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Conserved domains on  [gi|167045371|gb|ABZ10027|]
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putative iron-containing alcohol dehydrogenase [uncultured marine microorganism HF4000_APKG10F13]

Protein Classification

dehydroquinate synthase/iron-containing alcohol dehydrogenase family protein( domain architecture ID 760)

dehydroquinate synthase (DHQS)/iron-containing alcohol dehydrogenase (FeADH) family protein

CATH:  3.40.50.1970
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
DHQ_Fe-ADH super family cl02872
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ...
 7-347 9.15e-168

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.


The actual alignment was detected with superfamily member PRK00843:

Pssm-ID: 445950  Cd Length: 350  Bit Score: 471.30  E-value: 9.15e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   7 RSMVLPRMVVTGPGVIEQLPAVIAELDLPERGLLVCDAVTRKVAGDRVLAYLEETGHpVAVIEIDGASMEELARVEAAA- 85
Cdd:PRK00843   6 HWIQLPRDVVVGHGVLDDIGDVCSDLKLTGRALIVTGPTTKKIAGDRVEENLEDAGD-VEVVIVDEATMEEVEKVEEKAk 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  86 -EGCGFLAGVGGGRPVDLAKQAGYHLDLPFISVPTAASHDGFASARASIRAAGQKTSMEARPPIAVVADTTIIASAPRRL 164
Cdd:PRK00843  85 dVNAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGKPVSVKAKPPLAVIADTEIIAKAPYRL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 165 LAAGIGDIVSNQTAVLDWQLG-RDRGEEYSAYAAALSEMTARLVEENSGLVAEGGEEGVRLVVKALISSGVAMSIAGSSR 243
Cdd:PRK00843 165 LAAGCGDIISNYTAVKDWRLAhRLRGEYYSEYAAALSLMTAKMLIENADIIKPGLEESARLVVKALISSGVAMSIAGSSR 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 244 PASGGEHKFSHWLDANASSPALHGEQCGVGSIVTMQLHGGDWERIRDTLAAAGAPISAEQLGFGDDIVLQALCEAKTIRP 323
Cdd:PRK00843 245 PASGSEHLFSHALDRLAPGPALHGEQCGVGTIIMMYLHGGDWRKIRDALKKIGAPTTAKELGIDDEYIIEALTIAHTIRP 324

                        330       340
                 ....*....|....*....|....*.
gi 167045371 324 QRYTILDRE--SPEKIEQAARETGVV 347
Cdd:PRK00843 325 ERYTILGDRglTREAAEKAARITGVI 350
 
Name Accession Description Interval E-value
egsA PRK00843
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
 7-347 9.15e-168

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


Pssm-ID: 179139  Cd Length: 350  Bit Score: 471.30  E-value: 9.15e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   7 RSMVLPRMVVTGPGVIEQLPAVIAELDLPERGLLVCDAVTRKVAGDRVLAYLEETGHpVAVIEIDGASMEELARVEAAA- 85
Cdd:PRK00843   6 HWIQLPRDVVVGHGVLDDIGDVCSDLKLTGRALIVTGPTTKKIAGDRVEENLEDAGD-VEVVIVDEATMEEVEKVEEKAk 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  86 -EGCGFLAGVGGGRPVDLAKQAGYHLDLPFISVPTAASHDGFASARASIRAAGQKTSMEARPPIAVVADTTIIASAPRRL 164
Cdd:PRK00843  85 dVNAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGKPVSVKAKPPLAVIADTEIIAKAPYRL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 165 LAAGIGDIVSNQTAVLDWQLG-RDRGEEYSAYAAALSEMTARLVEENSGLVAEGGEEGVRLVVKALISSGVAMSIAGSSR 243
Cdd:PRK00843 165 LAAGCGDIISNYTAVKDWRLAhRLRGEYYSEYAAALSLMTAKMLIENADIIKPGLEESARLVVKALISSGVAMSIAGSSR 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 244 PASGGEHKFSHWLDANASSPALHGEQCGVGSIVTMQLHGGDWERIRDTLAAAGAPISAEQLGFGDDIVLQALCEAKTIRP 323
Cdd:PRK00843 245 PASGSEHLFSHALDRLAPGPALHGEQCGVGTIIMMYLHGGDWRKIRDALKKIGAPTTAKELGIDDEYIIEALTIAHTIRP 324

                        330       340
                 ....*....|....*....|....*.
gi 167045371 324 QRYTILDRE--SPEKIEQAARETGVV 347
Cdd:PRK00843 325 ERYTILGDRglTREAAEKAARITGVI 350
Gro1PDH cd08173
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ...
 11-346 8.37e-153

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: 433.13  E-value: 8.37e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  11 LPRMVVTGPGVIEQLPAVIAELDLPERGLLVCDAVTRKVAGDRVLAYLEETGhpVAVIEIDGASMEELARVE-----AAA 85
Cdd:cd08173    1 LPRNVVVGHGAINKIGEVLKKLLLGKRALIITGPNTYKIAGKRVEDLLESSG--VEVVIVDIATIEEAAEVEkvkklIKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  86 EGCGFLAGVGGGRPVDLAKQAGYHLDLPFISVPTAASHDGFASARASIRAAGQKTSMEARPPIAVVADTTIIASAPRRLL 165
Cdd:cd08173   79 SKADFIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIKGGDKPYSIKAKAPIAIIADTEIISKAPKRLL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 166 AAGIGDIVSNQTAVLDWQLGRD-RGEEYSAYAAALSEMTARLVEENSGLVAEGGEEGVRLVVKALISSGVAMSIAGSSRP 244
Cdd:cd08173  159 AAGCGDLISNITAVKDWRLAHRlKGEYYSEYAASLALMSAKLIIENADLIKPGLEEGVRTVVKALISSGVAMSIAGSSRP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 245 ASGGEHKFSHWLDANASSPALHGEQCGVGSIVTMQLHGGDWERIRDTLAAAGAPISAEQLGFGDDIVLQALCEAKTIRPQ 324
Cdd:cd08173  239 ASGSEHLFSHALDKLAPGPALHGEQCGVGTIMMAYLHGGDWKEIREALKKIGAPTTAKELGLDKEIIIEALTIAHKIRPE 318

                        330       340
                 ....*....|....*....|....
gi 167045371 325 RYTILDRE--SPEKIEQAARETGV 346
Cdd:cd08173  319 RYTILGDNglTEEAAERLARITGV 342
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 7-344 2.02e-104

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: 310.56  E-value: 2.02e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   7 RSMVLPRMVVTGPGVIEQLPAVIAELDlpERGLLVCDAVTRKVAGDRVLAYLEETGHPVAVIEIDG-ASMEELARV--EA 83
Cdd:COG0371    1 RVIILPRRYVQGEGALDELGEYLADLG--KRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGeCSEEEIERLaeEA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  84 AAEGCGFLAGVGGGRPVDLAKQAGYHLDLPFISVPTAASHDGFASARA---SIRAAGQKTSMEARPPIAVVADTTIIASA 160
Cdd:COG0371   79 KEQGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSviyTEDGAFDGYSFLAKNPDLVLVDTDIIAKA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 161 PRRLLAAGIGDIVSNQTAVLDWQLGRD--RGEEYSAYAAALSEMTARLVEENSGL----VAEG--GEEGVRLVVKALISS 232
Cdd:COG0371  159 PVRLLAAGIGDALAKWYEARDWSLAHRdlAGEYYTEAAVALARLCAETLLEYGEAaikaVEAGvvTPALERVVEANLLLS 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 233 GVAMSIaGSSRPASGGEHKFSHWLDA-NASSPALHGEQCGVGSIVTMQLHGGD--WERIRDTLAAAGAPISAEQLGFGDD 309
Cdd:COG0371  239 GLAMGI-GSSRPGSGAAHAIHNGLTAlPETHHALHGEKVAFGTLVQLVLEGRPeeIEELLDFLRSVGLPTTLADLGLDDE 317

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 167045371 310 IVLQALCEAKTIRPQRYTILDRE---SPEKIEQAARET 344
Cdd:COG0371  318 TEEELLTVAEAARPERYTILNLPfevTPEAVEAAILAT 355
Fe-ADH_2 pfam13685
Iron-containing alcohol dehydrogenase;
16-271 2.61e-72

Iron-containing alcohol dehydrogenase;


Pssm-ID: 404557 [Multi-domain]  Cd Length: 251  Bit Score: 224.87  E-value: 2.61e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   16 VTGPGVIEQLPAVIAELDLpERGLLVCDAVTRKVAGDRVLAYLEETG-HPVAVIEIDG-ASMEELARVEAAAE--GCGFL 91
Cdd:pfam13685   1 VIGPGALGRLGEYLAELGF-RRVALVADANTYAAAGRKVAESLKRAGiEVETRLEVAGnADMETAEKLVGALRerDADAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   92 AGVGGGRPVDLAKQAGYHLDLPFISVPTAASHDGFASARASIRAAGQKTSMEARPPIAVVADTTIIASAPRRLLAAGIGD 171
Cdd:pfam13685  80 VGVGGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASLTVDGKKRSIPAAAPFGVIADTDVIAAAPRRLLASGVGD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  172 IVSNQTAVLDWQLGRDrgeeySAYAAALSEMTARLVEENsglVAEGGEEGVRLVVKALISSGVAMSIAGSSRPASGGEHK 251
Cdd:pfam13685 160 LLAKITAVADWELAHA-----EEVAAPLALLSAAMVMNF---ADRPLRDPGDIEALAELLSALAMGGAGSSRPASGSEHL 231

                         250       260
                  ....*....|....*....|
gi 167045371  252 FSHWLDANASSPALHGEQCG 271
Cdd:pfam13685 232 ISHALDMIAPKQALHGEQVG 251
 
Name Accession Description Interval E-value
egsA PRK00843
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
 7-347 9.15e-168

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


Pssm-ID: 179139  Cd Length: 350  Bit Score: 471.30  E-value: 9.15e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   7 RSMVLPRMVVTGPGVIEQLPAVIAELDLPERGLLVCDAVTRKVAGDRVLAYLEETGHpVAVIEIDGASMEELARVEAAA- 85
Cdd:PRK00843   6 HWIQLPRDVVVGHGVLDDIGDVCSDLKLTGRALIVTGPTTKKIAGDRVEENLEDAGD-VEVVIVDEATMEEVEKVEEKAk 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  86 -EGCGFLAGVGGGRPVDLAKQAGYHLDLPFISVPTAASHDGFASARASIRAAGQKTSMEARPPIAVVADTTIIASAPRRL 164
Cdd:PRK00843  85 dVNAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGKPVSVKAKPPLAVIADTEIIAKAPYRL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 165 LAAGIGDIVSNQTAVLDWQLG-RDRGEEYSAYAAALSEMTARLVEENSGLVAEGGEEGVRLVVKALISSGVAMSIAGSSR 243
Cdd:PRK00843 165 LAAGCGDIISNYTAVKDWRLAhRLRGEYYSEYAAALSLMTAKMLIENADIIKPGLEESARLVVKALISSGVAMSIAGSSR 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 244 PASGGEHKFSHWLDANASSPALHGEQCGVGSIVTMQLHGGDWERIRDTLAAAGAPISAEQLGFGDDIVLQALCEAKTIRP 323
Cdd:PRK00843 245 PASGSEHLFSHALDRLAPGPALHGEQCGVGTIIMMYLHGGDWRKIRDALKKIGAPTTAKELGIDDEYIIEALTIAHTIRP 324

                        330       340
                 ....*....|....*....|....*.
gi 167045371 324 QRYTILDRE--SPEKIEQAARETGVV 347
Cdd:PRK00843 325 ERYTILGDRglTREAAEKAARITGVI 350
Gro1PDH cd08173
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ...
 11-346 8.37e-153

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: 433.13  E-value: 8.37e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  11 LPRMVVTGPGVIEQLPAVIAELDLPERGLLVCDAVTRKVAGDRVLAYLEETGhpVAVIEIDGASMEELARVE-----AAA 85
Cdd:cd08173    1 LPRNVVVGHGAINKIGEVLKKLLLGKRALIITGPNTYKIAGKRVEDLLESSG--VEVVIVDIATIEEAAEVEkvkklIKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  86 EGCGFLAGVGGGRPVDLAKQAGYHLDLPFISVPTAASHDGFASARASIRAAGQKTSMEARPPIAVVADTTIIASAPRRLL 165
Cdd:cd08173   79 SKADFIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIKGGDKPYSIKAKAPIAIIADTEIISKAPKRLL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 166 AAGIGDIVSNQTAVLDWQLGRD-RGEEYSAYAAALSEMTARLVEENSGLVAEGGEEGVRLVVKALISSGVAMSIAGSSRP 244
Cdd:cd08173  159 AAGCGDLISNITAVKDWRLAHRlKGEYYSEYAASLALMSAKLIIENADLIKPGLEEGVRTVVKALISSGVAMSIAGSSRP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 245 ASGGEHKFSHWLDANASSPALHGEQCGVGSIVTMQLHGGDWERIRDTLAAAGAPISAEQLGFGDDIVLQALCEAKTIRPQ 324
Cdd:cd08173  239 ASGSEHLFSHALDKLAPGPALHGEQCGVGTIMMAYLHGGDWKEIREALKKIGAPTTAKELGLDKEIIIEALTIAHKIRPE 318

                        330       340
                 ....*....|....*....|....
gi 167045371 325 RYTILDRE--SPEKIEQAARETGV 346
Cdd:cd08173  319 RYTILGDNglTEEAAERLARITGV 342
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 7-344 2.02e-104

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: 310.56  E-value: 2.02e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   7 RSMVLPRMVVTGPGVIEQLPAVIAELDlpERGLLVCDAVTRKVAGDRVLAYLEETGHPVAVIEIDG-ASMEELARV--EA 83
Cdd:COG0371    1 RVIILPRRYVQGEGALDELGEYLADLG--KRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGeCSEEEIERLaeEA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  84 AAEGCGFLAGVGGGRPVDLAKQAGYHLDLPFISVPTAASHDGFASARA---SIRAAGQKTSMEARPPIAVVADTTIIASA 160
Cdd:COG0371   79 KEQGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSviyTEDGAFDGYSFLAKNPDLVLVDTDIIAKA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 161 PRRLLAAGIGDIVSNQTAVLDWQLGRD--RGEEYSAYAAALSEMTARLVEENSGL----VAEG--GEEGVRLVVKALISS 232
Cdd:COG0371  159 PVRLLAAGIGDALAKWYEARDWSLAHRdlAGEYYTEAAVALARLCAETLLEYGEAaikaVEAGvvTPALERVVEANLLLS 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 233 GVAMSIaGSSRPASGGEHKFSHWLDA-NASSPALHGEQCGVGSIVTMQLHGGD--WERIRDTLAAAGAPISAEQLGFGDD 309
Cdd:COG0371  239 GLAMGI-GSSRPGSGAAHAIHNGLTAlPETHHALHGEKVAFGTLVQLVLEGRPeeIEELLDFLRSVGLPTTLADLGLDDE 317

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 167045371 310 IVLQALCEAKTIRPQRYTILDRE---SPEKIEQAARET 344
Cdd:COG0371  318 TEEELLTVAEAARPERYTILNLPfevTPEAVEAAILAT 355
G1PDH_related cd08549
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ...
 12-335 8.84e-95

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: 285.23  E-value: 8.84e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  12 PRMVVTGPGVIEQLPAVIAELDLpERGLLVCDAVTRKVAGDRVLAYLEETGHPVAVIEIDGASMEelaRVEAAAEGCgfL 91
Cdd:cd08549    1 PRYTIVGDGAINKIEEILKKLNL-KRVLIITGKNTKAKYCRFFYDQLKTVCDIVYYDNIDNLEDE---LKKYTFYDC--V 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  92 AGVGGGRPVDLAKQAGYHLDLPFISVPTAASHDGFASARASIRAAGQKTSMEARPPIAVVADTTIIASAPRRLLAAGIGD 171
Cdd:cd08549   75 IGIGGGRSIDTGKYLAYKLKIPFISVPTSASNDGIASPIVSLRIPGVKKTFMADAPIAIIADTEIIKKSPRRLLSAGIGD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 172 IVSNQTAVLDWQLG-RDRGEEYSAYAAALSEMTARLVEENSgLVAEGGEEGVRLVVKALISSGVAMSIAGSSRPASGGEH 250
Cdd:cd08549  155 LVSNITAVLDWKLAhKEKGEKYSEFAAILSKTSAKELVSYV-LKASDLEEYHRVLVKALVGSGIAMAIAGSSRPASGSEH 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 251 KFSHWLD----ANASSPALHGEQCGVGSIVTMQLHG-------GDWERIRDTLAAAGAPISAEQLGFGDDIVLQALCEAK 319
Cdd:cd08549  234 LFSHALDklkeEYLNINVLHGEQVGVGTIIMSYLHEkenkklsGLHERIKMILKKVGAPTTAKQLGIDEDLIIEALTEAH 313

                        330
                 ....*....|....*.
gi 167045371 320 TIRPQRYTILDRESPE 335
Cdd:cd08549  314 KIRPRRYTLLDGLSRE 329
G1PDH-like cd08174
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ...
 18-340 1.68e-87

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: 266.69  E-value: 1.68e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  18 GPGVIEQLPAVIAELDLPERGLLVC-DAVTRKVAGDRVLAYLEETGHPVAVIEIDGASMEELARVEAAAEGCGFLAGVGG 96
Cdd:cd08174    7 EEGALEHLGKYLADRNQGFGKVAIVtGEGIDELLGEDILESLEEAGEIVTVEENTDNSAEELAEKAFSLPKVDAIVGIGG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  97 GRPVDLAKQAGYHLDLPFISVPTAASHDGFASARASIRAAGQKTSMEARPPIAVVADTTIIASAPRRLLAAGIGDIVSNQ 176
Cdd:cd08174   87 GKVLDVAKYAAFLSKLPFISVPTSLSNDGIASPVAVLKVDGKRKSLGAKMPYGVIVDLDVIKSAPRRLILAGIGDLISNI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 177 TAVLDWQLGRDRG-EEYSAYAAALSEMTARLV--EENSGLvaeGGEEGVRLVVKALISSGVAMSIAGSSRPASGGEHKFS 253
Cdd:cd08174  167 TALYDWKLAEEKGgEPVDDFAYLLSRTAADSLlnTPGKDI---KDDEFLKELAESLVLSGIAMEIAGSSRPASGSEHLIS 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 254 HWLDANASSPALHGEQCGVGSIVTMQLHGGDWERIRDTLAAAGAPISAEQLGFGDDIVLQALCEAKTIRPQRYTILD--R 331
Cdd:cd08174  244 HALDKLFPGPALHGIQVGLGTYFMSFLQGQRYEEIRDVLKRTGFPLNPSDLGLTKEEFIEAVKLAPSTRPGRYTILEelD 323


                 ....*....
gi 167045371 332 ESPEKIEQA 340
Cdd:cd08174  324 LSEERLKEI 332
G1PDH cd08175
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ...
 15-330 6.57e-85

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: 260.14  E-value: 6.57e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  15 VVTGPGVIEQLPAVIAELDLPERGLLVCDAVTRKVAGDRVLAYLEETGHPVAVIEIDG-----ASMEELARVEAAAEG-C 88
Cdd:cd08175    4 IVIGEGALKKLPEYLKELFGGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGegdliADEAAVGKVLLELEKdT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  89 GFLAGVGGGRPVDLAKQAGYHLDLPFISVPTAASHDGFASARASIRAAGQKTSMEARPPIAVVADTTIIASAPRRLLAAG 168
Cdd:cd08175   84 DLIIAVGSGTINDLTKYAAYKLGIPYISVPTAPSMDGYTSSGAPIIVDGVKKTFPAHAPKAIFADLDVLANAPQRMIAAG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 169 IGDIVSNQTAVLDWQLGRDRGEEYsaYAAALSEMTARLVEE---NSGLVAEGGEEGVRLVVKALISSGVAMSIAGSSRPA 245
Cdd:cd08175  164 FGDLLGKYTALADWKLSHLLGGEY--YCPEVADLVQEALEKcldNAEGIAARDPEAIEALMEALILSGLAMQLVGNSRPA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 246 SGGEHKFSHWLD----ANASSPALHGEQCGVGSIVTM------QLHggDWERIRDTLAAAGAPISAEQLGFGDDIVLQAL 315
Cdd:cd08175  242 SGAEHHLSHYWEmeflRLGKPPVLHGEKVGVGTLLIAalyileQLP--PPEELRELLRKAGAPTTPEDLGIDRDLLRDSL 319

                        330
                 ....*....|....*
gi 167045371 316 CEAKTIRPqRYTILD 330
Cdd:cd08175  320 RLAKEIRD-RYTVLD 333
Fe-ADH_2 pfam13685
Iron-containing alcohol dehydrogenase;
16-271 2.61e-72

Iron-containing alcohol dehydrogenase;


Pssm-ID: 404557 [Multi-domain]  Cd Length: 251  Bit Score: 224.87  E-value: 2.61e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   16 VTGPGVIEQLPAVIAELDLpERGLLVCDAVTRKVAGDRVLAYLEETG-HPVAVIEIDG-ASMEELARVEAAAE--GCGFL 91
Cdd:pfam13685   1 VIGPGALGRLGEYLAELGF-RRVALVADANTYAAAGRKVAESLKRAGiEVETRLEVAGnADMETAEKLVGALRerDADAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   92 AGVGGGRPVDLAKQAGYHLDLPFISVPTAASHDGFASARASIRAAGQKTSMEARPPIAVVADTTIIASAPRRLLAAGIGD 171
Cdd:pfam13685  80 VGVGGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASLTVDGKKRSIPAAAPFGVIADTDVIAAAPRRLLASGVGD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  172 IVSNQTAVLDWQLGRDrgeeySAYAAALSEMTARLVEENsglVAEGGEEGVRLVVKALISSGVAMSIAGSSRPASGGEHK 251
Cdd:pfam13685 160 LLAKITAVADWELAHA-----EEVAAPLALLSAAMVMNF---ADRPLRDPGDIEALAELLSALAMGGAGSSRPASGSEHL 231

                         250       260
                  ....*....|....*....|
gi 167045371  252 FSHWLDANASSPALHGEQCG 271
Cdd:pfam13685 232 ISHALDMIAPKQALHGEQVG 251
GlyDH cd08170
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ...
 16-171 2.05e-30

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: 118.28  E-value: 2.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  16 VTGPGVIEQLPAVIAelDLPERGLLVCDAVTRKVAGDRVLAYLEETGHPVAVIEIDG-ASMEELARV--EAAAEGCGFLA 92
Cdd:cd08170    5 VQGPGALDRLGEYLA--PLGKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFGGeCSREEIERLaaIARANGADVVI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  93 GVGGGRPVDLAKQAGYHLDLPFISVPTAASHDGfasarasiraagqKTSMEA----------------RPPIAVVADTTI 156
Cdd:cd08170   83 GIGGGKTIDTAKAVADYLGLPVVIVPTIASTDA-------------PCSALSviytedgefdeylflpRNPDLVLVDTEI 149

                        170
                 ....*....|....*
gi 167045371 157 IASAPRRLLAAGIGD 171
Cdd:cd08170  150 IAKAPVRFLVAGMGD 164
GlyDH-like cd08550
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ...
 12-344 5.43e-27

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: 109.16  E-value: 5.43e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  12 PRMVVTGPGVIEQLPAVIAELDlpERGLLVCDAVTRKVAGDRVLAYLEETGHPVAVIEIDG-ASMEELARVEAAAEGCG- 89
Cdd:cd08550    1 PGRYIQEPGILAKAGEYIAPLG--KKALIIGGKTALEAVGEKLEKSLEEAGIDYEVEVFGGeCTEENIERLAEKAKEEGa 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  90 -FLAGVGGGRPVDLAKQAGYHLDLPFISVPTAA-------------SHDGFASARASiraagqktsmEARPPIAVVADTT 155
Cdd:cd08550   79 dVIIGIGGGKVLDTAKAVADRLGLPVVTVPTIAatcaawsalsvlyDEEGEFLGYSL----------LKRSPDLVLVDTD 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 156 IIASAPRRLLAAGIGD-------IVSNQTAvldwqlGRDRGEEYSAYAAAlsEMTARLVEENSGLVAEGGEEGVrlVVKA 228
Cdd:cd08550  149 IIAAAPVRYLAAGIGDtlakwyeARPSSRG------GPDDLALQAAVQLA--KLAYDLLLEYGVQAVEDVRQGK--VTPA 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 229 LIS--------SGVAMSIaGSSRPASGGEHKFSH---WLDANAssPALHGEQCGVGSIVTMQLHGGDWERIRDTLAAA-- 295
Cdd:cd08550  219 LEDvvdaiillAGLVGSL-GGGGCRTAAAHAIHNgltKLPETH--GTLHGEKVAFGLLVQLALEGRSEEEIEELIEFLrr 295

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 167045371 296 -GAPISAEQLGFGDDIV-LQALCEAKTIRPQRYTIL-DRESPEKIEQAARET 344
Cdd:cd08550  296 lGLPVTLEDLGLELTEEeLRKIAEYACDPPDMAHMLpFPVTPEMLAEAILAA 347
gldA PRK09423
glycerol dehydrogenase; Provisional
 6-171 1.78e-26

glycerol dehydrogenase; Provisional


Pssm-ID: 181843  Cd Length: 366  Bit Score: 107.98  E-value: 1.78e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   6 PRSMVLPRMVVTGPGVIEQLPAVIAelDLPERGLLVCDAVTRKVAGDRVLAYLEETGHPVAVIEIDG-ASMEELARVEAA 84
Cdd:PRK09423   2 DRIFISPSKYVQGKGALARLGEYLK--PLGKRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNGeCSDNEIDRLVAI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  85 AE--GCGFLAGVGGGRPVDLAKQAGYHLDLPFISVPTAASHDGfasarasiraagqKTS----------------MEARP 146
Cdd:PRK09423  80 AEenGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDA-------------PTSalsviyteegeferylFLPKN 146

                        170       180
                 ....*....|....*....|....*
gi 167045371 147 PIAVVADTTIIASAPRRLLAAGIGD 171
Cdd:PRK09423 147 PDLVLVDTAIIAKAPARFLAAGIGD 171
DHQ_Fe-ADH cd07766
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ...
 12-309 3.73e-17

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: 80.10  E-value: 3.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  12 PRMVVTGPGVIEQLPAVIaeLDLPERGLLVCDAVTRKVAGDRVLAYLEEtGHPVAVIEIDG--ASMEELAR-VEAA-AEG 87
Cdd:cd07766    1 PTRIVFGEGAIAKLGEIK--RRGFDRALVVSDEGVVKGVGEKVADSLKK-GLAVAIFDFVGenPTFEEVKNaVERArAAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  88 CGFLAGVGGGRPVDLAKQAGYHL--DLPFISVPTAASHDGFASARASIRAAGQKTSME--ARPPIAVVADTTIIASAPRR 163
Cdd:cd07766   78 ADAVIAVGGGSTLDTAKAVAALLnrGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVgpHYNPDVVFVDTDITKGLPPR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 164 LLAAGIGDivsnqtavldwqlgrdrgeeysayaaALSEMTARlveensglvaeggeegvrlvvKALISSGVAMSIAGSSR 243
Cdd:cd07766  158 QVASGGVD--------------------------ALAHAVEL---------------------EKVVEAATLAGMGLFES 190

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167045371 244 PASGGEHKFSHWLDanASSPALHGEQCGVGSIVTMQLH-------GGDWERIRDTLAAAGAPISAEQLGFGDD 309
Cdd:cd07766  191 PGLGLAHAIGHALT--AFEGIPHGEAVAVGLPYVLKVAndmnpepEAAIEAVFKFLEDLGLPTHLADLGVSKE 261
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
12-309 8.03e-15

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 74.56  E-value: 8.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   12 PRMVVTGPGVIEQLPAVIAELDLpeRGLLVCDAVTRKV-AGDRVLAYLEETGhpVAVIEIDGASME-ELARVEAAAE--- 86
Cdd:pfam00465   1 PTRIVFGAGALAELGEELKRLGA--RALIVTDPGSLKSgLLDKVLASLEEAG--IEVVVFDGVEPEpTLEEVDEAAAlar 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   87 --GCGFLAGVGGGRPVDLAKQAGYHLD------------------LPFISVPTAASHDGFASARA--SIRAAGQKTSMEA 144
Cdd:pfam00465  77 eaGADVIIAVGGGSVIDTAKAIALLLTnpgdvwdylggkpltkpaLPLIAIPTTAGTGSEVTPLAviTDTETGEKLGIFS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  145 RP--PIAVVADTTIIASAPRRLLAAGIGDIVSnqTAVldwqlgrdrgEEY-----SAYAAALSEMTARLVEENSG-LVAE 216
Cdd:pfam00465 157 PKllPDLAILDPELTLTLPPRLTAATGMDALA--HAV----------EAYvskgaNPLTDALALEAIRLIAENLPrAVAD 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  217 GGEEGVRL-VVKALISSGVAMSIAGS------SRPASGGEH---------KFSHWLDANASSPALHGEQCG--VGSIVTM 278
Cdd:pfam00465 225 GEDLEAREnMLLASTLAGLAFSNAGLgaahalAHALGGRYGiphglanaiLLPYVLRFNAPAAPEKLAQLAraLGEDSDE 304

                         330       340       350
                  ....*....|....*....|....*....|.
gi 167045371  279 QLHGGDWERIRDTLAAAGAPISAEQLGFGDD 309
Cdd:pfam00465 305 EAAEEAIEALRELLRELGLPTTLSELGVTEE 335
GlyDH-like cd08171
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 50-344 2.17e-13

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: 341450  Cd Length: 345  Bit Score: 70.24  E-value: 2.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  50 AGDRVLAYLEETGhpvavIEIDG-------ASMEELARVEAAAEGCGF--LAGVGGGRPVDLAKQAGYHLDLPFISVPTA 120
Cdd:cd08171   37 AKPKLRAALEGSG-----LEITDfiwyggeATYENVEKLKANPEVQEAdmIFAVGGGKAIDTVKVLADRLNKPVFTFPTI 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 121 AS--------------HDGFasarasiraagQKTSMEARPPIAVVADTTIIASAPRRLLAAGIGDIVSNQTAVldwqlgr 186
Cdd:cd08171  112 ASncaavtavsvmynpDGSF-----------KEYYFLKRPPVHTFIDTEIIAEAPEKYLWAGIGDTLAKYYEV------- 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 187 drgeEYSAYAAALsEMTARLVEENSGLVAEG----GEEGVR------------------LVVKALIS--------SGVAM 236
Cdd:cd08171  174 ----EFSARGDEL-DHTNALGVAISKMCSEPllkyGVQALEdcrankvsdaleqvvldiIVTTGLVSnlvepdynSSLAH 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 237 SI--AGSSRPASGGEHkfshwldanasspaLHGEQCGVGSIVTMQLHG--GDWERIRDTLAAAGAPISAEQLGFGDD--- 309
Cdd:cd08171  249 ALyyGLTTLPQIEEEH--------------LHGEVVSYGVLVLLTVDGqfEELEKVYAFNKSIGLPTCLADLGLTVEdle 314

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 167045371 310 IVLQALCEAKTIRPQRYTIldreSPEKIEQAARET 344
Cdd:cd08171  315 KVLDKALKTKDLRHSPYPI----TKEMFEEAIKDL 345
GlyDH-like cd08172
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 16-171 7.66e-13

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: 68.70  E-value: 7.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  16 VTGPGVIEQLPAVIAELDLpERGLLVCDAVTRKVAgdrvLAYL-EETGHPVAVIEIDG-ASMEELARV--EAAAEGCGFL 91
Cdd:cd08172    5 ICEEGALKELPELLSEFGI-KRPLIIHGEKSWQAA----KPYLpKLFEIEYPVLRYDGeCSYEEIDRLaeEAKEHQADVI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  92 AGVGGGRPVDLAKQAGYHLDLPFISVPTAAS------------HDGfasarasiraaGQKTSME--ARPPIAVVADTTII 157
Cdd:cd08172   80 IGIGGGKVLDTAKAVADKLNIPLILIPTLASncaawtplsviyDED-----------GEFIGYDyfPRSAYLVLVDPRLL 148

                        170
                 ....*....|....
gi 167045371 158 ASAPRRLLAAGIGD 171
Cdd:cd08172  149 LDSPKDYFVAGIGD 162
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 15-315 7.66e-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: 62.41  E-value: 7.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  15 VVTGPGVIEQLPAVIAELDLPERGLLVCDAVTRKVAGDRVLAYLEETGHPVAVIEIDGA----SMEELARVEAAAEGCGF 90
Cdd:COG0337   15 IRIGRGLLDELGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGeaskTLETLERILDALLEAGL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  91 -----LAGVGGGRPVDLAkqaG-----YHLDLPFISVPT-------AAshdgfasarasiraAGQKTSMEAR-------- 145
Cdd:COG0337   95 drddlVVALGGGVVGDLA---GfaaatYLRGVPFIQVPTtllaqvdSS--------------VGGKTGVNHPggknliga 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 146 --PPIAVVADTTIIASAPRRLLAAGIGDIV---------------SNQTAVLdwqlgrDRGEEYSAYAAALS-EMTARLV 207
Cdd:COG0337  158 fhQPRAVLIDLDFLKTLPERELRAGLAEVIkygliadaeffewleENADALL------ARDPEALEEAIARScEIKAEVV 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 208 EENsglvaEgGEEGVRlvvkALISSGvamsiagssrpasggeHKFSHWLDANASSPALHGEQCGVGSIVTMQL---HG-- 282
Cdd:COG0337  232 AAD-----E-RESGLR----ALLNFG----------------HTFGHAIEAATGYRLLHGEAVAIGMVFAARLsarLGll 285

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 167045371 283 --GDWERIRDTLAAAGAPISAEQLGFGDdiVLQAL 315
Cdd:COG0337  286 seEDVERIRALLEALGLPTRLPALDPEA--LLAAM 318
EutG COG1454
Alcohol dehydrogenase, class IV [Energy production and conversion];
8-121 3.60e-10

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


Pssm-ID: 441063 [Multi-domain]  Cd Length: 381  Bit Score: 60.52  E-value: 3.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   8 SMVLPRMVVTGPGVIEQLPAVIAELDLpERGLLVCDAVTRKvAG--DRVLAYLEETGHPVAVIeiDGASME-ELARVEAA 84
Cdd:COG1454    4 TFRLPTRIVFGAGALAELGEELKRLGA-KRALIVTDPGLAK-LGllDRVLDALEAAGIEVVVF--DDVEPNpTVETVEAG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  85 AE-----GCGFLAGVGGGRPVDLAK----QAGYHLD--------------LPFISVPTAA 121
Cdd:COG1454   80 AAaarefGADVVIALGGGSAIDAAKaialLATNPGDledylgikkvpgppLPLIAIPTTA 139
Fe-ADH cd08551
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ...
 12-121 1.21e-08

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.


Pssm-ID: 341481 [Multi-domain]  Cd Length: 372  Bit Score: 55.92  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  12 PRMVVTGPGVIEQLPAVIAELDLpERGLLVCDAVTRKvAG--DRVLAYLEETGHPVAVI-EIDG----ASMEELARVeAA 84
Cdd:cd08551    1 PTRIVFGAGALARLGEELKALGG-KKVLLVTDPGLVK-AGllDKVLESLKAAGIEVEVFdDVEPnptvETVEAAAEL-AR 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167045371  85 AEGCGFLAGVGGGRPVDLAKQA------GYHLD------------LPFISVPTAA 121
Cdd:cd08551   78 EEGADLVIAVGGGSVLDTAKAIavlatnGGSIRdyegigkvpkpgLPLIAIPTTA 132
Fe-ADH-like cd14863
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 8-121 1.48e-08

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: 55.62  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   8 SMVLPRMVVTGPGVIEQLPAVIAELDLpERGLLVCDAVTRKvAG--DRVLAYLEETGHPVAV---IEID--GASMEELAR 80
Cdd:cd14863    1 TYSQLTPVIFGAGAVEQIGELLKELGC-KKVLLVTDKGLKK-AGivDKIIDLLEEAGIEVVVfddVEPDppDEIVDEAAE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  81 VeAAAEGCGFLAGVGGGRPVDLAKQAGY-------------------HLDLPFISVPTAA 121
Cdd:cd14863   79 I-AREEGADGVIGIGGGSVLDTAKAIAVlltnpgpiidyalagppvpKPGIPLIAIPTTA 137
Fe-ADH-like cd08194
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 12-121 4.53e-08

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.


Pssm-ID: 341473 [Multi-domain]  Cd Length: 378  Bit Score: 54.07  E-value: 4.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  12 PRMVVTGPGVIEQLPAVIAELdLPERGLLVCDAVTRKV-AGDRVLAYLEETGHPVAVIeiDGASME-ELARVEAA----- 84
Cdd:cd08194    1 PRTIIIGGGALEELGEEAASL-GGKRALIVTDKVMVKLgLVDKVTQLLAEAGIAYAVF--DDVVSEpTDEMVEEGlalyk 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167045371  85 AEGCGFLAGVGGGRPVDLAKQAG-----------YHL-------DLPFISVPTAA 121
Cdd:cd08194   78 EGGCDFIVALGGGSPIDTAKAIAvlatnggpirdYMGprkvdkpGLPLIAIPTTA 132
Fe-ADH-like cd08196
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 8-121 5.30e-07

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: 341475 [Multi-domain]  Cd Length: 367  Bit Score: 50.66  E-value: 5.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   8 SMVLPRMVVTGPGVIEQLPAVIAELDLpERGLLVCDAVTRKV-AGDRVLAYLEetGHPVAVI-EI----DGASMEELARv 81
Cdd:cd08196    2 SYYQPVKIIFGEGILKELPDIIKELGG-KRGLLVTDPSFIKSgLAKRIVESLK--GRIVAVFsDVepnpTVENVDKCAR- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 167045371  82 EAAAEGCGFLAGVGGGRPVDLAKQAG-----------YHLD--------LPFISVPTAA 121
Cdd:cd08196   78 LARENGADFVIAIGGGSVLDTAKAAAclaktdgsiedYLEGkkkipkkgLPLIAIPTTA 136
Fe-ADH-like cd08183
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 15-121 2.84e-06

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341462 [Multi-domain]  Cd Length: 377  Bit Score: 48.65  E-value: 2.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  15 VVTGPGVIEQLPAVIAELDlpERGLLVCDA-VTRKVAGDRVLAYLEETGhpVAVIEIDGASMEELARVEAAAE-----GC 88
Cdd:cd08183    4 IVFGRGSLQELGELAAELG--KRALLVTGRsSLRSGRLARLLEALEAAG--IEVALFSVSGEPTVETVDAAVAlareaGC 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167045371  89 GFLAGVGGGRPVDLAK-------QAGYHLD---------------LPFISVPTAA 121
Cdd:cd08183   80 DVVIAIGGGSVIDAAKaiaalltNEGSVLDylevvgkgrplteppLPFIAIPTTA 134
Fe-ADH-like cd08189
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 14-121 4.24e-05

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 belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.


Pssm-ID: 341468 [Multi-domain]  Cd Length: 378  Bit Score: 44.77  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  14 MVVTGPGVIEQLPAVIAELDLpERGLLVCDAVTRKvAG--DRVLAYLEETGHPVAV---------IEIdgasmeelarVE 82
Cdd:cd08189    7 ELFEGAGSLLQLPEALKKLGI-KRVLIVTDKGLVK-LGllDPLLDALKKAGIEYVVfdgvvpdptIDN----------VE 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167045371  83 AAAE-----GC-GFLAgVGGGRPVDLAKQAG-------------------YHLDLPFISVPTAA 121
Cdd:cd08189   75 EGLAlykenGCdAIIA-IGGGSVIDCAKVIAaraanpkksvrklkgllkvRKKLPPLIAVPTTA 137
PPD-like cd08181
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ...
 9-121 4.30e-05

1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1,3-propanediol dehydrogenase (PPD) which is a member of the iron-containing alcohol dehydrogenase superfamily, and exhibits a dehydroquinate synthase-like fold. Protein sequence similarity search and other biochemical evidences suggest that they are close to the iron-containing 1,3-propanediol dehydrogenase (EC 1.1.1.202). 1,3-propanediol dehydrogenase catalyzes the oxidation of propane-1,3-diol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. The protein structure of Thermotoga maritima TM0920 gene contains one NADP+ and one iron ion.


Pssm-ID: 341460 [Multi-domain]  Cd Length: 358  Bit Score: 44.88  E-value: 4.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   9 MVLPRMVVTGPGVIEQLPAVIAELDlpERGLLVCDAVTRKVAG--DRVLAYLEETGHPVAV---IEIDgASME------E 77
Cdd:cd08181    1 FYMPTKVYFGKNCVEKHADELAALG--KKALIVTGKHSAKKNGslDDVTEALEENGIEYFIfdeVEEN-PSIEtvekgaE 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167045371  78 LARveaaAEGCGFLAGVGGGRPVDLAK----------------QAGYHLD-LPFISVPTAA 121
Cdd:cd08181   78 LAR----KEGADFVIGIGGGSPLDAAKaiallaankdgdedlfQNGKYNPpLPIVAIPTTA 134
DHQ-like cd08169
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ...
 32-275 1.00e-04

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: 43.55  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  32 LDLPERGLLVCDA-VTRKVAGD--RVLAYLEEtgHPVAVIEIDGA-----SMEELARVEAAAEGC--GFLAGVGGGRPVD 101
Cdd:cd08169   20 RDAFDQCLIIVDSgVPDLIVNYlaEYFGYYLE--VHVFIIQGGEAyktfqTVVEELERAAALHLNrhSAVVAVGGGATGD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 102 LAKQAG--YHLDLPFISVPT---AASHDGFASARASIRAAGQKTSMEARPPIAVVADTTIIASAPRRLLAAGIGDIVSNq 176
Cdd:cd08169   98 VVGFAAatYFRGIAFIRVPTtllAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFLKTLPFRQVRAGMAELVKM- 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371 177 tAVLdwqLGRDRGEEYSAYAAALSEMTARLVEEnsgLVAEGGEEGVRLVVKALISSGVamsiagsSRPASGGeHKFSHWL 256
Cdd:cd08169  177 -ALI---ADNDFFEFLEDKANSATVYSPEQLEK---LINKCISLKLDVVVADEDEQGK-------RRGLNYG-HTFGHAL 241

                        250
                 ....*....|....*....
gi 167045371 257 DANASSPALHGEQCGVGSI 275
Cdd:cd08169  242 ELASGYKIPHGEAVAVGMA 260
DOIS cd08197
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ...
 18-175 1.11e-04

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: 43.73  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  18 GPGVIEQLPAVIAELDLpERGLLVCDAVTRKVAGDRVLAYLEETGHPVAVIEI-DGASMEELARVEAAAE---GCGF--- 90
Cdd:cd08197    7 GRGILESLLSILEELKA-DRHFLVTDSNVNDLYGDRLLEGLKKAGIPVELLVVpAGESNKTLSTLTELAErliAAGItrr 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  91 --LAGVGGGRPVDLAKQA------GyhldLPFISVPTA--ASHDGfasarasirAAGQKTSMEAR----------PPIAV 150
Cdd:cd08197   86 svIIALGGGVVGNIAGLLagllyrG----IRLVHVPTTllAQSDS---------VLSLKQAVNGKsgknlvgsyyAPLFV 152

                        170       180
                 ....*....|....*....|....*
gi 167045371 151 VADTTIIASAPRRLLAAGIGDIVSN 175
Cdd:cd08197  153 FVDTEFLKTLPPRQIRSGLCEAIKN 177
Fe-ADH-like cd14865
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 15-121 3.48e-04

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: 341487 [Multi-domain]  Cd Length: 383  Bit Score: 42.14  E-value: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  15 VVTGPGVIEQLPAVIAELDLpERGLLVCDAVTRKvAG--DRVLAYLEETGHPVAVI-EI----DGASMEELARVeAAAEG 87
Cdd:cd14865    9 IVSGAGALENLPAELARLGA-RRPLIVTDKGLAA-AGllKKVEDALGDAIEIVGVFdDVppdsSVAVVNEAAAR-AREAG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 167045371  88 C-GFLAgVGGGRPVDLAK-------QAGYHLD------------LPFISVPTAA 121
Cdd:cd14865   86 AdGIIA-VGGGSVIDTAKgvnillsEGGDDLDdygganrltrplKPLIAIPTTA 138
PRK10586 PRK10586
putative oxidoreductase; Provisional
 81-171 6.07e-04

putative oxidoreductase; Provisional


Pssm-ID: 182570  Cd Length: 362  Bit Score: 41.25  E-value: 6.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  81 VEAAAEGCGFLAGVGGGRPVDLAKQAGYHLDLPFISVPT-AASHDGFASARASIRAAGQKTSMEARPPI--AVVADTTII 157
Cdd:PRK10586  80 AAASGDDRQVVIGVGGGALLDTAKALARRLGLPFVAIPTiAATCAAWTPLSVWYNDAGQALHFEIFDDAnfLVLVEPRII 159

                         90
                 ....*....|....
gi 167045371 158 ASAPRRLLAAGIGD 171
Cdd:PRK10586 160 LNAPQEYLLAGIGD 173
HEPD cd08182
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ...
 15-121 7.75e-04

Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.


Pssm-ID: 341461 [Multi-domain]  Cd Length: 370  Bit Score: 41.06  E-value: 7.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  15 VVTGPGVIEQLPAVIAELDlPERGLLVCDAvtRKVAGDRVLAYLEETGHPVAVIEIDG-------ASMEELARvEAAAEG 87
Cdd:cd08182    4 IIFGPGALAELKDLLGGLG-ARRVLLVTGP--SAVRESGAADILDALGGRIPVVVFSDfspnpdlEDLERGIE-LFRESG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 167045371  88 CGFLAGVGGGRPVDLAK--------------------QAGYHLDLPFISVPTAA 121
Cdd:cd08182   80 PDVIIAVGGGSVIDTAKaiaallgspgenllllrtgeKAPEENALPLIAIPTTA 133
Fe-ADH-like cd08185
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 18-104 1.05e-03

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341464 [Multi-domain]  Cd Length: 379  Bit Score: 40.56  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  18 GPGVIEQLPAVIAELDlpERGLLVCDAVTRKVAG--DRVLAYLEETGhpVAVIEIDGAS--------ME--ELARveaaA 85
Cdd:cd08185   10 GAGKLNELGEEALRPG--KKALIVTGKGSSKKTGllDRVKKLLEKAG--VEVVVFDKVEpnpltttvMEgaALAK----E 81

                         90
                 ....*....|....*....
gi 167045371  86 EGCGFLAGVGGGRPVDLAK 104
Cdd:cd08185   82 EGCDFVIGLGGGSSMDAAK 100
MAR cd08177
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ...
 15-119 1.17e-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: 40.18  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  15 VVTGPGVIEQLPAVIAELDLpERGLLVCDAvTRKVAGDRVLAYLeetgHPVAVIEIDGASM---EELAR--VEAAAE-GC 88
Cdd:cd08177    4 VVFGAGTLAELAEELERLGA-RRALVLSTP-RQRALAERVAALL----GDRVAGVFDGAVMhvpVEVAEraLAAAREaGA 77

                         90       100       110
                 ....*....|....*....|....*....|.
gi 167045371  89 GFLAGVGGGRPVDLAKQAGYHLDLPFISVPT 119
Cdd:cd08177   78 DGLVAIGGGSAIGLAKAIALRTGLPIVAVPT 108
Fe-ADH-like cd08191
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 11-121 1.69e-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: 39.90  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  11 LPRMVVTGPGVIEQLPAVIAELDLpeRGLLVCDAVTRKVAG-DRVLAYLEETGHPVAV----IEIDGASMEELARVEAAA 85
Cdd:cd08191    3 SPSRLLFGPGARRALGRVAARLGS--RVLIVTDPRLASTPLvAELLAALTAAGVAVEVfdggQPELPVSTVADAAAAARA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 167045371  86 EGCGFLAGVGGGRPVDLAKQAGYHLD------------------LPFISVPTAA 121
Cdd:cd08191   81 FDPDVVIGLGGGSNMDLAKVVALLLAhggdprdyygedrvpgpvLPLIAVPTTA 134
Fe-ADH-like cd14861
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ...
 18-121 2.93e-03

Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.


Pssm-ID: 341483 [Multi-domain]  Cd Length: 374  Bit Score: 39.03  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  18 GPGVIEQLPAVIAELDLpERGLLVCDAVTRKvAG--DRVLAYLEETGHPVAVI-EIDGASMEelARVEAAAE-----GCG 89
Cdd:cd14861    9 GAGAIAELPEELKALGI-RRPLLVTDPGLAA-LGivDRVLEALGAAGLSPAVFsDVPPNPTE--ADVEAGVAayregGCD 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 167045371  90 FLAGVGGGRPVDLAK----QAGYHLDL------------------PFISVPTAA 121
Cdd:cd14861   85 GIIALGGGSAIDAAKaialMATHPGPLwdyedgeggpaaitpavpPLIAIPTTA 138
Fe-ADH-like cd14864
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 9-174 9.47e-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: 341486 [Multi-domain]  Cd Length: 376  Bit Score: 37.67  E-value: 9.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371   9 MVLPRMVVTGPGVIEQLPAVIAELDlpERGLLVCDAVTRKV-AGDRVLAYLEETGHPVAV-IEIDGASmeELARVEAAAE 86
Cdd:cd14864    1 FKIPPNIVFGADSLERIGEEVKEYG--SRFLLITDPVLKESgLADKIVSSLEKAGISVIVfDEIPASA--TSDTIDEAAE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167045371  87 -----GCGFLAGVGGGRPVDLAKQA-------GYHLD-----------LPFISVPTAAsHDGFASARASIRAAGQKTSME 143
Cdd:cd14864   77 larkaGADGIIAVGGGKVLDTAKAVailanndGGAYDflegakpkkkpLPLIAVPTTP-RSGFEFSDRFPVVDSRSREVK 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 167045371 144 -----ARPPIAVVADTTIIASAPRRLLAAGIGDIVS 174
Cdd:cd14864  156 llkaqPGLPKAVIVDPNLMASLTGNQTAAMALAALA 191
 
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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