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UniProtKB/Swiss-Prot entry P39821


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

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Entry information
Entry name PROA_BACSU
Primary accession number P39821
Secondary accession number O35032
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on May 30, 2000 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 73)
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: BSU13130
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8083159 [NCBI, ExPASy, EBI, Israel, Japan]
Ogura M., Kawata-Mukai M., Itaya M., Takio K., Tanaka T.;
"Multiple copies of the proB gene enhance degS-dependent extracellular protease production in Bacillus subtilis.";
J. Bacteriol. 176:5673-5680(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Devine K.M.;
"Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
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
D26044; BAA05045.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ002571; CAA05592.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99110; CAB13170.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C69682; C69682.
RefSeq NP_389196.1; -.
3D structure databases
HSSP Q9WYC9; 1O20. [HSSP ENTRY / PDB]
ModBase P39821.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1315-MON; -.
Organism-specific databases
SubtiList BG10964; proA. [Micado]
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 P39821.
Genome annotation databases
GeneID 936166; -.
GenomeReviews AL009126_GR; BSU13130.
KEGG bsu:BSU13130; -.
NMPDR fig|224308.1.peg.1315; -.
Phylogenomic databases
HOGENOM P39821; -.
Genome annotation databases
CMR P39821; BSU13130.
Other
ProtoNet P39821.
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_0000189696
CONFLICT   108   108        E -> Q (in Ref. 1; BAA05045). 
CONFLICT   174   174        A -> T (in Ref. 1; BAA05045). 
CONFLICT   271   271        H -> N (in Ref. 1; BAA05045). 
CONFLICT   359   359        R -> A (in Ref. 1; BAA05045). 
Sequence information
Length: 415 AA [This is the length of the unprocessed precursor] Molecular weight: 45337 Da [This is the MW of the unprocessed precursor] CRC64: 8CA4B0D35F9F62D0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSEVSVKAKL AKEAAAEMIM KTTAEKDEAL SLIANGLRKE LDFLLAENAK DIVNGKENGL 

        70         80         90        100        110        120 
TPDIIDRLSL DEKRIRDIAD AVELLIDLAD PIGDSLETIE KENGLFIEKI RVPLGVVGMI 

       130        140        150        160        170        180 
YEARPNVTVD AATLCLKTGN AVVLRGSSSA IHSNKALVSV IYRALEQSAL PIHAVQLIED 

       190        200        210        220        230        240 
TSRETAKELF TLNDGLDVLI PRGGKKLIDL VVRESTVPVL ETGAGNCHIF IDETAKPQMA 

       250        260        270        280        290        300 
EKVVVNAKTQ RPSVCNAIES LLIHKAWARQ HGKELLDQLE NAGVEIRGDE LVCELHPSSK 

       310        320        330        340        350        360 
QASKEDWETE FLAPVLSVKT VENVQEAVKH IQQYGTNHSE AILTENDKNA VYFQTAVDRA 

       370        380        390        400        410 
AVYHNASTRF TDGFEFGYGA EIGISTQKLH ARGPMGLPAL TSTKYIIKGT GQIRE 

P39821 in FASTA format

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