P0C1E0 (PROA_CORGL) 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:	Cgl2354, cg2586

Organism

Corynebacterium glutamicum (Brevibacterium flavum)

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	432 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 Reference 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 – 432	432	Gamma-glutamyl phosphate reductase HAMAP MF_00412		PRO_0000189719

Sequences

	Sequence		Length	Mass (Da)
	P0C1E0 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: 1DC94EF2989B7E15	FASTA	432	45,667
	10 20 30 40 50 60 MSSTTLTDDQ IRDNERTEVL AKATAAKNIV PDIAVLGTGP KNAILRAAAD ELVARSAEII 70 80 90 100 110 120 EANASDIEAG RANGMEESMI DRLALDESRI EGIAGGLRQV AGLTDPVGEV LRGHVMENGI 130 140 150 160 170 180 QMKQVRVPLG VMGMVYEARP NVTVDAFGLA LKSGNVALLR GSSTAVHSNT KLVEILQDVL 190 200 210 220 230 240 ERFELPRETV QLLPCQTRGS VQDLITARGL VDVVIPRGGA GLINAVVTGA TVPTIETGTG 250 260 270 280 290 300 NCHFYIDAEA KLDQAIAMVI NGKTRRCSVC NATETALLDA ALSDSDKLAV VQALQEAGVT 310 320 330 340 350 360 IHGRVAELEA FGATDVVEAT ETDWDSEYLS FDIAVAVVDG VDGALAHIAK YSTKHTEAIA 370 380 390 400 410 420 TQNIETAQRF ADRVDAAAVM INASTAYTDG EQYGMGAEIG ISTQKLHARG PMALPELTST 430 KWILQGTGQI RP

References

[1]

"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

[2]

"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000036 Genomic DNA. Translation: BAB99747.1. BX927155 Genomic DNA. Translation: CAF21019.1.
RefSeq	NP_601555.1. NC_003450.3. YP_226599.1. NC_006958.1.
3D structure databases
ProteinModelPortal	P0C1E0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1020305. 3344874.
GenomeReviews	Gene locus Cgl2354 in contig BA000036_GR. Gene locus cg2586 in contig BX927147_GR.
KEGG	cgb:cg2586. cgl:NCgl2272.
PATRIC	21496716. VBICorGlu203724_2290.
Phylogenomic databases
HOGENOM	HBG318080.
OMA	HRIEAMA.
PhylomeDB	P0C1E0.
ProtClustDB	PRK00197.
Enzyme and pathway databases
BioCyc	CGLU196627:CG2586-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_CORGL

Accession

Primary (citable) accession number: P0C1E0
Secondary accession number(s): P45638

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	May 16, 2006
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program