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UniProtKB/Swiss-Prot entry Q6FEN5

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

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Entry information
Entry name PROA_ACIAD
Primary accession number Q6FEN5
Secondary accession numbers None
Integrated into Swiss-Prot on September 13, 2004
Sequence was last modified on July 19, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 35)
Name and origin of the protein
Protein name Gamma-glutamyl phosphate reductase
Synonyms GPR
EC 1.2.1.41
Glutamate-5-semialdehyde dehydrogenase
Glutamyl-gamma-semialdehyde dehydrogenase
GSA dehydrogenase
Gene name
Name: proA
OrderedLocusNames: ACIAD0547
From
Acinetobacter sp. (strain ADP1) [TaxID: 62977] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gkh910; PubMed=15514110 [NCBI, ExPASy, EBI, Israel, Japan]
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium.";
Nucleic Acids Res. 32:5766-5779(2004).
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
CR543861; CAG67473.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_045295.1; -.
3D structure databases
ModBase Q6FEN5.
Enzyme and pathway databases
BioCyc ASP62977:ACIAD0547-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004350; Molecular function: glutamate-5-semialdehyde dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006561; Biological process: proline biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00412; -; 1.
PBIL [Tree]
InterPro IPR016163; Ald_DHase_C.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
IPR000965; Gglut_pp_reduct.
IPR012134; Glu-5-SA_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11063:SF1; GSA_DH; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000151; GPR; 1.
TIGRFAMs TIGR00407; proA; 1.
PROSITE PS01223; PROA; 1.
ProtoNet Q6FEN5.
Genome annotation databases
GeneID 2880045; -.
GenomeReviews CR543861_GR; ACIAD0547.
KEGG aci:ACIAD0547; -.
NMPDR fig|62977.3.peg.34; -.
Phylogenomic databases
HOGENOM Q6FEN5; -.
Genome annotation databases
CMR Q6FEN5; ACIAD0547.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP; Oxidoreductase; Proline biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   421  421     Gamma-glutamyl phosphate reductase. PRO_0000189681
Sequence information
Length: 421 AA [This is the length of the unprocessed precursor] Molecular weight: 46059 Da [This is the MW of the unprocessed precursor] CRC64: 6086636708C835DF [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MQDSIEQYMQ AVGQQARKAS RVLSSASTHT KNNALSAIYT ALVNHEPEIL AANAVDMQKG 

        70         80         90        100        110        120 
RDSHLDSALL DRLELTPTRF KGMLQGLKDV IALTDPIGEI TDLAYRPSGI QLGKMRVPLG 

       130        140        150        160        170        180 
VIGMIYESRP NVTLEAASLA LKSGNAIILR GGSEALQSNK AIATAIQHGL KVAGLPEHAI 

       190        200        210        220        230        240 
QVIETADRAA VGQLITMTEY VDVIVPRGGK SLIERISNEA RIPVIKHLDG NCHVFIDVEA 

       250        260        270        280        290        300 
DLHKALPIAL NAKTHRYGVC NAMETLLVHE EIAEEFLPRI AELYAEKHVE LRGCQETRRI 

       310        320        330        340        350        360 
LGSSVKTATE EDWYTEYLAP ILAIKVVEHI DQAIEHINKY GSHHTDAIVT ENYSKVRKFL 

       370        380        390        400        410        420 
AEVDSSSVMI NASTRFADGF EYGLGAEIGI STDKIHARGP VGLEGLTSQK WIVFGDGQIR 


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Q6FEN5 in FASTA format

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