Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lactaldehyde dehydrogenase

Gene

aldA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts on lactaldehyde as well as other aldehydes.

Catalytic activityi

(S)-lactaldehyde + NAD+ + H2O = (S)-lactate + NADH.
Glycolaldehyde + NAD+ + H2O = glycolate + NADH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei251 – 2511By similarity
Active sitei285 – 2851By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi207 – 2137NADBy similarity

GO - Molecular functioni

  • glycolaldehyde dehydrogenase activity Source: EcoCyc
  • lactaldehyde dehydrogenase activity Source: EcoCyc
  • succinate-semialdehyde dehydrogenase (NAD+) activity Source: EcoCyc

GO - Biological processi

  • L-fucose catabolic process Source: EcoCyc
  • rhamnose catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciEcoCyc:LACTALDDEHYDROG-MONOMER.
ECOL316407:JW1412-MONOMER.
MetaCyc:LACTALDDEHYDROG-MONOMER.
BRENDAi1.2.1.22. 2026.
SABIO-RKP25553.

Names & Taxonomyi

Protein namesi
Recommended name:
Lactaldehyde dehydrogenase (EC:1.2.1.22)
Alternative name(s):
Aldehyde dehydrogenase A
Glycolaldehyde dehydrogenase (EC:1.2.1.21)
Gene namesi
Name:aldA
Synonyms:ald
Ordered Locus Names:b1415, JW1412
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10035. aldA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 479478Lactaldehyde dehydrogenasePRO_0000056564Add
BLAST

Proteomic databases

EPDiP25553.
PaxDbiP25553.
PRIDEiP25553.

2D gel databases

SWISS-2DPAGEP25553.

Expressioni

Inductioni

By growth on fucose, rhamnose, arabinose and amino acids such as glutamate.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi4260173. 9 interactions.
850044. 1 interaction.
DIPiDIP-9081N.
IntActiP25553. 5 interactions.
MINTiMINT-1313045.
STRINGi511145.b1415.

Structurei

Secondary structure

1
479
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 113Combined sources
Beta strandi14 – 163Combined sources
Beta strandi23 – 275Combined sources
Turni29 – 313Combined sources
Beta strandi34 – 396Combined sources
Helixi43 – 6220Combined sources
Helixi65 – 8117Combined sources
Helixi83 – 9412Combined sources
Helixi98 – 11619Combined sources
Turni117 – 1215Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi134 – 1429Combined sources
Beta strandi144 – 1496Combined sources
Beta strandi152 – 1543Combined sources
Helixi155 – 16814Combined sources
Beta strandi172 – 1765Combined sources
Helixi183 – 19513Combined sources
Beta strandi201 – 2044Combined sources
Turni209 – 2113Combined sources
Helixi212 – 2187Combined sources
Beta strandi222 – 2298Combined sources
Helixi231 – 24212Combined sources
Turni243 – 2453Combined sources
Beta strandi247 – 2515Combined sources
Beta strandi257 – 2604Combined sources
Helixi266 – 2749Combined sources
Turni279 – 2824Combined sources
Beta strandi285 – 2873Combined sources
Beta strandi289 – 2946Combined sources
Helixi295 – 2973Combined sources
Helixi298 – 31013Combined sources
Turni317 – 3193Combined sources
Helixi331 – 34616Combined sources
Beta strandi350 – 3534Combined sources
Beta strandi360 – 3623Combined sources
Beta strandi368 – 3725Combined sources
Helixi378 – 3814Combined sources
Beta strandi386 – 39611Combined sources
Helixi397 – 4059Combined sources
Beta strandi407 – 41610Combined sources
Helixi420 – 42910Combined sources
Beta strandi432 – 4398Combined sources
Beta strandi456 – 4583Combined sources
Helixi462 – 4676Combined sources
Beta strandi470 – 4789Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HG2X-ray2.20A1-479[»]
2ILUX-ray2.70A1-479[»]
2IMPX-ray2.10A1-479[»]
2OPXX-ray2.53A1-479[»]
ProteinModelPortaliP25553.
SMRiP25553. Positions 3-479.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25553.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271509.
InParanoidiP25553.
KOiK07248.
OMAiINEDHNA.
PhylomeDBiP25553.

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.
IPR029510. Ald_DH_CS_GLU.
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.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25553-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVPVQHPMY IDGQFVTWRG DAWIDVVNPA TEAVISRIPD GQAEDARKAI
60 70 80 90 100
DAAERAQPEW EALPAIERAS WLRKISAGIR ERASEISALI VEEGGKIQQL
110 120 130 140 150
AEVEVAFTAD YIDYMAEWAR RYEGEIIQSD RPGENILLFK RALGVTTGIL
160 170 180 190 200
PWNFPFFLIA RKMAPALLTG NTIVIKPSEF TPNNAIAFAK IVDEIGLPRG
210 220 230 240 250
VFNLVLGRGE TVGQELAGNP KVAMVSMTGS VSAGEKIMAT AAKNITKVCL
260 270 280 290 300
ELGGKAPAIV MDDADLELAV KAIVDSRVIN SGQVCNCAER VYVQKGIYDQ
310 320 330 340 350
FVNRLGEAMQ AVQFGNPAER NDIAMGPLIN AAALERVEQK VARAVEEGAR
360 370 380 390 400
VAFGGKAVEG KGYYYPPTLL LDVRQEMSIM HEETFGPVLP VVAFDTLEDA
410 420 430 440 450
ISMANDSDYG LTSSIYTQNL NVAMKAIKGL KFGETYINRE NFEAMQGFHA
460 470
GWRKSGIGGA DGKHGLHEYL QTQVVYLQS
Length:479
Mass (Da):52,273
Last modified:January 23, 2007 - v2
Checksum:iDA7819EA0C05C32F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64541 Genomic DNA. Translation: AAA23427.1.
U00096 Genomic DNA. Translation: AAC74497.1.
AP009048 Genomic DNA. Translation: BAA15032.1.
PIRiA38165.
RefSeqiNP_415933.1. NC_000913.3.
WP_000115943.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74497; AAC74497; b1415.
BAA15032; BAA15032; BAA15032.
GeneIDi945672.
KEGGiecj:JW1412.
eco:b1415.
PATRICi32118116. VBIEscCol129921_1478.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64541 Genomic DNA. Translation: AAA23427.1.
U00096 Genomic DNA. Translation: AAC74497.1.
AP009048 Genomic DNA. Translation: BAA15032.1.
PIRiA38165.
RefSeqiNP_415933.1. NC_000913.3.
WP_000115943.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HG2X-ray2.20A1-479[»]
2ILUX-ray2.70A1-479[»]
2IMPX-ray2.10A1-479[»]
2OPXX-ray2.53A1-479[»]
ProteinModelPortaliP25553.
SMRiP25553. Positions 3-479.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260173. 9 interactions.
850044. 1 interaction.
DIPiDIP-9081N.
IntActiP25553. 5 interactions.
MINTiMINT-1313045.
STRINGi511145.b1415.

2D gel databases

SWISS-2DPAGEP25553.

Proteomic databases

EPDiP25553.
PaxDbiP25553.
PRIDEiP25553.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74497; AAC74497; b1415.
BAA15032; BAA15032; BAA15032.
GeneIDi945672.
KEGGiecj:JW1412.
eco:b1415.
PATRICi32118116. VBIEscCol129921_1478.

Organism-specific databases

EchoBASEiEB0034.
EcoGeneiEG10035. aldA.

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271509.
InParanoidiP25553.
KOiK07248.
OMAiINEDHNA.
PhylomeDBiP25553.

Enzyme and pathway databases

BioCyciEcoCyc:LACTALDDEHYDROG-MONOMER.
ECOL316407:JW1412-MONOMER.
MetaCyc:LACTALDDEHYDROG-MONOMER.
BRENDAi1.2.1.22. 2026.
SABIO-RKP25553.

Miscellaneous databases

EvolutionaryTraceiP25553.
PROiP25553.

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.
IPR029510. Ald_DH_CS_GLU.
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.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALDA_ECOLI
AccessioniPrimary (citable) accession number: P25553
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.