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UniProtKB/Swiss-Prot entry Q6HHC2


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

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Entry information
Entry name PROA_BACHK
Primary accession number Q6HHC2
Secondary accession numbers None
Integrated into Swiss-Prot on August 30, 2005
Sequence was last modified on July 19, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 33)
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: BT9727_2730
From
Bacillus thuringiensis subsp. konkukian [TaxID: 180856] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus group.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=97-27;
DOI=10.1128/JB.188.9.3382-3390.2006; PubMed=16621833 [NCBI, ExPASy, EBI, Israel, Japan]
Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis.";
J. Bacteriol. 188:3382-3390(2006).
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
AE017355; AAT60127.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_037054.1; -.
3D structure databases
ModBase Q6HHC2.
Enzyme and pathway databases
BioCyc BTHU281309:BT9727_2730-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.
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 Q6HHC2.
Genome annotation databases
GeneID 2857793; -.
GenomeReviews AE017355_GR; BT9727_2730.
KEGG btk:BT9727_2730; -.
NMPDR fig|281309.1.peg.2694; -.
Phylogenomic databases
HOGENOM Q6HHC2; -.
Genome annotation databases
CMR Q6HHC2; BT9727_2730.
Other
ProtoNet Q6HHC2.
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   415  415     Gamma-glutamyl phosphate reductase. PRO_0000189692
Sequence information
Length: 415 AA [This is the length of the unprocessed precursor] Molecular weight: 45597 Da [This is the MW of the unprocessed precursor] CRC64: 99D90EDD6A76CC58 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNEVLAKGKK AKEIARELVL KSTEQKNEAL SAIADQLILE TAYILEENKK DIEEGKAKGF 

        70         80         90        100        110        120 
SDSLLDRLML NEQRIVDMTE GIKQLIELRD PVGECVSAWE RPNGLSIQEM RVPLGVVGMI 

       130        140        150        160        170        180 
YEARPNVTVD AATICLKTGN AVILRGSSSA IHSNKAIVAV IHRALKQTSL PQESVQLIED 

       190        200        210        220        230        240 
TTRDSAKQLF TMNDYLDVLI PRGGKQLIDT VVREASVPVL ETGAGNCHVF IDETADKQMA 

       250        260        270        280        290        300 
FDIIINAKTQ RPSVCNAIET IVLHEKWAEQ YGSELFSSLK KRGVELRGDQ KALAMDSSIV 

       310        320        330        340        350        360 
LASEEDWGTE FLSLTLAVKL VSSIEEAIHH INTYGSMHSE AIISENEENV SKFFVSVDAA 

       370        380        390        400        410 
ALYHNASTRF TDGSEFGFGA EIGISTQKLH VRGPMGLPAL TSTKYVIRGN GQIRK 

Q6HHC2 in FASTA format

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