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Reviewed, UniProtKB/Swiss-Prot Q81P27 (PROA_BACAN)

Last modified November 3, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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: BA_2992, GBAA_2992, BAS2781
OrganismBacillus anthracis [Complete proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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. HAMAP MF_00412

Catalytic activity

L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP MF_00412

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. HAMAP MF_00412

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the gamma-glutamyl phosphate reductase family.

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: UniProtKB-SubCell

   Molecular functionNADP or NADPH binding

Inferred from electronic annotation. Source: InterPro

glutamate-5-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 414414Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000189686

Sequences

Sequence LengthMass (Da)Tools
Q81P27-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 29EA3C4601C7D6C5

FASTA41445,436
        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 
FDIINAKTQR PSVCNAIETI VLHEKWAEQY GSELFSSLKK RGVELRGDQK ALAMDSTIVL 

       310        320        330        340        350        360 
ASEEDWGTEF LSLTPAVKLV SSIEEAIHHI NTYGSMHSEA IISENEEKVS KFFVSVDAAA 

       370        380        390        400        410 
LYHNASTRFT DGSEFGSGAE IGISTQKLHV RGPMGLPALT STKYVIRGNG QIRK 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

AE016879 Genomic DNA. Translation: AAP26811.1.
AE017334 Genomic DNA. Translation: AAT32110.1.
AE017225 Genomic DNA. Translation: AAT55090.1.
RefSeqNP_845325.1.
YP_019635.1.
YP_029039.1.

3D structure databases

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

Genome annotation databases

GeneID1088121.
2819264.
2848284.
GenomeReviewsGene locus BA_2992 in contig AE016879_GR.
Gene locus BAS2781 in contig AE017225_GR.
Gene locus GBAA_2992 in contig AE017334_GR.
KEGGban:BA2992.
bar:GBAA2992.
bat:BAS2781.
TIGRBA_2992.
GBAA_2992.

Phylogenomic databases

HOGENOMQ81P27.
OMAQYPAACN.

Enzyme and pathway databases

BioCycBANT260799:BAS2781-MON.
BANT261594:GBAA2992-MON.
BRENDA1.2.1.41. 267517.

Family and domain databases

HAMAPMF_00412.
[Tree]
InterProIPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR000965. G-glutamylP_reductase.
IPR020593. G-glutamylP_reductase_CS.
IPR012134. Glu-5-SA_DH.
[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...

Entry information

Entry namePROA_BACAN
AccessionPrimary (citable) accession number: Q81P27
Secondary accession number(s): Q6HX99, Q6KRC1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

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