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 B0CFL0

[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_ACAM1
Primary accession number B0CFL0
Secondary accession numbers None
Integrated into Swiss-Prot on May 20, 2008
Sequence was last modified on February 26, 2008 (Sequence version 1)
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: AM1_2014
From
Acaryochloris marina (strain MBIC 11017) [TaxID: 329726] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Acaryochloris.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0709772105; PubMed=18252824 [NCBI, ExPASy, EBI, Israel, Japan]
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.;
"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina.";
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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
CP000828; ABW27029.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001516343.1; -.
3D structure databases
ModBase B0CFL0.
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.
PIRSF PIRSF000151; GPR; 1.
TIGRFAMs TIGR00407; proA; 1.
PROSITE PS01223; PROA; 1.
BLOCKS B0CFL0.
ProtoNet B0CFL0.
Genome annotation databases
GeneID 5680828; -.
GenomeReviews CP000828_GR; AM1_2014.
KEGG amr:AM1_2014; -.
CMR B0CFL0; AM1_2014.
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   431  431     Gamma-glutamyl phosphate reductase. PRO_1000080474
Sequence information
Length: 431 AA [This is the length of the unprocessed precursor] Molecular weight: 45666 Da [This is the MW of the unprocessed precursor] CRC64: CCD327A05288B456 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTVLTNSLTE VAQQTRQAAI QLAGASTETK NQALEAVAQA LEAATPEILE ANVQDCQQAK 

        70         80         90        100        110        120 
AAGIANALYA RLKLDATKLK GAIAGVRSVA TLEDPVGTVQ LKRELDTDLV LSRVSCPLGV 

       130        140        150        160        170        180 
LGVIFEARPD AVMQIAALAM KSGNGVLLKG GQEALHSCQA LVKAIHQGLS NTAVSPNVVA 

       190        200        210        220        230        240 
LLTSREETLE LLNLDQDVNL IIPRGSNDFV RFVQENTRIP VLGHAEGICH LYVDQAAKLD 

       250        260        270        280        290        300 
QAVEIAVDSK IQYPAACNAV ETILVHDAIA PQYLPKLTAA LQDNHVKVLG DAKTQAIVDV 

       310        320        330        340        350        360 
GPATETDWAT EYGDLIVSIK VVASLSDAIA HINQYGSGHT DAIATEDDQA AAVFMNQVDA 

       370        380        390        400        410        420 
AGVFHNCSTR FADGFRYGFG AEVGISTQRM PPRGPVGLEG LVTYKYQLKG QGQIVATYAG 

       430 
SDARPFTHKD L
B0CFL0 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 ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!