NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.

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

CP000512; ABM35082.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_972856.1; -.

3D structure databases

ModBase

A1TVU4.

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.
IPR015590; Aldehyde_DHase.
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.

Pfam

PF00171; Aldedh; 1.
Pfam graphical view of domain structure.

PIRSF000151; GPR; 1.

TIGR00407; proA; 1.

PS01223; PROA; 1.

Genome annotation databases

GeneID

4667910; -.

GenomeReviews

CP000512_GR; Aave_4545.

KEGG

aav:Aave_4545; -.

NMPDR

fig|397945.5.peg.3914; -.

CMR

A1TVU4; Aave_4545.

Other

ProtoNet

A1TVU4.

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`	`1 426`	`426`		`Gamma-glutamyl phosphate reductase.`	`PRO_1000049929`

Sequence information

Length: 426 AA [This is the length of the unprocessed precursor]

Molecular weight: 45427 Da [This is the MW of the unprocessed precursor]

CRC64: CD037332B397AAA4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNAQHIAETL HALGSQAKAA SALMARAPSA VKNRALLALA RRLRDNTTAL QADNARDLER 

        70         80         90        100        110        120 
ARAAGLAEPM VDRLKLTPKV LETCALGCEQ LATMGDVIGE ISGMRQQPSG IRVGQMRVPI 

       130        140        150        160        170        180 
GVFGMIYESR PNVTIEAASL SIKSGNACIL RGGSEAIDSN RALARLVQEA LEEAGLPGDA 

       190        200        210        220        230        240 
VQLVQTTDRE AVGHLIAMPQ YVDVIIPRGG KGLIERISRD AKVPVIKHLD GNCHTYVDDP 

       250        260        270        280        290        300 
CDVAMAVKVA DNAKTQKYSP CNASEGLLVA RGVAAEFLPR IGAVYAAKGV EMRGCPETLA 

       310        320        330        340        350        360 
LLAGVPGATL VHATEQDWSE EYLAPIISIK VVEGLDEAIA HINRYGSHHT DAILTRDHMH 

       370        380        390        400        410        420 
AQRFLREVDS ASVMVNASTR FADGFEYGLG AEIGISTDKF HARGPVGIEG LTSLKWVVLG 


EGDIRA

A1TVU4 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