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 A9IMB2


[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 PROA_BART1
Primary accession number A9IMB2
Secondary accession numbers None
Integrated into Swiss-Prot on June 10, 2008
Sequence was last modified on June 10, 2008 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 8)
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: BT0174
From
Bartonella tribocorum (strain CIP 105476 / IBS 506) [TaxID: 382640] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bartonellaceae; Bartonella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/ng.2007.38; PubMed=18037886 [NCBI, ExPASy, EBI, Israel, Japan]
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors.";
Nat. Genet. 39:1469-1476(2007).
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
AM260525; CAK00658.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
ModBase A9IMB2.
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: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.
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.
PIRSF PIRSF000151; GPR; 1.
TIGRFAMs TIGR00407; proA; 1.
PROSITE PS01223; PROA; 1.
BLOCKS A9IMB2.
ProtoNet A9IMB2.
Genome annotation databases
GenomeReviews AM260525_GR; BT0174.
CMR A9IMB2; BT0174.
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   409  409     Gamma-glutamyl phosphate reductase. PRO_0000340872
Sequence information
Length: 409 AA [This is the length of the unprocessed precursor] Molecular weight: 44016 Da [This is the MW of the unprocessed precursor] CRC64: 799420BB60213866 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGQKARSAAA ALAVASSEQK NNALEMIALS LEAHSDEILR ANCLDLEKAT QNNLKAAMVD 

        70         80         90        100        110        120 
RLKLDELRLA AMIDSVRQVA RLSDPVGQIM SAWTRPNGLH ISRVRTPLGV IGIIYESRPN 

       130        140        150        160        170        180 
VTIDASSLCL KAGNAVILRG GSDSFHSSYA LHCALVQGLE HSGLPKSAIQ MVGTTDRAAV 

       190        200        210        220        230        240 
GEILKGLDGA IDVIVPRGGK SLVARVQSDA RVPVFAHLEG LCHIYIDKSA DLDMARNIVL 

       250        260        270        280        290        300 
NAKLRRTGIC GAVETVLIDN EALKKFLPVL TALQEKGCEI RATEDIAFLV PDVKLASEED 

       310        320        330        340        350        360 
WSHEYLDAIL SVKTVEGVEG AISHIKRYSS GHTESIIAED MEVVKKFFNH LDSAILLHNA 

       370        380        390        400 
STQFADGGEF GFGMEIGIAT GKMHARGPIG VEQLTSFQYH IKGNGQVRA 

A9IMB2 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!