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Conserved domains on  [gi|2398820936|ref|WP_268093308|]
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iron-containing alcohol dehydrogenase, partial [Enterobacter sp. JH602]

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); ...
 1-90 1.53e-58

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 PRK10586:

Pssm-ID: 445950  Cd Length: 362  Bit Score: 182.62  E-value: 1.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2398820936   1 QALHYEIFDDANFMVLVEPEIILNAPQQYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNAQAIRDVLLNSSEQAL 80
Cdd:PRK10586  138 QALHFEIFDDANFLVLVEPRIILNAPQEYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNALAIRDVLLNSSEQAL 217

                          90
                  ....*....|
gi 2398820936  81 SDQQNHQLTQ 90
Cdd:PRK10586  218 ADQQNGQLTQ 227
 
Name Accession Description Interval E-value
PRK10586 PRK10586
putative oxidoreductase; Provisional
 1-90 1.53e-58

putative oxidoreductase; Provisional


Pssm-ID: 182570  Cd Length: 362  Bit Score: 182.62  E-value: 1.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2398820936   1 QALHYEIFDDANFMVLVEPEIILNAPQQYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNAQAIRDVLLNSSEQAL 80
Cdd:PRK10586  138 QALHFEIFDDANFLVLVEPRIILNAPQEYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNALAIRDVLLNSSEQAL 217

                          90
                  ....*....|
gi 2398820936  81 SDQQNHQLTQ 90
Cdd:PRK10586  218 ADQQNGQLTQ 227
GlyDH-like cd08172
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 1-90 1.84e-39

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: 133.03  E-value: 1.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2398820936   1 QALHYEIFDDANFMVLVEPEIILNAPQQYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNAQAIRDVLLNSSEQAL 80
Cdd:cd08172   127 EFIGYDYFPRSAYLVLVDPRLLLDSPKDYFVAGIGDTLAKWYEADAILRQLEELPAFLQLARQAAKLCRDILLKDSEQAL 206

                          90
                  ....*....|
gi 2398820936  81 SDQQNHQLTQ 90
Cdd:cd08172   207 ADLEAGKLTP 216
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 3-90 9.36e-23

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: 89.07  E-value: 9.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2398820936   3 LHYEIFDDANFMVLVEPEIILNAPQQYLLAGIGDTLAKWYEAVV--LAPQPETLPLTVRLGINNAQAIRDVLLNSSEQAL 80
Cdd:COG0371   136 DGYSFLAKNPDLVLVDTDIIAKAPVRLLAAGIGDALAKWYEARDwsLAHRDLAGEYYTEAAVALARLCAETLLEYGEAAI 215

                          90
                  ....*....|
gi 2398820936  81 SDQQNHQLTQ 90
Cdd:COG0371   216 KAVEAGVVTP 225
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
4-46 8.77e-07

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 44.90  E-value: 8.77e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2398820936   4 HYEIFDDANF--MVLVEPEIILNAPQQYLLAGIGDTLAKWYEAVV 46
Cdd:pfam00465 151 KLGIFSPKLLpdLAILDPELTLTLPPRLTAATGMDALAHAVEAYV 195
 
Name Accession Description Interval E-value
PRK10586 PRK10586
putative oxidoreductase; Provisional
 1-90 1.53e-58

putative oxidoreductase; Provisional


Pssm-ID: 182570  Cd Length: 362  Bit Score: 182.62  E-value: 1.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2398820936   1 QALHYEIFDDANFMVLVEPEIILNAPQQYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNAQAIRDVLLNSSEQAL 80
Cdd:PRK10586  138 QALHFEIFDDANFLVLVEPRIILNAPQEYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNALAIRDVLLNSSEQAL 217

                          90
                  ....*....|
gi 2398820936  81 SDQQNHQLTQ 90
Cdd:PRK10586  218 ADQQNGQLTQ 227
GlyDH-like cd08172
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 1-90 1.84e-39

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: 133.03  E-value: 1.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2398820936   1 QALHYEIFDDANFMVLVEPEIILNAPQQYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNAQAIRDVLLNSSEQAL 80
Cdd:cd08172   127 EFIGYDYFPRSAYLVLVDPRLLLDSPKDYFVAGIGDTLAKWYEADAILRQLEELPAFLQLARQAAKLCRDILLKDSEQAL 206

                          90
                  ....*....|
gi 2398820936  81 SDQQNHQLTQ 90
Cdd:cd08172   207 ADLEAGKLTP 216
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 3-90 9.36e-23

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: 89.07  E-value: 9.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2398820936   3 LHYEIFDDANFMVLVEPEIILNAPQQYLLAGIGDTLAKWYEAVV--LAPQPETLPLTVRLGINNAQAIRDVLLNSSEQAL 80
Cdd:COG0371   136 DGYSFLAKNPDLVLVDTDIIAKAPVRLLAAGIGDALAKWYEARDwsLAHRDLAGEYYTEAAVALARLCAETLLEYGEAAI 215

                          90
                  ....*....|
gi 2398820936  81 SDQQNHQLTQ 90
Cdd:COG0371   216 KAVEAGVVTP 225
GlyDH-like cd08550
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ...
 1-90 4.17e-19

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: 79.12  E-value: 4.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2398820936   1 QALHYEIFDDANFMVLVEPEIILNAPQQYLLAGIGDTLAKWYEAVVLAPQPETlPLTVRLGINNAQAIRDVLLNSSEQAL 80
Cdd:cd08550   129 EFLGYSLLKRSPDLVLVDTDIIAAAPVRYLAAGIGDTLAKWYEARPSSRGGPD-DLALQAAVQLAKLAYDLLLEYGVQAV 207

                          90
                  ....*....|
gi 2398820936  81 SDQQNHQLTQ 90
Cdd:cd08550   208 EDVRQGKVTP 217
GlyDH-like cd08171
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 8-90 1.11e-16

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: 72.55  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2398820936   8 FDDANFM------VLVEPEIILNAPQQYLLAGIGDTLAKWYEaVVLAPQPETLPLTVRLGINNAQAIRDVLLNSSEQALS 81
Cdd:cd08171   131 FKEYYFLkrppvhTFIDTEIIAEAPEKYLWAGIGDTLAKYYE-VEFSARGDELDHTNALGVAISKMCSEPLLKYGVQALE 209


                  ....*....
gi 2398820936  82 DQQNHQLTQ 90
Cdd:cd08171   210 DCRANKVSD 218
GlyDH cd08170
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ...
 14-89 3.63e-12

Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.


Pssm-ID: 341449 [Multi-domain]  Cd Length: 351  Bit Score: 60.12  E-value: 3.63e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2398820936  14 MVLVEPEIILNAPQQYLLAGIGDTLAKWYEA-VVLAPQPETLPLTV--RLGINNAQAIRDVLLNSSEQALSDQQNHQLT 89
Cdd:cd08170   142 LVLVDTEIIAKAPVRFLVAGMGDALATYFEArACARSGAPNMAGGRptLAALALAELCYDTLLEYGVAAKAAVEAGVVT 220
gldA PRK09423
glycerol dehydrogenase; Provisional
 14-44 2.14e-08

glycerol dehydrogenase; Provisional


Pssm-ID: 181843  Cd Length: 366  Bit Score: 49.43  E-value: 2.14e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2398820936  14 MVLVEPEIILNAPQQYLLAGIGDTLAKWYEA 44
Cdd:PRK09423  149 LVLVDTAIIAKAPARFLAAGIGDALATWFEA 179
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
4-46 8.77e-07

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 44.90  E-value: 8.77e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2398820936   4 HYEIFDDANF--MVLVEPEIILNAPQQYLLAGIGDTLAKWYEAVV 46
Cdd:pfam00465 151 KLGIFSPKLLpdLAILDPELTLTLPPRLTAATGMDALAHAVEAYV 195
G1PDH-like cd08174
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ...
 13-45 2.61e-06

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: 43.28  E-value: 2.61e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2398820936  13 FMVLVEPEIILNAPQQYLLAGIGDTLAK------WYEAV 45
Cdd:cd08174   138 YGVIVDLDVIKSAPRRLILAGIGDLISNitalydWKLAE 176
Gro1PDH cd08173
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ...
 15-45 9.40e-04

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: 35.99  E-value: 9.40e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2398820936  15 VLVEPEIILNAPQQYLLAGIGDTLAKwYEAV 45
Cdd:cd08173   143 IIADTEIISKAPKRLLAAGCGDLISN-ITAV 172
 
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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