NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.01927-05; PubMed=16885469 [NCBI, ExPASy, EBI, Israel, Japan]
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.;
"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction.";
J. Bacteriol. 188:6002-6015(2006).

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

AM167904; CAJ50105.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_787007.1; -.

3D structure databases

ModBase

Q2KXE0.

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

6267189; -.

GenomeReviews

AM167904_GR; BAV2495.

KEGG

bav:BAV2495; -.

NMPDR

fig|521.1.peg.3; -.

Phylogenomic databases

HOGENOM

Q2KXE0; -.

Genome annotation databases

CMR

Q2KXE0; BAV2495.

Other

ProtoNet

Q2KXE0.

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`	`1 419`	`419`		`Gamma-glutamyl phosphate reductase.`	`PRO_0000252564`

Sequence information

Length: 419 AA [This is the length of the unprocessed precursor]

Molecular weight: 44373 Da [This is the MW of the unprocessed precursor]

CRC64: FD66A8A0D0A16518 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSIEQIMLT LGENARQASR AMMRASGTAK NRALLAMAEL IIDGKAALQA ANALDLEAAR 

        70         80         90        100        110        120 
ANGLEPALLD RLTLSDRSVQ LMAEGLRQIA ALPDPVGSLG PTQVRPNGMR VAQMRVPLGV 

       130        140        150        160        170        180 
IGIIYESRPN VTIDAAALCL KSGNATILRG GSEALHSNLA LGAIVQAGLA AAELPPAAVQ 

       190        200        210        220        230        240 
VVSTTDRAAV GKLVTMTEHI DVIVPRGGKG LIARLAQEAR VPLIKHLDGN CHVYIDAAAD 

       250        260        270        280        290        300 
PDRALEIAFN AKTYRYGVCG SMETLLVHRA IAPTQLPRIA RALIEHGVEL RGCERSQAIV 

       310        320        330        340        350        360 
PGMAAASEED WGTEYLGPVL AVRVVDDLDQ AMEHIARWGS GHTDAIVTEN LAAAQRFQRE 

       370        380        390        400        410 
VDSSSVYVNL PTVFADGFEY GLGAEIGIST NRLHARGPVG LEGLTTYKWV LTGEGQTRG

Q2KXE0 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