| Type | Description |
|---|---|
| Definition | D-arabinose 1-dehydrogenase (NAD(P)(+)) ARA1 |
| Date | Results | Publications |
|---|---|---|
| 2014-06-14 13:17:00 | A structural study of Ara1 revealed that induced fit upon NADPH binding yielded an intact active-site pocket that recognizes the substrate. | 24192347 |
| 2010-04-19 11:07:00 | Characterizeion of Ara1 as an oxidoreductase that can reduce racemic acetoin to meso-2,3-butanediol and (2S,3S)-2,3-butanediol in the presence of NADPH. | 19966022 |
| 2010-01-21 00:00:00 | It demonstrates that Ara2p, not Ara1p, mainly contributes to the production of Erythroascorbic acid from d-arabinose in S. cerevisiae. | 17097644 |
| 2010-01-21 00:00:00 | Ara1p catalyzed the reduction of the reactive alpha,beta-dicarbonyl compounds methylglyoxal, diacetyl, and pentanedione in a NADPH dependant manner. | 17030441 |
| Type | IDs |
|---|---|
| Gene |
UniProtKB-ID:
ARA1_YEAST
UniprotKB:
P38115
UniParc:
UPI0000048D4E
EMBL:
M95580,
BK006936,
Z36018
EnsemblGenome:
YBR149W
KO:
sce:YBR149W
|
| Nucleutide sequences |
EMBL-CDS:
CAA85107.1,
AAA35037.1,
DAA07264.1
Gene_ORFName:
YBR1127
EnsemblGenome_TRS:
YBR149W_mRNA
|
| Protein sequencees |
EnsemblGenome_PRO:
YBR149W
RefSeq:
NP_009707.3
|
| Others |
UniRef100:
UniRef100_P38115
UniRef90:
UniRef90_P38115
UniRef50:
UniRef50_P38115
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
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| Location | {{protein.contigId}} ( {{protein.positionStart}}..{{protein.positionEnd}} , {{protein.orientation}} ) | |||||||
| Conserved domain | Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
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