Skip Header

Contribute Send feedback
Read comments (?) or add your own

A8HS45 (A8HS45_AZOC5) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 37. Feed History...

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

Names and origin

Protein namesRecommended name:
Gamma-glutamyl phosphate reductase HAMAP MF_00412
Short name=GPR HAMAP MF_00412
EC=1.2.1.41 HAMAP MF_00412
Alternative name(s):
Glutamate-5-semialdehyde dehydrogenase HAMAP MF_00412
Glutamyl-gamma-semialdehyde dehydrogenase HAMAP MF_00412
Gene names
Name:proA HAMAP MF_00412
Ordered Locus Names:AZC_4138
OrganismAzorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / ORS 571) [Complete proteome] [HAMAP] EMBL BAF90136.1
Taxonomic identifier438753 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Xanthobacteraceae › Azorhizobium

Protein attributes

Sequence length439 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 MF_00412 SAAS SAAS020593

Catalytic activity

L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP MF_00412 SAAS SAAS020593

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. HAMAP MF_00412 SAAS SAAS020593

Subcellular location

Cytoplasm By similarity HAMAP MF_00412 SAAS SAAS020593.

Sequence similarities

Belongs to the gamma-glutamyl phosphate reductase family. HAMAP MF_00412

Sequences

Sequence LengthMass (Da)Tools
A8HS45 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 115186C4BB862B98

FASTA43945,393
        10         20         30         40         50         60 
MAMPHAARLS VAASAGSAAP VDVPAVLSQM GRAARAAART LALAPAEQKT AALKAAAARI 

        70         80         90        100        110        120 
RAATPEILAA NADDMARARA DGMSGAFQDR LALTESRIEA IAAGVEMVAG LPDPVGAVTE 

       130        140        150        160        170        180 
SWTRPNGLVI ERVRTPLGVI GVIYESRPNV TADAAALCVR AGNAVILRGG SDSLGSSGAI 

       190        200        210        220        230        240 
HKAFVAGLVD AGLSADCVQF VPFSDRTAVG LMLGGLDGNL DVIVPRGGKG LVARVQSEAR 

       250        260        270        280        290        300 
VPVFAHLDGI VHVYVHAAAD LDMAKTVLLN AKMRRTGICG AAETLLVDEK VAASQLKPLV 

       310        320        330        340        350        360 
EMLLDAGCEV RGDAAAQAVD PRVKPAVDAD WDTEYEDAII SVKLVPDLAA AIDHIETHGS 

       370        380        390        400        410        420 
HHTDSIITRD EAAAARFLRE VDSAIVMHNA STQFADGGEF GFGAEIGIAT GRMHARGPVG 

       430 
AEQLTSFKYR VHGNGQTRP

« Hide

References

[1]"Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium caulinodans ORS571."
Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009384 Genomic DNA. Translation: BAF90136.1.
RefSeqYP_001527054.1. NC_009937.1.

3D structure databases

ProteinModelPortalA8HS45.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8HS45.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5688722.
GenomeReviewsGene locus AZC_4138 in contig AP009384_GR.
KEGGazc:AZC_4138.
PATRIC21025163. VBIAzoCau17976_4317.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG318080.
OMAYGICGAM.
ProtClustDBPRK00197.

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 nameA8HS45_AZOC5
AccessionPrimary (citable) accession number: A8HS45
Entry history
Integrated into UniProtKB/TrEMBL: December 4, 2007
Last sequence update: December 4, 2007
Last modified: December 14, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info