Entry Information
Protein Name AldH
Accession No P23883
Protein description Gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase
pI/Mw (Da)
Theoretical Experimental
5.71/53418.63 5.82/55481
Protein function and expression Involved in the breakdown of putrescine. It was previously shown to have a weak but measurable ALDH enzyme activity that prefers NADP over NAD as coenzyme.
Reference(s) Champion, K. M., J. C. Nishihara, J. C. Joly, and D. Arnott. 2001. Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes. Proteomics 1:1133-1148. (NCBI)

2D gels information
Map ID38
Reference(s)Champion, K. M., J. C. Nishihara, J. C. Joly, and D. Arnott. 2001. Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes. Proteomics 1:1133-1148. (NCBI)
Protein function and expression(s)Map: A B
pI/Mw: 5.82/55481

A
2-DE profile of E. coli proteins at the end of anti-CD18 blank run fermentation.
B
2-DE analysis of E. coli proteins from Nutropin production fermentation.
Swiss-Prot Database Reference

Entry information
Entry Name PUUC_ECOLI
Primary accession number P23883
Secondary accession numbers P78250 Q5H774 
Integrated into Swiss-Prot on 1991-11-01
Sequence was last modified on 1997-11-01 (Sequence version 2)
Annotations were last modified on 2006-06-27 (Entry version 48)
Name and origin of the protein
Protein name Gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase
Synonyms EC 1.2.1.- Gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase
Gamma-Glu-gamma-aminobutyraldehyde dehydrogenase
Gene name Name : puuC
OrderedLocusName : b1300
SynonymName : aldH
From Escherichia coli [TaxID:562] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia;
References
[1] NUCLEOTIDE SEQUENCE [GENOMIC DNA].DOI=10.1016/0378-1119(91)90028-A;PubMed=1840553[NCBI, ExPASy, EBI, Israel, Japan]
Heim R. , Strehler E.E. ,
"Cloning an Escherichia coli gene encoding a protein remarkably similar to mammalian aldehyde dehydrogenases."
Gene99:15-23(1991) 
[2] NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
strain = K12
DOI=10.1074/jbc.M411114200;PubMed=15590624[NCBI, ExPASy, EBI, Israel, Japan]
Kurihara S. , Oda S. , Kato K. , Kim H.G. , Koyanagi T. , Kumagai H. , Suzuki H. ,
"A novel putrescine utilization pathway involves gamma-glutamylated intermediates of Escherichia coli K-12."
J. Biol. Chem.280:4602-4608(2005) 
[3] 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) 
[4] 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."
Science277:1453-1474(1997) 
[5] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
DOI=10.1038/msb4100049;
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) 
Comments
  • FUNCTION : Involved in the breakdown of putrescine. Was previously shown to have a weak but measurable ALDH enzyme activity that prefers NADP over NAD as coenzyme
  • CATALYTIC ACTIVITY : Gamma-glutamyl-gamma-aminobutyraldehyde + NAD(+) + H(2)O = gamma-glutamyl-gamma-aminobutyrate + NADH
  • PATHWAY : Polyamine metabolism; putrescine degradation; from gamma-glutamyl-gamma-aminobutyraldehyde to gamma-glutamyl-gamma-aminobutyrate: third step
  • SIMILARITY : Belongs to the aldehyde dehydrogenase family
  • Copyright
    Copyrighted by the UniProt Consortium, see http://www.uniprot.org/. Distributed under the Creative Commons Attribution-NoDerivs License.
    Cross-reference
    Sequence databases
    EMBL M38433;AAA23428.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    AB200319;BAD88708.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U00096;AAC74382.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    AP009048;BAA14869.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    PIR G64878;G64878.
    3D structure databases
    HSSP P20000;1AG8[HSSP ENTRY / PDB].
    ModBase P23883
    Protein-protein interaction databases
    DIP P23883
    Enzyme and pathway databases
    BioCyc EcoCyc:ALDHDEHYDROG-MONOMER;-.
    2D gel databases
    SWISS-2DPAGE Get region on 2D PAGE
    Organism-specific gene databases
    EchoBASE EB0035;-.
    EcoGene EG10036;puuC.
    HOGENOM [Family / Alignment / Tree]
    Family and domain databases
    InterPro IPR002086;Ald_DH.
    IPR012303;NAD_ADH.
    Graphical view of domain structure
    Pfam PF00171;Aldedh;1.
    Pfam graphical view of domain structure
    PIRSF PIRSF000147;DHA;1.
    BLOCKS P23883
    PROSITE PS00070;ALDEHYDE_DEHYDR_CYS;1.
    PS00687;ALDEHYDE_DEHYDR_GLU;1.
    Genome annotation databases
    GenomeReviews U00096_GR;b1300.
    Other
    ProtoNet P23883
    UniRef View cluster of proteins with at least 50% / 90% / 100% identity
    Keyword
    Complete proteome; NAD; Oxidoreductase;
    Features
    Feature table viewer Feature aligner
    Key  From   To Length  Description  FTId
    CHAIN    1   495    495  Gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase  PRO_0000056448
    NP_BIND  244   249      6  NAD; ADP group(by similarity)  
    ACT_SITE  267   267    (by similarity)  
    ACT_SITE  302   302    (by similarity)  
    CONFLICT  313   313    S -> R: (in Ref. 1)  
    Sequence information
    Length: 495AA [This is the length of the unprocessed precursor] Molecular weight: 53419Da [This is the MW of the unprocessed precursor] CRC64: A20929C55F51C709[This is a checksum on the sequence]
            10         20         30         40         50         60
    MNFHHLAYWQ DKALSLAIEN RLFINGEYTA AAENETFETV DPVTQAPLAK IARGKSVDID
            70         80         90        100        110        120
    RAMSAARGVF ERGDWSLSSP AKRKAVLNKL ADLMEAHAEE LALLETLDTG KPIRHSLRDD
           130        140        150        160        170        180
    IPGAARAIRW YAEAIDKVYG EVATTSSHEL AMIVREPVGV IAAIVPWNFP LLLTCWKLGP
           190        200        210        220        230        240
    ALAAGNSVIL KPSEKSPLSA IRLAGLAKEA GLPDGVLNVV TGFGHEAGQA LSRHNDIDAI
           250        260        270        280        290        300
    AFTGSTRTGK QLLKDAGDSN MKRVWLEAGG KSANIVFADC PDLQQAASAT AAGIFYNQGQ
           310        320        330        340        350        360
    VCIAGTRLLL EESIADEFLA LLKQQAQNWQ PGHPLDPATT MGTLIDCAHA DSVHSFIREG
           370        380        390        400        410        420
    ESKGQLLLDG RNAGLAAAIG PTIFVDVDPN ASLSREEIFG PVLVVTRFTS EEQALQLAND
           430        440        450        460        470        480
    SQYGLGAAVW TRDLSRAHRM SRRLKAGSVF VNNYNDGDMT VPFGGYKQSG NGRDKSLHAL
           490 
    EKFTELKTIW ISLEA
    P23883 in FASTA format