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)DescriptionActionsGraphical viewLength
Active sitei251By similarity1
Active sitei285By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi207 – 213NADBy similarity7

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000565642 – 479Lactaldehyde dehydrogenaseAdd BLAST478

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 interactors.
850044. 1 interactor.
DIPiDIP-9081N.
IntActiP25553. 5 interactors.
MINTiMINT-1313045.
STRINGi511145.b1415.

Structurei

Secondary structure

1479
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 11Combined sources3
Beta strandi14 – 16Combined sources3
Beta strandi23 – 27Combined sources5
Turni29 – 31Combined sources3
Beta strandi34 – 39Combined sources6
Helixi43 – 62Combined sources20
Helixi65 – 81Combined sources17
Helixi83 – 94Combined sources12
Helixi98 – 116Combined sources19
Turni117 – 121Combined sources5
Beta strandi125 – 127Combined sources3
Beta strandi134 – 142Combined sources9
Beta strandi144 – 149Combined sources6
Beta strandi152 – 154Combined sources3
Helixi155 – 168Combined sources14
Beta strandi172 – 176Combined sources5
Helixi183 – 195Combined sources13
Beta strandi201 – 204Combined sources4
Turni209 – 211Combined sources3
Helixi212 – 218Combined sources7
Beta strandi222 – 229Combined sources8
Helixi231 – 242Combined sources12
Turni243 – 245Combined sources3
Beta strandi247 – 251Combined sources5
Beta strandi257 – 260Combined sources4
Helixi266 – 274Combined sources9
Turni279 – 282Combined sources4
Beta strandi285 – 287Combined sources3
Beta strandi289 – 294Combined sources6
Helixi295 – 297Combined sources3
Helixi298 – 310Combined sources13
Turni317 – 319Combined sources3
Helixi331 – 346Combined sources16
Beta strandi350 – 353Combined sources4
Beta strandi360 – 362Combined sources3
Beta strandi368 – 372Combined sources5
Helixi378 – 381Combined sources4
Beta strandi386 – 396Combined sources11
Helixi397 – 405Combined sources9
Beta strandi407 – 416Combined sources10
Helixi420 – 429Combined sources10
Beta strandi432 – 439Combined sources8
Beta strandi456 – 458Combined sources3
Helixi462 – 467Combined sources6
Beta strandi470 – 478Combined sources9

3D structure databases

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

Protein-protein interaction databases

BioGridi4260173. 9 interactors.
850044. 1 interactor.
DIPiDIP-9081N.
IntActiP25553. 5 interactors.
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: November 2, 2016
This is version 140 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.