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Protein

Gamma-glutamyl phosphate reductase

Gene

proA

Organism
Bacillus anthracis
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH.UniRule annotation

Pathway:iL-proline biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamate 5-kinase (proB), Glutamate 5-kinase (proB)
  2. Gamma-glutamyl phosphate reductase (proA), Gamma-glutamyl phosphate reductase (proA)
This subpathway is part of the pathway L-proline biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate, the pathway L-proline biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Proline biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciANTHRA:PROA-MONOMER.
BANT260799:GJAJ-2844-MONOMER.
BANT261594:GJ7F-2951-MONOMER.
UniPathwayiUPA00098; UER00360.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamyl phosphate reductaseUniRule annotation (EC:1.2.1.41UniRule annotation)
Short name:
GPRUniRule annotation
Alternative name(s):
Glutamate-5-semialdehyde dehydrogenaseUniRule annotation
Glutamyl-gamma-semialdehyde dehydrogenaseUniRule annotation
Short name:
GSA dehydrogenaseUniRule annotation
Gene namesi
Name:proAUniRule annotation
Ordered Locus Names:BA_2992, GBAA_2992, BAS2781
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000000594 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 414414Gamma-glutamyl phosphate reductasePRO_0000189686Add
BLAST

Interactioni

Protein-protein interaction databases

IntActiQ81P27. 10 interactions.
STRINGi198094.BA_2992.

Structurei

3D structure databases

ProteinModelPortaliQ81P27.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the gamma-glutamyl phosphate reductase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0014.
HOGENOMiHOG000246356.
KOiK00147.
OMAiQYPAACN.
OrthoDBiEOG6FFSCX.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPiMF_00412. ProA.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR020593. G-glutamylP_reductase_CS.
IPR012134. Glu-5-SA_DH.
IPR000965. GPR_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFiPIRSF000151. GPR. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00407. proA. 1 hit.
PROSITEiPS01223. PROA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q81P27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEVLAKGKK AKEIARELVL KSTEQKNEAL SAIADQLILE TAYILEENKK
60 70 80 90 100
DIEEGKAKGF SDSLLDRLML NEQRIVDMTE GIKQLIELRD PVGECVSAWE
110 120 130 140 150
RPNGLSIQEM RVPLGVVGMI YEARPNVTVD AATICLKTGN AVILRGSSSA
160 170 180 190 200
IHSNKAIVAV IHRALKQTSL PQESVQLIED TTRDSAKQLF TMNDYLDVLI
210 220 230 240 250
PRGGKQLIDT VVREASVPVL ETGAGNCHVF IDETADKQMA FDIINAKTQR
260 270 280 290 300
PSVCNAIETI VLHEKWAEQY GSELFSSLKK RGVELRGDQK ALAMDSTIVL
310 320 330 340 350
ASEEDWGTEF LSLTPAVKLV SSIEEAIHHI NTYGSMHSEA IISENEEKVS
360 370 380 390 400
KFFVSVDAAA LYHNASTRFT DGSEFGSGAE IGISTQKLHV RGPMGLPALT
410
STKYVIRGNG QIRK
Length:414
Mass (Da):45,436
Last modified:June 1, 2003 - v1
Checksum:i29EA3C4601C7D6C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP26811.1.
AE017334 Genomic DNA. Translation: AAT32110.1.
AE017225 Genomic DNA. Translation: AAT55090.1.
RefSeqiNP_845325.1. NC_003997.3.
WP_001006638.1. NZ_KN050651.1.
YP_029039.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP26811; AAP26811; BA_2992.
AAT32110; AAT32110; GBAA_2992.
AAT55090; AAT55090; BAS2781.
GeneIDi1088121.
2848284.
KEGGiban:BA_2992.
bar:GBAA_2992.
bat:BAS2781.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP26811.1.
AE017334 Genomic DNA. Translation: AAT32110.1.
AE017225 Genomic DNA. Translation: AAT55090.1.
RefSeqiNP_845325.1. NC_003997.3.
WP_001006638.1. NZ_KN050651.1.
YP_029039.1. NC_005945.1.

3D structure databases

ProteinModelPortaliQ81P27.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ81P27. 10 interactions.
STRINGi198094.BA_2992.

Protocols and materials databases

DNASUi1088121.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP26811; AAP26811; BA_2992.
AAT32110; AAT32110; GBAA_2992.
AAT55090; AAT55090; BAS2781.
GeneIDi1088121.
2848284.
KEGGiban:BA_2992.
bar:GBAA_2992.
bat:BAS2781.

Phylogenomic databases

eggNOGiCOG0014.
HOGENOMiHOG000246356.
KOiK00147.
OMAiQYPAACN.
OrthoDBiEOG6FFSCX.

Enzyme and pathway databases

UniPathwayiUPA00098; UER00360.
BioCyciANTHRA:PROA-MONOMER.
BANT260799:GJAJ-2844-MONOMER.
BANT261594:GJ7F-2951-MONOMER.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPiMF_00412. ProA.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR020593. G-glutamylP_reductase_CS.
IPR012134. Glu-5-SA_DH.
IPR000965. GPR_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFiPIRSF000151. GPR. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00407. proA. 1 hit.
PROSITEiPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames / isolate Porton.
  2. 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.

Entry informationi

Entry nameiPROA_BACAN
AccessioniPrimary (citable) accession number: Q81P27
Secondary accession number(s): Q6HX99, Q6KRC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: July 22, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.