NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VF5;
DOI=10.1038/32831; PubMed=9537320 [NCBI, ExPASy, EBI, Israel, Japan]
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
Nature 392:353-358(1998).

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

AE000657; AAC07119.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C70392; C70392.

RefSeq

NP_213729.1; -.

3D structure databases

HSSP

Q9WYC9; 1O20. [HSSP ENTRY / PDB]

ModBase

O67166.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_1071-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: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

1193800; -.

GenomeReviews

AE000657_GR; aq_1071.

KEGG

aae:aq_1071; -.

NMPDR

fig|224324.1.peg.744; -.

Phylogenomic databases

HOGENOM

O67166; -.

Genome annotation databases

CMR

O67166; aq_1071.

Other

ProtoNet

O67166.

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_0000189684`

Sequence information

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

Molecular weight: 49119 Da [This is the MW of the unprocessed precursor]

CRC64: BE6500C58A2B2D61 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNYIEEKVNR ARSVLRELTS LKTSVKNETL LKVAELIDKN RDYIKEENRK DVEKAKEMGL 

        70         80         90        100        110        120 
RPAVVDRLVL NDKRIDGMVK VLKDVASLPD PVGEIIKMWN LPNGLKVGRM RVPLGVIFIV 

       130        140        150        160        170        180 
YESRPNVTIE ASSLCMKSSN AVILRGGKEA INSNKALVNL IKEACRETGF PEDAVQFIDR 

       190        200        210        220        230        240 
SEREIVWEIL KMEGKIDVAI PRGGESLIRA VVEHAKVPVI KHYKGVCNIY VDDEADLEKA 

       250        260        270        280        290        300 
YHIVYNAKVQ RPSVCNAVEN LVINRKILKE FFPKMAYYLG KAGVELRCDE ESLQVIKENP 

       310        320        330        340        350        360 
KLSFVNAKPA TEEDYYEEFL DLILAVKVVD DVDEAIAFIE KYGSKHSDAI ITENYTKAMK 

       370        380        390        400        410        420 
FLREVDSAAV YVNASTRFTD GNEFGLGAEM GISTDKIHAR GPMALEELTI PKFVILGEGQ 

       430 
VRDNFGVPEE WMKEF

O67166 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