Skip Header

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

A0LCZ1 (PROA_MAGSM) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 45. 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
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:Mmc1_3348
OrganismMagnetococcus sp. (strain MC-1) [Complete proteome] [HAMAP]
Taxonomic identifier156889 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Magnetococcus

Protein attributes

Sequence length423 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

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 – 423423Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000340891

Sequences

Sequence LengthMass (Da)Tools
A0LCZ1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 443AA65544540748

FASTA42345,608
        10         20         30         40         50         60 
MSNDSIKLID EIGKKARKAA RQLAWLDSGS KNATLHAMAD ALIACKKILQ VENEKDLEAG 

        70         80         90        100        110        120 
EKNGLTDAML DRLRLTDQVI ASMAEGIRQV AALPDPIGEI NHMRRLANQL QVGKMRVPLG 

       130        140        150        160        170        180 
VIGIIYESRP NVTADAAALC VKSGNAVILR GGSEAFHSNR AIAAALAQGM EKGRVPSDAV 

       190        200        210        220        230        240 
QVVSTTDRAA VSALLKADQY VDIIIPRGGK GLIQRVMDEA TIPVIKHLDG ICHTYIDADA 

       250        260        270        280        290        300 
DPAKAIDITF NGKMQRTGVC NATETLLIHE KVAKTILPAL AKRLNQADCV LRGCPETIRL 

       310        320        330        340        350        360 
VGEVAPVIPA TEEDWDTEYL AAILAIRVVK NLEEAMDHID AHSSRHTEVI VTENHATAMR 

       370        380        390        400        410        420 
FVREVDASAV MVNASSRFND GFQFGLGAEM GISTDKLHVR GPVGLEGLTC EKWIVLGDGQ 


LRS

« Hide

References

[1]"Complete sequence of Magnetococcus sp. MC-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Goodwin L.A., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000471 Genomic DNA. Translation: ABK45834.1.
RefSeqYP_867240.1. NC_008576.1.

3D structure databases

ProteinModelPortalA0LCZ1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0LCZ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4481624.
GenomeReviewsGene locus Mmc1_3348 in contig CP000471_GR.
KEGGmgm:Mmc1_3348.
NMPDRfig|156889.1.peg.1006.
PATRIC22433343. VBIMagSp23654_3399.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAYGICGAM.
PhylomeDBA0LCZ1.

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_MAGSM
AccessionPrimary (citable) accession number: A0LCZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 45 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents