Reviewed, UniProtKB/Swiss-Prot Q7WH30 (PROA_BORBR)

Names and origin

Protein names

Recommended name:
    Gamma-glutamyl phosphate reductase
      Short name=GPR
    EC=1.2.1.41
Alternative name(s):
    Glutamate-5-semialdehyde dehydrogenase
    Glutamyl-gamma-semialdehyde dehydrogenase
      Short name=GSA dehydrogenase

Gene names

Name:	proA
Ordered Locus Names:	BB3380

Organism

Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

518 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (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. HAMAP MF_00412
Catalytic activity	L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP MF_00412
Pathway	Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. HAMAP MF_00412
Subcellular location	Cytoplasm By similarity HAMAP MF_00412.
Sequence similarities	Belongs to the gamma-glutamyl phosphate reductase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Proline biosynthesis
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW proline biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro glutamate-5-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 419	419	Gamma-glutamyl phosphate reductase HAMAP MF_00412		PRO_0000189701

Sequences

	Sequence		Length	Mass (Da)
	Q7WH30-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 0F9DA046BBAC1F66	FASTA	419	44,277
	10 20 30 40 50 60 MSSIETYMQS VGEQARTASR AMMRATGAAK NQALLAMAEA ILAQRAELQA ANAKDVAAAR 70 80 90 100 110 120 ANGLEAALLD RLTLSDRSIA LMAEGLRQIA ALPDPVGSIT ATSVRPNGMR VAQMRVPLGV 130 140 150 160 170 180 IGIIYESRPN VTIDAAALCL KSGNATILRG GSEALHSNVA LGRIVQAGLQ AAGLPTAAVQ 190 200 210 220 230 240 VIDTTDRAAV GKLVTMTEHV DVIVPRGGKG LISRLAQEAR VPLIKHLDGN CHVYVDAAAD 250 260 270 280 290 300 LAKAHDIAFN AKTYRYGVCG AMETLLVHAD VAQRLLPVLG QALHEHGVEL RGCARALQWL 310 320 330 340 350 360 PEGKPADDAD WATEYLGPVL AVRVVDTIDE AMDHIARWGS GHTDAIVTEN LSAAQRFQRE 370 380 390 400 410 VDSSSVYVNL PTCFADGFEY GLGAEIGIST NRLHARGPVG LEGLTTLKWV LNGEGQVRG

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RB50 / ATCC BAA-588 / NCTC 13252.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640447 Genomic DNA. Translation: CAE33872.1.
RefSeq	NP_889914.1.
3D structure databases
SMR	Q7WH30. Positions 11-419.
ModBase	Search...
Genome annotation databases
GeneID	2659997.
KEGG	bbr:BB3380.
NMPDR	fig|257310.1.peg.3361.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG318080.
OMA	QYPAACN.
PhylomeDB	Q7WH30.
Enzyme and pathway databases
BioCyc	BBRO257310:BB3380-MONOMER.
BRENDA	1.2.1.41. 413.
Family and domain databases
HAMAP	MF_00412. ProA. [Tree]
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. IPR000965. G-glutamylP_reductase. IPR020593. G-glutamylP_reductase_CS. IPR012134. Glu-5-SA_DH. [Graphical view]
Gene3D	G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11063:SF1. GSA_DH. 1 hit.
Pfam	PF00171. Aldedh. 2 hits. [Graphical view]
PIRSF	PIRSF000151. GPR. 1 hit.
TIGRFAMs	TIGR00407. proA. 1 hit.
PROSITE	PS01223. PROA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PROA_BORBR

Accession

Primary (citable) accession number: Q7WH30

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)