Q735X3 (PROA_BACC1) Reviewed, UniProtKB/Swiss-Prot

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:	BCE_3028

Organism

Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]

Taxonomic identifier

222523 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	415 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	proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro glutamate-5-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 415	415	Gamma-glutamyl phosphate reductase HAMAP MF_00412		PRO_0000189687

Sequences

	Sequence		Length	Mass (Da)
	Q735X3 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 687D856F366A7E49	FASTA	415	45,735
	10 20 30 40 50 60 MNEVLAKGKR AKEVARELVL KSTHQKNEAL AAVANQLIHE TAYILEENKR DIEEGKAKGF 70 80 90 100 110 120 SDSLLDRLML TENRIIDMTE GIKQLIELRD PVGECVREWE RPNGLSIQEM RVPLGVVGMI 130 140 150 160 170 180 YEARPNVTVD AATICLKTGN TVILRGSSSA IHSNKAIVAV IHRALKQTSL PEESVQLIED 190 200 210 220 230 240 TTRDSAKQLF TMNDYLDVLI PRGGKQLIDT VVREASVPVL ETGAGNCHIF IDETADKQMA 250 260 270 280 290 300 IDIIINAKTQ RPSVCNAIET IVLHEKWAQQ HGSELFSSLK ERGVELRGDQ RALALDSSIV 310 320 330 340 350 360 LASEEDWGTE FLSLTLAVKV VSSIEEAIHH INTYGSMHSE AIISENEENV SKFFVSVDAA 370 380 390 400 410 ALYHNASTRF TDGSEFGFGA EIGISTQKLH VRGPMGLPAL TSTKYVIRGN GQIRK

References

[1]

"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10987.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017194 Genomic DNA. Translation: AAS41939.1.
RefSeq	NP_979331.1. NC_003909.8.
3D structure databases
ProteinModelPortal	Q735X3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q735X3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000026248; EBBACP00000025598; EBBACG00000026239.
GeneID	2751001.
GenomeReviews	Gene locus BCE_3028 in contig AE017194_GR.
KEGG	bca:BCE_3028.
NMPDR	fig|222523.1.peg.3003.
PATRIC	18854790. VBIBacCer118379_2895.
TIGR	BCE_3028.
Phylogenomic databases
eggNOG	COG0014.
GeneTree	EBGT00050000000020.
HOGENOM	HBG318080.
OMA	QYPAACN.
ProtClustDB	PRK00197.
Enzyme and pathway databases
BioCyc	BCER405917:BCE_3028-MONOMER.
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_dom. 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. 2 hits.
KO	K00147.
PANTHER	PTHR11063:SF1. GSA_DH. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
PIRSF	PIRSF000151. GPR. 1 hit.
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMs	TIGR00407. ProA. 1 hit.
PROSITE	PS01223. PROA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PROA_BACC1

Accession

Primary (citable) accession number: Q735X3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program