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Q5NLX5 (PROA_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. 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:ZMO1661
OrganismZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]
Taxonomic identifier264203 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas

Protein attributes

Sequence length428 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 By similarity. HAMAP-Rule MF_00412

Catalytic activity

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

Pathway

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

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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_processL-proline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00412
PRO_0000189820

Sequences

Sequence LengthMass (Da)Tools
Q5NLX5 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 33643683D7674537

FASTA42845,809
        10         20         30         40         50         60 
MTGNKIDQAT PTEMMAGMAK KARLASQILA QAPTAQKAEA LVLTADAIRR HSADILAANA 

        70         80         90        100        110        120 
QDVATAENNQ SSSAMVDRLR LTEARLENMA SALEVIAHLE DPVGQIIDKR TRPNGLELTR 

       130        140        150        160        170        180 
IRVPIGVIGI IYESRPNVTI DAAALTLMSG NAAILRGGSE AIHSNKALYQ TMREGLAKAG 

       190        200        210        220        230        240 
LPEEAIQLVP TTDRALVGAM LTASGLIDLV IPRGGKSLVA RVQQDARVPV LAHLDGINHS 

       250        260        270        280        290        300 
YVHKEADPEK VEKVVVNAKM RRTGICGATE SLLIDRGYPV EKVKSLLQAL HNAGCEIRGT 

       310        320        330        340        350        360 
AEIQKIDPEA KAVSEEDWGT EYLDAVLSVR FVDDMDDALS HIARYSSGHT DAILTENREV 

       370        380        390        400        410        420 
AEKFLASVDS AIVMWNASTQ FADGGEFGLG AEIGIATGRI HARGPVALEG LTSYKWQVRG 


TGQIRPVA 

« Hide

References

[1]"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4."
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. expand/collapse author list , Kang H.L., Lee S.Y., Lee K.J., Kang H.S.
Nat. Biotechnol. 23:63-68(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008692 Genomic DNA. Translation: AAV90285.1.
RefSeqYP_163396.1. NC_006526.2.

3D structure databases

ProteinModelPortalQ5NLX5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264203.ZMO1661.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV90285; AAV90285; ZMO1661.
GeneID3188730.
KEGGzmo:ZMO1661.
PATRIC32568586. VBIZymMob102260_1568.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHOG000246356.
KOK00147.
OMACNAIETL.
OrthoDBEOG6FFSCX.
ProtClustDBPRK00197.

Enzyme and pathway databases

UniPathwayUPA00098; UER00360.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPMF_00412. ProA.
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]
PANTHERPTHR11063:SF1. PTHR11063:SF1. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_ZYMMO
AccessionPrimary (citable) accession number: Q5NLX5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 1, 2005
Last modified: February 19, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways