NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(2002).

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.
CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate + NADP⁺ = L-glutamyl 5-phosphate + NADPH.
PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2 .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000040; BAC45694.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_767069.1; -.

3D structure databases

HSSP

Q9WYC9; 1O20. [HSSP ENTRY / PDB]

ModBase

Q89X85.

Enzyme and pathway databases

BioCyc

BJAP224911:BLR0429-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004350;	Molecular function: glutamate-5-semialdehyde dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006561;	Biological process: proline biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00412; -; 1.
PBIL [Tree]

InterPro

IPR016163; Ald_DHase_C.
IPR016162; Ald_DHase_N.
IPR000965; Gglut_pp_reduct.
IPR012134; Glu-5-SA_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11063:SF1; GSA_DH; 1.

PIRSF000151; GPR; 1.

TIGR00407; proA; 1.

PS01223; PROA; 1.

Genome annotation databases

GeneID

1054342; -.

GenomeReviews

BA000040_GR; blr0429.

KEGG

bja:blr0429; -.

NMPDR

fig|224911.1.peg.429; -.

Phylogenomic databases

HOGENOM

Q89X85; -.

Genome annotation databases

CMR

Q89X85; blr0429.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP; Oxidoreductase; Proline biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 435`	`435`		`Gamma-glutamyl phosphate reductase.`	`PRO_0000189704`

Sequence information

Length: 435 AA [This is the length of the unprocessed precursor]

Molecular weight: 45636 Da [This is the MW of the unprocessed precursor]

CRC64: C043AA17C4682B50 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAPLKAVDG NADRTGDLQA LMSDLAARAR AAARVLALAP PEQKNRALEA MERAIRSNAA 

        70         80         90        100        110        120 
AILAANAEDV AEARASSNMT ASFIDRLTLT PARVESMAEG IGIVRGIADP VGIVTESWQR 

       130        140        150        160        170        180 
PNGMTIERVR VPLGVVGVIF ESRPNVAADA GVLCLKSGNA VILRGGSDSF RSCRAIHECL 

       190        200        210        220        230        240 
VQGLREAGLP EAAITLVPTR DRAAVGMMLS GLNGAIDVIV PRGGKSLVAR VEQEARVPVF 

       250        260        270        280        290        300 
AHLEGVNHVY VDASADLAMA KSIVLNAKMR RTGVCGAAET LLVDRAAAAT SLKPLVEMLI 

       310        320        330        340        350        360 
EAGCEVRGDD VVQKTDARVK PANDDDWDTE YLDAIIAAKV VDGVDGAIAH IQNHGSHHTD 

       370        380        390        400        410        420 
AIVSENEAAA KKFLSEVDSA IVLHNASTQF ADGGEFGFGA EIGIATGRFH ARGPVGAEQL 

       430 
TSFKYRVHGT GQTRP

Q89X85 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools