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UniProtKB/Swiss-Prot entry Q32FQ5

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

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Entry information
Entry name ABDH_SHIDS
Primary accession number Q32FQ5
Secondary accession numbers None
Integrated into Swiss-Prot on January 9, 2007
Sequence was last modified on December 6, 2005 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 27)
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: SDY_1730
From
Shigella dysenteriae serotype 1 (strain Sd197) [TaxID: 300267] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Shigella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gki954; PubMed=16275786 [NCBI, ExPASy, EBI, Israel, Japan]
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.;
"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery.";
Nucleic Acids Res. 33:6445-6458(2005).
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
CP000034; ABB61850.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_403341.1; -.
3D structure databases
SMR Q32FQ5; 1-474.
ModBase Q32FQ5.
Enzyme and pathway databases
BioCyc SDYS300267:SDY_1730-MON; -.
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 3796294; -.
GenomeReviews CP000034_GR; SDY_1730.
KEGG sdy:SDY_1730; -.
NMPDR fig|216598.1.peg.4344; -.
Phylogenomic databases
HOGENOM Q32FQ5; -.
Genome annotation databases
CMR Q32FQ5; SDY_1730.
Other
ProtoNet Q32FQ5.
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_0000269701
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: 50881 Da [This is the MW of the unprocessed precursor] CRC64: B744AD5D2A467164 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MQHKLLINGE LVSGEGEKQP VYNPATGDVL LEIAEASAEQ VDAAVRAADA AFAEWGQTTP 

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

       130        140        150        160        170        180 
LAVGEYLEGH TSMIRRDPLG VVASIAPWNY LLMMAAWKLA PALAAGNCVV LKPSEITPLT 

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

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

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

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

       430        440        450        460        470 
VSARLQYGCT WVNTHFILVS EMPHGGQKLS GYGKDMSLYG LEDYTVVRHV MVKH
Q32FQ5 in FASTA format

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