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Q2IMG0 (PROA_ANADE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Adeh_0212
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
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 HAMAP MF_00412.

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 processproline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamate-5-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000252563

Sequences

Sequence LengthMass (Da)Tools
Q2IMG0 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: EA1F4626CCDB8EEB

FASTA42745,377
        10         20         30         40         50         60 
MRKEKSLGLA AEMRKLAEAS REAARALSHA DPRRKDAALR AAAEAIGRRE RRILSENARD 

        70         80         90        100        110        120 
VAAARAAGQN AAYLDRLKLD PKRLAGIAAS LREIAGLRDP VGEVTASWRR PNGLEIRKVR 

       130        140        150        160        170        180 
IPLGVVLMVY EARPNVTVDA AALCLKSGNA AILRPGSDAL RSSLALAEAF AEGLEKAGLP 

       190        200        210        220        230        240 
AASAQVVPTP DREATYELLA LDDLIDLAIP RGGPSLIRAV AERSRVPVLK HYQGVCHLYL 

       250        260        270        280        290        300 
DASAPPQQAV DLALNGKVQR PGVCNATECL LVHRAAAGKL LPPVGRALAD AGVELRCDPT 

       310        320        330        340        350        360 
ALTILKRAGV AAVPARPDDF GKEFLDKILA VRVVADLDGA LDHIARYGSL HTEAIVTRDL 

       370        380        390        400        410        420 
ASARRFQREV DASAVMVNAS TRFNDGGELG LGAEIGISTT KLHAFGPMGL AELTTQKFLV 


EGEGHVR 

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References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2CP-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000251 Genomic DNA. Translation: ABC79989.1.
RefSeqYP_463426.1. NC_007760.1.

3D structure databases

HSSPHSSP built from PDB template 2H5G based on UniProtKB P54886.
ProteinModelPortalQ2IMG0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2IMG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3886294.
GenomeReviewsGene locus Adeh_0212 in contig CP000251_GR.
KEGGade:Adeh_0212.
PATRIC20916447. VBIAnaDeh31384_0228.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAYGICGAM.
PhylomeDBQ2IMG0.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycADEH290397:ADEH_0212-MONOMER.

Family and domain databases

HAMAPMF_00412. ProA.
[Tree]
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
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. 2 hits.
KOK00147.
PANTHERPTHR11063:SF1. GSA_DH. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00407. ProA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_ANADE
AccessionPrimary (citable) accession number: Q2IMG0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: March 7, 2006
Last modified: January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families