NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1159/000079829; PubMed=15383718 [NCBI, ExPASy, EBI, Israel, Japan]
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential.";
J. Mol. Microbiol. Biotechnol. 7:204-211(2004).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1186/gb-2004-5-10-r77; PubMed=15461803 [NCBI, ExPASy, EBI, Israel, Japan]
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species.";
Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004).

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

AE017333; AAU40317.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000002; AAU22964.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_078602.1; -.
YP_091010.1; -.

3D structure databases

ModBase

Q65KU7.

Enzyme and pathway databases

BioCyc

BLIC279010:BL03751-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

3030461; -.
3097972; -.

GenomeReviews

CP000002_GR; BL03751.
AE017333_GR; BLi01413.

KEGG

bld:BLi01413; -.
bli:BL03751; -.

NMPDR

fig|279010.5.peg.867; -.

Phylogenomic databases

HOGENOM

Q65KU7; -.

Genome annotation databases

CMR

Q65KU7; BLi01413.

Other

ProtoNet

Q65KU7.

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`	`1 415`	`415`		`Gamma-glutamyl phosphate reductase 1.`	`PRO_0000189693`

Sequence information

Length: 415 AA [This is the length of the unprocessed precursor]

Molecular weight: 45473 Da [This is the MW of the unprocessed precursor]

CRC64: 473217C94BC4988F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSEVIEKAKK AKVAKEELVH QPTERKNEAL SFIAEAIRFK QDEILAENEK DIVRGKEKGF 

        70         80         90        100        110        120 
SPALLDRLAL TPERLNDIAD AVMLLTKLED PVGETLETIR KDNGLFIENV RVPLGVVGMI 

       130        140        150        160        170        180 
YEARPNVTVD AATLCLKTGN AVILRGSSSA INSNKALVRV IREALERSAL PEDAVQLIED 

       190        200        210        220        230        240 
TSKETAKQLF TLNDGLDVLI PRGGKNLIDM VVRESTVPVL ETGAGNCHIF IDESAQPDMA 

       250        260        270        280        290        300 
EQVVINAKTQ RPSVCNAIET VLIHKGWAEE HTKALLQKLE EAGVEIRGDE AVCTMLPSAV 

       310        320        330        340        350        360 
PARETDWGTE FLAPVVSIKT VAGIDEAIRH IRQYGTRHSE AILTENQENA RYFLTSVDAA 

       370        380        390        400        410 
AVYHNASTRF TDGFEFGYGA EIGISTQKLH ARGPMGLKAL TSSKYIIKGN GQIRI

Q65KU7 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