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UniProtKB/Swiss-Prot entry P25553


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ALDA_ECOLI
Primary accession number P25553
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 76)
Name and origin of the protein
Protein name Lactaldehyde dehydrogenase
Synonyms EC 1.2.1.22
Glycolaldehyde dehydrogenase
EC 1.2.1.21
Aldehyde dehydrogenase A
Gene name
Name: aldA
Synonyms: ald
OrderedLocusNames: b1415, JW1412
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
STRAIN=K12;
PubMed=1917845 [NCBI, ExPASy, EBI, Israel, Japan]
Hidalgo E., Chen Y.-M., Lin E.C.C., Aguilar J.;
"Molecular cloning and DNA sequencing of the Escherichia coli K-12 ald gene encoding aldehyde dehydrogenase.";
J. Bacteriol. 173:6118-6123(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.363; PubMed=9097039 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"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.";
DNA Res. 3:363-377(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 2-12.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[6]
CHARACTERIZATION.
PubMed=6345530 [NCBI, ExPASy, EBI, Israel, Japan]
Caballero E., Baldoma L., Ros J., Boronat A., Aguilar J.;
"Identification of lactaldehyde dehydrogenase and glycolaldehyde dehydrogenase as functions of the same protein in Escherichia coli.";
J. Biol. Chem. 258:7788-7792(1983).
[7]
CHARACTERIZATION.
PubMed=3308886 [NCBI, ExPASy, EBI, Israel, Japan]
Baldoma L., Aguilar J.;
"Involvement of lactaldehyde dehydrogenase in several metabolic pathways of Escherichia coli K12.";
J. Biol. Chem. 262:13991-13996(1987).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M64541; AAA23427.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74497.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15032.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A38165; A38165.
RefSeq AP_002040.1; -.
NP_415933.1; -.
3D structure databases
PDB
2HG2; X-ray; 2.20 A; A=1-479.[ExPASy / RCSB / EBI]
2ILU; X-ray; 2.70 A; A=1-479.[ExPASy / RCSB / EBI]
2IMP; X-ray; 2.10 A; A=1-479.[ExPASy / RCSB / EBI]
2OPX; X-ray; 2.53 A; A=1-479.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2HG2; -.
2ILU; -.
2IMP; -.
2OPX; -.
ModBase P25553.
Protein-protein interaction databases
DIP DIP:9081N; -.
Enzyme and pathway databases
BioCyc EcoCyc:LACTALDDEHYDROG-MON; -.
MetaCyc:LACTALDDEHYDROG-MON; -.
2D gel databases
SWISS-2DPAGE P25553; -.
Organism-specific databases
EchoBASE EB0034; -.
EcoGene EG10035; aldA.
Ontologies
GO
GO:0050569; Molecular function: glycolaldehyde dehydrogenase activity (inferred from electronic annotation from EC).
GO:0008911; Molecular function: lactaldehyde dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
ProtoNet P25553.
Genome annotation databases
GeneID 945672; -.
GenomeReviews U00096_GR; b1415.
AP009048_GR; JW1412.
KEGG ecj:JW1412; -.
eco:b1415; -.
Phylogenomic databases
HOGENOM P25553; -.
Genome annotation databases
CMR P25553; b1415.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   479  478     Lactaldehyde dehydrogenase. PRO_0000056564
NP_BIND   207   213  7     NAD (By similarity). 
ACT_SITE   251   251        By similarity. 
ACT_SITE   285   285        By similarity. 
STRAND   9    11  3      
STRAND   14    16  3      
STRAND   23    27  5      
TURN   29    31  3      
STRAND   34    39  6      
HELIX   43    62  20      
HELIX   65    81  17      
HELIX   83    94  12      
HELIX   98   116  19      
TURN   117   121  5      
STRAND   124   127  4      
STRAND   134   142  9      
STRAND   144   149  6      
STRAND   152   154  3      
HELIX   155   168  14      
STRAND   172   176  5      
HELIX   183   195  13      
STRAND   201   204  4      
TURN   209   211  3      
HELIX   212   218  7      
STRAND   222   229  8      
HELIX   231   242  12      
TURN   243   245  3      
STRAND   247   251  5      
STRAND   257   260  4      
HELIX   266   277  12      
HELIX   279   282  4      
STRAND   284   287  4      
STRAND   290   294  5      
HELIX   295   310  16      
TURN   317   319  3      
HELIX   331   347  17      
STRAND   350   353  4      
STRAND   360   362  3      
STRAND   368   372  5      
HELIX   378   380  3      
STRAND   386   396  11      
HELIX   397   405  9      
STRAND   406   416  11      
HELIX   420   429  10      
STRAND   432   439  8      
STRAND   456   458  3      
HELIX   462   467  6      
STRAND   470   478  9      
Sequence information
Length: 479 AA [This is the length of the unprocessed precursor] Molecular weight: 52273 Da [This is the MW of the unprocessed precursor] CRC64: DA7819EA0C05C32F [This is a checksum on the sequence]
        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 

P25553 in FASTA format

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View entry in raw text format (no links)
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