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Conserved domains on  [gi|1733419119|gb|QEK97894|]
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sn-glycerol-1-phosphate dehydrogenase [Bacillus amyloliquefaciens]

Protein Classification

sn-glycerol-1-phosphate dehydrogenase( domain architecture ID 10169355)

sn-glycerol-1-phosphate dehydrogenase catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P)

CATH:  3.40.50.1970
EC:  1.1.1.261
Gene Ontology:  GO:0046872|GO:0030554
PubMed:  9685163|35751426
SCOP:  3001905

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
G1PDH cd08175
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ...
 24-383 1.70e-152

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: 433.86  E-value: 1.70e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  24 IEDIVIGANAKEELLRFLQKKC-WNHPVIVCDRNTYEAAGRLLADELRAGGIKASKVIIPEHeaGAAAADERTLVYTLIN 102
Cdd:cd08175     1 IKEIVIGEGALKKLPEYLKELFgGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGE--GDLIADEAAVGKVLLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 103 LAEETDVIIAAGSGTIHDITRFAAYQRGLPFISFPTAPSVDGFTSAGAPLILNGIKTTIQTKAPIALFADTNVLKEAPRS 182
Cdd:cd08175    79 LEKDTDLIIAVGSGTINDLTKYAAYKLGIPYISVPTAPSMDGYTSSGAPIIVDGVKKTFPAHAPKAIFADLDVLANAPQR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 183 MTAAGFGDMLGKITSLADWEISRRLAGEPYSEAGAKLVKDALWQCIDHRAAIAMGTEAGIQILMEALIVSGLVMLALDHS 262
Cdd:cd08175   159 MIAAGFGDLLGKYTALADWKLSHLLGGEYYCPEVADLVQEALEKCLDNAEGIAARDPEAIEALMEALILSGLAMQLVGNS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 263 RPASGGEHHISHWIEMEMLKAKQPPILHGAKVGCACAVLSDIYkelacheklaelpphfreaiqsAYEGLPDGKTIAGWL 342
Cdd:cd08175   239 RPASGAEHHLSHYWEMEFLRLGKPPVLHGEKVGVGTLLIAALY----------------------ILEQLPPPEELRELL 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1733419119 343 ASAGGPACFDEIGVKQDLVSDALKHAHTLRDRYTGLTIINE 383
Cdd:cd08175   297 RKAGAPTTPEDLGIDRDLLRDSLRLAKEIRDRYTVLDLAWD 337
 
Name Accession Description Interval E-value
G1PDH cd08175
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ...
 24-383 1.70e-152

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: 433.86  E-value: 1.70e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  24 IEDIVIGANAKEELLRFLQKKC-WNHPVIVCDRNTYEAAGRLLADELRAGGIKASKVIIPEHeaGAAAADERTLVYTLIN 102
Cdd:cd08175     1 IKEIVIGEGALKKLPEYLKELFgGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGE--GDLIADEAAVGKVLLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 103 LAEETDVIIAAGSGTIHDITRFAAYQRGLPFISFPTAPSVDGFTSAGAPLILNGIKTTIQTKAPIALFADTNVLKEAPRS 182
Cdd:cd08175    79 LEKDTDLIIAVGSGTINDLTKYAAYKLGIPYISVPTAPSMDGYTSSGAPIIVDGVKKTFPAHAPKAIFADLDVLANAPQR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 183 MTAAGFGDMLGKITSLADWEISRRLAGEPYSEAGAKLVKDALWQCIDHRAAIAMGTEAGIQILMEALIVSGLVMLALDHS 262
Cdd:cd08175   159 MIAAGFGDLLGKYTALADWKLSHLLGGEYYCPEVADLVQEALEKCLDNAEGIAARDPEAIEALMEALILSGLAMQLVGNS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 263 RPASGGEHHISHWIEMEMLKAKQPPILHGAKVGCACAVLSDIYkelacheklaelpphfreaiqsAYEGLPDGKTIAGWL 342
Cdd:cd08175   239 RPASGAEHHLSHYWEMEFLRLGKPPVLHGEKVGVGTLLIAALY----------------------ILEQLPPPEELRELL 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1733419119 343 ASAGGPACFDEIGVKQDLVSDALKHAHTLRDRYTGLTIINE 383
Cdd:cd08175   297 RKAGAPTTPEDLGIDRDLLRDSLRLAKEIRDRYTVLDLAWD 337
Fe-ADH_2 pfam13685
Iron-containing alcohol dehydrogenase;
28-295 1.52e-75

Iron-containing alcohol dehydrogenase;


Pssm-ID: 404557 [Multi-domain]  Cd Length: 251  Bit Score: 234.89  E-value: 1.52e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  28 VIGANAKEELLRFLQKKCWNHPVIVCDRNTYEAAGRLLADELRAGGIKASKViipehEAGAAAADERTLVYTLINLAE-E 106
Cdd:pfam13685   1 VIGPGALGRLGEYLAELGFRRVALVADANTYAAAGRKVAESLKRAGIEVETR-----LEVAGNADMETAEKLVGALRErD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 107 TDVIIAAGSGTIHDITRFAAYQRGLPFISFPTAPSVDGFTSAGAPLILNGIKTTIQTKAPIALFADTNVLKEAPRSMTAA 186
Cdd:pfam13685  76 ADAVVGVGGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASLTVDGKKRSIPAAAPFGVIADTDVIAAAPRRLLAS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 187 GFGDMLGKITSLADWEISRRLA-GEPYSEAGAKLVKDALwqcidHRAAIAMGTEAGIQILMEALIVSGLVMlaldhSRPA 265
Cdd:pfam13685 156 GVGDLLAKITAVADWELAHAEEvAAPLALLSAAMVMNFA-----DRPLRDPGDIEALAELLSALAMGGAGS-----SRPA 225

                         250       260       270
                  ....*....|....*....|....*....|
gi 1733419119 266 SGGEHHISHWIEMEMLKakqpPILHGAKVG 295
Cdd:pfam13685 226 SGSEHLISHALDMIAPK----QALHGEQVG 251
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 27-376 2.91e-62

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: 203.86  E-value: 2.91e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  27 IVIGANAKEELLRFLQKKCwNHPVIVCDRNTYEAAGRLLADELRAGGIKASKVIIpEHEAGAAAADErtlvytLINLAEE 106
Cdd:COG0371     9 YVQGEGALDELGEYLADLG-KRALIITGPTALKAAGDRLEESLEDAGIEVEVEVF-GGECSEEEIER------LAEEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 107 --TDVIIAAGSGTIHDITRFAAYQRGLPFISFPTAPSVDGFTSAGAPLILNG---IKTTIQTKAPIALFADTNVLKEAPR 181
Cdd:COG0371    81 qgADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDgafDGYSFLAKNPDLVLVDTDIIAKAPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 182 SMTAAGFGDMLGKITSLADWEISRR-LAGEPYSEAGAKLVKDALWQCIDH-RAAIA-----MGTEAGIQILMEALIVSGL 254
Cdd:COG0371   161 RLLAAGIGDALAKWYEARDWSLAHRdLAGEYYTEAAVALARLCAETLLEYgEAAIKaveagVVTPALERVVEANLLLSGL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 255 VMlALDHSRPASGGEHHISHwiEMEMLKAKQpPILHGAKVGCACAVlsdiykelacheklaelpphfreaiQSAYEGLPD 334
Cdd:COG0371   241 AM-GIGSSRPGSGAAHAIHN--GLTALPETH-HALHGEKVAFGTLV-------------------------QLVLEGRPE 291

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1733419119 335 G-KTIAGWLASAGGPACFDEIGVKQDLVSDALKHAHTLR-DRYT 376
Cdd:COG0371   292 EiEELLDFLRSVGLPTTLADLGLDDETEEELLTVAEAARpERYT 335
egsA PRK00843
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
 26-386 6.55e-62

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


Pssm-ID: 179139  Cd Length: 350  Bit Score: 202.82  E-value: 6.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  26 DIVIGANAKEELLRFLQK-KCWNHPVIVCDRNTYEAAGRLLADELRAGGiKASKVIIPEheagaAAADErtlVYTLINLA 104
Cdd:PRK00843   13 DVVVGHGVLDDIGDVCSDlKLTGRALIVTGPTTKKIAGDRVEENLEDAG-DVEVVIVDE-----ATMEE---VEKVEEKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 105 EETDV--IIAAGSGTIHDITRFAAYQRGLPFISFPTAPSVDGFTSAGAPLILNGIKTTIQTKAPIALFADTNVLKEAPRS 182
Cdd:PRK00843   84 KDVNAgfLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGKPVSVKAKPPLAVIADTEIIAKAPYR 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 183 MTAAGFGDMLGKITSLADWEISRRLAGEPYSEAGAKLVKDALWQCIDHRAAIAMGTEAGIQILMEALIVSGLVMLALDHS 262
Cdd:PRK00843  164 LLAAGCGDIISNYTAVKDWRLAHRLRGEYYSEYAAALSLMTAKMLIENADIIKPGLEESARLVVKALISSGVAMSIAGSS 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 263 RPASGGEHHISHWIEMEMLKakqpPILHGAKVGCAcavlsdiykelacheklaelpphfreAIQSAYEGLPDGKTIAGWL 342
Cdd:PRK00843  244 RPASGSEHLFSHALDRLAPG----PALHGEQCGVG--------------------------TIIMMYLHGGDWRKIRDAL 293

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1733419119 343 ASAGGPACFDEIGVKQDLVSDALKHAHTLR-DRYT--GLTIINENAA 386
Cdd:PRK00843  294 KKIGAPTTAKELGIDDEYIIEALTIAHTIRpERYTilGDRGLTREAA 340
 
Name Accession Description Interval E-value
G1PDH cd08175
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ...
 24-383 1.70e-152

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: 433.86  E-value: 1.70e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  24 IEDIVIGANAKEELLRFLQKKC-WNHPVIVCDRNTYEAAGRLLADELRAGGIKASKVIIPEHeaGAAAADERTLVYTLIN 102
Cdd:cd08175     1 IKEIVIGEGALKKLPEYLKELFgGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGE--GDLIADEAAVGKVLLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 103 LAEETDVIIAAGSGTIHDITRFAAYQRGLPFISFPTAPSVDGFTSAGAPLILNGIKTTIQTKAPIALFADTNVLKEAPRS 182
Cdd:cd08175    79 LEKDTDLIIAVGSGTINDLTKYAAYKLGIPYISVPTAPSMDGYTSSGAPIIVDGVKKTFPAHAPKAIFADLDVLANAPQR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 183 MTAAGFGDMLGKITSLADWEISRRLAGEPYSEAGAKLVKDALWQCIDHRAAIAMGTEAGIQILMEALIVSGLVMLALDHS 262
Cdd:cd08175   159 MIAAGFGDLLGKYTALADWKLSHLLGGEYYCPEVADLVQEALEKCLDNAEGIAARDPEAIEALMEALILSGLAMQLVGNS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 263 RPASGGEHHISHWIEMEMLKAKQPPILHGAKVGCACAVLSDIYkelacheklaelpphfreaiqsAYEGLPDGKTIAGWL 342
Cdd:cd08175   239 RPASGAEHHLSHYWEMEFLRLGKPPVLHGEKVGVGTLLIAALY----------------------ILEQLPPPEELRELL 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1733419119 343 ASAGGPACFDEIGVKQDLVSDALKHAHTLRDRYTGLTIINE 383
Cdd:cd08175   297 RKAGAPTTPEDLGIDRDLLRDSLRLAKEIRDRYTVLDLAWD 337
G1PDH_related cd08549
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ...
 24-386 7.82e-90

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: 274.06  E-value: 7.82e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  24 IEDIVIGANAKEELLRFLQKKCWNHPVIVCDRNTYEAAGRLLADELraggiKASKVIIPeHEAGAAAADERTLVYTLinl 103
Cdd:cd08549     1 PRYTIVGDGAINKIEEILKKLNLKRVLIITGKNTKAKYCRFFYDQL-----KTVCDIVY-YDNIDNLEDELKKYTFY--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 104 aeetDVIIAAGSGTIHDITRFAAYQRGLPFISFPTAPSVDGFTSAGAPLILNGIKTTIQTKAPIALFADTNVLKEAPRSM 183
Cdd:cd08549    72 ----DCVIGIGGGRSIDTGKYLAYKLKIPFISVPTSASNDGIASPIVSLRIPGVKKTFMADAPIAIIADTEIIKKSPRRL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 184 TAAGFGDMLGKITSLADWEISRRLAGEPYSEAGAKLVKDALWQCIDHrAAIAMGTEAGIQILMEALIVSGLVMLALDHSR 263
Cdd:cd08549   148 LSAGIGDLVSNITAVLDWKLAHKEKGEKYSEFAAILSKTSAKELVSY-VLKASDLEEYHRVLVKALVGSGIAMAIAGSSR 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 264 PASGGEHHISHWIEMEMLKAKQPPILHGAKVGCACAVLSDIYKelacHEKLAELPPHFReaiqsayeglpdgktIAGWLA 343
Cdd:cd08549   227 PASGSEHLFSHALDKLKEEYLNINVLHGEQVGVGTIIMSYLHE----KENKKLSGLHER---------------IKMILK 287

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1733419119 344 SAGGPACFDEIGVKQDLVSDALKHAHTLR-DRYTGLTIINENAA 386
Cdd:cd08549   288 KVGAPTTAKQLGIDEDLIIEALTEAHKIRpRRYTLLDGLSREEA 331
Fe-ADH_2 pfam13685
Iron-containing alcohol dehydrogenase;
28-295 1.52e-75

Iron-containing alcohol dehydrogenase;


Pssm-ID: 404557 [Multi-domain]  Cd Length: 251  Bit Score: 234.89  E-value: 1.52e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  28 VIGANAKEELLRFLQKKCWNHPVIVCDRNTYEAAGRLLADELRAGGIKASKViipehEAGAAAADERTLVYTLINLAE-E 106
Cdd:pfam13685   1 VIGPGALGRLGEYLAELGFRRVALVADANTYAAAGRKVAESLKRAGIEVETR-----LEVAGNADMETAEKLVGALRErD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 107 TDVIIAAGSGTIHDITRFAAYQRGLPFISFPTAPSVDGFTSAGAPLILNGIKTTIQTKAPIALFADTNVLKEAPRSMTAA 186
Cdd:pfam13685  76 ADAVVGVGGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASLTVDGKKRSIPAAAPFGVIADTDVIAAAPRRLLAS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 187 GFGDMLGKITSLADWEISRRLA-GEPYSEAGAKLVKDALwqcidHRAAIAMGTEAGIQILMEALIVSGLVMlaldhSRPA 265
Cdd:pfam13685 156 GVGDLLAKITAVADWELAHAEEvAAPLALLSAAMVMNFA-----DRPLRDPGDIEALAELLSALAMGGAGS-----SRPA 225

                         250       260       270
                  ....*....|....*....|....*....|
gi 1733419119 266 SGGEHHISHWIEMEMLKakqpPILHGAKVG 295
Cdd:pfam13685 226 SGSEHLISHALDMIAPK----QALHGEQVG 251
Gro1PDH cd08173
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ...
 27-384 3.20e-66

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: 213.95  E-value: 3.20e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  27 IVIGANAKEELLRFLQKKCWNH-PVIVCDRNTYEAAGRLLADELRAGGIKASKVIIPEHEaGAAAADErtlvYTLINLAE 105
Cdd:cd08173     5 VVVGHGAINKIGEVLKKLLLGKrALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIE-EAAEVEK----VKKLIKES 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 106 ETDVIIAAGSGTIHDITRFAAYQRGLPFISFPTAPSVDGFTSAGAPLILNGIKTTIQTKAPIALFADTNVLKEAPRSMTA 185
Cdd:cd08173    80 KADFIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIKGGDKPYSIKAKAPIAIIADTEIISKAPKRLLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 186 AGFGDMLGKITSLADWEISRRLAGEPYSEAGAKLVKDALWQCIDHRAAIAMGTEAGIQILMEALIVSGLVMLALDHSRPA 265
Cdd:cd08173   160 AGCGDLISNITAVKDWRLAHRLKGEYYSEYAASLALMSAKLIIENADLIKPGLEEGVRTVVKALISSGVAMSIAGSSRPA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 266 SGGEHHISHWIEMEMLKakqpPILHGAKVGCACavlsdiykelacheklaelpphfreaIQSAYEGLPDGKTIAGWLASA 345
Cdd:cd08173   240 SGSEHLFSHALDKLAPG----PALHGEQCGVGT--------------------------IMMAYLHGGDWKEIREALKKI 289

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1733419119 346 GGPACFDEIGVKQDLVSDALKHAHTLRDRYTglTIINEN 384
Cdd:cd08173   290 GAPTTAKELGLDKEIIIEALTIAHKIRPERY--TILGDN 326
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 27-376 2.91e-62

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: 203.86  E-value: 2.91e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  27 IVIGANAKEELLRFLQKKCwNHPVIVCDRNTYEAAGRLLADELRAGGIKASKVIIpEHEAGAAAADErtlvytLINLAEE 106
Cdd:COG0371     9 YVQGEGALDELGEYLADLG-KRALIITGPTALKAAGDRLEESLEDAGIEVEVEVF-GGECSEEEIER------LAEEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 107 --TDVIIAAGSGTIHDITRFAAYQRGLPFISFPTAPSVDGFTSAGAPLILNG---IKTTIQTKAPIALFADTNVLKEAPR 181
Cdd:COG0371    81 qgADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDgafDGYSFLAKNPDLVLVDTDIIAKAPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 182 SMTAAGFGDMLGKITSLADWEISRR-LAGEPYSEAGAKLVKDALWQCIDH-RAAIA-----MGTEAGIQILMEALIVSGL 254
Cdd:COG0371   161 RLLAAGIGDALAKWYEARDWSLAHRdLAGEYYTEAAVALARLCAETLLEYgEAAIKaveagVVTPALERVVEANLLLSGL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 255 VMlALDHSRPASGGEHHISHwiEMEMLKAKQpPILHGAKVGCACAVlsdiykelacheklaelpphfreaiQSAYEGLPD 334
Cdd:COG0371   241 AM-GIGSSRPGSGAAHAIHN--GLTALPETH-HALHGEKVAFGTLV-------------------------QLVLEGRPE 291

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1733419119 335 G-KTIAGWLASAGGPACFDEIGVKQDLVSDALKHAHTLR-DRYT 376
Cdd:COG0371   292 EiEELLDFLRSVGLPTTLADLGLDDETEEELLTVAEAARpERYT 335
egsA PRK00843
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
 26-386 6.55e-62

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


Pssm-ID: 179139  Cd Length: 350  Bit Score: 202.82  E-value: 6.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  26 DIVIGANAKEELLRFLQK-KCWNHPVIVCDRNTYEAAGRLLADELRAGGiKASKVIIPEheagaAAADErtlVYTLINLA 104
Cdd:PRK00843   13 DVVVGHGVLDDIGDVCSDlKLTGRALIVTGPTTKKIAGDRVEENLEDAG-DVEVVIVDE-----ATMEE---VEKVEEKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 105 EETDV--IIAAGSGTIHDITRFAAYQRGLPFISFPTAPSVDGFTSAGAPLILNGIKTTIQTKAPIALFADTNVLKEAPRS 182
Cdd:PRK00843   84 KDVNAgfLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGKPVSVKAKPPLAVIADTEIIAKAPYR 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 183 MTAAGFGDMLGKITSLADWEISRRLAGEPYSEAGAKLVKDALWQCIDHRAAIAMGTEAGIQILMEALIVSGLVMLALDHS 262
Cdd:PRK00843  164 LLAAGCGDIISNYTAVKDWRLAHRLRGEYYSEYAAALSLMTAKMLIENADIIKPGLEESARLVVKALISSGVAMSIAGSS 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 263 RPASGGEHHISHWIEMEMLKakqpPILHGAKVGCAcavlsdiykelacheklaelpphfreAIQSAYEGLPDGKTIAGWL 342
Cdd:PRK00843  244 RPASGSEHLFSHALDRLAPG----PALHGEQCGVG--------------------------TIIMMYLHGGDWRKIRDAL 293

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1733419119 343 ASAGGPACFDEIGVKQDLVSDALKHAHTLR-DRYT--GLTIINENAA 386
Cdd:PRK00843  294 KKIGAPTTAKELGIDDEYIIEALTIAHTIRpERYTilGDRGLTREAA 340
G1PDH-like cd08174
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ...
 27-391 9.33e-49

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: 168.08  E-value: 9.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  27 IVIGANAKEELLRFL--QKKCWNHPVIVCDrntyEAAGRLLADELRAGGIKASKVIIPEHEAGAAAADERTLVYTLinla 104
Cdd:cd08174     4 LKIEEGALEHLGKYLadRNQGFGKVAIVTG----EGIDELLGEDILESLEEAGEIVTVEENTDNSAEELAEKAFSL---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 105 EETDVIIAAGSGTIHDITRFAAYQRGLPFISFPTAPSVDGFTSAGAPLILNGIKTTIQTKAPIALFADTNVLKEAPRSMT 184
Cdd:cd08174    76 PKVDAIVGIGGGKVLDVAKYAAFLSKLPFISVPTSLSNDGIASPVAVLKVDGKRKSLGAKMPYGVIVDLDVIKSAPRRLI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 185 AAGFGDMLGKITSLADWEISRRLAGEPYSEAGAKLVKDALWQCIDHRAAiAMGTEAGIQILMEALIVSGLVMLALDHSRP 264
Cdd:cd08174   156 LAGIGDLISNITALYDWKLAEEKGGEPVDDFAYLLSRTAADSLLNTPGK-DIKDDEFLKELAESLVLSGIAMEIAGSSRP 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 265 ASGGEHHISHWIEmEMLKAkqpPILHGAKVGCACAVLSDIYKELAcheklaelpphfreaiqsayeglpdgKTIAGWLAS 344
Cdd:cd08174   235 ASGSEHLISHALD-KLFPG---PALHGIQVGLGTYFMSFLQGQRY--------------------------EEIRDVLKR 284

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1733419119 345 AGGPACFDEIGVKQDLVSDALKHAHTLR-DRYTGLTIINENAALFAHH 391
Cdd:cd08174   285 TGFPLNPSDLGLTKEEFIEAVKLAPSTRpGRYTILEELDLSEERLKEI 332
DHQS cd08195
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 26-138 7.89e-13

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: 69.01  E-value: 7.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  26 DIVIGANAKEELLRFLQKKCWNHPVIVCDRNTYEAAGRLLADELRAGGIKASKVIIPEHEAgaaaadERTLvYTLINLAE 105
Cdd:cd08195     3 PILIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGEK------SKSL-ETVERIYD 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1733419119 106 E--------TDVIIAAGSGTIHDITRFAA--YQRGLPFISFPT 138
Cdd:cd08195    76 FlleagldrDSLLIALGGGVVGDLAGFVAstYMRGIPFIQVPT 118
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 26-189 1.21e-11

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: 65.50  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  26 DIVIGANAKEELLRFLQ-----KKCwnhpVIVCDRNTYEAAGRLLADELRAGGIKASKVIIPeheAGAAAADERTLVYTL 100
Cdd:COG0337    14 DIRIGRGLLDELGELLAellkgRRV----LVVTDENVAPLYGERLRAALEAAGFEVHLLVLP---DGEASKTLETLERIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 101 INLAEE----TDVIIAAGSGTIHDITRFAA--YQRGLPFISFPT-------ApSVdgftsagaplilnGIKTTIQTKA-- 165
Cdd:COG0337    87 DALLEAgldrDDLVVALGGGVVGDLAGFAAatYLRGVPFIQVPTtllaqvdS-SV-------------GGKTGVNHPGgk 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1733419119 166 --------PIALFADTNVLKEAPRSMTAAGFG 189
Cdd:COG0337   153 nligafhqPRAVLIDLDFLKTLPERELRAGLA 184
DHQ_Fe-ADH cd07766
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ...
 25-199 1.46e-10

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: 61.23  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  25 EDIVIGANA----KEELLRFLQKKcwnhpVIVCDRNTYEAAGRLLADELRAGgIKASKVIIPEHEAgaaaadERTLVYTL 100
Cdd:cd07766     2 TRIVFGEGAiaklGEIKRRGFDRA-----LVVSDEGVVKGVGEKVADSLKKG-LAVAIFDFVGENP------TFEEVKNA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 101 INL--AEETDVIIAAGSGTIHDITRFAAY--QRGLPFISFPTAPSVDGFTSAGAPLILNGIKTTIQT--KAPIALFADTN 174
Cdd:cd07766    70 VERarAAEADAVIAVGGGSTLDTAKAVAAllNRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVGphYNPDVVFVDTD 149

                         170       180
                  ....*....|....*....|....*
gi 1733419119 175 VLKEAPRSMTAAGFGDMLGKITSLA 199
Cdd:cd07766   150 ITKGLPPRQVASGGVDALAHAVELE 174
GlyDH-like cd08550
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ...
 47-194 6.49e-10

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: 59.86  E-value: 6.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  47 NHPVIVCDRNTYEAAGRLLADELRAGGIKASKVIIpEHEAGAAAADErtlvytLINLAEET--DVIIAAGSGTIHDITRF 124
Cdd:cd08550    23 KKALIIGGKTALEAVGEKLEKSLEEAGIDYEVEVF-GGECTEENIER------LAEKAKEEgaDVIIGIGGGKVLDTAKA 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1733419119 125 AAYQRGLPFISFPTAPSVDgftSAGAPL-IL---NGIKTTIQ--TKAPIALFADTNVLKEAPRSMTAAGFGDMLGK 194
Cdd:cd08550    96 VADRLGLPVVTVPTIAATC---AAWSALsVLydeEGEFLGYSllKRSPDLVLVDTDIIAAAPVRYLAAGIGDTLAK 168
GlyDH cd08170
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ...
 28-194 7.08e-10

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: 60.12  E-value: 7.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  28 VIGANAKEELLRFLqKKCWNHPVIVCDRNTYEAAGRLLADELRAGGIKASKVIIpEHEAGAAAADERTLVYTlinlAEET 107
Cdd:cd08170     5 VQGPGALDRLGEYL-APLGKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVF-GGECSREEIERLAAIAR----ANGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 108 DVIIAAGSGTIHDITRFAAYQRGLPFISFPTAPSVDGFTSAGAplIL---NG--IKTTIQTKAPIALFADTNVLKEAPRS 182
Cdd:cd08170    79 DVVIGIGGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALS--VIyteDGefDEYLFLPRNPDLVLVDTEIIAKAPVR 156

                         170
                  ....*....|..
gi 1733419119 183 MTAAGFGDMLGK 194
Cdd:cd08170   157 FLVAGMGDALAT 168
DHQ_synthase pfam01761
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ...
 108-358 1.47e-09

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: 58.28  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 108 DVIIAAGSGTIHDITRFAA--YQRGLPFISFPTA------PSVDGFTSAGAPLILNGIKTTIQtkaPIALFADTNVLKEA 179
Cdd:pfam01761  32 SLLIALGGGVIGDLAGFVAatYMRGIRFIQVPTTllaqvdSSVGGKTGINHPLGKNLIGAFYQ---PKAVLIDLDFLKTL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 180 PRSMTAAGFGDMLgKITSLADWEISRRLagEPYSEAGAKLVKDALwqcidhRAAIAMGTEAGIQILMEALIVSGL-VMLA 258
Cdd:pfam01761 109 PDREFRAGLAEVI-KYGLIADAEFFEWL--EENAEALLNLDPDAL------EEAIARSCEVKADVVAQDEKESGLrALLN 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 259 LDHSrpasggehhISHWIEMEMLKAKqppILHGAKV--GCACAVlsdiykELAchEKLAELPPHFREAIQSayeglpdgk 336
Cdd:pfam01761 180 LGHT---------FGHAIEALSGYGA---LLHGEAVaiGMVLAA------RLS--ERLGLLDEADVERIRA--------- 230

                         250       260
                  ....*....|....*....|..
gi 1733419119 337 tiagWLASAGGPACFDEIGVKQ 358
Cdd:pfam01761 231 ----LLKKYGLPTSLPDLDVEQ 248
EEVS cd08199
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ...
 50-302 3.00e-09

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: 57.92  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  50 VIVCDRNTYEAAGRLLADELRAGGIKASKVIIPEHEAgaaAADERTlVYTLINLAEE-----TDVIIAAGSGTIHDITRF 124
Cdd:cd08199    30 LVVVDENVDRLYGARIRAYFAAHGIEATILVLPGGEA---NKTMET-VLRIVDALDDfgldrREPVIAIGGGVLLDVVGF 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 125 AA--YQRGLPFISFPTapSVDGFTSAGAplilnGIKTTI---QTK-------APIALFADTNVLKEAPRSMTAAGFGDML 192
Cdd:cd08199   106 AAslYRRGVPYIRVPT--TLLGLVDAGV-----GIKTGVnfgGHKnrlgayyPPVATLLDRSFLKTLPRRHIRNGLAEII 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 193 gKITSLADWEISRRLAgepysEAGAKLVKDALWQcidhrAAIAMG-TEAGIQILMEALiVSGLVMLALDhsRP-ASGgeH 270
Cdd:cd08199   179 -KMALVKDAELFELLE-----EHGAALVETRFFQ-----DEVADEiIRRAIQGMLEEL-APNLWEHDLE--RLvDFG--H 242

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1733419119 271 HISHWIEMemlkAKQPPILHGAKV---GCACAVLS 302
Cdd:cd08199   243 TFSPILEM----AAAPELLHGEAVaidMALSAVLA 273
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
27-371 2.16e-08

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 55.30  E-value: 2.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  27 IVIGANAKEELLRFLQKKCWnHPVIVCDRNTYEAaGRL--LADELRAGGIKA---SKVI----IPEHEAGAAAADErtlv 97
Cdd:pfam00465   4 IVFGAGALAELGEELKRLGA-RALIVTDPGSLKS-GLLdkVLASLEEAGIEVvvfDGVEpeptLEEVDEAAALARE---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  98 ytlinlaEETDVIIAAGSGTIHDITRFAAY------------------QRGLPFISFPTAPSVDGFTSAGAPLIL--NGI 157
Cdd:pfam00465  78 -------AGADVIIAVGGGSVIDTAKAIALlltnpgdvwdylggkpltKPALPLIAIPTTAGTGSEVTPLAVITDteTGE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 158 KTTIQTKA--PIALFADTNVLKEAPRSMTAAGFGDMLGKI----TSLADWEISRRLAgepysEAGAKLVKDALWQCIDH- 230
Cdd:pfam00465 151 KLGIFSPKllPDLAILDPELTLTLPPRLTAATGMDALAHAveayVSKGANPLTDALA-----LEAIRLIAENLPRAVADg 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 231 -----RAAIAMG-TEAGIqilmeALIVSGLVML-ALDHsrpASGGEHHISHwiememlkakqpPILHGAKVGcacAVLSD 303
Cdd:pfam00465 226 edleaRENMLLAsTLAGL-----AFSNAGLGAAhALAH---ALGGRYGIPH------------GLANAILLP---YVLRF 282

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1733419119 304 IYKelACHEKLAEL-----PPHFREAIQSAYEGlpdgktIAGWLASAGGPACFDEIGVKQD----LVSDALKHAHTL 371
Cdd:pfam00465 283 NAP--AAPEKLAQLaralgEDSDEEAAEEAIEA------LRELLRELGLPTTLSELGVTEEdldaLAEAALRDRSLA 351
GlyDH-like cd08172
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 35-224 3.87e-08

Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.


Pssm-ID: 341451 [Multi-domain]  Cd Length: 346  Bit Score: 54.45  E-value: 3.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  35 EELLRFLQKKCWNHPVIVCDRNTYEAAGRLLADELRAGgikaSKVIIPEHEAGAAAADErtlvytLINLAEE--TDVIIA 112
Cdd:cd08172    12 KELPELLSEFGIKRPLIIHGEKSWQAAKPYLPKLFEIE----YPVLRYDGECSYEEIDR------LAEEAKEhqADVIIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 113 AGSGTIHDITRFAAYQRGLPFISFPTAPSvdgfTSAG-APLIL----NG--IKTTIQTKAPIALFADTNVLKEAPRSMTA 185
Cdd:cd08172    82 IGGGKVLDTAKAVADKLNIPLILIPTLAS----NCAAwTPLSViydeDGefIGYDYFPRSAYLVLVDPRLLLDSPKDYFV 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1733419119 186 AGFGDMLGK-------ITSLADWEISRRLAgepysEAGAKLVKDAL 224
Cdd:cd08172   158 AGIGDTLAKwyeadaiLRQLEELPAFLQLA-----RQAAKLCRDIL 198
gldA PRK09423
glycerol dehydrogenase; Provisional
 28-192 5.71e-07

glycerol dehydrogenase; Provisional


Pssm-ID: 181843  Cd Length: 366  Bit Score: 50.97  E-value: 5.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  28 VIGANAKEELLRFLqKKCWNHPVIVCDRNTYEAAGRLLADELRAGGIKASKVIIPeheaGAAAADErtlVYTLINLAEE- 106
Cdd:PRK09423   12 VQGKGALARLGEYL-KPLGKRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFN----GECSDNE---IDRLVAIAEEn 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 107 -TDVIIAAGSGTIHDITRFAAYQRGLPFISFPTAPSVDGFTSAGAplilngiktTIQT------------KAPIALFADT 173
Cdd:PRK09423   84 gCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALS---------VIYTeegeferylflpKNPDLVLVDT 154

                         170
                  ....*....|....*....
gi 1733419119 174 NVLKEAPRSMTAAGFGDML 192
Cdd:PRK09423  155 AIIAKAPARFLAAGIGDAL 173
PLN02834 PLN02834
3-dehydroquinate synthase
 27-192 9.59e-07

3-dehydroquinate synthase


Pssm-ID: 215448  Cd Length: 433  Bit Score: 50.54  E-value: 9.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  27 IVIGAN--AKEELLrflQKKCWNHPVIVCDRNTYEAA-GRLLADELRAGGIKAS--KVIIPEheaGAAAADERTLVYTLI 101
Cdd:PLN02834   81 IYIGSGllDHGELL---QRHVHGKRVLVVTNETVAPLyLEKVVEALTAKGPELTveSVILPD---GEKYKDMETLMKVFD 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 102 NLAE------ETdvIIAAGSGTIHDITRFAA--YQRGLPFISFPTA------PSVDGFTSAGAPLILNGIKTTIQtkaPI 167
Cdd:PLN02834  155 KALEsrldrrCT--FVALGGGVIGDMCGFAAasYQRGVNFVQIPTTvmaqvdSSVGGKTGVNHPLGKNMIGAFYQ---PQ 229

                         170       180
                  ....*....|....*....|....*
gi 1733419119 168 ALFADTNVLKEAPRSMTAAGFGDML 192
Cdd:PLN02834  230 CVLIDTDTLATLPDRELASGIAEVV 254
DOIS cd08197
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ...
 24-180 1.26e-06

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: 49.89  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  24 IEDIVIGANAKEELLRFLQKKCWNHPVIVCDRNTYEAAGRLLADELRAGGIKASKVIIPEHEAgaaaadERTLVyTLINL 103
Cdd:cd08197     1 LTDIYLGRGILESLLSILEELKADRHFLVTDSNVNDLYGDRLLEGLKKAGIPVELLVVPAGES------NKTLS-TLTEL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 104 AEE--------TDVIIAAGSGTIHDITRFAA---YqRGLPFISFPTA--PSVDGFTSagaplilngIKTTIQTK------ 164
Cdd:cd08197    74 AERliaagitrRSVIIALGGGVVGNIAGLLAgllY-RGIRLVHVPTTllAQSDSVLS---------LKQAVNGKsgknlv 143

                         170       180
                  ....*....|....*....|
gi 1733419119 165 ----APIALFADTNVLKEAP 180
Cdd:cd08197   144 gsyyAPLFVFVDTEFLKTLP 163
DHQ-like cd08169
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ...
 110-294 1.63e-06

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: 49.33  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 110 IIAAGSGTIHDITRFAA--YQRGLPFISFPTapSVDGFTSAGAplilnGIKTTIQTK----------APIALFADTNVLK 177
Cdd:cd08169    87 VVAVGGGATGDVVGFAAatYFRGIAFIRVPT--TLLAQSDSSV-----GIKVGINTRggknllgafyPPRAVFADFSFLK 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119 178 EAPRSMTAAGFGDMLgKITSLADWEISRRLagEPYSEAGAKLVKDALWQCIDHraaiamgteaGIQILMEaLIVSGLVML 257
Cdd:cd08169   160 TLPFRQVRAGMAELV-KMALIADNDFFEFL--EDKANSATVYSPEQLEKLINK----------CISLKLD-VVVADEDEQ 225

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1733419119 258 ALDhsRPASGGeHHISHWIEmemlKAKQPPILHGAKV 294
Cdd:cd08169   226 GKR--RGLNYG-HTFGHALE----LASGYKIPHGEAV 255
PRK14021 PRK14021
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
 22-207 6.12e-04

bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional


Pssm-ID: 184458 [Multi-domain]  Cd Length: 542  Bit Score: 41.77  E-value: 6.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  22 IQIEDIVIGANAKEELLRFLQKKcwnhPVIVCDRNT-----YEAAGRLLadeLRAGGIKASKVIIPEHEAGAAAADERTL 96
Cdd:PRK14021  186 IEPYDVRIGEGAMNHLPQVLGPK----PVKVALIHTqpvqrHSDRARTL---LRQGGYEVSDIVIPDAEAGKTIEVANGI 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733419119  97 vytLINLAEE----TDVIIAAGSGTIHDITRF--AAYQRGLPFISFPTA--PSVDGFTsagaplilnGIKTTIQTKA--- 165
Cdd:PRK14021  259 ---WQRLGNEgftrSDAIVGLGGGAATDLAGFvaATWMRGIRYVNCPTSllAMVDAST---------GGKTGINTPQgkn 326

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1733419119 166 -------PIALFADTNVLKEAPRSMTAAGFGDmLGKITSLADWEISRRL 207
Cdd:PRK14021  327 lvgsfytPAGVLADTKTLATLPNDIFIEGLGE-VAKSGFIRDPEILRIL 374
 
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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