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Reviewed, UniProtKB/Swiss-Prot B4UM59 (PROA_ANASK)

Last modified November 3, 2009. Version 13. 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: AnaeK_0225
OrganismAnaeromyxobacter sp. (strain K) [Complete proteome] [HAMAP]
Taxonomic identifier447217 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length427 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 By similarity.

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 – 427427Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000123773

Sequences

Sequence LengthMass (Da)Tools
B4UM59-1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 20E8AAF64CCCE4B7

FASTA42745,243
        10         20         30         40         50         60 
MRKEKSLGLA AEMRTLAEAS REAARALSHA DPRRKDAALR AAAEAIGRRE KRILSENARD 

        70         80         90        100        110        120 
VAAARAAGQN AAYLDRLKLD PKRLAGIAAA LHEIAGLRDP VGEVTASWRR PNGLEIRKVR 

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

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

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

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

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


EGEGHVR 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter sp. K."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G., Beliaev A.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001131 Genomic DNA. Translation: ACG71467.1.
RefSeqYP_002132596.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6787830.
GenomeReviewsGene locus AnaeK_0225 in contig CP001131_GR.
KEGGank:AnaeK_0225.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAFDTEWLD.

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_ANASK
AccessionPrimary (citable) accession number: B4UM59
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: November 3, 2009
This is version 13 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