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Reviewed, UniProtKB/Swiss-Prot P25553 (ALDA_ECOLI)

Last modified June 16, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lactaldehyde dehydrogenase
    EC=1.2.1.22
Alternative name(s):
    Glycolaldehyde dehydrogenase
    EC=1.2.1.21
    Aldehyde dehydrogenase A
Gene names
Name: aldA
Synonyms: ald
Ordered Locus Names: b1415, JW1412
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Acts on lactaldehyde as well as other aldehydes.

Catalytic activity

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

Glycolaldehyde + NAD+ + H2O = glycolate + NADH.

Subunit structure

Homotetramer.

Induction

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

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.5
Chain2 – 479478Lactaldehyde dehydrogenase
PRO_0000056564

Regions

Nucleotide binding207 – 2137NAD By similarity

Sites

Active site2511 By similarity
Active site2851 By similarity

Secondary structure

.................................................................................. 479
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25553-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DA7819EA0C05C32F

FASTA47952,273
        10         20         30         40         50         60 
MSVPVQHPMY IDGQFVTWRG DAWIDVVNPA TEAVISRIPD GQAEDARKAI DAAERAQPEW 

        70         80         90        100        110        120 
EALPAIERAS WLRKISAGIR ERASEISALI VEEGGKIQQL AEVEVAFTAD YIDYMAEWAR 

       130        140        150        160        170        180 
RYEGEIIQSD RPGENILLFK RALGVTTGIL PWNFPFFLIA RKMAPALLTG NTIVIKPSEF 

       190        200        210        220        230        240 
TPNNAIAFAK IVDEIGLPRG VFNLVLGRGE TVGQELAGNP KVAMVSMTGS VSAGEKIMAT 

       250        260        270        280        290        300 
AAKNITKVCL ELGGKAPAIV MDDADLELAV KAIVDSRVIN SGQVCNCAER VYVQKGIYDQ 

       310        320        330        340        350        360 
FVNRLGEAMQ AVQFGNPAER NDIAMGPLIN AAALERVEQK VARAVEEGAR VAFGGKAVEG 

       370        380        390        400        410        420 
KGYYYPPTLL LDVRQEMSIM HEETFGPVLP VVAFDTLEDA ISMANDSDYG LTSSIYTQNL 

       430        440        450        460        470 
NVAMKAIKGL KFGETYINRE NFEAMQGFHA GWRKSGIGGA DGKHGLHEYL QTQVVYLQS 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and DNA sequencing of the Escherichia coli K-12 ald gene encoding aldehyde dehydrogenase."
Hidalgo E., Chen Y.-M., Lin E.C.C., Aguilar J.
J. Bacteriol. 173:6118-6123(1991) [PubMed: 1917845] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11.
Strain: K12.
[2]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-12.
Strain: K12 / EMG2.
[6]"Identification of lactaldehyde dehydrogenase and glycolaldehyde dehydrogenase as functions of the same protein in Escherichia coli."
Caballero E., Baldoma L., Ros J., Boronat A., Aguilar J.
J. Biol. Chem. 258:7788-7792(1983) [PubMed: 6345530] [Abstract]
Cited for: CHARACTERIZATION.
[7]"Involvement of lactaldehyde dehydrogenase in several metabolic pathways of Escherichia coli K12."
Baldoma L., Aguilar J.
J. Biol. Chem. 262:13991-13996(1987) [PubMed: 3308886] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

M64541 Genomic DNA. Translation: AAA23427.1.
U00096 Genomic DNA. Translation: AAC74497.1.
AP009048 Genomic DNA. Translation: BAA15032.1.
PIRA38165.
RefSeqAP_002040.1.
NP_415933.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2HG2X-ray2.20A2-478[»]
2ILUX-ray2.70A2-478[»]
2IMPX-ray2.10A2-478[»]
2OPXX-ray2.53A1-479[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:9081N.

2-D gel databases

SWISS-2DPAGEP25553.

Genome annotation databases

GeneID945672.
GenomeReviewsGene locus JW1412 in contig AP009048_GR.
Gene locus b1415 in contig U00096_GR.
KEGGecj:JW1412.
eco:b1415.

Organism-specific databases

EchoBASEEB0034.
EcoGeneEG10035. aldA.
CMRSearch...

Phylogenomic databases

HOGENOMP25553.
OMAP25553. GENILVF.

Enzyme and pathway databases

BioCycEcoCyc:LACTALDDEHYDROG-MON.
MetaCyc:LACTALDDEHYDROG-MON.
BRENDA1.2.1.22. 246.

Family and domain databases

InterProIPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALDA_ECOLI
AccessionPrimary (citable) accession number: P25553
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents