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UniProtKB/Swiss-Prot entry A1WCP4

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

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Entry information
Entry name PROA_ACISJ
Primary accession number A1WCP4
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on February 6, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 20)
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: Ajs_3913
From
Acidovorax sp. (strain JS42) [TaxID: 232721] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Comamonadaceae; Acidovorax.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
"Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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
CP000539; ABM44019.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_988095.1; -.
3D structure databases
ModBase A1WCP4.
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 A1WCP4.
Genome annotation databases
GeneID 4672840; -.
GenomeReviews CP000539_GR; Ajs_3913.
KEGG ajs:Ajs_3913; -.
CMR A1WCP4; Ajs_3913.
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   426  426     Gamma-glutamyl phosphate reductase. PRO_1000049930
Sequence information
Length: 426 AA [This is the length of the unprocessed precursor] Molecular weight: 45246 Da [This is the MW of the unprocessed precursor] CRC64: 63D207A92DA2F2D6 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNALNIAEYT HTLGLQAKTA SAQMARAPAA IKNKALLALA RLLRQNVDAL QGDNARDLER 

        70         80         90        100        110        120 
ARAAGLAEPM VDRLKLTPKV LETCAQGCEQ LAAMPDIIGE IQGMKQQPSG IRVGQMRVPI 

       130        140        150        160        170        180 
GVFGMIYESR PNVTIEAASL SIKSGNACIL RGGSEAIDSN KALARLVAQA LAEAGLPEHG 

       190        200        210        220        230        240 
VQLVQTTDRA AVGQLIAMPQ YVDVIIPRGG KGLIERISAE AKVPVIKHLD GNCHTYVDDP 

       250        260        270        280        290        300 
CDIAMAVQVA DNAKTQKYSP CNASEGLLVA RGVAAQFLPQ IGAVYAAKGV EMRGCPEALA 

       310        320        330        340        350        360 
ILRAVPGVQL AEATEADWSE EYLAPIISVK VVAGVDEAIA HINRYGSHHT DAILTRDHMH 

       370        380        390        400        410        420 
AQQFLRDVDS ASVMVNASTR FADGFEYGLG AEIGISTDKF HARGPVGIEG LTSLKWVVLG 


EGEVRT
A1WCP4 in FASTA format

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