|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
10-369 |
0e+00 |
|
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440106 Cd Length: 355 Bit Score: 516.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 10 TVNVSLGARAYDILIGPGLLQSAGEEIARRLPGVRAAIVTDSNVAEGHLATLQAGLEAAGIEATAITVAPGERSKRFATL 89
Cdd:COG0337 3 TLTVNLGERSYDIRIGRGLLDELGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGEASKTLETL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 90 EEVVSGILDARLERGDIVIPLGGGVVGDLAGFAAGIVRRGMHFVQAPTSLLAQVDSSVGGKTGINTAHGKNLVGVFHQPQ 169
Cdd:COG0337 83 ERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQPR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 170 LVIADTAVLDTLPPREFRAGYAEVAKYGLIDRPDFFAWLEKNWQAVFDGGPE-RVEAIAQSCQAKADVVARDELEMGDRA 248
Cdd:COG0337 163 AVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEaLEEAIARSCEIKAEVVAADERESGLRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 249 LLNLGHTFGHALEAATGYdsaRLVHGEGVAIGMALAHRFSARLNLASPDDAGRVEAHLSAVGLPTRLSDVPgglpgAEQL 328
Cdd:COG0337 243 LLNFGHTFGHAIEAATGY---RLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPALD-----PEAL 314
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1426272485 329 LTYIAQDKKVSRGALTFILTRGIGQSFVAKDVPTSQVLSFL 369
Cdd:COG0337 315 LAAMKRDKKVRGGKLRFVLLRGIGKAVIVDDVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
20-369 |
5.04e-162 |
|
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: 457.29 E-value: 5.04e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 20 YDILIGPGLLQSAGEeIARRLPGVRAAIVTDSNVAEGHLATLQAGLEAAGIEATAITVAPGERSKRFATLEEVVSGILDA 99
Cdd:cd08195 2 YPILIGSGLLDKLGE-LLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGEKSKSLETVERIYDFLLEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 100 RLERGDIVIPLGGGVVGDLAGFAAGIVRRGMHFVQAPTSLLAQVDSSVGGKTGINTAHGKNLVGVFHQPQLVIADTAVLD 179
Cdd:cd08195 81 GLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 180 TLPPREFRAGYAEVAKYGLIDRPDFFAWLEKNWQAVFDGGPERV-EAIAQSCQAKADVVARDELEMGDRALLNLGHTFGH 258
Cdd:cd08195 161 TLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALeEIIARSVEIKADIVEEDEREKGLRAILNFGHTFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 259 ALEAATGYdsaRLVHGEGVAIGMALAHRFSARLNLASPDDAGRVEAHLSAVGLPTRLSDVPgglpgAEQLLTYIAQDKKV 338
Cdd:cd08195 241 AIESASGY---KLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKDLD-----PEELLEAMKRDKKN 312
|
330 340 350
....*....|....*....|....*....|.
gi 1426272485 339 SRGALTFILTRGIGQSFVAKDVPTSQVLSFL 369
Cdd:cd08195 313 RGGKIRFVLLKGIGKAVIVDDVSEEEIREAL 343
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
75-338 |
1.38e-132 |
|
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: 379.53 E-value: 1.38e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 75 ITVAPGERSKRFATLEEVVSGILDARLERGDIVIPLGGGVVGDLAGFAAGIVRRGMHFVQAPTSLLAQVDSSVGGKTGIN 154
Cdd:pfam01761 2 IVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 155 TAHGKNLVGVFHQPQLVIADTAVLDTLPPREFRAGYAEVAKYGLIDRPDFFAWLEKNWQAVFDGGPE-RVEAIAQSCQAK 233
Cdd:pfam01761 82 HPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDaLEEAIARSCEVK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 234 ADVVARDELEMGDRALLNLGHTFGHALEAATGYDsaRLVHGEGVAIGMALAHRFSARLNLASPDDAGRVEAHLSAVGLPT 313
Cdd:pfam01761 162 ADVVAQDEKESGLRALLNLGHTFGHAIEALSGYG--ALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLPT 239
|
250 260
....*....|....*....|....*
gi 1426272485 314 RLSDVPgglpgAEQLLTYIAQDKKV 338
Cdd:pfam01761 240 SLPDLD-----VEQLLAAMARDKKV 259
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
20-369 |
9.06e-129 |
|
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: 373.12 E-value: 9.06e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 20 YDILIGPGLLQSAGEEIArrlPGVRAAIVTDSNVAEGHLATLQAGLEAAGIEATAITVAPGERSKRFATLEEVVSGILDA 99
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEELA---EPSKLVIITDETVADLYGDKLLEALQALGYNVLKLTVPDGEESKSLETVQRLYDQLLEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 100 RLERGDIVIPLGGGVVGDLAGFAAGIVRRGMHFVQAPTSLLAQVDSSVGGKTGINTAHGKNLVGVFHQPQLVIADTAVLD 179
Cdd:TIGR01357 78 GLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 180 TLPPREFRAGYAEVAKYGLIDRPDFFAWLEKNWQAVFDGGPERV--EAIAQSCQAKADVVARDELEMGDRALLNLGHTFG 257
Cdd:TIGR01357 158 TLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQELEHleELIKRSIEVKASIVAEDEKESGLRAILNFGHTIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 258 HALEAATGYDSARlvHGEGVAIGMALAHRFSARLNLASPDDAGRVEAHLSAVGLPTRLSDVpgglPGAEQLLTYIAQDKK 337
Cdd:TIGR01357 238 HAIEAEAGYGKIP--HGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKD----LDVDELLNAMLNDKK 311
|
330 340 350
....*....|....*....|....*....|..
gi 1426272485 338 VSRGALTFILTRGIGQSFVAKDVPTSQVLSFL 369
Cdd:TIGR01357 312 NSGGKIRFVLLEEIGKAALAREVPDEMVLELL 343
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
10-373 |
2.63e-104 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 314.01 E-value: 2.63e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 10 TVNVSLGARAYDILIGPGLLQSaGEEIARRLPGVRAAIVTDSNVAEGHLATLQAGLEAAGIEATAITVA--PGERSKRFA 87
Cdd:PLN02834 69 VVKVDLGDRSYPIYIGSGLLDH-GELLQRHVHGKRVLVVTNETVAPLYLEKVVEALTAKGPELTVESVIlpDGEKYKDME 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 88 TLEEVVSGILDARLERGDIVIPLGGGVVGDLAGFAAGIVRRGMHFVQAPTSLLAQVDSSVGGKTGINTAHGKNLVGVFHQ 167
Cdd:PLN02834 148 TLMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 168 PQLVIADTAVLDTLPPREFRAGYAEVAKYGLIDRPDFFAWLEKNWQAVFDGGPERVE-AIAQSCQAKADVVARDELEMGD 246
Cdd:PLN02834 228 PQCVLIDTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAyAIKRSCENKAEVVSLDEKESGL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 247 RALLNLGHTFGHALEAATGYdsARLVHGEGVAIGMALAHRFSARLNLASPDDAGRVEAHLSAVGLPTRLSDvpggLPGAE 326
Cdd:PLN02834 308 RATLNLGHTFGHAIETGPGY--GEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPE----KMTVE 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1426272485 327 QLLTYIAQDKKVSRGALTFILTRG-IGQSFVAKDVPTSQvlsfLEESL 373
Cdd:PLN02834 382 MFKSLMAVDKKVADGLLRLILLKGeLGNCVFTGDFDREA----LEETL 425
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
20-352 |
7.56e-88 |
|
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: 268.51 E-value: 7.56e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 20 YDILIGPGLLQSAGEEIARRLPGvRAAIVTDSNVAEGHLATLQAGLeAAGIEATAITVAPGERSKRFATLEEVVSGILDA 99
Cdd:cd08169 2 YPVFFGEGVFESVNSYIPRDAFD-QCLIIVDSGVPDLIVNYLAEYF-GYYLEVHVFIIQGGEAYKTFQTVVEELERAAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 100 RLERGDIVIPLGGGVVGDLAGFAAGIVRRGMHFVQAPTSLLAQVDSSVGGKTGINTAHGKNLVGVFHQPQLVIADTAVLD 179
Cdd:cd08169 80 HLNRHSAVVAVGGGATGDVVGFAAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 180 TLPPREFRAGYAEVAKYGLIDRPDFFAWLEKNWQAVFDGGPERVEA-IAQSCQAKADVVARDELEMGDRALLNLGHTFGH 258
Cdd:cd08169 160 TLPFRQVRAGMAELVKMALIADNDFFEFLEDKANSATVYSPEQLEKlINKCISLKLDVVVADEDEQGKRRGLNYGHTFGH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 259 ALEAATGYdsaRLVHGEGVAIGMALAHRFSARLNLASPDDAGRVEAHLSAVGLPTrlsDVPGGLpGAEQLLTYIAQDKKV 338
Cdd:cd08169 240 ALELASGY---KIPHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWLLNKLGLPL---DHPLAL-DPDSLYEYLESDKKS 312
|
330
....*....|....
gi 1426272485 339 SRGALTFILTRGIG 352
Cdd:cd08169 313 LYGNLGMILLSGVG 326
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
19-365 |
2.16e-87 |
|
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: 267.91 E-value: 2.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 19 AYDILIGPGLLqsagEEIARRLPGVRAA---IVTDSNVAEGHLATLQAGLEAAGIEATAITVAPGERSKRFATLEEVVSG 95
Cdd:cd08197 1 LTDIYLGRGIL----ESLLSILEELKADrhfLVTDSNVNDLYGDRLLEGLKKAGIPVELLVVPAGESNKTLSTLTELAER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 96 ILDARLERGDIVIPLGGGVVGDLAGFAAGIVRRGMHFVQAPTSLLAQVDSSVGGKTGINTAHGKNLVGVFHQPQLVIADT 175
Cdd:cd08197 77 LIAAGITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 176 AVLDTLPPREFRAGYAEVAKYGLIDRPDFFAWLEKNWQAVFDGGPERVEAIAQSC-QAKADVVARDELEMGDRALLNLGH 254
Cdd:cd08197 157 EFLKTLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFLEKVIDLSiEAKLEVLSNDPYEKKEGLILEYGH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 255 TFGHALEAATGYdsaRLVHGEGVAIGMALAHRFSARLNLASPDDagrVEAH---LSAVGLPTRlsdVPGGLPgAEQLLTY 331
Cdd:cd08197 237 TVGHAIELLSGG---ELSHGEAVAIGMCVAAEISHLLGLLSEED---VDKHyelLEKIGLPTI---IPDGIS-VEAILEV 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 1426272485 332 IAQDKK-----VSRGALTFILTRGIGQSFVAKDVPTSQV 365
Cdd:cd08197 307 IRYDNKrgyikADADTIRMVLLEKLGKPANPDGDYLTPV 345
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
20-360 |
5.83e-69 |
|
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: 220.48 E-value: 5.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 20 YDILIGPGLLQSAGEEIAR--RLPGVRAAIVTDSNVAEGHLATLQAGLEAAGIEATAITVAPGERSKRFATLEEVVSGIL 97
Cdd:cd08199 2 YDVVLVDDLFDPENPTLADayGRPGRRRLVVVDENVDRLYGARIRAYFAAHGIEATILVLPGGEANKTMETVLRIVDALD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 98 DARLERGDIVIPLGGGVVGDLAGFAAGIVRRGMHFVQAPTSLLAQVDSSVGGKTGINTAHGKNLVGVFHQPQLVIADTAV 177
Cdd:cd08199 82 DFGLDRREPVIAIGGGVLLDVVGFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAYYPPVATLLDRSF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 178 LDTLPPREFRAGYAEVAKYGLIDRPDFFAWLEKNWQAV----FDGGPERVEAIAQSCQAKADVVARDELEMGDRALLNLG 253
Cdd:cd08199 162 LKTLPRRHIRNGLAEIIKMALVKDAELFELLEEHGAALvetrFFQDEVADEIIRRAIQGMLEELAPNLWEHDLERLVDFG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 254 HTFGHALEAATGYdsaRLVHGEGVAIGMALAHRFSARLNLASPDDAGRVEAHLSAVGLPTRLSdvpggLPGAEQLLTYIA 333
Cdd:cd08199 242 HTFSPILEMAAAP---ELLHGEAVAIDMALSAVLAYRRGLLSEEELDRILRLMRRLGLPVWHP-----LCTPDLLWRALE 313
|
330 340
....*....|....*....|....*..
gi 1426272485 334 QDKKVSRGALTFILTRGIGQSFVAKDV 360
Cdd:cd08199 314 DIVKHRDGLQRLPLPKGIGECVFVNDV 340
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
41-355 |
1.67e-55 |
|
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: 186.24 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 41 PGVRAAIVTDSNVAEGH--LAT-----LQAGLEAAGIEATAITVAPGERSKR-FATLEEVVSGILDARLERGDIVIPLGG 112
Cdd:cd08198 29 RRHRVLFVIDSGVAAAHpaLVKqieryFQAHPDRLELVAPPLIVPGGEAVKNdPALVEEILSAIHDHGLDRHSYVVVIGG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 113 GVVGDLAGFAAGIVRRGMHFVQAPTSLLAQVDSSVGGKTGINTAHGKNLVGVFHQPQLVIADTAVLDTLPPREFRAGYAE 192
Cdd:cd08198 109 GAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGINFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 193 VAKYGLIDRPDFFAWLEKNWQAVFDGGPERVE-AIAQSCQAKADVVAR--DELEMGDRALLNLGHTFGHALEAATGYDsa 269
Cdd:cd08198 189 AVKVALIKDASFFEWLERNAAALRQRDPDAMEkLIRRCAELHLDHIAAsgDPFETGSARPLDFGHWSAHKLEQLSGYA-- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 270 rLVHGEGVAIGMALAHRFSARLNLASPDDAGRVEAHLSAVGLPT-----RLSDVPGGLPGAEQLLTYIAqdkkvsrGALT 344
Cdd:cd08198 267 -LRHGEAVAIGIALDSLYARLLGLLSREDFDRILALLQNLGLPLwhpllERDGVLELLDGLEEFREHLG-------GRLT 338
|
330
....*....|.
gi 1426272485 345 FILTRGIGQSF 355
Cdd:cd08198 339 ITLLRGIGVGV 349
|
|
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
34-353 |
8.85e-53 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 179.71 E-value: 8.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 34 EEIARRLPG--VRAAIVTDSNVAEGH---LATLQAGLEAAG----IEATAITVAPGERSKR-FATLEEVVSGILDARLER 103
Cdd:PRK06203 32 EVLAADGEGkpKKVLVVIDSGVLRAHpdlLEQITAYFAAHAdvleLVAEPLVVPGGEAAKNdPALVEALHAAINRHGIDR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 104 GDIVIPLGGGVVGDLAGFAAGIVRRGMHFVQAPTSLLAQVDSSVGGKTGINTAHGKNLVGVFHQPQLVIADTAVLDTLPP 183
Cdd:PRK06203 112 HSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKNGINAFGKKNFLGTFAPPYAVINDFAFLTTLPD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 184 REFRAGYAEVAKYGLIDRPDFFAWLEKNWQAVFDGGPERVE-AIAQSCQAKADVVAR--DELEMGDRALLNLGHTFGHAL 260
Cdd:PRK06203 192 RDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAARDPEAMEeLIYRCAELHLEHIAGggDPFEFGSSRPLDFGHWSAHKL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 261 EAATGYdsaRLVHGEGVAIGMALAHRFSARLNLASPDDAGRVEAHLSAVGLPTRLSDVPGGLPGAEQLLTYIAQDKKVSR 340
Cdd:PRK06203 272 EQLTNY---ALRHGEAVAIGIALDSLYSYLLGLLSEAEAQRILALLRALGFPLYHPALATRDSKGRELLKGLEEFREHLG 348
|
330
....*....|...
gi 1426272485 341 GALTFILTRGIGQ 353
Cdd:PRK06203 349 GRLTITLLTGIGR 361
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
16-365 |
8.12e-50 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 175.43 E-value: 8.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 16 GARAYDILIGPGLLQSAGEEIARRlPGVRAAIVTDSnvAEGHLATLQAGLEAAGIEATAITVAPGERSKRFatleEVVSG 95
Cdd:PRK14021 185 GIEPYDVRIGEGAMNHLPQVLGPK-PVKVALIHTQP--VQRHSDRARTLLRQGGYEVSDIVIPDAEAGKTI----EVANG 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 96 IL----DARLERGDIVIPLGGGVVGDLAGFAAGIVRRGMHFVQAPTSLLAQVDSSVGGKTGINTAHGKNLVGVFHQPQLV 171
Cdd:PRK14021 258 IWqrlgNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMVDASTGGKTGINTPQGKNLVGSFYTPAGV 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 172 IADTAVLDTLPPREFRAGYAEVAKYGLIDRPDFFAWLEKNWQ-------AVFDGGPER---VEAIAQSCQAKADVVARDE 241
Cdd:PRK14021 338 LADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAelrafdgSTFLGSPLEdvvAELIERTVKVKAYHVSSDL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 242 LEMGDRALLNLGHTFGHALEAATGYdsaRLVHGEGVAIGMALAHRFSARLNLASPDDAGRVEAHLSAVGLPTRLSDvpgg 321
Cdd:PRK14021 418 KEAGLREFLNYGHTLGHAIEKLEHF---RWRHGNAVAVGMVYAAELAHLLGYIDQDLVDYHRSLLASLGLPTSWNG---- 490
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1426272485 322 lPGAEQLLTYIAQDKKVSRGALTFILTRGIGQSFVAKDVPTSQV 365
Cdd:PRK14021 491 -GSFDDVLALMHRDKKARGNELRFVVLDEIGHPVHLDNPPAEAV 533
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
80-342 |
1.19e-33 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 130.41 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 80 GERSKRFATLEEVVSGILDARLERGDIVIPLGGGVVGDLAGFAAGIVRRGMHFVQAPTSLLAQVDSSVGGKTGINTAHGK 159
Cdd:PRK13951 214 GEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQVDASVGGKNAIDFAGVK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 160 NLVGVFHQPQLVIADTAVLDTLPPREFRAGYAEVAKYGLIDRPDFFawLEKNWQAVFDGGPERV-EAIAQSCQAKADVVA 238
Cdd:PRK13951 294 NVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSGRGVE--LFDEPEKIEKRNLRVLsEMVKISVEEKARIVM 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 239 RDELEMGDRALLNLGHTFGHALEAATGydsarLVHGEGVAIGMALAHRFSARLNLASPDDAGRVEAHLSA-VGLPTRLSD 317
Cdd:PRK13951 372 EDPYDMGLRHALNLGHTLGHVYEMLEG-----VPHGIAVAWGIEKETMYLYRKGIVPKETMRWIVEKVKQiVPIPVPSVD 446
|
250 260
....*....|....*....|....*
gi 1426272485 318 VpgglpgaEQLLTYIAQDKKVSRGA 342
Cdd:PRK13951 447 V-------EKARNLILNDKKILKGS 464
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
20-318 |
2.66e-31 |
|
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: 119.78 E-value: 2.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 20 YDILIGPGLLQSAGEEiaRRLPGVRAAIVTDSNVAEGHLATLQAGLEAagIEATAITVAPGERskrfATLEEVVSGILDA 99
Cdd:cd07766 2 TRIVFGEGAIAKLGEI--KRRGFDRALVVSDEGVVKGVGEKVADSLKK--GLAVAIFDFVGEN----PTFEEVKNAVERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 100 RLERGDIVIPLGGGVVGDLAGFAAGIVRRGMHFVQAPTSLLAqvDSSVGGKTGINTAHGKNLVGVFH-QPQLVIADTAVL 178
Cdd:cd07766 74 RAAEADAVIAVGGGSTLDTAKAVAALLNRGIPFIIVPTTAST--DSEVSPKSVITDKGGKNKQVGPHyNPDVVFVDTDIT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 179 DTLPPREFRAGYAEVAKYGLidrpdffawleknwqavfdggpERVEAIAQSCQAKADVVArdelemgdRALLNLGHTFGH 258
Cdd:cd07766 152 KGLPPRQVASGGVDALAHAV----------------------ELEKVVEAATLAGMGLFE--------SPGLGLAHAIGH 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 259 ALEAATGYDsarlvHGEGVAIGMALAHRFSARLNLASPDDAGRVEAHLSAVGLPTRLSDV 318
Cdd:cd07766 202 ALTAFEGIP-----HGEAVAVGLPYVLKVANDMNPEPEAAIEAVFKFLEDLGLPTHLADL 256
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
24-278 |
4.08e-15 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 74.26 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 24 IGPGLLQSAGEEIaRRLPGVRAAIVTDSNVAEGHLATLQAGLEAAGIEATAITVAPGErskrfATLEEVVSGILDARLER 103
Cdd:pfam13685 2 IGPGALGRLGEYL-AELGFRRVALVADANTYAAAGRKVAESLKRAGIEVETRLEVAGN-----ADMETAEKLVGALRERD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 104 GDIVIPLGGGVVGDLAGFAAGivRRGMHFVQAPTSllAQVD---SSV------GGKTGINTAhgknlvgvfhQPQLVIAD 174
Cdd:pfam13685 76 ADAVVGVGGGTVIDLAKYAAF--KLGKPFISVPTA--ASNDgfaSPGasltvdGKKRSIPAA----------APFGVIAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 175 TAVLDTLPPREFRAGYAEvakyglidrpdffawLEKNWQAVFD---GGPERVEA-----IAQSCQAKADVVARD--ELEM 244
Cdd:pfam13685 142 TDVIAAAPRRLLASGVGD---------------LLAKITAVADwelAHAEEVAAplallSAAMVMNFADRPLRDpgDIEA 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1426272485 245 GDRALLNLG--------------HTFGHALEAATGydsARLVHGEGVA 278
Cdd:pfam13685 207 LAELLSALAmggagssrpasgseHLISHALDMIAP---KQALHGEQVG 251
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
22-317 |
2.09e-13 |
|
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: 70.58 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 22 ILIGPGLLQSAGEEIARRlpGVRAAIVTDSNVAEGHLATLQAGLEAAGIEATAITVaPGErskrfATLEEVVSGILDARL 101
Cdd:COG0371 9 YVQGEGALDELGEYLADL--GKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVF-GGE-----CSEEEIERLAEEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 102 ERGDIVIPLGGGVVGDLAGFAAgiVRRGMHFVQAPTSllAQVDS-----SVggktgINTAHGKNLVGVF--HQPQLVIAD 174
Cdd:COG0371 81 QGADVIIGVGGGKALDTAKAVA--YRLGLPVVSVPTI--ASTDApasplSV-----IYTEDGAFDGYSFlaKNPDLVLVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 175 TAVLDTLPPREFRAGYAE-VAKYglidrPDFFAWLEKNWQAVFDGGPERVEAIAQSC---------QAKADVVAR---DE 241
Cdd:COG0371 152 TDIIAKAPVRLLAAGIGDaLAKW-----YEARDWSLAHRDLAGEYYTEAAVALARLCaetlleygeAAIKAVEAGvvtPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 242 LE---------------MGD-RALLNLGHTFGHALEAATgyDSARLVHGEGVAIG----MALAHRfsarlnlasPDDAGR 301
Cdd:COG0371 227 LErvveanlllsglamgIGSsRPGSGAAHAIHNGLTALP--ETHHALHGEKVAFGtlvqLVLEGR---------PEEIEE 295
|
330
....*....|....*.
gi 1426272485 302 VEAHLSAVGLPTRLSD 317
Cdd:COG0371 296 LLDFLRSVGLPTTLAD 311
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
22-318 |
6.00e-13 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 69.17 E-value: 6.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 22 ILIGPGLLQSAGEEIARRlpGVRAAIVTDSNVAE-GHLATLQAGLEAAGIEATAITVAPGErskrfATLEEVVSGILDAR 100
Cdd:pfam00465 4 IVFGAGALAELGEELKRL--GARALIVTDPGSLKsGLLDKVLASLEEAGIEVVVFDGVEPE-----PTLEEVDEAAALAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 101 LERGDIVIPLGGGVVGDLAGFAA----------------GIVRRGMHFVQAPTslLAQVDSSVGGKTGINTAHGKNLVGV 164
Cdd:pfam00465 77 EAGADVIIAVGGGSVIDTAKAIAllltnpgdvwdylggkPLTKPALPLIAIPT--TAGTGSEVTPLAVITDTETGEKLGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 165 FH---QPQLVIADTAVLDTLPPRefragyaeVAKYGLIDRpdFFAWLE----KNWQAVFDGGPER-----VEAIAQSCQA 232
Cdd:pfam00465 155 FSpklLPDLAILDPELTLTLPPR--------LTAATGMDA--LAHAVEayvsKGANPLTDALALEairliAENLPRAVAD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 233 KADVVARDELEMG--------DRALLNLGHTFGHALEAATGydsarLVHGEGVAIGMALAHRFSAR------------LN 292
Cdd:pfam00465 225 GEDLEARENMLLAstlaglafSNAGLGAAHALAHALGGRYG-----IPHGLANAILLPYVLRFNAPaapeklaqlaraLG 299
|
330 340 350
....*....|....*....|....*....|.
gi 1426272485 293 LASPDDAG-----RVEAHLSAVGLPTRLSDV 318
Cdd:pfam00465 300 EDSDEEAAeeaieALRELLRELGLPTTLSEL 330
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
21-193 |
9.21e-12 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 65.69 E-value: 9.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 21 DILIGPGLLQSAGEEIARRLPGVRAAIVTDSNVAEGHLATLQAGLEAAGiEATAITVapgerskRFATLEEVVSGILDAR 100
Cdd:PRK00843 13 DVVVGHGVLDDIGDVCSDLKLTGRALIVTGPTTKKIAGDRVEENLEDAG-DVEVVIV-------DEATMEEVEKVEEKAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 101 LERGDIVIPLGGGVVGDLAGFAAgiVRRGMHFVQAPTSllAQVDSSVGGKTGINTAHGKNLVGVfHQPQLVIADTAVLDT 180
Cdd:PRK00843 85 DVNAGFLIGVGGGKVIDVAKLAA--YRLGIPFISVPTA--ASHDGIASPRASIKGGGKPVSVKA-KPPLAVIADTEIIAK 159
|
170
....*....|...
gi 1426272485 181 LPPREFRAGYAEV 193
Cdd:PRK00843 160 APYRLLAAGCGDI 172
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
21-317 |
9.14e-10 |
|
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: 59.45 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 21 DILIGPGLLQSAGEEIARRLPGVRAAIVTDSNVAEGHLATLQAGLEAAGIeaTAITVAPGERSKRFATLEEVVSGILDAR 100
Cdd:cd08175 3 EIVIGEGALKKLPEYLKELFGGKKVLVVADENTYAAAGEEVEAALEEAGV--TVCLLIFPGEGDLIADEAAVGKVLLELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 101 LErGDIVIPLGGGVVGDLAGFAAGivRRGMHFVQAPTSllAQVD---SSV------GGKTGINTahgknlvgvfHQPQLV 171
Cdd:cd08175 81 KD-TDLIIAVGSGTINDLTKYAAY--KLGIPYISVPTA--PSMDgytSSGapiivdGVKKTFPA----------HAPKAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 172 IADTAVLDTLPPREFRAGYAEV-AKY-GLIDrpdffawleknWQ--AVFDGGP--ERVEAIAQSCQAK-----ADVVARD 240
Cdd:cd08175 146 FADLDVLANAPQRMIAAGFGDLlGKYtALAD-----------WKlsHLLGGEYycPEVADLVQEALEKcldnaEGIAARD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 241 ELEMGD--RALLNLG----------------HTFGHALE-AATGYDSARLVHGEGVAIGMALAHRFSARLNLASPDDagr 301
Cdd:cd08175 215 PEAIEAlmEALILSGlamqlvgnsrpasgaeHHLSHYWEmEFLRLGKPPVLHGEKVGVGTLLIAALYILEQLPPPEE--- 291
|
330
....*....|....*.
gi 1426272485 302 VEAHLSAVGLPTRLSD 317
Cdd:cd08175 292 LRELLRKAGAPTTPED 307
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
25-317 |
1.04e-08 |
|
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: 56.27 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 25 GPGLLQSAGEEIARRlpGVRAAIVTDSNVAEGHLATLQAGLEAAGIEATAITVApGErskrfATLEEVVSGILDARLERG 104
Cdd:cd08170 7 GPGALDRLGEYLAPL--GKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFG-GE-----CSREEIERLAAIARANGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 105 DIVIPLGGGVVGDLAGFAAgiVRRGMHFV--------QAPTSLLaqvdsSVggktgINTAHGKnLVGVFHQPQ---LVIA 173
Cdd:cd08170 79 DVVIGIGGGKTIDTAKAVA--DYLGLPVVivptiastDAPCSAL-----SV-----IYTEDGE-FDEYLFLPRnpdLVLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 174 DTAVLDTLPPREFRAGYAE-VAKYglidrpdFFAwlEKNWQA----VFDGGPERV-EAIAQSC---------QAKADVVA 238
Cdd:cd08170 146 DTEIIAKAPVRFLVAGMGDaLATY-------FEA--RACARSgapnMAGGRPTLAaLALAELCydtlleygvAAKAAVEA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 239 R---DELEMGDRA--LLN-LG---------HTFGHALEAATGydSARLVHGEGVAIGMaLAHRFsarLNLASPDDAGRVE 303
Cdd:cd08170 217 GvvtPALEAVIEAntLLSgLGfesgglaaaHAIHNGLTALPE--THHLLHGEKVAFGT-LVQLV---LEGRPDEEIEEVI 290
|
330
....*....|....
gi 1426272485 304 AHLSAVGLPTRLSD 317
Cdd:cd08170 291 RFCRSVGLPVTLAD 304
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
22-318 |
3.79e-08 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 54.74 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 22 ILIGPGLLQSAGEEIARRlpGV-RAAIVTDSNVAE-GHLATLQAGLEAAGIEATAITVAPGErskrfATLEEVVSGILDA 99
Cdd:COG1454 11 IVFGAGALAELGEELKRL--GAkRALIVTDPGLAKlGLLDRVLDALEAAGIEVVVFDDVEPN-----PTVETVEAGAAAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 100 RLERGDIVIPLGGG-----------------VVGDLAGFAAgIVRRGMHFVQAPT-----------SLLaqVDSSVGGKT 151
Cdd:COG1454 84 REFGADVVIALGGGsaidaakaiallatnpgDLEDYLGIKK-VPGPPLPLIAIPTtagtgsevtpfAVI--TDPETGVKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 152 GINtahGKNLVgvfhqPQLVIADTAVLDTLPPREFRA-----------GYAEVAKYGLIDrpdffAWLEKNWQAVFdggp 220
Cdd:COG1454 161 GIA---DPELL-----PDVAILDPELTLTLPPSLTAAtgmdalthaieAYVSKGANPLTD-----ALALEAIRLIA---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 221 ervEAIAQSCQAKADVVARDELEMG--------DRALLNLGHTFGHALEAATGydsarLVHGEGVAIGMALAHRFSAR-- 290
Cdd:COG1454 224 ---RNLPRAVADGDDLEAREKMALAsllagmafANAGLGAVHALAHPLGGLFH-----VPHGLANAILLPHVLRFNAPaa 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1426272485 291 ------------LNLASPDDAG------RVEAHLSAVGLPTRLSDV 318
Cdd:COG1454 296 peryaeiaralgLDVGLSDEEAaealieAIRELLRDLGIPTRLSEL 341
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
22-196 |
6.54e-08 |
|
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: 53.71 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 22 ILIGPGLLQSAGEEIARRLPGVRAAIVTDSNVAEGHLATLQAGLEAAGIEATAITVAPGERSkrfATLEEVVSGILDarl 101
Cdd:cd08173 5 VVVGHGAINKIGEVLKKLLLGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIEEA---AEVEKVKKLIKE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 102 ERGDIVIPLGGGVVGDLAGFAAgiVRRGMHFVQAPTSL-----------LAQVDSSVGGKTgintahgknlvgvfHQPQL 170
Cdd:cd08173 79 SKADFIIGVGGGKVIDVAKYAA--YKLNLPFISIPTSAshdgiaspfasIKGGDKPYSIKA--------------KAPIA 142
|
170 180
....*....|....*....|....*..
gi 1426272485 171 VIADTAVLDTLPPREFRAGYAE-VAKY 196
Cdd:cd08173 143 IIADTEIISKAPKRLLAAGCGDlISNI 169
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
22-313 |
2.72e-07 |
|
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: 51.80 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 22 ILIGPGLLQSAGEeIARRLPGVRAAIVTDSNVAEGHLATLQAGLEaagieataitvapgerskrfaTLEEVVS--GILDA 99
Cdd:cd08549 4 TIVGDGAINKIEE-ILKKLNLKRVLIITGKNTKAKYCRFFYDQLK---------------------TVCDIVYydNIDNL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 100 RLERG-----DIVIPLGGGVVGDLAGFAAGIvrRGMHFVQAPTSllAQVD--SSVGGKTGINtahGKNLVGVFHQPQLVI 172
Cdd:cd08549 62 EDELKkytfyDCVIGIGGGRSIDTGKYLAYK--LKIPFISVPTS--ASNDgiASPIVSLRIP---GVKKTFMADAPIAII 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 173 ADTAVLDTLPPREFRAGYAE-VAKYGLIDRPDFFAWLEKnwQAVFDGGPERVEAIAQSCQAKADVVARDELEMGD--RAL 249
Cdd:cd08549 135 ADTEIIKKSPRRLLSAGIGDlVSNITAVLDWKLAHKEKG--EKYSEFAAILSKTSAKELVSYVLKASDLEEYHRVlvKAL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 250 LNLG----------------HTFGHALEA-ATGYDSARLVHGEGVAIG---MALAHRFSARLNLASPDdagRVEAHLSAV 309
Cdd:cd08549 213 VGSGiamaiagssrpasgseHLFSHALDKlKEEYLNINVLHGEQVGVGtiiMSYLHEKENKKLSGLHE---RIKMILKKV 289
|
....
gi 1426272485 310 GLPT 313
Cdd:cd08549 290 GAPT 293
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
22-184 |
3.72e-07 |
|
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: 51.68 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 22 ILIGPGLLQSAGEEIaRRLPGVRAAIVTDSNVAE-GHLATLQAGLEAAGIEATAITVAPGErskrfATLEEVVSGILDAR 100
Cdd:cd08551 4 IVFGAGALARLGEEL-KALGGKKVLLVTDPGLVKaGLLDKVLESLKAAGIEVEVFDDVEPN-----PTVETVEAAAELAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 101 LERGDIVIPLGGGVVGDLAGFAA----------------GIVRRGMHFVQAPT-----------SLLAqvDSSVGGKTGI 153
Cdd:cd08551 78 EEGADLVIAVGGGSVLDTAKAIAvlatnggsirdyegigKVPKPGLPLIAIPTtagtgsevtpnAVIT--DPETGRKMGI 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1426272485 154 NTAHgknlvgvfhqpqlVIADTAVLD-----TLPPR 184
Cdd:cd08551 156 VSPY-------------LLPDVAILDpeltlSLPPS 178
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
25-334 |
5.57e-07 |
|
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: 51.00 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 25 GPGLLQSAGEEIARRlpGVRAAIVTDSNVAEGHLATLQAGLEAAGIEaTAITVAPGERSkrFATLEEVVSgilDARLERG 104
Cdd:cd08550 7 EPGILAKAGEYIAPL--GKKALIIGGKTALEAVGEKLEKSLEEAGID-YEVEVFGGECT--EENIERLAE---KAKEEGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 105 DIVIPLGGGVVGDLAGFAAgiVRRGMHFVQAPTSllAQVDSSVGGKTGINTAHGKNLVGVFHQ--PQLVIADTAVLDTLP 182
Cdd:cd08550 79 DVIIGIGGGKVLDTAKAVA--DRLGLPVVTVPTI--AATCAAWSALSVLYDEEGEFLGYSLLKrsPDLVLVDTDIIAAAP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 183 PREFRAGYAE-VAKyglidrpdffaWLEknWQAVFDGGPERVEAIAQSCQAKadvVARDEL-EMGDRALLNLG-HTFGHA 259
Cdd:cd08550 155 VRYLAAGIGDtLAK-----------WYE--ARPSSRGGPDDLALQAAVQLAK---LAYDLLlEYGVQAVEDVRqGKVTPA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 260 LEAA-------TG------------------YDSARLV-------HGEGVAIGMALahrfSARLNLASPDDAGRVEAHLS 307
Cdd:cd08550 219 LEDVvdaiillAGlvgslggggcrtaaahaiHNGLTKLpethgtlHGEKVAFGLLV----QLALEGRSEEEIEELIEFLR 294
|
330 340
....*....|....*....|....*..
gi 1426272485 308 AVGLPTRLSDVpgGLPGAEQLLTYIAQ 334
Cdd:cd08550 295 RLGLPVTLEDL--GLELTEEELRKIAE 319
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
22-129 |
2.13e-06 |
|
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: 49.15 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 22 ILIGPGLLQSAGEeIARRLpGVRAAIVTDSNVAE-GHLATLQAGLEAAGIEATAIT-VAPGERSkrfATLEEVVSgilDA 99
Cdd:cd08191 7 LLFGPGARRALGR-VAARL-GSRVLIVTDPRLAStPLVAELLAALTAAGVAVEVFDgGQPELPV---STVADAAA---AA 78
|
90 100 110
....*....|....*....|....*....|
gi 1426272485 100 RLERGDIVIPLGGGVVGDLAGFAAGIVRRG 129
Cdd:cd08191 79 RAFDPDVVIGLGGGSNMDLAKVVALLLAHG 108
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
22-371 |
6.85e-06 |
|
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: 47.53 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 22 ILIGPGLLQSAGEeIARRLPGVRAAIVTDSNVAE-GHLATLQAGLEAAGIEATAITVAPGErskrfATLEEVVSGILDAR 100
Cdd:cd14863 8 VIFGAGAVEQIGE-LLKELGCKKVLLVTDKGLKKaGIVDKIIDLLEEAGIEVVVFDDVEPD-----PPDEIVDEAAEIAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 101 LERGDIVIPLGGGVVGDLA-----------------GFAAGIVRRGMHFVQAPTSllaqvdssvGGkTG---------IN 154
Cdd:cd14863 82 EEGADGVIGIGGGSVLDTAkaiavlltnpgpiidyaLAGPPVPKPGIPLIAIPTT---------AG-TGsevtpiaviTD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 155 TAHG--KNLVGVFhqpqlVIADTAVLD-----TLPPREFRA-----------GYAEVAKYGLIDrpdFFA---------W 207
Cdd:cd14863 152 EENGvkKSLLGPF-----LVPDLAILDpeltvGLPPSLTAAtgmdalshaieAYTSKLANPMTD---ALAlqairlivkN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 208 LEKnwqAVFDGGperveaiaqscqakaDVVARDELEMG--------DRALLNLGHTFGHALEAAtgydsARLVHGEGVAI 279
Cdd:cd14863 224 LPR---AVKDGD---------------NLEARENMLLAsnlagiafNNAGTHIGHAIAHALGAL-----YHIPHGLACAL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 280 GM----------------ALAHRFSARLNLASPDDAG-----RVEAHLSAVGLPTRLSDVPGGLPGAEQLLTYIAQDkkv 338
Cdd:cd14863 281 ALpvvlefnaeaypekvkKIAKALGVSFPGESDEELGeavadAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVLKD--- 357
|
410 420 430
....*....|....*....|....*....|...
gi 1426272485 339 srgaltfiltrgIGQSFVAKDVPTSQVLSFLEE 371
Cdd:cd14863 358 ------------PFAMFNPRPITEEEVAEILEA 378
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
24-189 |
2.66e-04 |
|
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: 42.51 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 24 IGPGLLQSAGEEIA-RRLPGVRAAIVTDSNVAEGHLATLQAGLEAAGIEATaitvapgersKRFATLEEVVSGILDARLE 102
Cdd:cd08174 6 IEEGALEHLGKYLAdRNQGFGKVAIVTGEGIDELLGEDILESLEEAGEIVT----------VEENTDNSAEELAEKAFSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 103 RG-DIVIPLGGGVVGDLAGFAAGIVRRGmhFVQAPTSL----LAqvdSSV------GGKTGINTAhgknlvgvfhQPQLV 171
Cdd:cd08174 76 PKvDAIVGIGGGKVLDVAKYAAFLSKLP--FISVPTSLsndgIA---SPVavlkvdGKRKSLGAK----------MPYGV 140
|
170
....*....|....*...
gi 1426272485 172 IADTAVLDTLPPREFRAG 189
Cdd:cd08174 141 IVDLDVIKSAPRRLILAG 158
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
25-189 |
7.17e-04 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 41.34 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 25 GPGLLQSAGEEIARRlpGVRAAIVTDSNVAEGHLATLQAGLEAAGIEATaITVAPGERSkrfatlEEVVSGILD-ARLER 103
Cdd:PRK09423 14 GKGALARLGEYLKPL--GKRALVIADEFVLGIVGDRVEASLKEAGLTVV-FEVFNGECS------DNEIDRLVAiAEENG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272485 104 GDIVIPLGGGVVGDLAGFAAGIVRRGMHFV------QAPTSLLaqvdsSVggktgINTAHGknlvgVF-------HQPQL 170
Cdd:PRK09423 85 CDVVIGIGGGKTLDTAKAVADYLGVPVVIVptiastDAPTSAL-----SV-----IYTEEG-----EFerylflpKNPDL 149
|
170
....*....|....*....
gi 1426272485 171 VIADTAVLDTLPPREFRAG 189
Cdd:PRK09423 150 VLVDTAIIAKAPARFLAAG 168
|
|
| |
