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Q28399

- ALDH1_ELEED

UniProt

Q28399 - ALDH1_ELEED

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Protein

Aldehyde dehydrogenase, cytosolic 1

Gene

ALDH1

Organism
Elephantulus edwardii (Cape long-eared elephant shrew)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Major component of the eye of elephant shrews, which in contrast to other mammals, possesses both a lens- and a non-lens class-1 aldehyde dehydrogenase 1. This eye-specific form is a structural protein of the lens and, in other part of the eye, serves as the major form of ALDH1. Can convert/oxidize retinaldehyde to retinoic acid.1 Publication

Catalytic activityi

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei170 – 1701Transition state stabilizer
Active sitei269 – 2691Proton acceptor
Active sitei303 – 3031Nucleophile

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi246 – 2516NAD1 Publication

GO - Molecular functioni

  1. aldehyde dehydrogenase (NAD) activity Source: UniProtKB-EC

GO - Biological processi

  1. ethanol catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.2.1.36. 7360.
UniPathwayiUPA00780; UER00768.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde dehydrogenase, cytosolic 1 (EC:1.2.1.3)
Alternative name(s):
ALDH class 1
ETA-crystallin
Gene namesi
Name:ALDH1
OrganismiElephantulus edwardii (Cape long-eared elephant shrew)
Taxonomic identifieri28737 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaAfrotheriaMacroscelideaMacroscelididaeElephantulus

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501Aldehyde dehydrogenase, cytosolic 1PRO_0000056427Add
BLAST

Proteomic databases

PRIDEiQ28399.

Expressioni

Tissue specificityi

Eye specific, with very high expression in the lens.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
501
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 254Combined sources
Beta strandi28 – 303Combined sources
Beta strandi37 – 415Combined sources
Turni43 – 453Combined sources
Beta strandi48 – 536Combined sources
Helixi57 – 7115Combined sources
Helixi76 – 794Combined sources
Helixi82 – 9817Combined sources
Helixi100 – 11112Combined sources
Helixi115 – 1206Combined sources
Helixi122 – 13615Combined sources
Helixi137 – 1393Combined sources
Beta strandi142 – 1454Combined sources
Beta strandi148 – 15912Combined sources
Beta strandi162 – 1665Combined sources
Helixi172 – 18514Combined sources
Beta strandi189 – 1935Combined sources
Helixi200 – 21213Combined sources
Beta strandi218 – 2214Combined sources
Turni226 – 2283Combined sources
Helixi229 – 2346Combined sources
Beta strandi241 – 2466Combined sources
Helixi248 – 26013Combined sources
Beta strandi265 – 2695Combined sources
Beta strandi274 – 2785Combined sources
Helixi284 – 29613Combined sources
Helixi297 – 3004Combined sources
Beta strandi306 – 3127Combined sources
Helixi313 – 32614Combined sources
Helixi348 – 36417Combined sources
Beta strandi367 – 3704Combined sources
Beta strandi373 – 3797Combined sources
Beta strandi385 – 3906Combined sources
Helixi395 – 3984Combined sources
Beta strandi403 – 4119Combined sources
Helixi414 – 4229Combined sources
Beta strandi423 – 4253Combined sources
Beta strandi428 – 4336Combined sources
Helixi437 – 44610Combined sources
Beta strandi449 – 4557Combined sources
Helixi470 – 4723Combined sources
Beta strandi473 – 4753Combined sources
Helixi479 – 4835Combined sources
Helixi484 – 4863Combined sources
Beta strandi487 – 4959Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O9JX-ray2.40A/B/C/D1-501[»]
1PEJmodel-A1-501[»]
ProteinModelPortaliQ28399.
SMRiQ28399. Positions 8-501.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ28399.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

HOVERGENiHBG000097.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q28399-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSSGMPDLP APLTNIKIQH TKLFINNEWH ESVSGKTFPV FNPATEEKIC
60 70 80 90 100
EVEEADKEDV DKAVKAAREA FQMGSPWRTM DASERGQLIY KLADLIERDR
110 120 130 140 150
LLLATLESIN AGKVFASAYL MDLDYCIKAL RYCAGWADKI QGRTIPVDGE
160 170 180 190 200
FFSYTRHEPI GVCGLIFPWN APMILLACKI GPALCCGNTV IVKPAEQTPL
210 220 230 240 250
TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD KVAFTGSTEV
260 270 280 290 300
GKMIQEAAAK SNLKRVTLEL GAKNPCIVFA DADLDSAVEF AHQGVFTNQG
310 320 330 340 350
QSCIAASKLF VEEAIYDEFV QRSVERAKKY VFGNPLTPGV NHGPQINKAQ
360 370 380 390 400
HNKIMELIES GKKEGAKLEC GGGPWGNKGY FIQPTVFSNV TDDMRIAKEE
410 420 430 440 450
IFGPVQQIMK FKSLDEVIKR ANNTYYGLVA GVFTKDLDKA VTVSSALQAG
460 470 480 490 500
TVWVNCYLAA SAQSPAGGFK MSGHGREMGE YGIHEYTEVK TVTMKISEKN

S
Length:501
Mass (Da):54,538
Last modified:November 1, 1996 - v1
Checksum:i9E3D5BBE083ACAD7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02483 mRNA. Translation: AAB60268.1.
RefSeqiNP_001277088.1. NM_001290159.1.

Genome annotation databases

GeneIDi102867337.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02483 mRNA. Translation: AAB60268.1 .
RefSeqi NP_001277088.1. NM_001290159.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1O9J X-ray 2.40 A/B/C/D 1-501 [» ]
1PEJ model - A 1-501 [» ]
ProteinModelPortali Q28399.
SMRi Q28399. Positions 8-501.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q28399.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 102867337.

Organism-specific databases

CTDi 102867337.

Phylogenomic databases

HOVERGENi HBG000097.

Enzyme and pathway databases

UniPathwayi UPA00780 ; UER00768 .
BRENDAi 1.2.1.36. 7360.

Miscellaneous databases

EvolutionaryTracei Q28399.

Family and domain databases

Gene3Di 3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "A retinaldehyde dehydrogenase as a structural protein in a mammalian eye lens. Gene recruitment of eta-crystallin."
    Graham C., Hodin J., Wistow G.
    J. Biol. Chem. 271:15623-15628(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lens.
  2. "Crystal structure of eta-crystallin: adaptation of a class 1 aldehyde dehydrogenase for a new role in the eye lens."
    Bateman O.A., Purkiss A.G., van Montfort R., Slingsby C., Graham C., Wistow G.
    Biochemistry 42:4349-4356(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, HOMOTETRAMERIZATION.

Entry informationi

Entry nameiALDH1_ELEED
AccessioniPrimary (citable) accession number: Q28399
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3