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Conserved domains on  [gi|2506145|sp|P45579|]
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RecName: Full=Hydroxycarboxylate dehydrogenase A; AltName: Full=2-oxobutanoate reductase; AltName: Full=2-oxoglutarate reductase

Protein Classification

iron-containing alcohol dehydrogenase( domain architecture ID 10793422)

iron-containing alcohol dehydrogenase catalyzes the iron-dependent reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P) to NAD(P)H; similar to Escherichia coli hydroxycarboxylate dehydrogenase A

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
PRK10586 PRK10586
putative oxidoreductase; Provisional
 1-362 0e+00

putative oxidoreductase; Provisional


:

Pssm-ID: 182570  Cd Length: 362  Bit Score: 699.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145     1 MPHNPIRVVVGPANYFSHPGSFNHLHDFFTDEQLSRAVWIYGKRAIAAAQTKLPPAFGLPGAKHILFRGHCSESDVQQLA 80
Cdd:PRK10586   1 MSHNPIRVVVGPANYFSHPGSIDHLHDFFTDEQLSRAVWIYGERAIAAAQPYLPPAFELPGAKHILFRGHCSESDVAQLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145    81 AESGDDRSVVIGVGGGALLDTAKALARRLGLPFVAVPTIAATCAAWTPLSVWYNDAGQALHYEIFDDANFMVLVEPEIIL 160
Cdd:PRK10586  81 AASGDDRQVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQALHFEIFDDANFLVLVEPRIIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   161 NAPQQYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNAQAIRDVLLNSSEQALSDQQNQQLTQSFCDVVDAIIAGG 240
Cdd:PRK10586 161 NAPQEYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNALAIRDVLLNSSEQALADQQNGQLTQDFCDVVDAIIAGG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   241 GMVGGLGDRFTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDDVLAQLTGAYQRFHLPTTLAELEVDINN 320
Cdd:PRK10586 241 GMVGGLGERYTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDDVLAQLIGAYQRFHLPTTLAELDVDINN 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 2506145   321 QAEIDKVIAHTLRPVESIHYLPVTLTPDTLRAAFKKVESFKA 362
Cdd:PRK10586 321 QAEIDRVIAHTLRPVESIHYLPVTLTPDTLRAAFEKVESFKA 362
 
Name Accession Description Interval E-value
PRK10586 PRK10586
putative oxidoreductase; Provisional
 1-362 0e+00

putative oxidoreductase; Provisional


Pssm-ID: 182570  Cd Length: 362  Bit Score: 699.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145     1 MPHNPIRVVVGPANYFSHPGSFNHLHDFFTDEQLSRAVWIYGKRAIAAAQTKLPPAFGLPGAKHILFRGHCSESDVQQLA 80
Cdd:PRK10586   1 MSHNPIRVVVGPANYFSHPGSIDHLHDFFTDEQLSRAVWIYGERAIAAAQPYLPPAFELPGAKHILFRGHCSESDVAQLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145    81 AESGDDRSVVIGVGGGALLDTAKALARRLGLPFVAVPTIAATCAAWTPLSVWYNDAGQALHYEIFDDANFMVLVEPEIIL 160
Cdd:PRK10586  81 AASGDDRQVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQALHFEIFDDANFLVLVEPRIIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   161 NAPQQYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNAQAIRDVLLNSSEQALSDQQNQQLTQSFCDVVDAIIAGG 240
Cdd:PRK10586 161 NAPQEYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNALAIRDVLLNSSEQALADQQNGQLTQDFCDVVDAIIAGG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   241 GMVGGLGDRFTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDDVLAQLTGAYQRFHLPTTLAELEVDINN 320
Cdd:PRK10586 241 GMVGGLGERYTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDDVLAQLIGAYQRFHLPTTLAELDVDINN 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 2506145   321 QAEIDKVIAHTLRPVESIHYLPVTLTPDTLRAAFKKVESFKA 362
Cdd:PRK10586 321 QAEIDRVIAHTLRPVESIHYLPVTLTPDTLRAAFEKVESFKA 362
GlyDH-like cd08172
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 12-357 5.50e-162

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: 456.98  E-value: 5.50e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   12 PANYFSHPGSFNHLHDFFTDEQLSRAVWIYGKRAIAAAQTKLPPAFGLPgAKHILFRGHCSESDVQQLAAESGDDRS-VV 90
Cdd:cd08172   1 PQEYICEEGALKELPELLSEFGIKRPLIIHGEKSWQAAKPYLPKLFEIE-YPVLRYDGECSYEEIDRLAEEAKEHQAdVI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   91 IGVGGGALLDTAKALARRLGLPFVAVPTIAATCAAWTPLSVWYNDAGQALHYEIFDDANFMVLVEPEIILNAPQQYLLAG 170
Cdd:cd08172  80 IGIGGGKVLDTAKAVADKLNIPLILIPTLASNCAAWTPLSVIYDEDGEFIGYDYFPRSAYLVLVDPRLLLDSPKDYFVAG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  171 IGDTLAKWYEAVVLAPQPETLPLTVRLGINNAQAIRDVLLNSSEQALSDQQNQQLTQSFCDVVDAIIAGGGMVGGLGDRF 250
Cdd:cd08172 160 IGDTLAKWYEADAILRQLEELPAFLQLARQAAKLCRDILLKDSEQALADLEAGKLTPAFIKVVETIIALAGMVGGFGDEY 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  251 TRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDDVLAQLTGAYQRFHLPTTLAELEVDINNQAEIDKVIAH 330
Cdd:cd08172 240 GRSAGAHAIHNGLTKLPETHHFLHGEKVAYGILVQLALEGKWDEIKKLLPFYRRLGLPTSLADLGLTDDTEEALQKIAAF 319

                       330       340
                ....*....|....*....|....*..
gi 2506145  331 TLRPVESIHYLPVTLTPDTLRAAFKKV 357
Cdd:cd08172 320 AASPEESIHLLPPDVTAEEVLQAIEKL 346
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 7-357 6.84e-120

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: 350.62  E-value: 6.84e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145    7 RVVVGPANYFSHPGSFNHLHDFfTDEQLSRAVWIYGKRAIAAAQTKLPPAFGLPG--AKHILFRGHCSESDVQQLAAESG 84
Cdd:COG0371   1 RVIILPRRYVQGEGALDELGEY-LADLGKRALIITGPTALKAAGDRLEESLEDAGieVEVEVFGGECSEEEIERLAEEAK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   85 DDRS-VVIGVGGGALLDTAKALARRLGLPFVAVPTIAATCAAWTPLSVWYNDAGQALHYEIFDDANFMVLVEPEIILNAP 163
Cdd:COG0371  80 EQGAdVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVLVDTDIIAKAP 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  164 QQYLLAGIGDTLAKWYEAVV--LAPQPETLPLTVRLGINNAQAIRDVLLNSSEQALSDQQNQQLTQSFCDVVDAIIAGGG 241
Cdd:COG0371 160 VRLLAAGIGDALAKWYEARDwsLAHRDLAGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLSG 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  242 MVGGLGDRFTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDDVLAQLTGAYQRFHLPTTLAELEVDINNQ 321
Cdd:COG0371 240 LAMGIGSSRPGSGAAHAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGRPEEIEELLDFLRSVGLPTTLADLGLDDETE 319

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 2506145  322 AEIDKVIAHTLRPVESIHYLPVTLTPDTLRAAFKKV 357
Cdd:COG0371 320 EELLTVAEAARPERYTILNLPFEVTPEAVEAAILAT 355
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
12-350 1.06e-38

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 141.20  E-value: 1.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145     12 PANYFSHPGSFNHLHDFFTDEQlSRAVWIYGKRAIAAAQT-KLPPAFGLPGAKHILF---RGHCSESDVQQLAA---ESG 84
Cdd:pfam00465   1 PTRIVFGAGALAELGEELKRLG-ARALIVTDPGSLKSGLLdKVLASLEEAGIEVVVFdgvEPEPTLEEVDEAAAlarEAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145     85 DDrsVVIGVGGGALLDTAKALARRLG------------------LPFVAVPTIAATCAAWTPLSVWYNDAGQAlHYEIFD 146
Cdd:pfam00465  80 AD--VIIAVGGGSVIDTAKAIALLLTnpgdvwdylggkpltkpaLPLIAIPTTAGTGSEVTPLAVITDTETGE-KLGIFS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145    147 DANF--MVLVEPEIILNAPQQYLLAGIGDTLAKWYEAVVlapQPETLPLTVRLGInnaQAIRdVLLNSSEQALSDQQNqq 224
Cdd:pfam00465 157 PKLLpdLAILDPELTLTLPPRLTAATGMDALAHAVEAYV---SKGANPLTDALAL---EAIR-LIAENLPRAVADGED-- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145    225 lTQSFCDVVDA-IIAGGGMVGglgdrfTRVAAAHAVHNGLT-VLPQTEKFLHGTKVAYGI----------LVQSALL--- 289
Cdd:pfam00465 228 -LEARENMLLAsTLAGLAFSN------AGLGAAHALAHALGgRYGIPHGLANAILLPYVLrfnapaapekLAQLARAlge 300

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506145    290 -----GQDDVLAQLTGAYQRFHLPTTLAELEVDinnQAEIDKVIAHTLRPvESIHYLPVTLTPDTL 350
Cdd:pfam00465 301 dsdeeAAEEAIEALRELLRELGLPTTLSELGVT---EEDLDALAEAALRD-RSLANNPRPLTAEDI 362
 
Name Accession Description Interval E-value
PRK10586 PRK10586
putative oxidoreductase; Provisional
 1-362 0e+00

putative oxidoreductase; Provisional


Pssm-ID: 182570  Cd Length: 362  Bit Score: 699.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145     1 MPHNPIRVVVGPANYFSHPGSFNHLHDFFTDEQLSRAVWIYGKRAIAAAQTKLPPAFGLPGAKHILFRGHCSESDVQQLA 80
Cdd:PRK10586   1 MSHNPIRVVVGPANYFSHPGSIDHLHDFFTDEQLSRAVWIYGERAIAAAQPYLPPAFELPGAKHILFRGHCSESDVAQLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145    81 AESGDDRSVVIGVGGGALLDTAKALARRLGLPFVAVPTIAATCAAWTPLSVWYNDAGQALHYEIFDDANFMVLVEPEIIL 160
Cdd:PRK10586  81 AASGDDRQVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQALHFEIFDDANFLVLVEPRIIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   161 NAPQQYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNAQAIRDVLLNSSEQALSDQQNQQLTQSFCDVVDAIIAGG 240
Cdd:PRK10586 161 NAPQEYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNALAIRDVLLNSSEQALADQQNGQLTQDFCDVVDAIIAGG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   241 GMVGGLGDRFTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDDVLAQLTGAYQRFHLPTTLAELEVDINN 320
Cdd:PRK10586 241 GMVGGLGERYTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDDVLAQLIGAYQRFHLPTTLAELDVDINN 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 2506145   321 QAEIDKVIAHTLRPVESIHYLPVTLTPDTLRAAFKKVESFKA 362
Cdd:PRK10586 321 QAEIDRVIAHTLRPVESIHYLPVTLTPDTLRAAFEKVESFKA 362
GlyDH-like cd08172
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 12-357 5.50e-162

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: 456.98  E-value: 5.50e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   12 PANYFSHPGSFNHLHDFFTDEQLSRAVWIYGKRAIAAAQTKLPPAFGLPgAKHILFRGHCSESDVQQLAAESGDDRS-VV 90
Cdd:cd08172   1 PQEYICEEGALKELPELLSEFGIKRPLIIHGEKSWQAAKPYLPKLFEIE-YPVLRYDGECSYEEIDRLAEEAKEHQAdVI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   91 IGVGGGALLDTAKALARRLGLPFVAVPTIAATCAAWTPLSVWYNDAGQALHYEIFDDANFMVLVEPEIILNAPQQYLLAG 170
Cdd:cd08172  80 IGIGGGKVLDTAKAVADKLNIPLILIPTLASNCAAWTPLSVIYDEDGEFIGYDYFPRSAYLVLVDPRLLLDSPKDYFVAG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  171 IGDTLAKWYEAVVLAPQPETLPLTVRLGINNAQAIRDVLLNSSEQALSDQQNQQLTQSFCDVVDAIIAGGGMVGGLGDRF 250
Cdd:cd08172 160 IGDTLAKWYEADAILRQLEELPAFLQLARQAAKLCRDILLKDSEQALADLEAGKLTPAFIKVVETIIALAGMVGGFGDEY 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  251 TRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDDVLAQLTGAYQRFHLPTTLAELEVDINNQAEIDKVIAH 330
Cdd:cd08172 240 GRSAGAHAIHNGLTKLPETHHFLHGEKVAYGILVQLALEGKWDEIKKLLPFYRRLGLPTSLADLGLTDDTEEALQKIAAF 319

                       330       340
                ....*....|....*....|....*..
gi 2506145  331 TLRPVESIHYLPVTLTPDTLRAAFKKV 357
Cdd:cd08172 320 AASPEESIHLLPPDVTAEEVLQAIEKL 346
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 7-357 6.84e-120

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: 350.62  E-value: 6.84e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145    7 RVVVGPANYFSHPGSFNHLHDFfTDEQLSRAVWIYGKRAIAAAQTKLPPAFGLPG--AKHILFRGHCSESDVQQLAAESG 84
Cdd:COG0371   1 RVIILPRRYVQGEGALDELGEY-LADLGKRALIITGPTALKAAGDRLEESLEDAGieVEVEVFGGECSEEEIERLAEEAK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   85 DDRS-VVIGVGGGALLDTAKALARRLGLPFVAVPTIAATCAAWTPLSVWYNDAGQALHYEIFDDANFMVLVEPEIILNAP 163
Cdd:COG0371  80 EQGAdVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVLVDTDIIAKAP 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  164 QQYLLAGIGDTLAKWYEAVV--LAPQPETLPLTVRLGINNAQAIRDVLLNSSEQALSDQQNQQLTQSFCDVVDAIIAGGG 241
Cdd:COG0371 160 VRLLAAGIGDALAKWYEARDwsLAHRDLAGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLSG 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  242 MVGGLGDRFTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDDVLAQLTGAYQRFHLPTTLAELEVDINNQ 321
Cdd:COG0371 240 LAMGIGSSRPGSGAAHAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGRPEEIEELLDFLRSVGLPTTLADLGLDDETE 319

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 2506145  322 AEIDKVIAHTLRPVESIHYLPVTLTPDTLRAAFKKV 357
Cdd:COG0371 320 EELLTVAEAARPERYTILNLPFEVTPEAVEAAILAT 355
GlyDH-like cd08550
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ...
 12-357 1.09e-104

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: 311.39  E-value: 1.09e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   12 PANYFSHPGSFNHLHDFFTdEQLSRAVWIYGKRAIAAAQTKLPPAFGLPG--AKHILFRGHCSESDVQQLAA---ESGDD 86
Cdd:cd08550   1 PGRYIQEPGILAKAGEYIA-PLGKKALIIGGKTALEAVGEKLEKSLEEAGidYEVEVFGGECTEENIERLAEkakEEGAD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   87 rsVVIGVGGGALLDTAKALARRLGLPFVAVPTIAATCAAWTPLSVWYNDAGQALHYEIFDDANFMVLVEPEIILNAPQQY 166
Cdd:cd08550  80 --VIIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSPDLVLVDTDIIAAAPVRY 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  167 LLAGIGDTLAKWYEAVVLAPQPETlPLTVRLGINNAQAIRDVLLNSSEQALSDQQNQQLTQSFCDVVDAIIAGGGMVGGL 246
Cdd:cd08550 158 LAAGIGDTLAKWYEARPSSRGGPD-DLALQAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILLAGLVGSL 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  247 GDRFTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLG-QDDVLAQLTGAYQRFHLPTTLAELEVDInNQAEID 325
Cdd:cd08550 237 GGGGCRTAAAHAIHNGLTKLPETHGTLHGEKVAFGLLVQLALEGrSEEEIEELIEFLRRLGLPVTLEDLGLEL-TEEELR 315

                       330       340       350
                ....*....|....*....|....*....|..
gi 2506145  326 KVIAHTLRPVESIHYLPVTLTPDTLRAAFKKV 357
Cdd:cd08550 316 KIAEYACDPPDMAHMLPFPVTPEMLAEAILAA 347
GlyDH cd08170
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ...
 12-360 2.97e-74

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: 233.84  E-value: 2.97e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   12 PANYFSHPGSFNHLHDFfTDEQLSRAVWIYGKRAIAAAQTKLPPAFGLPGAKHIL--FRGHCSESDVQQLAAESGDDRS- 88
Cdd:cd08170   1 PSRYVQGPGALDRLGEY-LAPLGKKALVIADPFVLDLVGERLEESLEKAGLEVVFevFGGECSREEIERLAAIARANGAd 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   89 VVIGVGGGALLDTAKALARRLGLPFVAVPTIAAT---CAAwtpLSVWYNDAGQALHYEIFDDANFMVLVEPEIILNAPQQ 165
Cdd:cd08170  80 VVIGIGGGKTIDTAKAVADYLGLPVVIVPTIASTdapCSA---LSVIYTEDGEFDEYLFLPRNPDLVLVDTEIIAKAPVR 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  166 YLLAGIGDTLAKWYEA-VVLAPQPETLPLTV--RLGINNAQAIRDVLLNSSEQALSDQQNQQLTQSFCDVVDAIIagggm 242
Cdd:cd08170 157 FLVAGMGDALATYFEArACARSGAPNMAGGRptLAALALAELCYDTLLEYGVAAKAAVEAGVVTPALEAVIEANTllsgl 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  243 vgglgdrftrVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDD-VLAQLTGAYQRFHLPTTLAELEVDINNQ 321
Cdd:cd08170 237 g----fesggLAAAHAIHNGLTALPETHHLLHGEKVAFGTLVQLVLEGRPDeEIEEVIRFCRSVGLPVTLADLGLEDVTD 312

                       330       340       350
                ....*....|....*....|....*....|....*....
gi 2506145  322 AEIDKVIAHTLRPVESIHYLPVTLTPDTLRAAFKKVESF 360
Cdd:cd08170 313 EELRKVAEAACAPGETIHNMPFPVTPEDVVDAILAADAL 351
GlyDH-like cd08171
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 36-357 4.54e-71

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: 225.48  E-value: 4.54e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   36 RAVWIYGKRAIAAAQTKLPPAF---GLPGAKHILFRGHCSESDVQQLAAESGDDRS-VVIGVGGGALLDTAKALARRLGL 111
Cdd:cd08171  24 KVVVIGGKKALAAAKPKLRAALegsGLEITDFIWYGGEATYENVEKLKANPEVQEAdMIFAVGGGKAIDTVKVLADRLNK 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  112 PFVAVPTIAATCAAWTPLSVWYNDAGQALHYEIFDDANFMVLVEPEIILNAPQQYLLAGIGDTLAKWYEaVVLAPQPETL 191
Cdd:cd08171 104 PVFTFPTIASNCAAVTAVSVMYNPDGSFKEYYFLKRPPVHTFIDTEIIAEAPEKYLWAGIGDTLAKYYE-VEFSARGDEL 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  192 PLTVRLGINNAQAIRDVLLNSSEQALSDQQNQQLTQSFCDVVDAIIAGGGMVGGLGDRFTRVAAAHAVHNGLTVLPQTE- 270
Cdd:cd08171 183 DHTNALGVAISKMCSEPLLKYGVQALEDCRANKVSDALEQVVLDIIVTTGLVSNLVEPDYNSSLAHALYYGLTTLPQIEe 262

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  271 KFLHGTKVAYGILVQSALLGQDDVLAQLTGAYQRFHLPTTLAELEVDInnqAEIDKVIAHTLRPVESIHYlPVTLTPDTL 350
Cdd:cd08171 263 EHLHGEVVSYGVLVLLTVDGQFEELEKVYAFNKSIGLPTCLADLGLTV---EDLEKVLDKALKTKDLRHS-PYPITKEMF 338


                ....*..
gi 2506145  351 RAAFKKV 357
Cdd:cd08171 339 EEAIKDL 345
gldA PRK09423
glycerol dehydrogenase; Provisional
 6-353 1.28e-59

glycerol dehydrogenase; Provisional


Pssm-ID: 181843  Cd Length: 366  Bit Score: 196.19  E-value: 1.28e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145     6 IRVVVGPANYFSHPGSFNHLHDF---FTDEQL---SRAVW-IYGKRAIAAAQtklppAFGLPgAKHILFRGHCSESDVQQ 78
Cdd:PRK09423   2 DRIFISPSKYVQGKGALARLGEYlkpLGKRALviaDEFVLgIVGDRVEASLK-----EAGLT-VVFEVFNGECSDNEIDR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145    79 LAAESGDDRS-VVIGVGGGALLDTAKALARRLGLPFVAVPTIAATCAAWTPLSVWYNDAGQALHYEIFDDANFMVLVEPE 157
Cdd:PRK09423  76 LVAIAEENGCdVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   158 IILNAPQQYLLAGIGDTLAKWYEA-VVLAPQPETlpLTVRLGINNAQAI----RDVLLNSSEQALSDQQNQQLTQSFCDV 232
Cdd:PRK09423 156 IIAKAPARFLAAGIGDALATWFEArACSRSGGTT--MAGGKPTLAALALaelcYETLLEDGLKAKLAVEAKVVTPALENV 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   233 VDAII---------AGggmvgglgdrftrVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDDV-LAQLTGAY 302
Cdd:PRK09423 234 IEANTllsglgfesGG-------------LAAAHAIHNGLTALEDTHHLTHGEKVAFGTLTQLVLENRPKEeIEEVIDFC 300

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 2506145   303 QRFHLPTTLAELEVDINNQAEIDKVIAHTLRPVESIHYLPVTLTPDTLRAA 353
Cdd:PRK09423 301 HAVGLPTTLADLGLKEDSDEELRKVAEAACAEGETIHNMPFKVTPEDVAAA 351
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
12-350 1.06e-38

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 141.20  E-value: 1.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145     12 PANYFSHPGSFNHLHDFFTDEQlSRAVWIYGKRAIAAAQT-KLPPAFGLPGAKHILF---RGHCSESDVQQLAA---ESG 84
Cdd:pfam00465   1 PTRIVFGAGALAELGEELKRLG-ARALIVTDPGSLKSGLLdKVLASLEEAGIEVVVFdgvEPEPTLEEVDEAAAlarEAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145     85 DDrsVVIGVGGGALLDTAKALARRLG------------------LPFVAVPTIAATCAAWTPLSVWYNDAGQAlHYEIFD 146
Cdd:pfam00465  80 AD--VIIAVGGGSVIDTAKAIALLLTnpgdvwdylggkpltkpaLPLIAIPTTAGTGSEVTPLAVITDTETGE-KLGIFS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145    147 DANF--MVLVEPEIILNAPQQYLLAGIGDTLAKWYEAVVlapQPETLPLTVRLGInnaQAIRdVLLNSSEQALSDQQNqq 224
Cdd:pfam00465 157 PKLLpdLAILDPELTLTLPPRLTAATGMDALAHAVEAYV---SKGANPLTDALAL---EAIR-LIAENLPRAVADGED-- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145    225 lTQSFCDVVDA-IIAGGGMVGglgdrfTRVAAAHAVHNGLT-VLPQTEKFLHGTKVAYGI----------LVQSALL--- 289
Cdd:pfam00465 228 -LEARENMLLAsTLAGLAFSN------AGLGAAHALAHALGgRYGIPHGLANAILLPYVLrfnapaapekLAQLARAlge 300

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506145    290 -----GQDDVLAQLTGAYQRFHLPTTLAELEVDinnQAEIDKVIAHTLRPvESIHYLPVTLTPDTL 350
Cdd:pfam00465 301 dsdeeAAEEAIEALRELLRELGLPTTLSELGVT---EEDLDALAEAALRD-RSLANNPRPLTAEDI 362
Gro1PDH cd08173
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ...
 5-182 6.72e-16

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: 77.59  E-value: 6.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145    5 PIRVVVGPanyfshpGSFNHLHDFFTDEQLSRAVWI---------YGKRAIAAAQTKLPPAFGlpgAKHILFRGHCSESD 75
Cdd:cd08173   2 PRNVVVGH-------GAINKIGEVLKKLLLGKRALIitgpntykiAGKRVEDLLESSGVEVVI---VDIATIEEAAEVEK 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   76 VQQLAAESGDDrsVVIGVGGGALLDTAKALARRLGLPFVAVPTIAATCAAWTPL-SVWYNDagqaLHYEIFDDANFMVLV 154
Cdd:cd08173  72 VKKLIKESKAD--FIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFaSIKGGD----KPYSIKAKAPIAIIA 145

                       170       180
                ....*....|....*....|....*...
gi 2506145  155 EPEIILNAPQQYLLAGIGDTLAKwYEAV 182
Cdd:cd08173 146 DTEIISKAPKRLLAAGCGDLISN-ITAV 172
G1PDH-like cd08174
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ...
 18-177 7.77e-16

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: 77.56  E-value: 7.77e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   18 HPGSFNHLHDFFTDE--QLSRAVWIYGKRAIAAAQTKLPPAFGLPGAKHILFrgHCSESDVQQLAAE--SGDDRSVVIGV 93
Cdd:cd08174   7 EEGALEHLGKYLADRnqGFGKVAIVTGEGIDELLGEDILESLEEAGEIVTVE--ENTDNSAEELAEKafSLPKVDAIVGI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   94 GGGALLDTAKALARRLGLPFVAVPTIAATCAAWTPLSVWYNDAG-QALHYEIfddaNFMVLVEPEIILNAPQQYLLAGIG 172
Cdd:cd08174  85 GGGKVLDVAKYAAFLSKLPFISVPTSLSNDGIASPVAVLKVDGKrKSLGAKM----PYGVIVDLDVIKSAPRRLILAGIG 160


                ....*
gi 2506145  173 DTLAK 177
Cdd:cd08174 161 DLISN 165
Fe-ADH_2 pfam13685
Iron-containing alcohol dehydrogenase;
18-178 5.38e-14

Iron-containing alcohol dehydrogenase;


Pssm-ID: 404557 [Multi-domain]  Cd Length: 251  Bit Score: 70.79  E-value: 5.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145     18 HPGSFNHLHDFFTDEQLSRAVWIYGKRAIAAAQTKLPPAFGLPGAKHILFR---GHCSESDVQQLAAESGDDRS-VVIGV 93
Cdd:pfam13685   3 GPGALGRLGEYLAELGFRRVALVADANTYAAAGRKVAESLKRAGIEVETRLevaGNADMETAEKLVGALRERDAdAVVGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145     94 GGGALLDTAKALARRLGLPFVAVPT------IAATCAAWTplsvwyndaGQALHYEIFDDANFMVLVEPEIILNAPQQYL 167
Cdd:pfam13685  83 GGGTVIDLAKYAAFKLGKPFISVPTaasndgFASPGASLT---------VDGKKRSIPAAAPFGVIADTDVIAAAPRRLL 153

                         170
                  ....*....|.
gi 2506145    168 LAGIGDTLAKW 178
Cdd:pfam13685 154 ASGVGDLLAKI 164
DHQ_Fe-ADH cd07766
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ...
 58-328 9.92e-14

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: 70.47  E-value: 9.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   58 GLPGAKHILFRGHCSESDVQQLA-AESGDDRSVVIGVGGGALLDTAKALARRL--GLPFVAVPTIAATCAAWTPLSVWYN 134
Cdd:cd07766  48 GLAVAIFDFVGENPTFEEVKNAVeRARAAEADAVIAVGGGSTLDTAKAVAALLnrGIPFIIVPTTASTDSEVSPKSVITD 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  135 DAGQALHYEIFDDANFmVLVEPEIILNAPQQYLLAGIGDTLAKWYEavvlapqpetlpltvrlginnaqaiRDVLLNSSE 214
Cdd:cd07766 128 KGGKNKQVGPHYNPDV-VFVDTDITKGLPPRQVASGGVDALAHAVE-------------------------LEKVVEAAT 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  215 QALSDQQNQqltqsfcdvvdaiiagggmvgglgdrfTRVAAAHAVHNGLTVLpqtEKFLHGTKVAYGILVQSAL-----L 289
Cdd:cd07766 182 LAGMGLFES---------------------------PGLGLAHAIGHALTAF---EGIPHGEAVAVGLPYVLKVandmnP 231

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 2506145  290 GQDDVLAQLTGAYQRFHLPTTLAELEVDinnQAEIDKVI 328
Cdd:cd07766 232 EPEAAIEAVFKFLEDLGLPTHLADLGVS---KEDIPKLA 267
G1PDH_related cd08549
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ...
 89-334 1.09e-11

Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids.


Pssm-ID: 341479 [Multi-domain]  Cd Length: 331  Bit Score: 65.28  E-value: 1.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   89 VVIGVGGGALLDTAKALARRLGLPFVAVPTIAAT---CAAWTPLSVwyndagQALHYEIFDDANFMVLVEPEIILNAPQQ 165
Cdd:cd08549  73 CVIGIGGGRSIDTGKYLAYKLKIPFISVPTSASNdgiASPIVSLRI------PGVKKTFMADAPIAIIADTEIIKKSPRR 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  166 YLLAGIGDTLAK------WYEAVVLAPQPETlPLTVRLGINNAQAIRDVLLNSSEqalsdqqnqqLTQSFCDVVDAIIAG 239
Cdd:cd08549 147 LLSAGIGDLVSNitavldWKLAHKEKGEKYS-EFAAILSKTSAKELVSYVLKASD----------LEEYHRVLVKALVGS 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  240 GGMVGGLGDRFTRVAAAHAVHNGLTVLPQTEK---FLHGTKVAYGILVQSALLGQddVLAQLTGAYQRFH-------LPT 309
Cdd:cd08549 216 GIAMAIAGSSRPASGSEHLFSHALDKLKEEYLninVLHGEQVGVGTIIMSYLHEK--ENKKLSGLHERIKmilkkvgAPT 293

                       250       260
                ....*....|....*....|....*
gi 2506145  310 TLAELEVDINNqAEIDKVIAHTLRP 334
Cdd:cd08549 294 TAKQLGIDEDL-IIEALTEAHKIRP 317
egsA PRK00843
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
 88-334 1.34e-10

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


Pssm-ID: 179139  Cd Length: 350  Bit Score: 61.83  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145    88 SVVIGVGGGALLDTAKALARRLGLPFVAVPT------IAATCAAW----TPLSVwyndagQAlhyeifdDANFMVLVEPE 157
Cdd:PRK00843  89 GFLIGVGGGKVIDVAKLAAYRLGIPFISVPTaashdgIASPRASIkgggKPVSV------KA-------KPPLAVIADTE 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   158 IILNAPQQYLLAGIGDTLAKwYEAVvlapqpetlpLTVRLginnAQAIRDVLLNSSEQALS-----------DQQNQQLT 226
Cdd:PRK00843 156 IIAKAPYRLLAAGCGDIISN-YTAV----------KDWRL----AHRLRGEYYSEYAAALSlmtakmlienaDIIKPGLE 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   227 QSFCDVVDAIIAGGGMVGGLGDrfTRVAA------AHAVHnglTVLPqtEKFLHGTKVAYGILVQSALLGQD-----DVL 295
Cdd:PRK00843 221 ESARLVVKALISSGVAMSIAGS--SRPASgsehlfSHALD---RLAP--GPALHGEQCGVGTIIMMYLHGGDwrkirDAL 293

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 2506145   296 AQLtGAyqrfhlPTTLAELEVDinnqaeiDKVI------AHTLRP 334
Cdd:PRK00843 294 KKI-GA------PTTAKELGID-------DEYIiealtiAHTIRP 324
Fe-ADH-like cd08196
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 74-351 1.94e-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: 52.20  E-value: 1.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   74 SDVQQLAAESGDDR-SVVIGVGGGALLDTAKALA---------RRL----------GLPFVAVPTIAATCAAWTPLSV-W 132
Cdd:cd08196  70 ENVDKCARLARENGaDFVIAIGGGSVLDTAKAAAclaktdgsiEDYlegkkkipkkGLPLIAIPTTAGTGSEVTPVAVlT 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  133 YNDAGQ---ALHYEIFDDAnfmVLVEPEIILNAPqQYLLAGIG-DTLAKWYEAV-VLAPQPETLPLTVRlginnaqAIRD 207
Cdd:cd08196 150 DKEKGKkapLVSPGFYPDI---AIVDPELTYSMP-PKVTASTGiDALCHAIEAYwSINHQPISDALALE-------AAKL 218

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  208 VlLNSSEQALSDQQNQQLTQSFCdvVDAIIAGGGmvgglgdrF--TRVAAAHAVHngltvLPQTEKF--LHGTKVAYGI- 282
Cdd:cd08196 219 V-LENLEKAYNNPNDKEAREKMA--LASLLAGLA--------FsqTRTTASHACS-----YPLTSHFgiPHGEACALTLp 282

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145  283 ----LVQSALLGQDDVLAQLTGAY-------------QRFHLPTTLAELEVDINnqaEIDKVIAHTLRPvESIHYLPVTL 345
Cdd:cd08196 283 sfirLNAEALPGRLDELAKQLGFKdaeeladkieelkKRIGLRTRLSELGITEE---DLEEIVEESFHP-NRANNNPVEV 358


                ....*.
gi 2506145  346 TPDTLR 351
Cdd:cd08196 359 TKEDLE 364
G1PDH cd08175
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ...
 70-177 3.49e-07

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: 51.36  E-value: 3.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   70 HCSESDVQQLAAESGDDRSVVIGVGGGALLDTAKALARRLGLPFVAVPTiAAtcaawtplSV-WYNDAGQAL-------- 140
Cdd:cd08175  66 IADEAAVGKVLLELEKDTDLIIAVGSGTINDLTKYAAYKLGIPYISVPT-AP--------SMdGYTSSGAPIivdgvkkt 136

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 2506145  141 ---HYEIFddanfmVLVEPEIILNAPQQYLLAGIGDTLAK 177
Cdd:cd08175 137 fpaHAPKA------IFADLDVLANAPQRMIAAGFGDLLGK 170
Fe-ADH-like cd08183
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 35-122 4.01e-07

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: 51.35  E-value: 4.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   35 SRAVWIYGKRAIAAAQTK-LPPAFGLPGAKHILFRGhCSESDVQ------QLAAESGDDrsVVIGVGGGALLDTAKALA- 106
Cdd:cd08183  23 KRALLVTGRSSLRSGRLArLLEALEAAGIEVALFSV-SGEPTVEtvdaavALAREAGCD--VVIAIGGGSVIDAAKAIAa 99

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 2506145  107 ---------------------RRLGLPFVAVPTIAAT 122
Cdd:cd08183 100 lltnegsvldylevvgkgrplTEPPLPFIAIPTTAGT 136
HEPD cd08182
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ...
 75-163 1.84e-06

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: 49.15  E-value: 1.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   75 DVQQLAAESGDDR-SVVIGVGGGALLDTAKALARRLG--------------------LPFVAVPTIAATCAAWTPLS-VW 132
Cdd:cd08182  67 DLERGIELFRESGpDVIIAVGGGSVIDTAKAIAALLGspgenllllrtgekapeenaLPLIAIPTTAGTGSEVTPFAtIW 146

                        90       100       110
                ....*....|....*....|....*....|...
gi 2506145  133 YNDAGQalHYEIFDDANF--MVLVEPEIILNAP 163
Cdd:cd08182 147 DEAEGK--KYSLAHPSLYpdAAILDPELTLSLP 177
Fe-ADH_KdnB-like cd08184
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ...
 76-171 7.17e-06

Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing 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 or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.


Pssm-ID: 341463 [Multi-domain]  Cd Length: 348  Bit Score: 47.26  E-value: 7.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   76 VQQLAAESGDDRSVVIGVGGGALLDTAKALARRL------------------GLPFVAVPTIAATCAAWTPLSVWYNdAG 137
Cdd:cd08184  72 RAQIRAENDKLPAAVVGIGGGSTMDIAKAVSNMLtnpgsaadyqgwdlvknpGIYKIGVPTLSGTGAEASRTAVLTG-PE 150

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 2506145  138 QAL----HYEIFDDanfmVLVEPEIILNAPQ-QYLLAGI 171
Cdd:cd08184 151 KKLginsDYTVFDQ----VILDPELIATVPRdQYFYTGM 185
MAR cd08177
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ...
 70-118 4.40e-05

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: 44.80  E-value: 4.40e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 2506145   70 HCSESDVQQ---LAAESGDDrsVVIGVGGGALLDTAKALARRLGLPFVAVPT 118
Cdd:cd08177  59 HVPVEVAERalaAAREAGAD--GLVAIGGGSAIGLAKAIALRTGLPIVAVPT 108
EutG COG1454
Alcohol dehydrogenase, class IV [Energy production and conversion];
3-163 5.73e-05

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


Pssm-ID: 441063 [Multi-domain]  Cd Length: 381  Bit Score: 44.73  E-value: 5.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145    3 HNPIRVVVGPanyfshpGSFNHLHDFFTDEQLSRAVWIYGKRAIAAAQT-KLPPAFGLPGAKHILF---RGHCSESDVQ- 77
Cdd:COG1454   6 RLPTRIVFGA-------GALAELGEELKRLGAKRALIVTDPGLAKLGLLdRVLDALEAAGIEVVVFddvEPNPTVETVEa 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   78 --QLAAESGDDrsVVIGVGGGALLDTAKALA------------------RRLGLPFVAVPTIAATCAAWTPLSVWYNDAG 137
Cdd:COG1454  79 gaAAAREFGAD--VVIALGGGSAIDAAKAIAllatnpgdledylgikkvPGPPLPLIAIPTTAGTGSEVTPFAVITDPET 156

                       170       180
                ....*....|....*....|....*...
gi 2506145  138 QaLHYEIFDDANF--MVLVEPEIILNAP 163
Cdd:COG1454 157 G-VKKGIADPELLpdVAILDPELTLTLP 183
BDH cd08187
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ...
 89-176 6.71e-05

Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process; The butanol dehydrogenase (BDH) is involved in the final step of the butanol formation pathway in anaerobic micro-organism. Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process. Activity in the reverse direction is 50-fold lower than that in the forward direction. The NADH-BDH has higher activity with longer chained aldehydes and is inhibited by metabolites containing an adenine moiety. This protein family belongs to the so-called iron-containing alcohol dehydrogenase superfamily. Since members of this superfamily use different divalent ions, preferentially iron or zinc, it has been suggested to be renamed to family III metal-dependent polyol dehydrogenases. This family also includes E. coli YqhD enzyme, an NADP-dependent dehydrogenase whose activity measurements with several alcohols demonstrate preference for alcohols longer than C3. The active site of YqhD contains a Zn metal, and a modified NADPH cofactor bearing OH groups on the saturated C5 and C6 atoms, possibly due to oxygen stress on the enzyme, which would functionally work under anaerobic conditions.


Pssm-ID: 341466 [Multi-domain]  Cd Length: 382  Bit Score: 44.35  E-value: 6.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   89 VVIGVGGGALLDTAKALArrLG--------------------LPFVAVPTIAATCAAWTPLSVWYNDAGQaLHYEIFDDA 148
Cdd:cd08187  89 FILAVGGGSVIDAAKAIA--AGakydgdvwdfftgkappekaLPVGTVLTLAATGSEMNGGAVITNEETK-EKLGFGSPL 165

                        90       100       110
                ....*....|....*....|....*....|
gi 2506145  149 NFMV--LVEPEIILNAPQQYLLAGIGDTLA 176
Cdd:cd08187 166 LRPKfsILDPELTYTLPKYQTAAGIVDIFS 195
PPD-like cd08181
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ...
 78-176 9.99e-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: 43.73  E-value: 9.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   78 QLAAESGDDrsVVIGVGGGALLDTAKALA---------RRL--------GLPFVAVPTIAATCAAWTPLSVWYNDAGQaL 140
Cdd:cd08181  77 ELARKEGAD--FVIGIGGGSPLDAAKAIAllaankdgdEDLfqngkynpPLPIVAIPTTAGTGSEVTPYSILTDHEKG-T 153

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 2506145  141 HYEIFDDANF--MVLVEPEIILNAPQQYLLAGIGDTLA 176
Cdd:cd08181 154 KKSFGNPLIFpkLALLDPKYTLSLPEELTIDTAVDALS 191
Fe-ADH-like cd08191
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 80-136 1.08e-04

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


Pssm-ID: 341470 [Multi-domain]  Cd Length: 392  Bit Score: 43.76  E-value: 1.08e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506145   80 AAESGDDRSVVIGVGGGALLDTAKALARRL------------------GLPFVAVPTIAATCAAWTPLSVWYNDA 136
Cdd:cd08191  76 AAARAFDPDVVIGLGGGSNMDLAKVVALLLahggdprdyygedrvpgpVLPLIAVPTTAGTGSEVTPVAVLTDPA 150
Fe-ADH-like cd08189
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 90-125 3.99e-04

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and 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: 42.07  E-value: 3.99e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   90 VIGVGGGALLDTAKALA-------------------RRLGLPFVAVPTIA-----ATCAA 125
Cdd:cd08189  88 IIAIGGGSVIDCAKVIAaraanpkksvrklkgllkvRKKLPPLIAVPTTAgtgseATIAA 147
Fe-ADH-like cd14864
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 78-176 5.77e-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: 341486 [Multi-domain]  Cd Length: 376  Bit Score: 41.52  E-value: 5.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   78 QLAAESGDDrsVVIGVGGGALLDTAKALARRLG------------------LPFVAVPTIAATCAAWTP-LSVWYNDAGQ 138
Cdd:cd14864  76 ELARKAGAD--GIIAVGGGKVLDTAKAVAILANndggaydflegakpkkkpLPLIAVPTTPRSGFEFSDrFPVVDSRSRE 153

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 2506145  139 ALHYEIFDDANFMVLVEPEIILNAPQQYLLAGIGDTLA 176
Cdd:cd14864 154 VKLLKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALA 191
Fe-ADH-like cd08185
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 78-122 6.43e-04

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: 41.33  E-value: 6.43e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506145   78 QLAAESGDDrsVVIGVGGGALLDTAKALA-------------------RRLG---LPFVAVPTIAAT 122
Cdd:cd08185  77 ALAKEEGCD--FVIGLGGGSSMDAAKAIAfmatnpgdiwdyifggtgkGPPPekaLPIIAIPTTAGT 141
Fe-ADH-like cd14863
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 90-136 8.11e-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: 341485 [Multi-domain]  Cd Length: 380  Bit Score: 40.98  E-value: 8.11e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506145   90 VIGVGGGALLDTAKALARRL-------------------GLPFVAVPTIAATCAAWTPLSVWYNDA 136
Cdd:cd14863  88 VIGIGGGSVLDTAKAIAVLLtnpgpiidyalagppvpkpGIPLIAIPTTAGTGSEVTPIAVITDEE 153
Fe-ADH cd08551
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ...
 78-122 8.21e-04

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: 40.89  E-value: 8.21e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506145   78 QLAAESGDDrsVVIGVGGGALLDTAKALA------------------RRLGLPFVAVPTIAAT 122
Cdd:cd08551  74 ELAREEGAD--LVIAVGGGSVLDTAKAIAvlatnggsirdyegigkvPKPGLPLIAIPTTAGT 134
DHQS-like cd08198
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 74-137 8.92e-04

Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; This family contains dehydroquinate synthase-like proteins. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. The activity of DHQS requires NAD as cofactor. Proteins of this family share sequence similarity and functional motifs with that of dehydroquinate synthase, but the specific function has not been characterized.


Pssm-ID: 341477  Cd Length: 366  Bit Score: 41.02  E-value: 8.92e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506145   74 SDVQQLAAESGDDR-SVVIGVGGGALLDT---AKALARRlGLPFVAVPTiaatcaawTPLSvwYNDAG 137
Cdd:cd08198  86 EEILSAIHDHGLDRhSYVVVIGGGAVLDAvgfAAAIAHR-GIRLIRVPT--------TVLA--QNDSG 142
DHQ_synthase pfam01761
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ...
 75-118 4.90e-03

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: 38.25  E-value: 4.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2506145     75 DVQQLAAESGDDR-SVVIGVGGGALLDTA---KALARRlGLPFVAVPT 118
Cdd:pfam01761  18 RIYDALLEAGLDRsSLLIALGGGVIGDLAgfvAATYMR-GIRFIQVPT 64
Fe-ADH-like cd14865
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 75-122 5.80e-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: 341487 [Multi-domain]  Cd Length: 383  Bit Score: 38.29  E-value: 5.80e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506145   75 DVQQLAAESGDDrsVVIGVGGGALLDTAKALA--------------------RRLgLPFVAVPTIAAT 122
Cdd:cd14865  76 EAAARAREAGAD--GIIAVGGGSVIDTAKGVNillseggddlddygganrltRPL-KPLIAIPTTAGT 140
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 74-118 6.20e-03

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: 38.15  E-value: 6.20e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 2506145   74 SDVQQLAAESGDDR-SVVIGVGGGALLDT---AKALARRlGLPFVAVPT 118
Cdd:COG0337  83 ERILDALLEAGLDRdDLVVALGGGVVGDLagfAAATYLR-GVPFIQVPT 130
Fe-ADH-like cd08194
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 89-122 8.04e-03

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: 37.90  E-value: 8.04e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 2506145   89 VVIGVGGGALLDTAKALAR------------------RLGLPFVAVPTIAAT 122
Cdd:cd08194  83 FIVALGGGSPIDTAKAIAVlatnggpirdymgprkvdKPGLPLIAIPTTAGT 134
Fe-ADH-like cd14861
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ...
 30-122 8.18e-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: 37.88  E-value: 8.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506145   30 TDEQLSRAVWIygKRAIAAaqtkLPPAfglpGAKHILF---RGHCSESDVQQLAA---ESGDDrsVVIGVGGGALLDTAK 103
Cdd:cd14861  32 TDPGLAALGIV--DRVLEA----LGAA----GLSPAVFsdvPPNPTEADVEAGVAayrEGGCD--GIIALGGGSAIDAAK 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 2506145  104 ALARRLG----------------------LPFVAVPTIAAT 122
Cdd:cd14861 100 AIALMAThpgplwdyedgeggpaaitpavPPLIAIPTTAGT 140
 
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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