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 Q3MH53

[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_ANAVT
Primary accession number Q3MH53
Secondary accession numbers None
Integrated into Swiss-Prot on April 4, 2006
Sequence was last modified on April 4, 2006 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 23)
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: Ava_0057
From
Anabaena variabilis (strain ATCC 29413 / PCC 7937) [TaxID: 240292] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
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 T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
"Complete sequence of Anabaena variabilis ATCC 29413.";
Submitted (SEP-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
CP000117; ABA19683.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_320578.1; -.
3D structure databases
ModBase Q3MH53.
Enzyme and pathway databases
BioCyc AVAR240292:AVA_0057-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: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.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000151; GPR; 1.
TIGRFAMs TIGR00407; proA; 1.
PROSITE PS01223; PROA; 1.
BLOCKS Q3MH53.
ProtoNet Q3MH53.
Genome annotation databases
GeneID 3683469; -.
GenomeReviews CP000117_GR; Ava_0057.
KEGG ava:Ava_0057; -.
NMPDR fig|240292.3.peg.363; -.
Phylogenomic databases
HOGENOM Q3MH53; -.
Genome annotation databases
CMR Q3MH53; Ava_0057.
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   434  434     Gamma-glutamyl phosphate reductase. PRO_0000229992
Sequence information
Length: 434 AA [This is the length of the unprocessed precursor] Molecular weight: 46945 Da [This is the MW of the unprocessed precursor] CRC64: 3393756F7C3684DA [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTTLQVASSL NDIAQQTRQA ASLLAMLSTE AKNQAIAAVA QALESAKEEI LQANIADCEA 

        70         80         90        100        110        120 
ATAEGIAKPL YKRLQLDEHK LRDAIAGVRD VGKLADPIGQ VQIQRELDTG LVLKRITCPL 

       130        140        150        160        170        180 
GVLGIIFEAR PEAAIQIISL AIKSGNGVIL KCGKEAVRSC EAIVKAVKQG LSTTDVNPDV 

       190        200        210        220        230        240 
VQLLTTREET LELLRLDKYV DLIIPRGSNS FVRFVQENTR IPVLGHADGI CHVYIDKSAD 

       250        260        270        280        290        300 
IEKAIAVSVD AKVQYPAACN AIETLLVHHS IAAEFLPKVA QALAERQVEL KGDERTLQIL 

       310        320        330        340        350        360 
PEIAAATAID WETEYSDFIL SIKIVDSLTE AIAHINQYGS RHTDAIITED VAAVETFFGL 

       370        380        390        400        410        420 
VNSAGVFHNC STRFADGFRY GFGAEVGIST QQMPPRGPVG LEGLVTYKYQ MTGTGHIVAT 

       430 
YTGENAKPFT HQDF
Q3MH53 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!