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Conserved domains on  [gi|1246355839|gb|ATE54687|]
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3-dehydroquinate synthase [Actinosynnema pretiosum]

Protein Classification

3-dehydroquinate synthase family protein( domain architecture ID 10785327)

3-dehydroquinate synthase family protein similar to 3-dehydroquinate synthase that catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate to dehydroquinate in the shikimate pathway

CATH:  1.20.1090.10|3.40.50.1970
EC:  4.2.3.-
Gene Ontology:  GO:0003856|GO:0046872|GO:0003856|GO:0000166
PubMed:  9685163
SCOP:  4002924|3001905

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 8-336 4.05e-126

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: 365.57  E-value: 4.05e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839   8 REVRVELGERAYTVHIGHGVRAALPDVVRAL-GARRAVVVT---------ARPPDQTPDPGVPSLVLPARDGEHDKTLAT 77
Cdd:COG0337     2 QTLTVNLGERSYDIRIGRGLLDELGELLAELlKGRRVLVVTdenvaplygERLRAALEAAGFEVHLLVLPDGEASKTLET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  78 VAHLCSRFAEFGLTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKTAVNLPEGKNLVGSYWQP 157
Cdd:COG0337    82 LERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 158 AAVLCDLDLLATLPERELRNGLGEIARCHFIGAPGL--------------DRLPLLDQVAASVALKARVVAADERDRGLR 223
Cdd:COG0337   162 RAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFfewleenadallarDPEALEEAIARSCEIKAEVVAADERESGLR 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 224 HTLNYGHTLGHALELATGFAVRHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLPVALpPGVPDDELLRFVRR 303
Cdd:COG0337   242 ALLNFGHTFGHAIEAATGYRLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRL-PALDPEALLAAMKR 320

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1246355839 304 DKKSTGG-LAFVLdgPRG---AELVRDVDEHVVAATL 336
Cdd:COG0337   321 DKKVRGGkLRFVL--LRGigkAVIVDDVDEELLRAAL 355
 
Name Accession Description Interval E-value
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 8-336 4.05e-126

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: 365.57  E-value: 4.05e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839   8 REVRVELGERAYTVHIGHGVRAALPDVVRAL-GARRAVVVT---------ARPPDQTPDPGVPSLVLPARDGEHDKTLAT 77
Cdd:COG0337     2 QTLTVNLGERSYDIRIGRGLLDELGELLAELlKGRRVLVVTdenvaplygERLRAALEAAGFEVHLLVLPDGEASKTLET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  78 VAHLCSRFAEFGLTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKTAVNLPEGKNLVGSYWQP 157
Cdd:COG0337    82 LERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 158 AAVLCDLDLLATLPERELRNGLGEIARCHFIGAPGL--------------DRLPLLDQVAASVALKARVVAADERDRGLR 223
Cdd:COG0337   162 RAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFfewleenadallarDPEALEEAIARSCEIKAEVVAADERESGLR 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 224 HTLNYGHTLGHALELATGFAVRHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLPVALpPGVPDDELLRFVRR 303
Cdd:COG0337   242 ALLNFGHTFGHAIEAATGYRLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRL-PALDPEALLAAMKR 320

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1246355839 304 DKKSTGG-LAFVLdgPRG---AELVRDVDEHVVAATL 336
Cdd:COG0337   321 DKKVRGGkLRFVL--LRGigkAVIVDDVDEELLRAAL 355
DHQS cd08195
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 19-336 4.27e-125

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: 362.53  E-value: 4.27e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  19 YTVHIGHGVRAALPDVVRALGARRAVVVT---------ARPPDQTPDPGVPSLVLPARDGEHDKTLATVAHLCSRFAEFG 89
Cdd:cd08195     2 YPILIGSGLLDKLGELLELKKGSKVVIVTdenvaklygELLLKSLEAAGFKVEVIVIPAGEKSKSLETVERIYDFLLEAG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  90 LTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKTAVNLPEGKNLVGSYWQPAAVLCDLDLLAT 169
Cdd:cd08195    82 LDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLKT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 170 LPERELRNGLGEIARCHFIGAPGL--------------DRLPLLDQVAASVALKARVVAADERDRGLRHTLNYGHTLGHA 235
Cdd:cd08195   162 LPEREFRSGLAEVIKYGLIADKELfefleknldkilarDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTFGHA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 236 LELATGFAVRHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLPVALPPgVPDDELLRFVRRDKKSTGG-LAFV 314
Cdd:cd08195   242 IESASGYKLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKD-LDPEELLEAMKRDKKNRGGkIRFV 320

                         330       340
                  ....*....|....*....|....*
gi 1246355839 315 LdgPRG---AELVRDVDEHVVAATL 336
Cdd:cd08195   321 L--LKGigkAVIVDDVSEEEIREAL 343
DHQ_synthase pfam01761
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ...
 61-307 3.90e-106

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: 310.97  E-value: 3.90e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  61 SLVLParDGEHDKTLATVAHLCSRFAEFGLTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKT 140
Cdd:pfam01761   1 TIVIP--DGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 141 AVNLPEGKNLVGSYWQPAAVLCDLDLLATLPERELRNGLGEIARCHFIGAPGLDRL--------------PLLDQVAASV 206
Cdd:pfam01761  79 GINHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWleenaeallnldpdALEEAIARSC 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 207 ALKARVVAADERDRGLRHTLNYGHTLGHALELATGF-AVRHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLP 285
Cdd:pfam01761 159 EVKADVVAQDEKESGLRALLNLGHTFGHAIEALSGYgALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLP 238

                         250       260
                  ....*....|....*....|..
gi 1246355839 286 VALPPGVPdDELLRFVRRDKKS 307
Cdd:pfam01761 239 TSLPDLDV-EQLLAAMARDKKV 259
aroB TIGR01357
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ...
 19-336 3.74e-91

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: 276.05  E-value: 3.74e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  19 YTVHIGHGVRAALpdVVRALGARRAVVVT---------ARPPDQTPDPGVPSLVLPARDGEHDKTLATVAHLCSRFAEFG 89
Cdd:TIGR01357   1 YPVHVGEGLLDQL--VEELAEPSKLVIITdetvadlygDKLLEALQALGYNVLKLTVPDGEESKSLETVQRLYDQLLEAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  90 LTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKTAVNLPEGKNLVGSYWQPAAVLCDLDLLAT 169
Cdd:TIGR01357  79 LDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 170 LPERELRNGLGEIARCHFI-GAPGLDRL--------------PLLDQVAASVALKARVVAADERDRGLRHTLNYGHTLGH 234
Cdd:TIGR01357 159 LPDRELRSGMAEVIKHGLIaDAELFDELesndklrlnlqeleHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTIGH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 235 ALELATGF-AVRHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLPVALPPGVPDDELLRFVRRDKKSTGG-LA 312
Cdd:TIGR01357 239 AIEAEAGYgKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGkIR 318

                         330       340
                  ....*....|....*....|....*
gi 1246355839 313 FVLDGPRG-AELVRDVDEHVVAATL 336
Cdd:TIGR01357 319 FVLLEEIGkAALAREVPDEMVLELL 343
PLN02834 PLN02834
3-dehydroquinate synthase
 2-339 1.09e-68

3-dehydroquinate synthase


Pssm-ID: 215448  Cd Length: 433  Bit Score: 221.18  E-value: 1.09e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839   2 PTTATTREVRVELGERAYTVHIGHGVRAALPDVVRALGARRAVVVTarppDQTPDP-----------------GVPSLVL 64
Cdd:PLN02834   62 ASATVTTVVKVDLGDRSYPIYIGSGLLDHGELLQRHVHGKRVLVVT----NETVAPlylekvvealtakgpelTVESVIL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  65 ParDGEHDKTLATVAHLCSRFAEFGLTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKTAVNL 144
Cdd:PLN02834  138 P--DGEKYKDMETLMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNH 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 145 PEGKNLVGSYWQPAAVLCDLDLLATLPERELRNGLGEIARCHFI------------GAPGLDRLP--LLDQVAASVALKA 210
Cdd:PLN02834  216 PLGKNMIGAFYQPQCVLIDTDTLATLPDRELASGIAEVVKYGLIrdaeffewqeanMEKLLARDPgaLAYAIKRSCENKA 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 211 RVVAADERDRGLRHTLNYGHTLGHALELATGFAV-RHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLPVALP 289
Cdd:PLN02834  296 EVVSLDEKESGLRATLNLGHTFGHAIETGPGYGEwLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPP 375

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1246355839 290 PGVPDDELLRFVRRDKKSTGGLA--FVLDGPRGAEL-VRDVDEHVVAATLAAM 339
Cdd:PLN02834  376 EKMTVEMFKSLMAVDKKVADGLLrlILLKGELGNCVfTGDFDREALEETLRAF 428
 
Name Accession Description Interval E-value
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 8-336 4.05e-126

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: 365.57  E-value: 4.05e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839   8 REVRVELGERAYTVHIGHGVRAALPDVVRAL-GARRAVVVT---------ARPPDQTPDPGVPSLVLPARDGEHDKTLAT 77
Cdd:COG0337     2 QTLTVNLGERSYDIRIGRGLLDELGELLAELlKGRRVLVVTdenvaplygERLRAALEAAGFEVHLLVLPDGEASKTLET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  78 VAHLCSRFAEFGLTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKTAVNLPEGKNLVGSYWQP 157
Cdd:COG0337    82 LERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 158 AAVLCDLDLLATLPERELRNGLGEIARCHFIGAPGL--------------DRLPLLDQVAASVALKARVVAADERDRGLR 223
Cdd:COG0337   162 RAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFfewleenadallarDPEALEEAIARSCEIKAEVVAADERESGLR 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 224 HTLNYGHTLGHALELATGFAVRHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLPVALpPGVPDDELLRFVRR 303
Cdd:COG0337   242 ALLNFGHTFGHAIEAATGYRLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRL-PALDPEALLAAMKR 320

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1246355839 304 DKKSTGG-LAFVLdgPRG---AELVRDVDEHVVAATL 336
Cdd:COG0337   321 DKKVRGGkLRFVL--LRGigkAVIVDDVDEELLRAAL 355
DHQS cd08195
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 19-336 4.27e-125

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: 362.53  E-value: 4.27e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  19 YTVHIGHGVRAALPDVVRALGARRAVVVT---------ARPPDQTPDPGVPSLVLPARDGEHDKTLATVAHLCSRFAEFG 89
Cdd:cd08195     2 YPILIGSGLLDKLGELLELKKGSKVVIVTdenvaklygELLLKSLEAAGFKVEVIVIPAGEKSKSLETVERIYDFLLEAG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  90 LTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKTAVNLPEGKNLVGSYWQPAAVLCDLDLLAT 169
Cdd:cd08195    82 LDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDFLKT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 170 LPERELRNGLGEIARCHFIGAPGL--------------DRLPLLDQVAASVALKARVVAADERDRGLRHTLNYGHTLGHA 235
Cdd:cd08195   162 LPEREFRSGLAEVIKYGLIADKELfefleknldkilarDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTFGHA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 236 LELATGFAVRHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLPVALPPgVPDDELLRFVRRDKKSTGG-LAFV 314
Cdd:cd08195   242 IESASGYKLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKD-LDPEELLEAMKRDKKNRGGkIRFV 320

                         330       340
                  ....*....|....*....|....*
gi 1246355839 315 LdgPRG---AELVRDVDEHVVAATL 336
Cdd:cd08195   321 L--LKGigkAVIVDDVSEEEIREAL 343
DHQ_synthase pfam01761
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ...
 61-307 3.90e-106

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: 310.97  E-value: 3.90e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  61 SLVLParDGEHDKTLATVAHLCSRFAEFGLTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKT 140
Cdd:pfam01761   1 TIVIP--DGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 141 AVNLPEGKNLVGSYWQPAAVLCDLDLLATLPERELRNGLGEIARCHFIGAPGLDRL--------------PLLDQVAASV 206
Cdd:pfam01761  79 GINHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWleenaeallnldpdALEEAIARSC 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 207 ALKARVVAADERDRGLRHTLNYGHTLGHALELATGF-AVRHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLP 285
Cdd:pfam01761 159 EVKADVVAQDEKESGLRALLNLGHTFGHAIEALSGYgALLHGEAVAIGMVLAARLSERLGLLDEADVERIRALLKKYGLP 238

                         250       260
                  ....*....|....*....|..
gi 1246355839 286 VALPPGVPdDELLRFVRRDKKS 307
Cdd:pfam01761 239 TSLPDLDV-EQLLAAMARDKKV 259
aroB TIGR01357
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ...
 19-336 3.74e-91

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: 276.05  E-value: 3.74e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  19 YTVHIGHGVRAALpdVVRALGARRAVVVT---------ARPPDQTPDPGVPSLVLPARDGEHDKTLATVAHLCSRFAEFG 89
Cdd:TIGR01357   1 YPVHVGEGLLDQL--VEELAEPSKLVIITdetvadlygDKLLEALQALGYNVLKLTVPDGEESKSLETVQRLYDQLLEAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  90 LTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKTAVNLPEGKNLVGSYWQPAAVLCDLDLLAT 169
Cdd:TIGR01357  79 LDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 170 LPERELRNGLGEIARCHFI-GAPGLDRL--------------PLLDQVAASVALKARVVAADERDRGLRHTLNYGHTLGH 234
Cdd:TIGR01357 159 LPDRELRSGMAEVIKHGLIaDAELFDELesndklrlnlqeleHLEELIKRSIEVKASIVAEDEKESGLRAILNFGHTIGH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 235 ALELATGF-AVRHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLPVALPPGVPDDELLRFVRRDKKSTGG-LA 312
Cdd:TIGR01357 239 AIEAEAGYgKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLPKDLDVDELLNAMLNDKKNSGGkIR 318

                         330       340
                  ....*....|....*....|....*
gi 1246355839 313 FVLDGPRG-AELVRDVDEHVVAATL 336
Cdd:TIGR01357 319 FVLLEEIGkAALAREVPDEMVLELL 343
DOIS cd08197
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ...
 59-319 1.15e-73

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: 231.70  E-value: 1.15e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  59 VPSLVLPArdGEHDKTLATVAHLCSRFAEFGLTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGG 138
Cdd:cd08197    53 VELLVVPA--GESNKTLSTLTELAERLIAAGITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 139 KTAVNLPEGKNLVGSYWQPAAVLCDLDLLATLPERELRNGLGEIARCHFIGAPG-LDRL-----PLLDQ--------VAA 204
Cdd:cd08197   131 KQAVNGKSGKNLVGSYYAPLFVFVDTEFLKTLPPRQIRSGLCEAIKNALIQDPEfLDYLedylnSDLDYdpeflekvIDL 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 205 SVALKARVVAAD--ERDRGLrhTLNYGHTLGHALELATGFAVRHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGY 282
Cdd:cd08197   211 SIEAKLEVLSNDpyEKKEGL--ILEYGHTVGHAIELLSGGELSHGEAVAIGMCVAAEISHLLGLLSEEDVDKHYELLEKI 288

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1246355839 283 GLPVALPPGVPDDELLRFVRRDKKsTGGLAFVLDGPR 319
Cdd:cd08197   289 GLPTIIPDGISVEAILEVIRYDNK-RGYIKADADTIR 324
PLN02834 PLN02834
3-dehydroquinate synthase
 2-339 1.09e-68

3-dehydroquinate synthase


Pssm-ID: 215448  Cd Length: 433  Bit Score: 221.18  E-value: 1.09e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839   2 PTTATTREVRVELGERAYTVHIGHGVRAALPDVVRALGARRAVVVTarppDQTPDP-----------------GVPSLVL 64
Cdd:PLN02834   62 ASATVTTVVKVDLGDRSYPIYIGSGLLDHGELLQRHVHGKRVLVVT----NETVAPlylekvvealtakgpelTVESVIL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  65 ParDGEHDKTLATVAHLCSRFAEFGLTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKTAVNL 144
Cdd:PLN02834  138 P--DGEKYKDMETLMKVFDKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNH 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 145 PEGKNLVGSYWQPAAVLCDLDLLATLPERELRNGLGEIARCHFI------------GAPGLDRLP--LLDQVAASVALKA 210
Cdd:PLN02834  216 PLGKNMIGAFYQPQCVLIDTDTLATLPDRELASGIAEVVKYGLIrdaeffewqeanMEKLLARDPgaLAYAIKRSCENKA 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 211 RVVAADERDRGLRHTLNYGHTLGHALELATGFAV-RHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLPVALP 289
Cdd:PLN02834  296 EVVSLDEKESGLRATLNLGHTFGHAIETGPGYGEwLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPP 375

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1246355839 290 PGVPDDELLRFVRRDKKSTGGLA--FVLDGPRGAEL-VRDVDEHVVAATLAAM 339
Cdd:PLN02834  376 EKMTVEMFKSLMAVDKKVADGLLrlILLKGELGNCVfTGDFDREALEETLRAF 428
DHQ-like cd08169
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ...
 59-311 4.44e-63

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: 203.41  E-value: 4.44e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  59 VPSLVLPArdGEHDKTLATVAHLCSRFAEFGLTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGG 138
Cdd:cd08169    52 VHVFIIQG--GEAYKTFQTVVEELERAAALHLNRHSAVVAVGGGATGDVVGFAAATYFRGIAFIRVPTTLLAQSDSSVGI 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 139 KTAVNLPEGKNLVGSYWQPAAVLCDLDLLATLPERELRNGLGEIARCHFIGAP-------------------GLDRLpll 199
Cdd:cd08169   130 KVGINTRGGKNLLGAFYPPRAVFADFSFLKTLPFRQVRAGMAELVKMALIADNdffefledkansatvyspeQLEKL--- 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 200 dqVAASVALKARVVAADERDRGLRHTLNYGHTLGHALELATGFAVRHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVV 279
Cdd:cd08169   207 --INKCISLKLDVVVADEDEQGKRRGLNYGHTFGHALELASGYKIPHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWLL 284

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1246355839 280 AGYGLPVALPPGVPDDELLRFVRRDKKSTGGL 311
Cdd:cd08169   285 NKLGLPLDHPLALDPDSLYEYLESDKKSLYGN 316
PRK14021 PRK14021
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
 19-317 8.56e-62

bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional


Pssm-ID: 184458 [Multi-domain]  Cd Length: 542  Bit Score: 206.25  E-value: 8.56e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  19 YTVHIGHGVRAALPDVVRALGARRAVVVT---------ARPPDQTPDPGVPSLVLParDGEHDKTLATVAHLCSRFAEFG 89
Cdd:PRK14021  189 YDVRIGEGAMNHLPQVLGPKPVKVALIHTqpvqrhsdrARTLLRQGGYEVSDIVIP--DAEAGKTIEVANGIWQRLGNEG 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  90 LTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKTAVNLPEGKNLVGSYWQPAAVLCDLDLLAT 169
Cdd:PRK14021  267 FTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMVDASTGGKTGINTPQGKNLVGSFYTPAGVLADTKTLAT 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 170 LPERELRNGLGEIARCHFIGAPGLDRL-------------------PLLDQVAA----SVALKARVVAADERDRGLRHTL 226
Cdd:PRK14021  347 LPNDIFIEGLGEVAKSGFIRDPEILRIledhaaelrafdgstflgsPLEDVVAElierTVKVKAYHVSSDLKEAGLREFL 426

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 227 NYGHTLGHALELATGFAVRHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLPVALPPGVPDDeLLRFVRRDKK 306
Cdd:PRK14021  427 NYGHTLGHAIEKLEHFRWRHGNAVAVGMVYAAELAHLLGYIDQDLVDYHRSLLASLGLPTSWNGGSFDD-VLALMHRDKK 505

                         330
                  ....*....|...
gi 1246355839 307 STGG-LAFV-LDG 317
Cdd:PRK14021  506 ARGNeLRFVvLDE 518
EEVS cd08199
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ...
 19-298 3.25e-59

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: 194.28  E-value: 3.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  19 YTVHIGHGV----RAALPDVVRALGARRAVVVtarppDQTPDP-------------GVPSLVLPARDGEHDKTLATVAHL 81
Cdd:cd08199     2 YDVVLVDDLfdpeNPTLADAYGRPGRRRLVVV-----DENVDRlygarirayfaahGIEATILVLPGGEANKTMETVLRI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  82 CSRFAEFGLTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKTAVNLPEGKNLVGSYWQPAAVL 161
Cdd:cd08199    77 VDALDDFGLDRREPVIAIGGGVLLDVVGFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAYYPPVATL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 162 CDLDLLATLPERELRNGLGEIAR--------------CHfiGAPGLDRLPLLDQVAASVALKARVVAADE-----RDRGL 222
Cdd:cd08199   157 LDRSFLKTLPRRHIRNGLAEIIKmalvkdaelfelleEH--GAALVETRFFQDEVADEIIRRAIQGMLEElapnlWEHDL 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246355839 223 RHTLNYGHTLGHALELATGFAVRHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLPVALPpgVPDDELL 298
Cdd:cd08199   235 ERLVDFGHTFSPILEMAAAPELLHGEAVAIDMALSAVLAYRRGLLSEEELDRILRLMRRLGLPVWHP--LCTPDLL 308
DHQS-like cd08198
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 26-286 2.01e-34

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: 129.23  E-value: 2.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  26 GVRAALPDVVRALGARravvvTARPPDQTPDPGvPSLVLPArdGEHDK-TLATVAHLCSRFAEFGLTRADVVVSCGGGTT 104
Cdd:cd08198    40 GVAAAHPALVKQIERY-----FQAHPDRLELVA-PPLIVPG--GEAVKnDPALVEEILSAIHDHGLDRHSYVVVIGGGAV 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 105 TDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKTAVNLPEGKNLVGSYWQPAAVLCDLDLLATLPERELRNGLGEIAR 184
Cdd:cd08198   112 LDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGINFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVK 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 185 CHFIGapglDRLPLLDQVAASVALKARVVAADER------DRGLRHT--------------LNYGHTLGHALELATGFAV 244
Cdd:cd08198   192 VALIK----DASFFEWLERNAAALRQRDPDAMEKlirrcaELHLDHIaasgdpfetgsarpLDFGHWSAHKLEQLSGYAL 267

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1246355839 245 RHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLPV 286
Cdd:cd08198   268 RHGEAVAIGIALDSLYARLLGLLSREDFDRILALLQNLGLPL 309
PRK13951 PRK13951
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
62-253 1.10e-33

bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;


Pssm-ID: 172457 [Multi-domain]  Cd Length: 488  Bit Score: 129.64  E-value: 1.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  62 LVLParDGEHDKTLATVAHLCSRFAEFGLTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKTA 141
Cdd:PRK13951  209 LLFP--DGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQVDASVGGKNA 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 142 VNLPEGKNLVGSYWQPAAVLCDLDLLATLPERELRNGLGEIARCHFIGAPGLDRLPLLDQ------------VAASVALK 209
Cdd:PRK13951  287 IDFAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSGRGVELFDEPEKiekrnlrvlsemVKISVEEK 366

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1246355839 210 ARVVAADERDRGLRHTLNYGHTLGHALELATGfaVRHGEGVAIG 253
Cdd:PRK13951  367 ARIVMEDPYDMGLRHALNLGHTLGHVYEMLEG--VPHGIAVAWG 408
aroB PRK06203
3-dehydroquinate synthase; Reviewed
 60-253 7.84e-31

3-dehydroquinate synthase; Reviewed


Pssm-ID: 235740  Cd Length: 389  Bit Score: 120.00  E-value: 7.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  60 PSLVLPArdGEHDKT-LATVAHLCSRFAEFGLTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGG 138
Cdd:PRK06203   80 EPLVVPG--GEAAKNdPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGV 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 139 KTAVNLPEGKNLVGSYWQPAAVLCDLDLLATLPERELRNGLGEIARCHFI-----------GAPGL---DRLPLLDQVAA 204
Cdd:PRK06203  158 KNGINAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIkdaaffdwleaHAAALaarDPEAMEELIYR 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1246355839 205 SVALKARVVAA--DERDRGLRHTLNYGHTLGHALELATGFAVRHGEGVAIG 253
Cdd:PRK06203  238 CAELHLEHIAGggDPFEFGSSRPLDFGHWSAHKLEQLTNYALRHGEAVAIG 288
DHQ_Fe-ADH cd07766
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ...
 91-296 2.34e-22

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: 94.74  E-value: 2.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  91 TRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAqvDASVGGKTAVNLPEGKNL-VGSYWQPAAVLCDLDLLAT 169
Cdd:cd07766    76 AEADAVIAVGGGSTLDTAKAVAALLNRGIPFIIVPTTAST--DSEVSPKSVITDKGGKNKqVGPHYNPDVVFVDTDITKG 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 170 LPERELRNGLGeiarchfigapgldrlpllDQVAASVALKARVVAADERDRGL--RHTLNYGHTLGHALELATGfaVRHG 247
Cdd:cd07766   154 LPPRQVASGGV-------------------DALAHAVELEKVVEAATLAGMGLfeSPGLGLAHAIGHALTAFEG--IPHG 212

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1246355839 248 EGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLPVALPPGVPDDE 296
Cdd:cd07766   213 EAVAVGLPYVLKVANDMNPEPEAAIEAVFKFLEDLGLPTHLADLGVSKE 261
Fe-ADH_2 pfam13685
Iron-containing alcohol dehydrogenase;
23-251 6.83e-09

Iron-containing alcohol dehydrogenase;


Pssm-ID: 404557 [Multi-domain]  Cd Length: 251  Bit Score: 55.77  E-value: 6.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  23 IGHGVRAALPDVVRALGARRAVVVTarppdqtpDPGVPSLVLPA---------------RDGEHDKTLATVAHLCSRFAE 87
Cdd:pfam13685   2 IGPGALGRLGEYLAELGFRRVALVA--------DANTYAAAGRKvaeslkragievetrLEVAGNADMETAEKLVGALRE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  88 fglTRADVVVSCGGGTTTDAVGLAAslYHRGTPVVHVPTSllaqvdASVGGKTAVNLP---EGKNLVGSYWQPAAVLCDL 164
Cdd:pfam13685  74 ---RDADAVVGVGGGTVIDLAKYAA--FKLGKPFISVPTA------ASNDGFASPGASltvDGKKRSIPAAAPFGVIADT 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 165 DLLATLPERELRNGLGEIA------RCHFIGAPGLDRLPLLDQVAASVALKARVVAADERDRGLRHTLNYG--------- 229
Cdd:pfam13685 143 DVIAAAPRRLLASGVGDLLakitavADWELAHAEEVAAPLALLSAAMVMNFADRPLRDPGDIEALAELLSAlamggagss 222

                         250       260
                  ....*....|....*....|....*....
gi 1246355839 230 -------HTLGHALELATGFAVRHGEGVA 251
Cdd:pfam13685 223 rpasgseHLISHALDMIAPKQALHGEQVG 251
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 21-211 5.10e-07

Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440140 [Multi-domain]  Cd Length: 355  Bit Score: 50.94  E-value: 5.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  21 VHIGHGVRAALPDVVRALGaRRAVVVT-------ARP--PDQTPDPGVPSLVLPArdgEHDKTLATVAHLCSRFAEFGlt 91
Cdd:COG0371     9 YVQGEGALDELGEYLADLG-KRALIITgptalkaAGDrlEESLEDAGIEVEVEVF---GGECSEEEIERLAEEAKEQG-- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  92 rADVVVSCGGGTTTDAVGLAAslYHRGTPVVHVPTSllAQVDASVGGKTAVNLPEGKNLVGSYW--QPAAVLCDLDLLAT 169
Cdd:COG0371    83 -ADVIIGVGGGKALDTAKAVA--YRLGLPVVSVPTI--ASTDAPASPLSVIYTEDGAFDGYSFLakNPDLVLVDTDIIAK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1246355839 170 LPERELRNGLG-------EIARChfIGAPGLDRLPLLDQVAASVALKAR 211
Cdd:COG0371   158 APVRLLAAGIGdalakwyEARDW--SLAHRDLAGEYYTEAAVALARLCA 204
EutG COG1454
Alcohol dehydrogenase, class IV [Energy production and conversion];
20-126 2.41e-06

Alcohol dehydrogenase, class IV [Energy production and conversion];


Pssm-ID: 441063 [Multi-domain]  Cd Length: 381  Bit Score: 48.58  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  20 TVHIGHGVRAALPDVVRALGARRAVVVTarppdqtpDPGVPSL--------VLPARDGEH--------DKTLATVAHLCS 83
Cdd:COG1454    10 RIVFGAGALAELGEELKRLGAKRALIVT--------DPGLAKLglldrvldALEAAGIEVvvfddvepNPTVETVEAGAA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246355839  84 RFAEFGltrADVVVSCGGGTTTD---AVGLAAS-------------LYHRGTPVVHVPT 126
Cdd:COG1454    82 AAREFG---ADVVIALGGGSAIDaakAIALLATnpgdledylgikkVPGPPLPLIAIPT 137
egsA PRK00843
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
 21-182 4.39e-05

NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed


Pssm-ID: 179139  Cd Length: 350  Bit Score: 44.88  E-value: 4.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  21 VHIGHGVRAALPDVVRALG-ARRAVVVTARPP---------DQTPDPGVPSLVLpARDGehdkTLATVAHlCSRFAEfgL 90
Cdd:PRK00843   14 VVVGHGVLDDIGDVCSDLKlTGRALIVTGPTTkkiagdrveENLEDAGDVEVVI-VDEA----TMEEVEK-VEEKAK--D 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  91 TRADVVVSCGGGTTTDAVGLAAslYHRGTPVVHVPTSllAQVDASVGGKTAVNLPEGKNLVGSYwQPAAVLCDLDLLATL 170
Cdd:PRK00843   86 VNAGFLIGVGGGKVIDVAKLAA--YRLGIPFISVPTA--ASHDGIASPRASIKGGGKPVSVKAK-PPLAVIADTEIIAKA 160

                         170
                  ....*....|..
gi 1246355839 171 PERELRNGLGEI 182
Cdd:PRK00843  161 PYRLLAAGCGDI 172
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 6-104 1.20e-04

3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 42.86  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839   6 TTREVRVELGEraYTVHIGHGVRAALPDVVRALGARRAVVVTARPPDQ---TPDPGVP-------SLVLPARDG-EHDKT 74
Cdd:COG2897   119 ETGPPTPAPGD--FTARPDPELLADADEVLAALGDPDAVLVDARSPERyrgEVEPIDPraghipgAVNLPWTDLlDEDGT 196

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1246355839  75 LATVAHLCSRFAEFGLTRAD-VVVSCGGGTT 104
Cdd:COG2897   197 FKSAEELRALFAALGIDPDKpVITYCGSGVR 227
Fe-ADH-like cd08183
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 21-126 2.73e-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 domains. Proteins of this family have not been characterized.


Pssm-ID: 341462 [Multi-domain]  Cd Length: 377  Bit Score: 42.49  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  21 VHIGHGVRAALPDVVRALGaRRAVVVTARPPDQTP----------DPGVPSLVLPardGEHDKTLATVAHLCSRFAEFGl 90
Cdd:cd08183     4 IVFGRGSLQELGELAAELG-KRALLVTGRSSLRSGrlarllealeAAGIEVALFS---VSGEPTVETVDAAVALAREAG- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1246355839  91 trADVVVSCGGGTTTDA--------------------VGLAASLYHRGTPVVHVPT 126
Cdd:cd08183    79 --CDVVIAIGGGSVIDAakaiaalltnegsvldylevVGKGRPLTEPPLPFIAIPT 132
GlyDH-like cd08550
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ...
 24-180 2.96e-04

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: 42.14  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  24 GHGVRAALPDVVRALGaRRAVVVT-ARPPDQTPDPGVPSLvlpARDGEH--------DKTLATVAHLCSRFAEFGltrAD 94
Cdd:cd08550     7 EPGILAKAGEYIAPLG-KKALIIGgKTALEAVGEKLEKSL---EEAGIDyevevfggECTEENIERLAEKAKEEG---AD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  95 VVVSCGGGTTTDAVGLAAslYHRGTPVVHVPTSllAQVDASVggkTAVNL---PEGkNLVGSYWQ---PAAVLCDLDLLA 168
Cdd:cd08550    80 VIIGIGGGKVLDTAKAVA--DRLGLPVVTVPTI--AATCAAW---SALSVlydEEG-EFLGYSLLkrsPDLVLVDTDIIA 151

                         170
                  ....*....|..
gi 1246355839 169 TLPERELRNGLG 180
Cdd:cd08550   152 AAPVRYLAAGIG 163
G1PDH_related cd08549
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ...
 94-182 3.23e-04

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: 42.17  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  94 DVVVSCGGGTTTDAVGLAAslYHRGTPVVHVPTSllaqvdASVGGKTAVNLPEGKNLVGSYWQ---PAAVLCDLDLLATL 170
Cdd:cd08549    72 DCVIGIGGGRSIDTGKYLA--YKLKIPFISVPTS------ASNDGIASPIVSLRIPGVKKTFMadaPIAIIADTEIIKKS 143

                          90
                  ....*....|..
gi 1246355839 171 PERELRNGLGEI 182
Cdd:cd08549   144 PRRLLSAGIGDL 155
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 29-115 5.72e-04

Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the second repeat. Only the second repeat contains the catalytically active Cys residue.


Pssm-ID: 238726 [Multi-domain]  Cd Length: 118  Bit Score: 39.15  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  29 AALPDVVRALGARRAVVVTARPPDQ------TPDPGVP------SLVLPARDG-EHDKTLATVAHLCSRFAEFGLTRAD- 94
Cdd:cd01449     1 VTAEEVLANLDSGDVQLVDARSPERfrgevpEPRPGLRsghipgAVNIPWTSLlDEDGTFKSPEELRALFAALGITPDKp 80

                          90       100
                  ....*....|....*....|.
gi 1246355839  95 VVVSCGGGTTTDAVGLAASLY 115
Cdd:cd01449    81 VIVYCGSGVTACVLLLALELL 101
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
20-252 9.91e-04

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 40.66  E-value: 9.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  20 TVHIGHGVRAALPDVVRALGARrAVVVTarppdqtpDPGVPSLVLPAR----------------DGEHDKTLATVAHLCS 83
Cdd:pfam00465   3 RIVFGAGALAELGEELKRLGAR-ALIVT--------DPGSLKSGLLDKvlasleeagievvvfdGVEPEPTLEEVDEAAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  84 RFAEFGltrADVVVSCGGGTTTDAVGLAASLYHRGT----------------PVVHVPTslLAQVDASVGGKTAVNLPEG 147
Cdd:pfam00465  74 LAREAG---ADVIIAVGGGSVIDTAKAIALLLTNPGdvwdylggkpltkpalPLIAIPT--TAGTGSEVTPLAVITDTET 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839 148 KN---LVGSYWQPAAVLCDLDLLATLPERELRNGLGEiARCHFIGA-PGLDRLPLLDQVAAS----VALKARVVAADERD 219
Cdd:pfam00465 149 GEklgIFSPKLLPDLAILDPELTLTLPPRLTAATGMD-ALAHAVEAyVSKGANPLTDALALEairlIAENLPRAVADGED 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1246355839 220 RGLRHTLNYGHTLG------------HALE--LATGFAVRHGEGVAI 252
Cdd:pfam00465 228 LEARENMLLASTLAglafsnaglgaaHALAhaLGGRYGIPHGLANAI 274
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 2-342 1.09e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 41.01  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839    2 PTTATTREVRVELGERAYTVHIGHGVRAALPDVVRALGARRAVVVTARPPDQTPDPGVPSLVLPARDGEHDKTLATVAHL 81
Cdd:COG3321    864 PTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALL 943

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839   82 CSRFAEFGLTRADVVVSCGGGTTTDAVGLAASLYHRGTPVVHVPTSLLAQVDASVGGKTAVnLPEGKNLVGSYWQPAAVL 161
Cdd:COG3321    944 ALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALAL-LAAAALLLAAAAAAAALL 1022

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  162 CDLDLLATLPERELRNGLGEIARCHFIGAPGLDRLPLLDQVAASVALKARVVAADERDRGLRHTLNYGHTLGHALELATG 241
Cdd:COG3321   1023 ALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAAL 1102

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  242 FAVRHGEGVAIGTVFAGRLAGALGRIGPDRVAEHHAVVAGYGLPVALPPGVPDDELLRFVRRDKKSTGGLAFVLDGPRGA 321
Cdd:COG3321   1103 AAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALA 1182

                          330       340
                   ....*....|....*....|.
gi 1246355839  322 ELVRDVDEHVVAATLAAMPRA 342
Cdd:COG3321   1183 AALAAALAGLAALLLAALLAA 1203
Fe-ADH-like cd08191
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 20-120 4.63e-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 domain. Proteins of this family have not been characterized.


Pssm-ID: 341470 [Multi-domain]  Cd Length: 392  Bit Score: 38.36  E-value: 4.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  20 TVHIGHGVRAALPDVVRALGARRAVVVTARPPDQtpdPGVPSLVLPAR----------DGEHDKTLATVAHLCSRFAEFg 89
Cdd:cd08191     6 RLLFGPGARRALGRVAARLGSRVLIVTDPRLAST---PLVAELLAALTaagvavevfdGGQPELPVSTVADAAAAARAF- 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1246355839  90 ltRADVVVSCGGGTTTD-AVGLAASLYHRGTP 120
Cdd:cd08191    82 --DPDVVIGLGGGSNMDlAKVVALLLAHGGDP 111
MAR cd08177
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ...
 18-126 6.04e-03

Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer and is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.


Pssm-ID: 341456 [Multi-domain]  Cd Length: 337  Bit Score: 38.25  E-value: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  18 AYTVHIGHGVRAALPDVVRALGARRAVVVTArpPDQTPDPGVPSLVLPARD-GEHDK-------TLATVAHlcsrfAEFG 89
Cdd:cd08177     1 PQRVVFGAGTLAELAEELERLGARRALVLST--PRQRALAERVAALLGDRVaGVFDGavmhvpvEVAERAL-----AAAR 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1246355839  90 LTRADVVVSCGGGTTTdavGLAASL-YHRGTPVVHVPT 126
Cdd:cd08177    74 EAGADGLVAIGGGSAI---GLAKAIaLRTGLPIVAVPT 108
Fe-ADH-like cd14863
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 21-126 6.67e-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: 37.90  E-value: 6.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246355839  21 VHIGHGVRAALPDVVRALGARRAVVVTarppdqtpDPGVPSLVLPAR----------------DGEHDKTLATVAHLCSR 84
Cdd:cd14863     8 VIFGAGAVEQIGELLKELGCKKVLLVT--------DKGLKKAGIVDKiidlleeagievvvfdDVEPDPPDEIVDEAAEI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246355839  85 FAEFGltrADVVVSCGGGTTTDAV-----------------GLAASLYHRGTPVVHVPT 126
Cdd:cd14863    80 AREEG---ADGVIGIGGGSVLDTAkaiavlltnpgpiidyaLAGPPVPKPGIPLIAIPT 135
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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