFFEYISTYAHALVCRDLNRMQNVIYRCAQ 253
Cdd:pfam01761 80 INHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 254 LHMDHIAnnGDSFEKGSSRPLDFGHWAAHKLEQLTNY-RLRHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLGF 332
Cdd:pfam01761 160 VKADVVA--QDEKESGLRALLNLGHTFGHAIEALSGYgALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGL 237
|
....*...
gi 1199832887 333 VLYLPELS 340
Cdd:pfam01761 238 PTSLPDLD 245
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
42-340 |
2.04e-82 |
|
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: 256.22 E-value: 2.04e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 42 LLAKVIATDGETKPKKVLAVVDSGLLQSrrmllkqiatYSDHYADTLKLAADPIIVL---GGEEAKNdPNELLKIHQTIN 118
Cdd:cd08195 10 LLDKLGELLELKKGSKVVIVTDENVAKL----------YGELLLKSLEAAGFKVEVIvipAGEKSKS-LETVERIYDFLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 119 EVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNGINAFGKKNFLGTFAPPYAVLNDFTF 198
Cdd:cd08195 79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 199 LTSLNDRDWRSGIAEAVKVALIKDADFFEYISTYAHALVCRDLNRMQNVIYRCAQLHMDHIANngDSFEKGSSRPLDFGH 278
Cdd:cd08195 159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEE--DEREKGLRAILNFGH 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199832887 279 WAAHKLEQLTNYRLRHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLGFVLYLPELS 340
Cdd:cd08195 237 TFGHAIESASGYKLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKDLD 298
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
27-343 |
1.35e-80 |
|
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: 251.68 E-value: 1.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 27 YGVHFTNAVFDTKNPLLAKViatdGETKPKKVLAVVDSgllQSRRMLLKQIATYSDHYadtlKLAADPIIVLGGEEAKNd 106
Cdd:cd08199 2 YDVVLVDDLFDPENPTLADA----YGRPGRRRLVVVDE---NVDRLYGARIRAYFAAH----GIEATILVLPGGEANKT- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 107 PNELLKIHQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNGINAFGKKNFLGTF 186
Cdd:cd08199 70 METVLRIVDALDDFGLDRREPVIAIGGGVLLDVVGFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 187 APPYAVLNDFTFLTSLNDRDWRSGIAEAVKVALIKDADFFEYISTYAHALV--CRDLNRM-QNVIYRCAQLHMDHIANNg 263
Cdd:cd08199 150 YPPVATLLDRSFLKTLPRRHIRNGLAEIIKMALVKDAELFELLEEHGAALVetRFFQDEVaDEIIRRAIQGMLEELAPN- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 264 dSFEKGSSRPLDFGHWAAHKLEQLTNYRLRHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLGFVLYLPELSEQM 343
Cdd:cd08199 229 -LWEHDLERLVDFGHTFSPILEMAAAPELLHGEAVAIDMALSAVLAYRRGLLSEEELDRILRLMRRLGLPVWHPLCTPDL 307
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
27-331 |
2.85e-63 |
|
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: 206.71 E-value: 2.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 27 YGVHFTNAVFDTKNPLLAKviatdgetkPKKVLAVVDSgllqsrrmllkqiaTYSDHYADTLKLA-------ADPIIVLG 99
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEELAE---------PSKLVIITDE--------------TVADLYGDKLLEAlqalgynVLKLTVPD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 100 GEEAKNDPNeLLKIHQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNGINAFGK 179
Cdd:TIGR01357 58 GEESKSLET-VQRLYDQLLEAGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 180 KNFLGTFAPPYAVLNDFTFLTSLNDRDWRSGIAEAVKVALIKDADFFEYISTYAHALVCR-DLNRMQNVIYRCAQLHMDH 258
Cdd:TIGR01357 137 KNLIGTFYQPKAVLIDPDFLKTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLqELEHLEELIKRSIEVKASI 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199832887 259 IAnnGDSFEKGSSRPLDFGHWAAHKLEQLTNYR-LRHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLG 331
Cdd:TIGR01357 217 VA--EDEKESGLRAILNFGHTIGHAIEAEAGYGkIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYG 288
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
84-316 |
3.93e-54 |
|
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: 183.17 E-value: 3.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 84 YADTLK-------LAADPIIVLGGEEAKNDP--NELLkihQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLI 154
Cdd:cd08197 38 YGDRLLeglkkagIPVELLVVPAGESNKTLStlTELA---ERLIAAGITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 155 RIPTTVLAQNDSGIGVKNGINAFGKKNFLGTFAPPYAVLNDFTFLTSLNDRDWRSGIAEAVKVALIKDADFFEYISTYAH 234
Cdd:cd08197 115 HVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEFLKTLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 235 ALVCRDLNRMQNVIYRCAQLHMdhIANNGDSFEKGSSRPLDFGHWAAHKLEQLTNYRLRHGEAVAIGIALDSTYSYLIGL 314
Cdd:cd08197 195 SDLDYDPEFLEKVIDLSIEAKL--EVLSNDPYEKKEGLILEYGHTVGHAIELLSGGELSHGEAVAIGMCVAAEISHLLGL 272
|
..
gi 1199832887 315 LS 316
Cdd:cd08197 273 LS 274
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
56-344 |
4.27e-54 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 185.36 E-value: 4.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 56 KKVLAVVDSGLlqsRRMLLKQIATYSDHYADtlKLAADPIIVLGGEEAKNdPNELLKIHQTINEVGLCRHSYLLGIGGGA 135
Cdd:PLN02834 101 KRVLVVTNETV---APLYLEKVVEALTAKGP--ELTVESVILPDGEKYKD-METLMKVFDKALESRLDRRCTFVALGGGV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 136 VLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNGINAFGKKNFLGTFAPPYAVLNDFTFLTSLNDRDWRSGIAEAV 215
Cdd:PLN02834 175 IGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTDTLATLPDRELASGIAEVV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 216 KVALIKDADFFEYISTYAHALVCRDLNRMQNVIYRCAQLHMDHIANngDSFEKGSSRPLDFGHWAAHKLEQLTNY-RLRH 294
Cdd:PLN02834 255 KYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSL--DEKESGLRATLNLGHTFGHAIETGPGYgEWLH 332
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1199832887 295 GEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLGfvlyLP-ELSEQMT 344
Cdd:PLN02834 333 GEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAK----LPtNPPEKMT 379
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
113-332 |
2.23e-31 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 125.36 E-value: 2.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 113 IHQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNGINAFGKKNFLGTFAPPYAV 192
Cdd:PRK14021 258 IWQRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMVDASTGGKTGINTPQGKNLVGSFYTPAGV 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 193 LNDFTFLTSLNDRDWRSGIAEAVKVALIKDADFFEYISTYAHALVCRDLNRMQN---------VIYRCAQLHMDHIAnnG 263
Cdd:PRK14021 338 LADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAELRAFDGSTFLGspledvvaeLIERTVKVKAYHVS--S 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199832887 264 DSFEKGSSRPLDFGHWAAHKLEQLTNYRLRHGEAVAIGIALDSTYSYLIGLLSR--LEWRRILntLLSLGF 332
Cdd:PRK14021 416 DLKEAGLREFLNYGHTLGHAIEKLEHFRWRHGNAVAVGMVYAAELAHLLGYIDQdlVDYHRSL--LASLGL 484
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
100-330 |
1.21e-27 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 114.23 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 100 GEEAKnDPNELLKIHQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTVLAQNDSGIGVKNGINAFGK 179
Cdd:PRK13951 214 GEEVK-TLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQVDASVGGKNAIDFAGV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 180 KNFLGTFAPPYAVLNDFTFLTSLNDRDWRSGIAEAVKVALIKDADFFEYIStyAHALVCRDLNRMQNVIYRCAQLHMDHI 259
Cdd:PRK13951 293 KNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSGRGVELFDE--PEKIEKRNLRVLSEMVKISVEEKARIV 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199832887 260 ANngDSFEKGSSRPLDFGHWAAHKLEQLTNyrLRHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSL 330
Cdd:PRK13951 371 ME--DPYDMGLRHALNLGHTLGHVYEMLEG--VPHGIAVAWGIEKETMYLYRKGIVPKETMRWIVEKVKQI 437
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
44-339 |
6.17e-14 |
|
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: 71.63 E-value: 6.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 44 AKVIATDGETKP---KKVLAVVDSGLLQSrrmLLKQIATYSDHYADTLKLaadpiIVLGGEEAKNDPNELLKIHQTinev 120
Cdd:cd07766 8 EGAIAKLGEIKRrgfDRALVVSDEGVVKG---VGEKVADSLKKGLAVAIF-----DFVGENPTFEEVKNAVERARA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 121 glCRHSYLLGIGGGAVLDLVGYAAATAHRGIRLIRIPTTvlAQNDSGIGVKNGINAFGKKN-FLGTFAPPYAVLNDFTFL 199
Cdd:cd07766 76 --AEADAVIAVGGGSTLDTAKAVAALLNRGIPFIIVPTT--ASTDSEVSPKSVITDKGGKNkQVGPHYNPDVVFVDTDIT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 200 TSLNDRDWRSGIAEAVKVALIkdadffeyistyahalvcrdlnrMQNVIYRCAQLHMDHIANNGDSfekgssrpldFGHW 279
Cdd:cd07766 152 KGLPPRQVASGGVDALAHAVE-----------------------LEKVVEAATLAGMGLFESPGLG----------LAHA 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 280 AAHKLEQLtnYRLRHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLGFVLYLPEL 339
Cdd:cd07766 199 IGHALTAF--EGIPHGEAVAVGLPYVLKVANDMNPEPEAAIEAVFKFLEDLGLPTHLADL 256
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
57-331 |
6.28e-11 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 63.37 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 57 KVLAVVDSGLLQSRRMLL-----KQIAtySDHYADTLKLAADPIIVLGGEeakNDPNELLKIHQTINEVGLcrhSYLLGI 131
Cdd:PRK00843 23 DIGDVCSDLKLTGRALIVtgpttKKIA--GDRVEENLEDAGDVEVVIVDE---ATMEEVEKVEEKAKDVNA---GFLIGV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 132 GGGAVLDLVGYAAatAHRGIRLIRIPTTvlAQNDsGIGVKNG-INAFGKKNFLGTfAPPYAVLNDFTFLTSLNDRDWRSG 210
Cdd:PRK00843 95 GGGKVIDVAKLAA--YRLGIPFISVPTA--ASHD-GIASPRAsIKGGGKPVSVKA-KPPLAVIADTEIIAKAPYRLLAAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 211 IAEAV-KVALIKDADFF-----EYISTYAHALvcrdlnrmqnviyrcAQLHMDHIANNGDSFEK---------------- 268
Cdd:PRK00843 169 CGDIIsNYTAVKDWRLAhrlrgEYYSEYAAAL---------------SLMTAKMLIENADIIKPgleesarlvvkaliss 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199832887 269 -------GSSRPLDFG-HWAAHKLEQLTNYRLRHGEAVAIG--IALdstysYLIGllsrLEWRRILNTLLSLG 331
Cdd:PRK00843 234 gvamsiaGSSRPASGSeHLFSHALDRLAPGPALHGEQCGVGtiIMM-----YLHG----GDWRKIRDALKKIG 297
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
105-332 |
5.31e-09 |
|
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: 57.18 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 105 NDPNELLKIHQTINEvglCRHSYLLGIGGGAVLDLVGYAAATAhrGIRLIRIPTTvlAQNDsGIG-----VKNGINAFGK 179
Cdd:cd08173 64 EEAAEVEKVKKLIKE---SKADFIIGVGGGKVIDVAKYAAYKL--NLPFISIPTS--ASHD-GIAspfasIKGGDKPYSI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 180 KNflgtfAPPYAVLNDFTFLTSLNDRDWRSGIAEAV-KVALIKDADFF-----EYISTYAHALvcrdlnrmqnviyrcAQ 253
Cdd:cd08173 136 KA-----KAPIAIIADTEIISKAPKRLLAAGCGDLIsNITAVKDWRLAhrlkgEYYSEYAASL---------------AL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 254 LHMDHIANNGDSFEK-----------------------GSSRPLDfG--HWAAHKLEQLTNYRLRHGEAVAIG-IALdst 307
Cdd:cd08173 196 MSAKLIIENADLIKPgleegvrtvvkalissgvamsiaGSSRPAS-GseHLFSHALDKLAPGPALHGEQCGVGtIMM--- 271
|
250 260
....*....|....*....|....*
gi 1199832887 308 ySYLIGllsrLEWRRILNTLLSLGF 332
Cdd:cd08173 272 -AYLHG----GDWKEIREALKKIGA 291
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
95-339 |
3.74e-07 |
|
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 51.71 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 95 IIVLGGEeakNDPNELLKIHQTINEVGlcrHSYLLGIGGGAVLDLVGYAAatAHRGIRLIRIPTTvlAQND---SGIGV- 170
Cdd:COG0371 59 VEVFGGE---CSEEEIERLAEEAKEQG---ADVIIGVGGGKALDTAKAVA--YRLGLPVVSVPTI--ASTDapaSPLSVi 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 171 KNGINAFGKKNFLGTfaPPYAVLNDFT--------FLtslndrdwRSGIAEA------VKVALIKDADFF-EYISTYAHA 235
Cdd:COG0371 129 YTEDGAFDGYSFLAK--NPDLVLVDTDiiakapvrLL--------AAGIGDAlakwyeARDWSLAHRDLAgEYYTEAAVA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 236 L--VCRDLnrmqnvIYRCAQLHMDHIANN--GDSFEK---------------GSSRPldfGHWAAHK----LEQL-TNYR 291
Cdd:COG0371 199 LarLCAET------LLEYGEAAIKAVEAGvvTPALERvveanlllsglamgiGSSRP---GSGAAHAihngLTALpETHH 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1199832887 292 LRHGEAVAIGIaldstysyLIGLL---SRLEWRRILNTLLSLGFVLYLPEL 339
Cdd:COG0371 270 ALHGEKVAFGT--------LVQLVlegRPEEIEELLDFLRSVGLPTTLADL 312
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
116-339 |
2.68e-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: 49.06 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 116 TINEVGLCRHSY--LLGIGGGAVLDLVGYAAATahRGIRLIRIPTTVlaQND---SGIGVkngINAFGKKNFLGTfAPPY 190
Cdd:cd08174 67 ELAEKAFSLPKVdaIVGIGGGKVLDVAKYAAFL--SKLPFISVPTSL--SNDgiaSPVAV---LKVDGKRKSLGA-KMPY 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 191 AVLNDFTFLTSLNDRDWRSGIAEAV-KVALIKDADF-----FEYISTYAHAL---VCRD-LNRMQNVIyRCAQLhMDHIA 260
Cdd:cd08174 139 GVIVDLDVIKSAPRRLILAGIGDLIsNITALYDWKLaeekgGEPVDDFAYLLsrtAADSlLNTPGKDI-KDDEF-LKELA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 261 N----NGDSFE-KGSSRPLDfG--HWAAHKLEQLTNYRLRHGEAVAIGialdstySYLIGLLSRLEWRRILNTLLSLGFV 333
Cdd:cd08174 217 EslvlSGIAMEiAGSSRPAS-GseHLISHALDKLFPGPALHGIQVGLG-------TYFMSFLQGQRYEEIRDVLKRTGFP 288
|
....*.
gi 1199832887 334 LYLPEL 339
Cdd:cd08174 289 LNPSDL 294
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
128-339 |
4.43e-06 |
|
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: 48.33 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 128 LLGIGGGAVLDLVGYAAATahRGIRLIRIPTTvlAQNDsgiGVKNGINAFGKKNFLGTF--APPYAVLNDFTFLTSLNDR 205
Cdd:cd08549 74 VIGIGGGRSIDTGKYLAYK--LKIPFISVPTS--ASND---GIASPIVSLRIPGVKKTFmaDAPIAIIADTEIIKKSPRR 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199832887 206 DWRSGIAEAV-KVALIKDADFF-----EYISTYAHALVCRDLNRMQNVIYRCAQLH------MDHIANNGDSFE-KGSSR 272
Cdd:cd08549 147 LLSAGIGDLVsNITAVLDWKLAhkekgEKYSEFAAILSKTSAKELVSYVLKASDLEeyhrvlVKALVGSGIAMAiAGSSR 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1199832887 273 PLD-----FGH-WAAHKLEQLTNYRLrHGEAVAIGIALDSTYSYLIGLLSRLEWRRILNTLLSLGFVLYLPEL 339
Cdd:cd08549 227 PASgsehlFSHaLDKLKEEYLNINVL-HGEQVGVGTIIMSYLHEKENKKLSGLHERIKMILKKVGAPTTAKQL 298
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
113-164 |
6.28e-04 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. 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.
Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 41.73 E-value: 6.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1199832887 113 IHQTINEVGLCRHSYLLGIGGGAVLDLVGYAAATAHrgIRLIRIPTtvLAQN 164
Cdd:cd08172 64 IDRLAEEAKEHQADVIIGIGGGKVLDTAKAVADKLN--IPLILIPT--LASN 111
|
|
| |
