|
Name |
Accession |
Description |
Interval |
E-value |
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
205-549 |
1.89e-176 |
|
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: 501.20 E-value: 1.89e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 205 SYPVFVDWGILDKLGEKmTQAGLSGTANIISDETVFSIYGTQVKKTLEKAGFIVNCFAVPPGEASKNIAQAVKIYDFLIE 284
Cdd:cd08195 1 SYPILIGSGLLDKLGEL-LELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGEKSKSLETVERIYDFLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 285 HRVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSLIAMTDASIGGKVAVDHPQGKNLMGAFYQPSLVLADVRTL 364
Cdd:cd08195 80 AGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 365 TTLPQRELTSGWAEVIKHGLILDADFLQLIEGNVKDLIKLKQSITSKVIARSAAIKCQVVSEDERETGKRTLLNYGHTVA 444
Cdd:cd08195 160 KTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 445 HGLEAAGKYdRFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGLPTDCSGVPLTDVLAAMELDKKVRGKAIR 524
Cdd:cd08195 240 HAIESASGY-KLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKDLDPEELLEAMKRDKKNRGGKIR 318
|
330 340
....*....|....*....|....*
gi 2108393370 525 WVLLEDIGKAVIRSDIPKKEVLNVL 549
Cdd:cd08195 319 FVLLKGIGKAVIVDDVSEEEIREAL 343
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
199-549 |
1.06e-174 |
|
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: 497.31 E-value: 1.06e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 199 VETNIASYPVFVDWGILDKLGEKMTQAGLSGTANIISDETVFSIYGTQVKKTLEKAGFIVNCFAVPPGEASKNIAQAVKI 278
Cdd:COG0337 6 VNLGERSYDIRIGRGLLDELGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGEASKTLETLERI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 279 YDFLIEHRVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSLIAMTDASIGGKVAVDHPQGKNLMGAFYQPSLVL 358
Cdd:COG0337 86 LDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQPRAVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 359 ADVRTLTTLPQRELTSGWAEVIKHGLILDADFLQLIEGNVKDLIKLKQSITSKVIARSAAIKCQVVSEDERETGKRTLLN 438
Cdd:COG0337 166 IDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESGLRALLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 439 YGHTVAHGLEAAGKYdRFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGLPTDCSGVPLTDVLAAMELDKKV 518
Cdd:COG0337 246 FGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPALDPEALLAAMKRDKKV 324
|
330 340 350
....*....|....*....|....*....|.
gi 2108393370 519 RGKAIRWVLLEDIGKAVIRSDIPKKEVLNVL 549
Cdd:COG0337 325 RGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
206-549 |
7.99e-136 |
|
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: 397.77 E-value: 7.99e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 206 YPVFVDWGILDKLGEKMTQAGlsgTANIISDETVFSIYGTQVKKTLEKAGFIVNCFAVPPGEASKNIAQAVKIYDFLIEH 285
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEELAEPS---KLVIITDETVADLYGDKLLEALQALGYNVLKLTVPDGEESKSLETVQRLYDQLLEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 286 RVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSLIAMTDASIGGKVAVDHPQGKNLMGAFYQPSLVLADVRTLT 365
Cdd:TIGR01357 78 GLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 366 TLPQRELTSGWAEVIKHGLILDADFLQLIEGNVKD-LIKLKQSITSKVIARSAAIKCQVVSEDERETGKRTLLNYGHTVA 444
Cdd:TIGR01357 158 TLPDRELRSGMAEVIKHGLIADAELFDELESNDKLrLNLQELEHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 445 HGLEAAGKYDRFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGLPTDC-SGVPLTDVLAAMELDKKVRGKAI 523
Cdd:TIGR01357 238 HAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLpKDLDVDELLNAMLNDKKNSGGKI 317
|
330 340
....*....|....*....|....*.
gi 2108393370 524 RWVLLEDIGKAVIRSDIPKKEVLNVL 549
Cdd:TIGR01357 318 RFVLLEEIGKAALAREVPDEMVLELL 343
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
261-519 |
8.36e-133 |
|
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: 386.85 E-value: 8.36e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 261 FAVPPGEASKNIAQAVKIYDFLIEHRVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSLIAMTDASIGGKVAVD 340
Cdd:pfam01761 2 IVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 341 HPQGKNLMGAFYQPSLVLADVRTLTTLPQRELTSGWAEVIKHGLILDADFLQLIEGNVKDLIKLKQSITSKVIARSAAIK 420
Cdd:pfam01761 82 HPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEVK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 421 CQVVSEDERETGKRTLLNYGHTVAHGLEAAGKYDRFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGLPTDC 500
Cdd:pfam01761 162 ADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPTSL 241
|
250
....*....|....*....
gi 2108393370 501 SGVPLTDVLAAMELDKKVR 519
Cdd:pfam01761 242 PDLDVEQLLAAMARDKKVR 260
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
205-549 |
4.46e-98 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 304.38 E-value: 4.46e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 205 SYPVFVDWGILDKlGEKMTQAGLSGTANIISDETVFSIYGTQVKKTLEKAGF--IVNCFAVPPGEASKNIAQAVKIYDFL 282
Cdd:PLN02834 78 SYPIYIGSGLLDH-GELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGPelTVESVILPDGEKYKDMETLMKVFDKA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 283 IEHRVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSLIAMTDASIGGKVAVDHPQGKNLMGAFYQPSLVLADVR 362
Cdd:PLN02834 157 LESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTD 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 363 TLTTLPQRELTSGWAEVIKHGLILDADFLQLIEGNVKDLIKLKQSITSKVIARSAAIKCQVVSEDERETGKRTLLNYGHT 442
Cdd:PLN02834 237 TLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRATLNLGHT 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 443 VAHGLEAAGKYDRFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGLPTDCSgvPLTDV---LAAMELDKKVR 519
Cdd:PLN02834 317 FGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPP--EKMTVemfKSLMAVDKKVA 394
|
330 340 350
....*....|....*....|....*....|.
gi 2108393370 520 GKAIRWVLLE-DIGKAVIRSDIPKKEVLNVL 549
Cdd:PLN02834 395 DGLLRLILLKgELGNCVFTGDFDREALEETL 425
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
10-176 |
1.54e-60 |
|
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440467 [Multi-domain] Cd Length: 165 Bit Score: 197.27 E-value: 1.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 10 IALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAIV 89
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEEENAVIATGGGAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 90 DPKNQKLLLDTSVVVCLEARPETIHQRLLHDSlysashvVRPLLAGDNPLERIKQLKATRQPYYA-IADWTVHTDNLTLD 168
Cdd:COG0703 81 SPENRELLKEHGTVVYLDASPETLLERLRRDD-------NRPLLQGEDPRERLEELLAEREPLYReVADITVDTDGRSPE 153
|
....*...
gi 2108393370 169 EVSQEVIK 176
Cdd:COG0703 154 EVVDEILE 161
|
|
| PRK13947 |
PRK13947 |
shikimate kinase; Provisional |
9-178 |
2.20e-53 |
|
shikimate kinase; Provisional
Pssm-ID: 184412 [Multi-domain] Cd Length: 171 Bit Score: 178.75 E-value: 2.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 9 NIALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAI 88
Cdd:PRK13947 3 NIVLIGFMGTGKTTVGKRVATTLSFGFIDTDKEIEKMTGMTVAEIFEKDGEVRFRSEEKLLVKKLARLKNLVIATGGGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 89 VDPKNQKLLLDTSVVVCLEARPETIHQRLLHDSlysashvVRPLLAGDNPLERIKQLKATRQPYYAIADWTVHTDNLTLD 168
Cdd:PRK13947 83 LNPENVVQLRKNGVVICLKARPEVILRRVGKKK-------SRPLLMVGDPEERIKELLKEREPFYDFADYTIDTGDMTID 155
|
170
....*....|
gi 2108393370 169 EVSQEVIKGW 178
Cdd:PRK13947 156 EVAEEIIKAY 165
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
9-169 |
3.58e-48 |
|
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.
Pssm-ID: 238260 [Multi-domain] Cd Length: 154 Bit Score: 164.27 E-value: 3.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 9 NIALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAI 88
Cdd:cd00464 1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLLLTKENAVIATGGGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 89 VDPKNQKLLLDTSVVVCLEARPETIHQRLLHDSlysashvVRPLLAGDNPlERIKQLKATRQPYYA-IADWTVHTDNLTL 167
Cdd:cd00464 81 LREENRRLLLENGIVVWLDASPEELLERLARDK-------TRPLLQDEDP-ERLRELLEEREPLYReVADLTIDTDELSP 152
|
..
gi 2108393370 168 DE 169
Cdd:cd00464 153 EE 154
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
18-176 |
1.88e-41 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 146.57 E-value: 1.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 18 TGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAIVDPKNQKLL 97
Cdd:pfam01202 3 AGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEHGLVIATGGGAVLSEENRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 98 LDTSVVVCLEARPETIHQRLLHDSlysashvVRPLLAGDNPLE-RIKQLKATRQPYYA-IADWTVHTDNLTLDEVSQEVI 175
Cdd:pfam01202 83 KERGIVIYLDAPLEVLLERLKRDK-------TRPLLQNKDPEEeLLELLFEERDPLYEeAADIVIDTDESSPEEVATEIL 155
|
.
gi 2108393370 176 K 176
Cdd:pfam01202 156 E 156
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
205-549 |
1.89e-176 |
|
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: 501.20 E-value: 1.89e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 205 SYPVFVDWGILDKLGEKmTQAGLSGTANIISDETVFSIYGTQVKKTLEKAGFIVNCFAVPPGEASKNIAQAVKIYDFLIE 284
Cdd:cd08195 1 SYPILIGSGLLDKLGEL-LELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGEKSKSLETVERIYDFLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 285 HRVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSLIAMTDASIGGKVAVDHPQGKNLMGAFYQPSLVLADVRTL 364
Cdd:cd08195 80 AGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 365 TTLPQRELTSGWAEVIKHGLILDADFLQLIEGNVKDLIKLKQSITSKVIARSAAIKCQVVSEDERETGKRTLLNYGHTVA 444
Cdd:cd08195 160 KTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 445 HGLEAAGKYdRFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGLPTDCSGVPLTDVLAAMELDKKVRGKAIR 524
Cdd:cd08195 240 HAIESASGY-KLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKDLDPEELLEAMKRDKKNRGGKIR 318
|
330 340
....*....|....*....|....*
gi 2108393370 525 WVLLEDIGKAVIRSDIPKKEVLNVL 549
Cdd:cd08195 319 FVLLKGIGKAVIVDDVSEEEIREAL 343
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
199-549 |
1.06e-174 |
|
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: 497.31 E-value: 1.06e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 199 VETNIASYPVFVDWGILDKLGEKMTQAGLSGTANIISDETVFSIYGTQVKKTLEKAGFIVNCFAVPPGEASKNIAQAVKI 278
Cdd:COG0337 6 VNLGERSYDIRIGRGLLDELGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGEASKTLETLERI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 279 YDFLIEHRVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSLIAMTDASIGGKVAVDHPQGKNLMGAFYQPSLVL 358
Cdd:COG0337 86 LDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQPRAVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 359 ADVRTLTTLPQRELTSGWAEVIKHGLILDADFLQLIEGNVKDLIKLKQSITSKVIARSAAIKCQVVSEDERETGKRTLLN 438
Cdd:COG0337 166 IDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESGLRALLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 439 YGHTVAHGLEAAGKYdRFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGLPTDCSGVPLTDVLAAMELDKKV 518
Cdd:COG0337 246 FGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPALDPEALLAAMKRDKKV 324
|
330 340 350
....*....|....*....|....*....|.
gi 2108393370 519 RGKAIRWVLLEDIGKAVIRSDIPKKEVLNVL 549
Cdd:COG0337 325 RGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
206-549 |
7.99e-136 |
|
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: 397.77 E-value: 7.99e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 206 YPVFVDWGILDKLGEKMTQAGlsgTANIISDETVFSIYGTQVKKTLEKAGFIVNCFAVPPGEASKNIAQAVKIYDFLIEH 285
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEELAEPS---KLVIITDETVADLYGDKLLEALQALGYNVLKLTVPDGEESKSLETVQRLYDQLLEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 286 RVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSLIAMTDASIGGKVAVDHPQGKNLMGAFYQPSLVLADVRTLT 365
Cdd:TIGR01357 78 GLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 366 TLPQRELTSGWAEVIKHGLILDADFLQLIEGNVKD-LIKLKQSITSKVIARSAAIKCQVVSEDERETGKRTLLNYGHTVA 444
Cdd:TIGR01357 158 TLPDRELRSGMAEVIKHGLIADAELFDELESNDKLrLNLQELEHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 445 HGLEAAGKYDRFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGLPTDC-SGVPLTDVLAAMELDKKVRGKAI 523
Cdd:TIGR01357 238 HAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLpKDLDVDELLNAMLNDKKNSGGKI 317
|
330 340
....*....|....*....|....*.
gi 2108393370 524 RWVLLEDIGKAVIRSDIPKKEVLNVL 549
Cdd:TIGR01357 318 RFVLLEEIGKAALAREVPDEMVLELL 343
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
261-519 |
8.36e-133 |
|
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: 386.85 E-value: 8.36e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 261 FAVPPGEASKNIAQAVKIYDFLIEHRVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSLIAMTDASIGGKVAVD 340
Cdd:pfam01761 2 IVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 341 HPQGKNLMGAFYQPSLVLADVRTLTTLPQRELTSGWAEVIKHGLILDADFLQLIEGNVKDLIKLKQSITSKVIARSAAIK 420
Cdd:pfam01761 82 HPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEVK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 421 CQVVSEDERETGKRTLLNYGHTVAHGLEAAGKYDRFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGLPTDC 500
Cdd:pfam01761 162 ADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPTSL 241
|
250
....*....|....*....
gi 2108393370 501 SGVPLTDVLAAMELDKKVR 519
Cdd:pfam01761 242 PDLDVEQLLAAMARDKKVR 260
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
205-549 |
4.46e-98 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 304.38 E-value: 4.46e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 205 SYPVFVDWGILDKlGEKMTQAGLSGTANIISDETVFSIYGTQVKKTLEKAGF--IVNCFAVPPGEASKNIAQAVKIYDFL 282
Cdd:PLN02834 78 SYPIYIGSGLLDH-GELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGPelTVESVILPDGEKYKDMETLMKVFDKA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 283 IEHRVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSLIAMTDASIGGKVAVDHPQGKNLMGAFYQPSLVLADVR 362
Cdd:PLN02834 157 LESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTD 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 363 TLTTLPQRELTSGWAEVIKHGLILDADFLQLIEGNVKDLIKLKQSITSKVIARSAAIKCQVVSEDERETGKRTLLNYGHT 442
Cdd:PLN02834 237 TLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRATLNLGHT 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 443 VAHGLEAAGKYDRFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGLPTDCSgvPLTDV---LAAMELDKKVR 519
Cdd:PLN02834 317 FGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPP--EKMTVemfKSLMAVDKKVA 394
|
330 340 350
....*....|....*....|....*....|.
gi 2108393370 520 GKAIRWVLLE-DIGKAVIRSDIPKKEVLNVL 549
Cdd:PLN02834 395 DGLLRLILLKgELGNCVFTGDFDREALEETL 425
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
205-533 |
7.88e-98 |
|
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: 301.04 E-value: 7.88e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 205 SYPVFVDWGILDKLGEKMTQAGLSgTANIISDETVFSIYGTQVKKTLEKAGFIVNCFAVPPGEASKNIAQAVKIYDFLIE 284
Cdd:cd08197 1 LTDIYLGRGILESLLSILEELKAD-RHFLVTDSNVNDLYGDRLLEGLKKAGIPVELLVVPAGESNKTLSTLTELAERLIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 285 HRVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSLIAMTDASIGGKVAVDHPQGKNLMGAFYQPSLVLADVRTL 364
Cdd:cd08197 80 AGITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 365 TTLPQRELTSGWAEVIKHGLILDADFLQLIEGNVKDLIKLKQSITSKVIARSAAIKCQVVSEDERETGKRTLLNYGHTVA 444
Cdd:cd08197 160 KTLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFLEKVIDLSIEAKLEVLSNDPYEKKEGLILEYGHTVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 445 HGLEAAGKYdRFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGLPTDC-SGVPLTDVLAAMELDKKVRGKA- 522
Cdd:cd08197 240 HAIELLSGG-ELSHGEAVAIGMCVAAEISHLLGLLSEEDVDKHYELLEKIGLPTIIpDGISVEAILEVIRYDNKRGYIKa 318
|
330
....*....|....*
gi 2108393370 523 ----IRWVLLEDIGK 533
Cdd:cd08197 319 dadtIRMVLLEKLGK 333
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
12-545 |
1.99e-96 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 303.71 E-value: 1.99e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 12 LIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAIVDP 91
Cdd:PRK14021 11 IIGMMGAGKTRVGKEVAQMMRLPFADADVEIEREIGMSIPSYFEEYGEPAFREVEADVVADMLEDFDGIFSLGGGAPMTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 92 KNQKLLL----DTSVVVCLEARPETIHQRllhdslySASHVVRPLLAGDNPlERIKQLKATRQPYY-AIADWTVHTDNLT 166
Cdd:PRK14021 91 STQHALAsyiaHGGRVVYLDADPKEAMER-------ANRGGGRPMLNGDAN-KRWKKLFKQRDPVFrQVANVHVHTRGLT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 167 LDEVSQEVIkgwQYVSKHhrskqstkidSVCMVETNIASYPVFVDWGIL----DKLGEKMTQAGLSGTANIisdetvfSI 242
Cdd:PRK14021 163 PQAAAKKLI---DMVAER----------TVHVTGAGIEPYDVRIGEGAMnhlpQVLGPKPVKVALIHTQPV-------QR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 243 YGTQVKKTLEKAGFIVNCFAVPPGEASKNIAQAVKIYDFLIEHRVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVP 322
Cdd:PRK14021 223 HSDRARTLLRQGGYEVSDIVIPDAEAGKTIEVANGIWQRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 323 TSLIAMTDASIGGKVAVDHPQGKNLMGAFYQPSLVLADVRTLTTLPQRELTSGWAEVIKHGLILDADFLQLIEGNVKDLI 402
Cdd:PRK14021 303 TSLLAMVDASTGGKTGINTPQGKNLVGSFYTPAGVLADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAELR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 403 KLKQS---------ITSKVIARSAAIKCQVVSEDERETGKRTLLNYGHTVAHGLEAAGKYdRFLHGEAVAIGMMVAARLS 473
Cdd:PRK14021 383 AFDGStflgspledVVAELIERTVKVKAYHVSSDLKEAGLREFLNYGHTLGHAIEKLEHF-RWRHGNAVAVGMVYAAELA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108393370 474 QRLGLLSPHSVEHQKSILRKFGLPTDCSGVPLTDVLAAMELDKKVRGKAIRWVLLEDIGKAVIRSDIPKKEV 545
Cdd:PRK14021 462 HLLGYIDQDLVDYHRSLLASLGLPTSWNGGSFDDVLALMHRDKKARGNELRFVVLDEIGHPVHLDNPPAEAV 533
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
205-533 |
2.45e-85 |
|
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: 267.74 E-value: 2.45e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 205 SYPVFVDWGILDKLGEKMTqAGLSGTANIISDETVFSIYGTQVKKTLeKAGFIVNCFAVPPGEASKNIAQAVKIYDFLIE 284
Cdd:cd08169 1 EYPVFFGEGVFESVNSYIP-RDAFDQCLIIVDSGVPDLIVNYLAEYF-GYYLEVHVFIIQGGEAYKTFQTVVEELERAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 285 HRVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSLIAMTDASIGGKVAVDHPQGKNLMGAFYQPSLVLADVRTL 364
Cdd:cd08169 79 LHLNRHSAVVAVGGGATGDVVGFAAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 365 TTLPQRELTSGWAEVIKHGLILDADFLQLIEGNVKDLIKLKQSITSKVIARSAAIKCQVVSEDERETGKRTLLNYGHTVA 444
Cdd:cd08169 159 KTLPFRQVRAGMAELVKMALIADNDFFEFLEDKANSATVYSPEQLEKLINKCISLKLDVVVADEDEQGKRRGLNYGHTFG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 445 HGLEAAGKYdRFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGLPTDcsGVPLTD---VLAAMELDKKVRGK 521
Cdd:cd08169 239 HALELASGY-KIPHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWLLNKLGLPLD--HPLALDpdsLYEYLESDKKSLYG 315
|
330
....*....|..
gi 2108393370 522 AIRWVLLEDIGK 533
Cdd:cd08169 316 NLGMILLSGVGD 327
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
233-540 |
2.11e-68 |
|
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: 224.33 E-value: 2.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 233 IISDETVFSIYGTQVKKTLEKAGFIVNCFAVPPGEASKNIAQAVKIYDFLIEHRVERNDVIVALGGGMVGDLAGFAAATF 312
Cdd:cd08199 31 VVVDENVDRLYGARIRAYFAAHGIEATILVLPGGEANKTMETVLRIVDALDDFGLDRREPVIAIGGGVLLDVVGFAASLY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 313 LRGLPWIQVPTSLIAMTDASIGGKVAVDHPQGKNLMGAFYQPSLVLADVRTLTTLPQRELTSGWAEVIKHGLILDADFLQ 392
Cdd:cd08199 111 RRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAYYPPVATLLDRSFLKTLPRRHIRNGLAEIIKMALVKDAELFE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 393 LIEGNVKDLIKLK---QSITSKVIARSAAIKCQVVSEDERETGKRTLLNYGHTVAHGLEAAGKYdRFLHGEAVAIGMMVA 469
Cdd:cd08199 191 LLEEHGAALVETRffqDEVADEIIRRAIQGMLEELAPNLWEHDLERLVDFGHTFSPILEMAAAP-ELLHGEAVAIDMALS 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2108393370 470 ARLSQRLGLLSPHSVEHQKSILRKFGLPTDCSGVPLTDVLAAMELDKKVRGKAIRWVLLEDIGKAVIRSDI 540
Cdd:cd08199 270 AVLAYRRGLLSEEELDRILRLMRRLGLPVWHPLCTPDLLWRALEDIVKHRDGLQRLPLPKGIGECVFVNDV 340
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
10-176 |
1.54e-60 |
|
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440467 [Multi-domain] Cd Length: 165 Bit Score: 197.27 E-value: 1.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 10 IALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAIV 89
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEEENAVIATGGGAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 90 DPKNQKLLLDTSVVVCLEARPETIHQRLLHDSlysashvVRPLLAGDNPLERIKQLKATRQPYYA-IADWTVHTDNLTLD 168
Cdd:COG0703 81 SPENRELLKEHGTVVYLDASPETLLERLRRDD-------NRPLLQGEDPRERLEELLAEREPLYReVADITVDTDGRSPE 153
|
....*...
gi 2108393370 169 EVSQEVIK 176
Cdd:COG0703 154 EVVDEILE 161
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
10-533 |
3.03e-59 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 204.37 E-value: 3.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 10 IALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAIV 89
Cdd:PRK13951 3 IFLVGMMGSGKSTIGKRVSEVLDLQFIDMDEEIERREGRSVRRIFEEDGEEYFRLKEKELLRELVERDNVVVATGGGVVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 90 DPKNQKLLLDTSVVVcLEARPETIHQRLLHDSlysashvvRPLLAgdNPLERIKQLKATRQPYYAIADwTVHTDNLTLDE 169
Cdd:PRK13951 83 DPENRELLKKEKTLF-LYAPPEVLMERVTTEN--------RPLLR--EGKERIREIWERRKQFYTEFR-GIDTSKLNEWE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 170 VSQEVIkgWQYVSKHHRSKqstkIDSVCMVETNIASYPVFVDWGIldklgekmtqaglsgtanIISDETVFSIYGTQVKK 249
Cdd:PRK13951 151 TTALVV--LEALDEKEIST----IEKPHLVKIILGGFKRVRNEEL------------------VFTTERVEKIYGRYLPE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 250 tlekagfivNCFAVPPGEASKNIAQAVKIYDFLIEHRVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSLIAMT 329
Cdd:PRK13951 207 ---------NRLLFPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 330 DASIGGKVAVDHPQGKNLMGAFYQPSLVLADVRTLTTLPQRELTSGWAEVIKHGLILDADFlQLIEgNVKDLIKLKQSIT 409
Cdd:PRK13951 278 DASVGGKNAIDFAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSGRGV-ELFD-EPEKIEKRNLRVL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 410 SKVIARSAAIKCQVVSEDERETGKRTLLNYGHTVAHGLEAAgkyDRFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKS 489
Cdd:PRK13951 356 SEMVKISVEEKARIVMEDPYDMGLRHALNLGHTLGHVYEML---EGVPHGIAVAWGIEKETMYLYRKGIVPKETMRWIVE 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2108393370 490 ILRKFgLPTDCSGVPLTDVLAAMELDKKV-RGKAIRWVLLEDIGK 533
Cdd:PRK13951 433 KVKQI-VPIPVPSVDVEKARNLILNDKKIlKGSRVRLPYVKEIGK 476
|
|
| PRK13947 |
PRK13947 |
shikimate kinase; Provisional |
9-178 |
2.20e-53 |
|
shikimate kinase; Provisional
Pssm-ID: 184412 [Multi-domain] Cd Length: 171 Bit Score: 178.75 E-value: 2.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 9 NIALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAI 88
Cdd:PRK13947 3 NIVLIGFMGTGKTTVGKRVATTLSFGFIDTDKEIEKMTGMTVAEIFEKDGEVRFRSEEKLLVKKLARLKNLVIATGGGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 89 VDPKNQKLLLDTSVVVCLEARPETIHQRLLHDSlysashvVRPLLAGDNPLERIKQLKATRQPYYAIADWTVHTDNLTLD 168
Cdd:PRK13947 83 LNPENVVQLRKNGVVICLKARPEVILRRVGKKK-------SRPLLMVGDPEERIKELLKEREPFYDFADYTIDTGDMTID 155
|
170
....*....|
gi 2108393370 169 EVSQEVIKGW 178
Cdd:PRK13947 156 EVAEEIIKAY 165
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
9-176 |
1.14e-51 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 174.22 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 9 NIALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAI 88
Cdd:PRK00131 6 NIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLIEARAGKSIPEIFEEEGEAAFRELEEEVLAELLARHNLVISTGGGAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 89 VDPKNQKLLLDTSVVVCLEARPETIHQRLLHDSlysashvVRPLLAGDNPLERIKQLKATRQPYYA-IADWTVHTDNLTL 167
Cdd:PRK00131 86 LREENRALLRERGTVVYLDASFEELLRRLRRDR-------NRPLLQTNDPKEKLRDLYEERDPLYEeVADITVETDGRSP 158
|
....*....
gi 2108393370 168 DEVSQEVIK 176
Cdd:PRK00131 159 EEVVNEILE 167
|
|
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
260-497 |
1.72e-48 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 172.77 E-value: 1.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 260 CFAVPPGEASKNIAQAV-KIYDFLIEHRVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSLIAMTDASIGGKVA 338
Cdd:PRK06203 81 PLVVPGGEAAKNDPALVeALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKNG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 339 VDHPQGKNLMGAFYQPSLVLADVRTLTTLPQRELTSGWAEVIKHGLILDADFLQLIEGNVKDLIKLKQSITSKVIARSAA 418
Cdd:PRK06203 161 INAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAARDPEAMEELIYRCAE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 419 IKCQVV--SEDERETGKRTLLNYGHTVAHGLEAAGKYdRFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGL 496
Cdd:PRK06203 241 LHLEHIagGGDPFEFGSSRPLDFGHWSAHKLEQLTNY-ALRHGEAVAIGIALDSLYSYLLGLLSEAEAQRILALLRALGF 319
|
.
gi 2108393370 497 P 497
Cdd:PRK06203 320 P 320
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
9-169 |
3.58e-48 |
|
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.
Pssm-ID: 238260 [Multi-domain] Cd Length: 154 Bit Score: 164.27 E-value: 3.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 9 NIALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAI 88
Cdd:cd00464 1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLLLTKENAVIATGGGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 89 VDPKNQKLLLDTSVVVCLEARPETIHQRLLHDSlysashvVRPLLAGDNPlERIKQLKATRQPYYA-IADWTVHTDNLTL 167
Cdd:cd00464 81 LREENRRLLLENGIVVWLDASPEELLERLARDK-------TRPLLQDEDP-ERLRELLEEREPLYReVADLTIDTDELSP 152
|
..
gi 2108393370 168 DE 169
Cdd:cd00464 153 EE 154
|
|
| PRK13948 |
PRK13948 |
shikimate kinase; Provisional |
10-186 |
5.00e-45 |
|
shikimate kinase; Provisional
Pssm-ID: 184413 [Multi-domain] Cd Length: 182 Bit Score: 156.87 E-value: 5.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 10 IALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAIV 89
Cdd:PRK13948 13 VALAGFMGTGKSRIGWELSRALMLHFIDTDRYIERVTGKSIPEIFRHLGEAYFRRCEAEVVRRLTRLDYAVISLGGGTFM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 90 DPKNQKLLLDTSVVVCLEARPETIHQRLLHDSlysashvvRPLLAGDNPLERIKQLKATRQPYYAIADWTVHTDNLTLDE 169
Cdd:PRK13948 93 HEENRRKLLSRGPVVVLWASPETIYERTRPGD--------RPLLQVEDPLGRIRTLLNEREPVYRQATIHVSTDGRRSEE 164
|
170
....*....|....*...
gi 2108393370 170 VSQEVI-KGWQYVSKHHR 186
Cdd:PRK13948 165 VVEEIVeKLWAWAEARGA 182
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
261-500 |
1.60e-44 |
|
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: 161.58 E-value: 1.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 261 FAVPPGEASKNIAQAVK-IYDFLIEHRVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSLIAMTDASIGGKVAV 339
Cdd:cd08198 70 LIVPGGEAVKNDPALVEeILSAIHDHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 340 DHPQGKNLMGAFYQPSLVLADVRTLTTLPQRELTSGWAEVIKHGLILDADFLQLIEGNVKDLIKLKQSITSKVIARSAAI 419
Cdd:cd08198 150 NFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLERNAAALRQRDPDAMEKLIRRCAEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 420 KCQ--VVSEDERETGKRTLLNYGHTVAHGLEAAGKYDrFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGLP 497
Cdd:cd08198 230 HLDhiAASGDPFETGSARPLDFGHWSAHKLEQLSGYA-LRHGEAVAIGIALDSLYARLLGLLSREDFDRILALLQNLGLP 308
|
...
gi 2108393370 498 TDC 500
Cdd:cd08198 309 LWH 311
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
18-176 |
1.88e-41 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 146.57 E-value: 1.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 18 TGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAIVDPKNQKLL 97
Cdd:pfam01202 3 AGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEHGLVIATGGGAVLSEENRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 98 LDTSVVVCLEARPETIHQRLLHDSlysashvVRPLLAGDNPLE-RIKQLKATRQPYYA-IADWTVHTDNLTLDEVSQEVI 175
Cdd:pfam01202 83 KERGIVIYLDAPLEVLLERLKRDK-------TRPLLQNKDPEEeLLELLFEERDPLYEeAADIVIDTDESSPEEVATEIL 155
|
.
gi 2108393370 176 K 176
Cdd:pfam01202 156 E 156
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
206-507 |
1.08e-35 |
|
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: 134.41 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 206 YPVFVDWGILDKLGEkmTQAGLSGTANIISDETVFSIYGTQVKKTLeKAGFIVNCFAVPPGEAS-KNIAQAVKIYdflie 284
Cdd:cd07766 2 TRIVFGEGAIAKLGE--IKRRGFDRALVVSDEGVVKGVGEKVADSL-KKGLAVAIFDFVGENPTfEEVKNAVERA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 285 hRVERNDVIVALGGGMVGDLAGFAAATFLRGLPWIQVPTSliAMTDASIGGKVAVDHPQGKNLM-GAFYQPSLVLADVRT 363
Cdd:cd07766 74 -RAAEADAVIAVGGGSTLDTAKAVAALLNRGIPFIIVPTT--ASTDSEVSPKSVITDKGGKNKQvGPHYNPDVVFVDTDI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 364 LTTLPQRELTSGWAEVIKHGLILDAdflqLIEGNvkdlIKLKQSITSKVIarsaaikcqvvsederetgkrtlLNYGHTV 443
Cdd:cd07766 151 TKGLPPRQVASGGVDALAHAVELEK----VVEAA----TLAGMGLFESPG-----------------------LGLAHAI 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108393370 444 AHGLEAAGKYdrfLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGLPTDCSGVPLTD 507
Cdd:cd07766 200 GHALTAFEGI---PHGEAVAVGLPYVLKVANDMNPEPEAAIEAVFKFLEDLGLPTHLADLGVSK 260
|
|
| PRK13946 |
PRK13946 |
shikimate kinase; Provisional |
9-176 |
7.31e-33 |
|
shikimate kinase; Provisional
Pssm-ID: 184411 [Multi-domain] Cd Length: 184 Bit Score: 123.88 E-value: 7.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 9 NIALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAI 88
Cdd:PRK13946 12 TVVLVGLMGAGKSTVGRRLATMLGLPFLDADTEIERAARMTIAEIFAAYGEPEFRDLERRVIARLLKGGPLVLATGGGAF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 89 VDPKNQKLLLDTSVVVCLEARPETIHQRLLHdslysasHVVRPLLAGDNPLERIKQLKATRQPYYAIADWTVHTDNLTLD 168
Cdd:PRK13946 92 MNEETRAAIAEKGISVWLKADLDVLWERVSR-------RDTRPLLRTADPKETLARLMEERYPVYAEADLTVASRDVPKE 164
|
....*...
gi 2108393370 169 EVSQEVIK 176
Cdd:PRK13946 165 VMADEVIE 172
|
|
| aroK |
PRK05057 |
shikimate kinase AroK; |
9-176 |
9.33e-32 |
|
shikimate kinase AroK;
Pssm-ID: 235335 [Multi-domain] Cd Length: 172 Bit Score: 120.59 E-value: 9.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 9 NIALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAI 88
Cdd:PRK05057 6 NIFLVGPMGAGKSTIGRQLAQQLNMEFYDSDQEIEKRTGADIGWVFDVEGEEGFRDREEKVINELTEKQGIVLATGGGSV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 89 VDPKNQKLLLDTSVVVCLEArpeTIHQRLLHdslySASHVVRPLLAGDNPLERIKQLKATRQPYY-AIADWTVHTDNLTL 167
Cdd:PRK05057 86 KSRETRNRLSARGVVVYLET---TIEKQLAR----TQRDKKRPLLQVDDPREVLEALANERNPLYeEIADVTIRTDDQSA 158
|
....*....
gi 2108393370 168 DEVSQEVIK 176
Cdd:PRK05057 159 KVVANQIIH 167
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
213-498 |
2.76e-21 |
|
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: 95.23 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 213 GILDKLGEKMtqAGLSGTANIISDETVFSIYGTQVKKTLEKAGFIVNCFAVPpGEAS-KNIAQAVKIYdfliehRVERND 291
Cdd:COG0371 14 GALDELGEYL--ADLGKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFG-GECSeEEIERLAEEA------KEQGAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 292 VIVALGGGMVGDLAGFAAatFLRGLPWIQVPTslIAMTDAsIGGKVAV-DHPQGKNLMGAFY--QPSLVLADVRTLTTLP 368
Cdd:COG0371 85 VIIGVGGGKALDTAKAVA--YRLGLPVVSVPT--IASTDA-PASPLSViYTEDGAFDGYSFLakNPDLVLVDTDIIAKAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 369 QRELTSG-------WAEVikhglildadflQLIEGNVKDLIKLKQSITSKVIARS-------------AAIKCQVVSED- 427
Cdd:COG0371 160 VRLLAAGigdalakWYEA------------RDWSLAHRDLAGEYYTEAAVALARLcaetlleygeaaiKAVEAGVVTPAl 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 428 ERETGKRTLL----------NYG----HTVAHGLEAAGKYDRFLHGEAVAIGMMVAARLSQRlgllsPHSVEHQKSILRK 493
Cdd:COG0371 228 ERVVEANLLLsglamgigssRPGsgaaHAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGR-----PEEIEELLDFLRS 302
|
....*
gi 2108393370 494 FGLPT 498
Cdd:COG0371 303 VGLPT 307
|
|
| PRK13949 |
PRK13949 |
shikimate kinase; Provisional |
10-169 |
7.32e-21 |
|
shikimate kinase; Provisional
Pssm-ID: 140006 [Multi-domain] Cd Length: 169 Bit Score: 89.79 E-value: 7.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 10 IALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAIV 89
Cdd:PRK13949 4 IFLVGYMGAGKTTLGKALARELGLSFIDLDFFIENRFHKTVGDIFAERGEAVFRELERNMLHEVAEFEDVVISTGGGAPC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 90 DPKNQKLLLDTSVVVCLEARPETIHQRLLhdslySASHvVRPLLAGDNP---LERIKQLKATRQPYYAIADWTVHTDNLT 166
Cdd:PRK13949 84 FFDNMELMNASGTTVYLKVSPEVLFVRLR-----LAKQ-QRPLLKGKSDeelLDFIIEALEKRAPFYRQAKIIFNADKLE 157
|
...
gi 2108393370 167 LDE 169
Cdd:PRK13949 158 DES 160
|
|
| PRK08154 |
PRK08154 |
anaerobic benzoate catabolism transcriptional regulator; Reviewed |
2-176 |
3.93e-20 |
|
anaerobic benzoate catabolism transcriptional regulator; Reviewed
Pssm-ID: 236167 [Multi-domain] Cd Length: 309 Bit Score: 91.17 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 2 PRRKATNNIALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQ-AV 80
Cdd:PRK08154 128 RRAARRRRIALIGLRGAGKSTLGRMLAARLGVPFVELNREIEREAGLSVSEIFALYGQEGYRRLERRALERLIAEHEeMV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 81 IATGGGAIVDPKNQKLLLDTSVVVCLEARPETIHQRLLhdslysASHVVRPLLAGDNPLERIKQLKATRQPYYAIADWTV 160
Cdd:PRK08154 208 LATGGGIVSEPATFDLLLSHCYTVWLKASPEEHMARVR------AQGDLRPMADNREAMEDLRRILASREPLYARADAVV 281
|
170
....*....|....*.
gi 2108393370 161 HTDNLTLDEVSQEVIK 176
Cdd:PRK08154 282 DTSGLTVAQSLARLRE 297
|
|
| aroL |
PRK03731 |
shikimate kinase AroL; |
7-154 |
8.83e-19 |
|
shikimate kinase AroL;
Pssm-ID: 235153 [Multi-domain] Cd Length: 171 Bit Score: 83.84 E-value: 8.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 7 TNNIALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIFKQDGEDKFRQLEHKVLsQACQKKQAVIATGGG 86
Cdd:PRK03731 2 TQPLFLVGARGCGKTTVGMALAQALGYRFVDTDQWLQSTSNMTVAEIVEREGWAGFRARESAAL-EAVTAPSTVIATGGG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108393370 87 AIVDPKNQKLLLDTSVVVCLEARPETIHQRLlhdSLYSASHvVRPLLAGDNPLERIKQLKATRQPYYA 154
Cdd:PRK03731 81 IILTEENRHFMRNNGIVIYLCAPVSVLANRL---EANPEED-QRPTLTGKPISEEVAEVLAEREALYR 144
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
213-498 |
4.83e-14 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 73.70 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 213 GILDKLGEKMtqAGLSGTANIISDETVFSIYGTQVKKTLEKAGFIVNcFAVPPGEASKN-IAQAVKIYdfliehRVERND 291
Cdd:PRK09423 16 GALARLGEYL--KPLGKRALVIADEFVLGIVGDRVEASLKEAGLTVV-FEVFNGECSDNeIDRLVAIA------EENGCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 292 VIVALGGGMVGDLAgfAAATFLRGLPWIQVPTslIAMTDASIGGKVAVDHPQGKNLMGAFY--QPSLVLADVRTLTTLPQ 369
Cdd:PRK09423 87 VVIGIGGGKTLDTA--KAVADYLGVPVVIVPT--IASTDAPTSALSVIYTEEGEFERYLFLpkNPDLVLVDTAIIAKAPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 370 RELTSG-------WAEvikhglildADflQLIEGNVKDLIKLKQSITSKVIAR-------------SAAIKCQVVSED-E 428
Cdd:PRK09423 163 RFLAAGigdalatWFE---------AR--ACSRSGGTTMAGGKPTLAALALAElcyetlledglkaKLAVEAKVVTPAlE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 429 RETGKRTLL------NYG----HTVAHGLEAAGKYDRFLHGEAVAIGMMVAARLSQRlgllSPHSVEHQKSILRKFGLPT 498
Cdd:PRK09423 232 NVIEANTLLsglgfeSGGlaaaHAIHNGLTALEDTHHLTHGEKVAFGTLTQLVLENR----PKEEIEEVIDFCHAVGLPT 307
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
213-553 |
5.65e-14 |
|
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: 73.36 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 213 GILDKLGEKMTQAGLSGTANIISDETVFSIYGTQVKKTLEKAG---FIVNCFAVppgEASKNIAQAVKIydflieHRVER 289
Cdd:cd08173 10 GAINKIGEVLKKLLLGKRALIITGPNTYKIAGKRVEDLLESSGvevVIVDIATI---EEAAEVEKVKKL------IKESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 290 NDVIVALGGGMVGDLAGFAAatFLRGLPWIQVPTSL----IAMTDASIGGKvavDHPQGKNLMgafyQPSLVLADVRTLT 365
Cdd:cd08173 81 ADFIIGVGGGKVIDVAKYAA--YKLNLPFISIPTSAshdgIASPFASIKGG---DKPYSIKAK----APIAIIADTEIIS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 366 TLPQRELTSGWAEVI-KHGLILD---ADFL-----------------QLIEGNVkDLIK----------LKQSITSKV-- 412
Cdd:cd08173 152 KAPKRLLAAGCGDLIsNITAVKDwrlAHRLkgeyyseyaaslalmsaKLIIENA-DLIKpgleegvrtvVKALISSGVam 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 413 -IARSAaikcQVVSEDEretgkrtllnygHTVAHGLEAAGKyDRFLHGEAVAIGMMVAARLsqrlgllspHSVEHQ--KS 489
Cdd:cd08173 231 sIAGSS----RPASGSE------------HLFSHALDKLAP-GPALHGEQCGVGTIMMAYL---------HGGDWKeiRE 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108393370 490 ILRKFGLPTDCS--GVPLTDVLAAMELDKKVRGKaiRWVLLEDIGkavirsdIPKKEVLNVLK--GII 553
Cdd:cd08173 285 ALKKIGAPTTAKelGLDKEIIIEALTIAHKIRPE--RYTILGDNG-------LTEEAAERLARitGVI 343
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
213-498 |
7.64e-14 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; 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: 341449 [Multi-domain] Cd Length: 351 Bit Score: 72.83 E-value: 7.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 213 GILDKLGEKMtqAGLSGTANIISDETVFSIYGTQVKKTLEKAGFIVnCFAVPPGEASKN-IAQAVKIydflieHRVERND 291
Cdd:cd08170 9 GALDRLGEYL--APLGKKALVIADPFVLDLVGERLEESLEKAGLEV-VFEVFGGECSREeIERLAAI------ARANGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 292 VIVALGGGMVGDLAGfAAATFLrGLPWIQVPTslIAMTDASIGGKVAVDHPQGKNLMGAFYQ--PSLVLADVRTLTTLPQ 369
Cdd:cd08170 80 VVIGIGGGKTIDTAK-AVADYL-GLPVVIVPT--IASTDAPCSALSVIYTEDGEFDEYLFLPrnPDLVLVDTEIIAKAPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 370 RELTSG-------WAEVikhglildadfLQLIEGNVKDLIKLKQSITSKVIARS-------------AAIKCQVVSED-E 428
Cdd:cd08170 156 RFLVAGmgdalatYFEA-----------RACARSGAPNMAGGRPTLAALALAELcydtlleygvaakAAVEAGVVTPAlE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 429 R--ETgkRTLL------NYG----HTVAHGLEAAGKYDRFLHGEAVAIGMMVAARLSQRlgllSPHSVEHQKSILRKFGL 496
Cdd:cd08170 225 AviEA--NTLLsglgfeSGGlaaaHAIHNGLTALPETHHLLHGEKVAFGTLVQLVLEGR----PDEEIEEVIRFCRSVGL 298
|
..
gi 2108393370 497 PT 498
Cdd:cd08170 299 PV 300
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
208-519 |
5.42e-13 |
|
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: 70.23 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 208 VFVDWGILDKLGEKMTQAGLSGTANIISDETVFSIYGTQVKKTLEKAGFIVnCFAVPPGEA-----SKNIAQavkiydfL 282
Cdd:cd08175 4 IVIGEGALKKLPEYLKELFGGKKVLVVADENTYAAAGEEVEAALEEAGVTV-CLLIFPGEGdliadEAAVGK-------V 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 283 IEHRVERNDVIVALGGGMVGDLAGFAAatFLRGLPWIQVPTSliAMTD--ASIGGKVAVDhpqG-KNLMGAFYqPSLVLA 359
Cdd:cd08175 76 LLELEKDTDLIIAVGSGTINDLTKYAA--YKLGIPYISVPTA--PSMDgyTSSGAPIIVD---GvKKTFPAHA-PKAIFA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 360 DVRTLTTLPQRELTSGWAEVI-K----------HgLILDADFLQLIEGNVKDLIKlkqsitsKVIARSAAIKcqvvSEDE 428
Cdd:cd08175 148 DLDVLANAPQRMIAAGFGDLLgKytaladwklsH-LLGGEYYCPEVADLVQEALE-------KCLDNAEGIA----ARDP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 429 RETGK--RTLLNYG----------------HTVAHGLE----AAGKYDrFLHGEAVAIGMMVAARLSQRLGLLSPHSVEH 486
Cdd:cd08175 216 EAIEAlmEALILSGlamqlvgnsrpasgaeHHLSHYWEmeflRLGKPP-VLHGEKVGVGTLLIAALYILEQLPPPEELRE 294
|
330 340 350
....*....|....*....|....*....|....*
gi 2108393370 487 qksILRKFGLPTDCS--GVPLTDVLAAMELDKKVR 519
Cdd:cd08175 295 ---LLRKAGAPTTPEdlGIDRDLLRDSLRLAKEIR 326
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
213-498 |
1.47e-11 |
|
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: 65.66 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 213 GILDKLGEkMTQAGLSGTANIISDETVFSIYGTQVKKTLEKagfivNCfAVPPGEASKNIAQAVKIYDFLiehrvernDV 292
Cdd:cd08549 9 GAINKIEE-ILKKLNLKRVLIITGKNTKAKYCRFFYDQLKT-----VC-DIVYYDNIDNLEDELKKYTFY--------DC 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 293 IVALGGGMVGDLAGFAAatFLRGLPWIQVPTSliAMTDASIGGKVAVDHPQGKNLMGAfYQPSLVLADVRTLTTLPQREL 372
Cdd:cd08549 74 VIGIGGGRSIDTGKYLA--YKLKIPFISVPTS--ASNDGIASPIVSLRIPGVKKTFMA-DAPIAIIADTEIIKKSPRRLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 373 TSGWAEVI-KHGLILDADFLQLIEGNVKDLIKLKQSITSKVIARSAAIKCQVVSEDERETGKrTLLNYG----------- 440
Cdd:cd08549 149 SAGIGDLVsNITAVLDWKLAHKEKGEKYSEFAAILSKTSAKELVSYVLKASDLEEYHRVLVK-ALVGSGiamaiagssrp 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108393370 441 -----HTVAHGLEA---AGKYDRFLHGEAVAIGMMVAARLSQRLGLLSPHSVEHQKSILRKFGLPT 498
Cdd:cd08549 228 asgseHLFSHALDKlkeEYLNINVLHGEQVGVGTIIMSYLHEKENKKLSGLHERIKMILKKVGAPT 293
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
213-498 |
9.27e-11 |
|
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: 63.32 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 213 GILDKLGEKMTQAGLsgTANIISDETVFSIYGTQVKKTLEKAGFIVNcFAVPPGEASKN----IAQAVKIYDFliehrve 288
Cdd:cd08550 9 GILAKAGEYIAPLGK--KALIIGGKTALEAVGEKLEKSLEEAGIDYE-VEVFGGECTEEnierLAEKAKEEGA------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 289 rnDVIVALGGGMVGDLAGFAAAtfLRGLPWIQVPTslIAMTDA-----SIggkvaVDHPQGKNLMGAFYQ--PSLVLADV 361
Cdd:cd08550 79 --DVIIGIGGGKVLDTAKAVAD--RLGLPVVTVPT--IAATCAawsalSV-----LYDEEGEFLGYSLLKrsPDLVLVDT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 362 RTLTTLPQRELTSGwaevikhglILDA-----DFLQLIEGNVKDL---IKLKQS-ITSKVIARSA-----AIKCQVVSED 427
Cdd:cd08550 148 DIIAAAPVRYLAAG---------IGDTlakwyEARPSSRGGPDDLalqAAVQLAkLAYDLLLEYGvqaveDVRQGKVTPA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 428 ERET-----------------GKRTLLnyGHTVAHGLEAAGKYDRFLHGEAVAIGMMVAARLSQRlgllSPHSVEHQKSI 490
Cdd:cd08550 219 LEDVvdaiillaglvgslgggGCRTAA--AHAIHNGLTKLPETHGTLHGEKVAFGLLVQLALEGR----SEEEIEELIEF 292
|
....*...
gi 2108393370 491 LRKFGLPT 498
Cdd:cd08550 293 LRRLGLPV 300
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
208-498 |
9.88e-11 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 63.37 E-value: 9.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 208 VFVDWGILDKLGEKMTQAGLSGTANIISDETVFSIYGTQVKKTLEKAG----FIVncfavppGEASKNIAQAVkiydflI 283
Cdd:PRK00843 14 VVVGHGVLDDIGDVCSDLKLTGRALIVTGPTTKKIAGDRVEENLEDAGdvevVIV-------DEATMEEVEKV------E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 284 EH-RVERNDVIVALGGGMVGDLAGFAAatFLRGLPWIQVPTSL----IAMTDASI---GGKVAVD-HPqgknlmgafyqP 354
Cdd:PRK00843 81 EKaKDVNAGFLIGVGGGKVIDVAKLAA--YRLGIPFISVPTAAshdgIASPRASIkggGKPVSVKaKP-----------P 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 355 SLVLADVRTLTTLPQRELTSGWAEVI-KHGLILD---------------ADFLQLIEGNV----KDLIKL---------- 404
Cdd:PRK00843 148 LAVIADTEIIAKAPYRLLAAGCGDIIsNYTAVKDwrlahrlrgeyyseyAAALSLMTAKMlienADIIKPgleesarlvv 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 405 KQSITSKViARSAAIKCQVVSEDEretgkrtllnygHTVAHGLEAAGKyDRFLHGEAVAIGMMVAARLsqrlgllspHSV 484
Cdd:PRK00843 228 KALISSGV-AMSIAGSSRPASGSE------------HLFSHALDRLAP-GPALHGEQCGVGTIIMMYL---------HGG 284
|
330
....*....|....*.
gi 2108393370 485 EHQK--SILRKFGLPT 498
Cdd:PRK00843 285 DWRKirDALKKIGAPT 300
|
|
| PLN02199 |
PLN02199 |
shikimate kinase |
12-167 |
1.35e-10 |
|
shikimate kinase
Pssm-ID: 177850 [Multi-domain] Cd Length: 303 Bit Score: 62.79 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 12 LIGFSATGKSVIAMKVAERLKWMSIDTDDEIAK-LSGKTIPEIFKQDGEDKFRQLEHKVLSQACQKKQAVIATGGGAIVD 90
Cdd:PLN02199 107 LVGMMGSGKTTVGKLMSKVLGYTFFDCDTLIEQaMNGTSVAEIFVHHGENFFRGKETDALKKLSSRYQVVVSTGGGAVIR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 91 PKNQKlLLDTSVVVCLEARPETIHQRLLHDSLYSashvvRPLL---AGDN---PLERIKQLKATRQPYYAIADWTVHTDN 164
Cdd:PLN02199 187 PINWK-YMHKGISIWLDVPLEALAHRIAAVGTDS-----RPLLhdeSGDAysvAFKRLSAIWDERGEAYTNANARVSLEN 260
|
...
gi 2108393370 165 LTL 167
Cdd:PLN02199 261 IAA 263
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
213-519 |
9.19e-10 |
|
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: 60.23 E-value: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 213 GILDKLGEKMTQAGLSGT-ANIISDETVFSIYGTQVKKTLEKAGFIVNCFAVPPGEASkNIAQAVKIydfliehrVERND 291
Cdd:cd08174 9 GALEHLGKYLADRNQGFGkVAIVTGEGIDELLGEDILESLEEAGEIVTVEENTDNSAE-ELAEKAFS--------LPKVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 292 VIVALGGGMVGDLAGFAAatFLRGLPWIQVPTSL----IAMTDASI---GGK--VAVDHPQGknlmgafyqpslVLADVR 362
Cdd:cd08174 80 AIVGIGGGKVLDVAKYAA--FLSKLPFISVPTSLsndgIASPVAVLkvdGKRksLGAKMPYG------------VIVDLD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 363 TLTTLPQRELTSG-------------W-AEVIKHGLILDaDF------------LQLIEGNVKDLIKLKQSITSKV---I 413
Cdd:cd08174 146 VIKSAPRRLILAGigdlisnitalydWkLAEEKGGEPVD-DFayllsrtaadslLNTPGKDIKDDEFLKELAESLVlsgI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 414 ARSAAIKCQVVSEDEretgkrtllnygHTVAHGLEAAGKyDRFLHGEAVAIGMMVAARLsQRlgllspHSVEHQKSILRK 493
Cdd:cd08174 225 AMEIAGSSRPASGSE------------HLISHALDKLFP-GPALHGIQVGLGTYFMSFL-QG------QRYEEIRDVLKR 284
|
330 340
....*....|....*....|....*...
gi 2108393370 494 FGLPTDCSGVPLT--DVLAAMELDKKVR 519
Cdd:cd08174 285 TGFPLNPSDLGLTkeEFIEAVKLAPSTR 312
|
|
| PRK00625 |
PRK00625 |
shikimate kinase; Provisional |
9-122 |
2.30e-08 |
|
shikimate kinase; Provisional
Pssm-ID: 134335 [Multi-domain] Cd Length: 173 Bit Score: 53.99 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 9 NIALIGFSATGKSVIAMKVAERLKWMSIDTDDEI-AKLSGKTIP---EIFKQDGEDKFRQLEHKVLSQACqKKQAVIATG 84
Cdd:PRK00625 2 QIFLCGLPTVGKTSFGKALAKFLSLPFFDTDDLIvSNYHGALYSspkEIYQAYGEEGFCREEFLALTSLP-VIPSIVALG 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 2108393370 85 GGAIVDPKNQKLLLDTSVVVCLEARPETIHQRLLHDSL 122
Cdd:PRK00625 81 GGTLMIEPSYAHIRNRGLLVLLSLPIATIYQRLQKRGL 118
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
213-468 |
1.72e-07 |
|
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: 53.29 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 213 GILDKLGEKMTQAGLSgTANIISDETVFSIygtqVKK---TLEKAGFIVNCFAvppGEASKNIAQAVKiyDFLIEHRVer 289
Cdd:cd08172 9 GALKELPELLSEFGIK-RPLIIHGEKSWQA----AKPylpKLFEIEYPVLRYD---GECSYEEIDRLA--EEAKEHQA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 290 nDVIVALGGGMVGDLAGFAAATFlrGLPWIQVPTslIAMTDASIGGKVAVDHPQGKNLMGAFY--QPSLVLADVRTLTTL 367
Cdd:cd08172 77 -DVIIGIGGGKVLDTAKAVADKL--NIPLILIPT--LASNCAAWTPLSVIYDEDGEFIGYDYFprSAYLVLVDPRLLLDS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 368 PQRELTSG-------W--AEVIKHGLILDADFLQL---IEGNVKDLIkLKQSitskvIARSAAIKCQVVSEDER---ET- 431
Cdd:cd08172 152 PKDYFVAGigdtlakWyeADAILRQLEELPAFLQLarqAAKLCRDIL-LKDS-----EQALADLEAGKLTPAFIkvvETi 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2108393370 432 ----------GKRtllnYG-HTVAH----GLEAAGKYDRFLHGEAVAIGMMV 468
Cdd:cd08172 226 ialagmvggfGDE----YGrSAGAHaihnGLTKLPETHHFLHGEKVAYGILV 273
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
10-151 |
1.74e-07 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 50.39 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 10 IALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEI-FKQDGEDKFRQLEHKVLSQACQKKQAVIATGGgaI 88
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLEELGAVRLSSDDERKRLFGEGRPSIsYYTDATDRTYERLHELARIALRAGRPVILDAT--N 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2108393370 89 VDPKNQKLLLD--------TSVVVClEARPETIHQRLL--HDSLYSASHVvrpllagdnPLERIKQLKATRQP 151
Cdd:pfam13671 80 LRRDERARLLAlareygvpVRIVVF-EAPEEVLRERLAarARAGGDPSDV---------PEEVLDRQKARFEP 142
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
212-370 |
1.16e-05 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They 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, among 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: 341481 [Multi-domain] Cd Length: 372 Bit Score: 47.83 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 212 WGILDKLGEKMTQAGLSGTAnIISDETVFSI-YGTQVKKTLEKAGFIVNCFA-VPPGEASKNIAQAVKIYdfliehRVER 289
Cdd:cd08551 8 AGALARLGEELKALGGKKVL-LVTDPGLVKAgLLDKVLESLKAAGIEVEVFDdVEPNPTVETVEAAAELA------REEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 290 NDVIVALGGGMVGDLAGfAAATFL-----------------RGLPWIQVPT-----------SLIamTDASIGGKVAVDH 341
Cdd:cd08551 81 ADLVIAVGGGSVLDTAK-AIAVLAtnggsirdyegigkvpkPGLPLIAIPTtagtgsevtpnAVI--TDPETGRKMGIVS 157
|
170 180
....*....|....*....|....*....
gi 2108393370 342 PqgkNLMgafyqPSLVLADVRTLTTLPQR 370
Cdd:cd08551 158 P---YLL-----PDVAILDPELTLSLPPS 178
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
10-119 |
1.29e-05 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 45.67 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 10 IALIGFSATGKSVIAMKVAERLKWMSIDTDDEIAKLSGKTIPEIfkQDGEDKFRQLEHKVLSQAcqkkQAVIATGGGAIV 89
Cdd:COG0645 2 ILVCGLPGSGKSTLARALAERLGAVRLRSDVVRKRLFGAGLAPL--ERSPEATARTYARLLALA----RELLAAGRSVIL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2108393370 90 D-----PKNQKLLLD-------TSVVVCLEARPETIHQRLLH 119
Cdd:COG0645 76 DatflrRAQREAFRAlaeeagaPFVLIWLDAPEEVLRERLEA 117
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
213-323 |
3.16e-05 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 46.37 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 213 GILDKLGEKMtqAGLSGT-ANIISDETVFSI-YGTQVKKTLEKAGFIVNCFA-VPPGEASKNIAQAVKIYdfliehRVER 289
Cdd:cd08194 9 GALEELGEEA--ASLGGKrALIVTDKVMVKLgLVDKVTQLLAEAGIAYAVFDdVVSEPTDEMVEEGLALY------KEGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2108393370 290 NDVIVALGGG-----------MV---GDLAGFAAATFL--RGLPWIQVPT 323
Cdd:cd08194 81 CDFIVALGGGspidtakaiavLAtngGPIRDYMGPRKVdkPGLPLIAIPT 130
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
208-373 |
5.54e-05 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 45.50 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 208 VFVDWGILDKLGEKMTQAGLSGTAnIISDETVFSI-YGTQVKKTLEKAGFIVNCFAVPPGEAS-KNIAQAVKIYdflieh 285
Cdd:COG1454 11 IVFGAGALAELGEELKRLGAKRAL-IVTDPGLAKLgLLDRVLDALEAAGIEVVVFDDVEPNPTvETVEAGAAAA------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 286 RVERNDVIVALGGG--M---------------VGDLAGFAAATfLRGLPWIQVPT--------SLIA-MTDASIGGKVAV 339
Cdd:COG1454 84 REFGADVVIALGGGsaIdaakaiallatnpgdLEDYLGIKKVP-GPPLPLIAIPTtagtgsevTPFAvITDPETGVKKGI 162
|
170 180 190
....*....|....*....|....*....|....
gi 2108393370 340 DHPqgkNLMgafyqPSLVLADVRTLTTLPqRELT 373
Cdd:COG1454 163 ADP---ELL-----PDVAILDPELTLTLP-PSLT 187
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
212-498 |
5.54e-05 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 45.67 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 212 WGILDKLGEKMTQAGLSgtANIISDETVF-SIYGTQVKKTLEKAGFIVNCFAVPPGEAS-KNIAQAVKIYdfliehRVER 289
Cdd:pfam00465 8 AGALAELGEELKRLGAR--ALIVTDPGSLkSGLLDKVLASLEEAGIEVVVFDGVEPEPTlEEVDEAAALA------REAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 290 NDVIVALGGGMVGDLAGFAAATFLRG----------------LPWIQVPTslIA-----MTDASiggkVAVDHPQG--KN 346
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPgdvwdylggkpltkpaLPLIAIPT--TAgtgseVTPLA----VITDTETGekLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 347 LMGAFYQPSLVLADVRTLTTLPQRELTSGwaevikhglILDAdFLQLIEGnvkdLIKLKQSITSKVIARSA---AIKC-Q 422
Cdd:pfam00465 154 IFSPKLLPDLAILDPELTLTLPPRLTAAT---------GMDA-LAHAVEA----YVSKGANPLTDALALEAirlIAENlP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 423 VVSEDERETGKRTLLNYG----------------HTVAHGLeaAGKYDrFLHGEAVAIgMMVA-------------ARLS 473
Cdd:pfam00465 220 RAVADGEDLEARENMLLAstlaglafsnaglgaaHALAHAL--GGRYG-IPHGLANAI-LLPYvlrfnapaapeklAQLA 295
|
330 340 350
....*....|....*....|....*....|
gi 2108393370 474 QRLGLLSPHS-----VEHQKSILRKFGLPT 498
Cdd:pfam00465 296 RALGEDSDEEaaeeaIEALRELLRELGLPT 325
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
208-339 |
1.83e-04 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 44.14 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 208 VFVDWGILDKLGEKMTQAGLSgtANIISDETVFSIYG-TQVKKTLEKAGFIVNCFA-VPPGEASKNIAQAVKiydfliEH 285
Cdd:cd08191 7 LLFGPGARRALGRVAARLGSR--VLIVTDPRLASTPLvAELLAALTAAGVAVEVFDgGQPELPVSTVADAAA------AA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108393370 286 RVERNDVIVALGGGMVGDLAGFAAATFLRG----------------LPWIQVPT--------SLIA-MTDASIGGKVAV 339
Cdd:cd08191 79 RAFDPDVVIGLGGGSNMDLAKVVALLLAHGgdprdyygedrvpgpvLPLIAVPTtagtgsevTPVAvLTDPARGMKVGV 157
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
245-373 |
1.20e-03 |
|
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341483 [Multi-domain] Cd Length: 374 Bit Score: 41.34 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 245 TQVKKTLEKAGFIVNCFA-VPPGEASKNIAQAVKIYdfliehRVERNDVIVALGGG-----------MV---GDLAGFAA 309
Cdd:cd14861 43 DRVLEALGAAGLSPAVFSdVPPNPTEADVEAGVAAY------REGGCDGIIALGGGsaidaakaialMAthpGPLWDYED 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 310 ATFLRGL------PWIQVPT-----------SLIamTDASIGGKVAVDHPqgkNLMgafyqPSLVLADVRTLTTLPQReL 372
Cdd:cd14861 117 GEGGPAAitpavpPLIAIPTtagtgsevgraAVI--TDDDTGRKKIIFSP---KLL-----PKVAICDPELTLGLPPR-L 185
|
.
gi 2108393370 373 T 373
Cdd:cd14861 186 T 186
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
246-395 |
1.82e-03 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 40.95 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 246 QVKKTLEKAGFIVNCFAVPpGEAS-KNIAQAVKIYdfliehRVERNDVIVALGGGMVGDLAGFAAA---------TFL-- 313
Cdd:cd08183 41 RLLEALEAAGIEVALFSVS-GEPTvETVDAAVALA------REAGCDVVIAIGGGSVIDAAKAIAAlltnegsvlDYLev 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 314 ---------RGLPWIQVPT-----------SLIamTDASIGGKVAVDHPqgknlmgaFYQPSLVLADVRTLTTLPqRELT 373
Cdd:cd08183 114 vgkgrpltePPLPFIAIPTtagtgsevtknAVL--SSPEHGVKVSLRSP--------SMLPDVALVDPELTLSLP-PEVT 182
|
170 180
....*....|....*....|....
gi 2108393370 374 --SGwaevikhgliLDAdFLQLIE 395
Cdd:cd08183 183 aaSG----------LDA-LTQLIE 195
|
|
| Cmk |
COG0283 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
10-38 |
5.70e-03 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440052 [Multi-domain] Cd Length: 220 Bit Score: 38.47 E-value: 5.70e-03
10 20
....*....|....*....|....*....
gi 2108393370 10 IALIGFSATGKSVIAMKVAERLKWMSIDT 38
Cdd:COG0283 3 IAIDGPAGSGKSTVAKALAKRLGYHYLDT 31
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
207-305 |
7.15e-03 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 39.06 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108393370 207 PVFVDWGILDKLGEKMTQAGLSgTANIISDETVFSI-YGTQVKKTLEKAGFIVNCFAVPPGEAS-KNIAQAVKIYdflie 284
Cdd:cd14863 7 PVIFGAGAVEQIGELLKELGCK-KVLLVTDKGLKKAgIVDKIIDLLEEAGIEVVVFDDVEPDPPdEIVDEAAEIA----- 80
|
90 100
....*....|....*....|.
gi 2108393370 285 hRVERNDVIVALGGGMVGDLA 305
Cdd:cd14863 81 -REEGADGVIGIGGGSVLDTA 100
|
|
| |
