ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8FHK7

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ABDH_ECOL6
Primary accession number Q8FHK7
Secondary accession numbers None
Integrated into Swiss-Prot on January 9, 2007
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 44)
Name and origin of the protein
Protein name Gamma-aminobutyraldehyde dehydrogenase
Synonyms EC 1.2.1.19
1-pyrroline dehydrogenase
4-aminobutanal dehydrogenase
ABALDH
Gene name
Name: ydcW
OrderedLocusNames: c1869
From
Escherichia coli O6 [TaxID: 217992] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
DOI=10.1073/pnas.252529799; PubMed=12471157 [NCBI, ExPASy, EBI, Israel, Japan]
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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
AE014075; AAN80331.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_753769.1; -.
3D structure databases
HSSP P56533; 1A4S. [HSSP ENTRY / PDB]
SMR Q8FHK7; 1-474.
ModBase Q8FHK7.
Ontologies
GO
GO:0019145; Molecular function: aminobutyraldehyde dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from HAMAP).
GO:0016646; Molecular function: oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009447; Biological process: putrescine catabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01275; -; 1.
PBIL [Tree]
InterPro IPR017749; 1-pyrroline_dehydrogenase.
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; FALSE_NEG.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
Genome annotation databases
GeneID 1035695; -.
GenomeReviews AE014075_GR; c1869.
KEGG ecc:c1869; -.
Phylogenomic databases
HOGENOM Q8FHK7; -.
Genome annotation databases
CMR Q8FHK7; c1869.
Other
ProtoNet Q8FHK7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   474  474     Gamma-aminobutyraldehyde dehydrogenase. PRO_0000269694
NP_BIND   172   175  4     NAD (By similarity). 
NP_BIND   225   231  7     NAD (By similarity). 
ACT_SITE   246   246        By similarity. 
ACT_SITE   280   280        Nucleophile (By similarity). 
BINDING   146   146        NAD; via carbonyl oxygen (By similarity). 
BINDING   209   209        NAD (By similarity). 
Sequence information
Length: 474 AA [This is the length of the unprocessed precursor] Molecular weight: 50859 Da [This is the MW of the unprocessed precursor] CRC64: 876ED25B0BE019B9 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MQHKLLINGE LVSGEGEKQP VYNPATGDVL LEIAEASAEQ VNAAVRAADA AFAEWGQTTP 

        70         80         90        100        110        120 
KARAECLLKL ADVIEENGQV FAELESRNCG KPLHSAFNDE IPAIVDVFRF FAGAARCLNG 

       130        140        150        160        170        180 
LAAGEYLEGH TSMIRRDPLG VVASIAPWNY PLMMAAWKLA PALAAGNCVV LKPSEITPLT 

       190        200        210        220        230        240 
ALKLAELAKD IFPAGVINVL FGRGKTVGDP LTGHPKVRMV SLTGSIATGE HIISHTAPSI 

       250        260        270        280        290        300 
KRTHMELGGK APVIVFDDAD IEAVVEGVRT FGYYNAGQDC TAACRIYAQK GIYDTLVEKL 

       310        320        330        340        350        360 
GAAVATLKSG SPDDESTELG PLSSLAHLER VSKAVEEAKA TGHIKVITGG EKRKGNGYYY 

       370        380        390        400        410        420 
APTLLAGALQ DDAIVQKEVF GPVVSVTLFD NEEQVVNWAN DSQYGLASSV WTKDVGRAHR 

       430        440        450        460        470 
VSARLQYGCT WVNTHFMLVS EMPHGGQKLS GYGKDMSLYG LEDYTVVRHV MVKH
Q8FHK7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!