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UniProtKB/Swiss-Prot entry Q2SZ88


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

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Entry information
Entry name PROA_BURTA
Primary accession number Q2SZ88
Secondary accession numbers None
Integrated into Swiss-Prot on October 17, 2006
Sequence was last modified on January 24, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 24)
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: BTH_I1214
From
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [TaxID: 271848] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R., Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D., Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F., Roberts K., Hatch B., Smith H.O., Venter J.C.;
Submitted (JUL-2005) 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
CP000086; ABC38329.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_441761.1; -.
3D structure databases
ModBase Q2SZ88.
Enzyme and pathway databases
BioCyc BTHA271848:BTH_I1214-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: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.
BLOCKS Q2SZ88.
Genome annotation databases
GeneID 3849726; -.
GenomeReviews CP000086_GR; BTH_I1214.
KEGG bte:BTH_I1214; -.
TIGR BTH_I1214; -.
Phylogenomic databases
HOGENOM Q2SZ88; -.
Other
ProtoNet Q2SZ88.
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   423  423     Gamma-glutamyl phosphate reductase. PRO_0000252566
Sequence information
Length: 423 AA [This is the length of the unprocessed precursor] Molecular weight: 45309 Da [This is the MW of the unprocessed precursor] CRC64: BFC044A712674A8C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDIDQYMTDV GRRARRASRS IARASTAAKN AALEAVARAI ERDAGALKAA NARDVARAKD 

        70         80         90        100        110        120 
KGLDAAFVDR LTLSDKALKT MVEGLRQVAT LPDPIGEMSN LKYRPSGIQV GQMRVPLGVI 

       130        140        150        160        170        180 
GIIYESRPNV TIDAAALCLK SGNATILRGG SEALESNTAL AKLIGEGLAE AGLPQDTVQV 

       190        200        210        220        230        240 
VETADRAAVG RLITMTEYVD VIVPRGGKSL IERLINEARV PMIKHLDGIC HVYVDDRASV 

       250        260        270        280        290        300 
TKALTVCDNA KTHRYGTCNT METLLVARGI APAVLSPLGR LYREKGVELR VDADARAVLE 

       310        320        330        340        350        360 
AAGVGPLVDA TDEDWRTEYL APVLAIKIVD GIDAAIEHIN EYGSHHTDAI VTEDHDRAMR 

       370        380        390        400        410        420 
FLREVDSASV MVNASTRFAD GFEFGLGAEI GISNDKLHAR GPVGLEGLTS LKYVVLGHGE 


GRQ 

Q2SZ88 in FASTA format

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