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Annotation rule MF_02127 |
General rule information
[?]
Accession |
MF_02127 |
Dates |
21-NOV-2011 (Created) 20-NOV-2019 (Last updated, Version 10) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
Protein name |
RecName:
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Full=Glucose 1-dehydrogenase;
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Short=GDH;
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Short=GlcDH;
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EC 1.1.1.47;
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case <OC:Halobacteria>
Function |
Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a modified Entner-Doudoroff pathway. |
else
Function |
Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a non-phosphorylative variant of the Entner-Doudoroff pathway. |
end case
case <FTGroup:1> and <FTGroup:2>
Cofactor |
Zn(2+) Note: Binds 2 Zn(2+) ions per subunit. One of the zinc atoms is essential for catalytic activity while the other has a structural function. |
else
end case
Similarity |
Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily. |
GO:0005536; Molecular function: glucose binding.
GO:0047936; Molecular function: glucose 1-dehydrogenase [NAD(P)] activity.
GO:0070401; Molecular function: NADP+ binding.
GO:0070403; Molecular function: NAD+ binding.
GO:0008270; Molecular function: zinc ion binding.
GO:0019595; Biological process: non-phosphorylated glucose catabolic process.
From: GLCDH_SACSO (O93715) |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
|
NP_BIND (Optional)
|
|
189
|
|
192
|
|
NADP
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|
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|
[TNSA]-x-x-[ILV]
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|
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NP_BIND (Optional)
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|
211
|
|
213
|
|
NADP
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|
|
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N-x-[RH]
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|
|
NP_BIND (Optional)
|
|
277
|
|
279
|
|
NADP
|
|
|
|
[FL]-x-[FVILT]
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|
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NP_BIND
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|
305
|
|
307
|
|
NADP
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|
|
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[LSTAV]-x-[ND]
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|
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BINDING
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|
41
|
|
41
|
|
Substrate
|
|
|
|
[TS]
|
|
|
BINDING (Optional)
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|
89
|
|
89
|
|
Substrate
|
|
|
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N
|
|
|
BINDING (Optional)
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|
114
|
|
114
|
|
Substrate
|
|
|
|
E
|
|
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BINDING
|
|
150
|
|
150
|
|
Substrate
|
|
|
|
[QE]
|
|
|
BINDING (Optional)
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154
|
|
154
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|
Substrate
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|
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[DN]
|
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BINDING
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|
307
|
|
307
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Substrate
|
|
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[ND]
|
|
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METAL
|
|
39
|
|
39
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Zinc #1; catalytic
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|
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[CD]
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1
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METAL
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66
|
|
66
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Zinc #1; via tele nitrogen; catalytic
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|
|
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H
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1
|
METAL
|
|
67
|
|
67
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Zinc #1; catalytic
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|
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E
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1
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METAL (Optional)
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93
|
|
93
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Zinc #2; structural
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|
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C
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2
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METAL (Optional)
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96
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96
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Zinc #2; structural
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|
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C
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2
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METAL (Optional)
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|
99
|
|
99
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|
Zinc #2; structural
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|
|
|
C
|
|
2
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METAL (Optional)
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|
107
|
|
107
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|
Zinc #2; structural
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|
|
|
C
|
|
2
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METAL
|
|
150
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|
150
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Zinc #1; catalytic
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|
|
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[QE]
|
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1
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BINDING (Optional)
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354
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354
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NADP
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K
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case not <FT:2>
From: GLCDH_HALMT (Q977U7) |
NP_BIND (Optional)
|
|
207
|
|
208
|
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NADP
|
|
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R-R
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end case
Additional information
[?]
Size range |
347-368 amino acids |
Related rules |
None |
Fusion |
None |
Comments |
Some members of this family also display good catalytic efficiency with D-galactose as substrate (SULSF, Q6L047 in PICTO, THEAC), which seems to be a physiological substrate in some species. |