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Reviewed, UniProtKB/Swiss-Prot P39821 (PROA_BACSU)

Last modified November 25, 2008. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Gamma-glutamyl phosphate reductase
      Short name=GPR
    EC=1.2.1.41
Alternative name(s):
    Glutamate-5-semialdehyde dehydrogenase
    Glutamyl-gamma-semialdehyde dehydrogenase
      Short name=GSA dehydrogenase
Gene names
Name: proA
Ordered Locus Names: BSU13130
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.

Catalytic activity

L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH.

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.

Subcellular location

CytoplasmBy similarity.

Sequence similarities

Belongs to the gamma-glutamyl phosphate reductase family.

Sequence caution

The sequence BAA05045.1 differs from that shown. Reason: Frameshift at position 375.

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Ontologies

Keywords

   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

proline biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: HAMAP

   Molecular functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamate-5-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 415415Gamma-glutamyl phosphate reductase
PRO_0000189696

Experimental info

Sequence conflict1081E → Q in BAA05045. Ref.1
Sequence conflict1741A → T in BAA05045. Ref.1
Sequence conflict2711H → N in BAA05045. Ref.1
Sequence conflict3591R → A in BAA05045. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P39821-1 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 8CA4B0D35F9F62D0

FASTA41545,337
        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

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References

« Hide 'large scale' references
[1]"Multiple copies of the proB gene enhance degS-dependent extracellular protease production in Bacillus subtilis."
Ogura M., Kawata-Mukai M., Itaya M., Takio K., Tanaka T.
J. Bacteriol. 176:5673-5680(1994) [PubMed: 8083159] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"Sequence of the Bacillus subtilis genome between xlyA and ykoR."
Devine K.M.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
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. expand/collapse author list , 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.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

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Cross-references

Sequence databases

D26044 Genomic DNA. Translation: BAA05045.1. Frameshift.
AJ002571 Genomic DNA. Translation: CAA05592.1.
Z99110 Genomic DNA. Translation: CAB13170.1.
PIRC69682.
RefSeqNP_389196.1.

3D structure databases

HSSPHSSP built from PDB template 1O20 based on UniProtKB Q9WYC9.
ModBaseSearch...

Genome annotation databases

GeneID936166.
GenomeReviewsGene locus BSU13130 in contig AL009126_GR.
KEGGbsu:BSU13130.
NMPDRfig|224308.1.peg.1315.

Organism-specific databases

SubtiListBG10964. proA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP39821.

Enzyme and pathway databases

BioCycBSUB224308:BSU1315-MON.

Family and domain databases

HAMAPMF_00412.
[Tree]
InterProIPR016163. Ald_DHase_C.
IPR016162. Ald_DHase_N.
IPR000965. Gglut_pp_reduct.
IPR012134. Glu-5-SA_DHase.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11063:SF1. GSA_DH. 1 hit.
PIRSFPIRSF000151. GPR. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePROA_BACSU
AccessionPrimary (citable) accession number: P39821
Secondary accession number(s): O35032
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 30, 2000
Last modified: November 25, 2008
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents