A9GVS8 (PROA_SORC5) 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:	sce3676

Organism

Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So ce56)) [Complete proteome] [HAMAP]

Taxonomic identifier

448385 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Sorangiineae › Polyangiaceae › Sorangium

Protein attributes

Sequence length	426 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 By similarity. 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 – 426	426	Gamma-glutamyl phosphate reductase HAMAP MF_00412		PRO_0000340920

Sequences

	Sequence		Length	Mass (Da)
	A9GVS8 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: D14D6CC5325FF237	FASTA	426	45,048
	10 20 30 40 50 60 MEQSNIDLEG ALRALCQRAR TAARALAPLD RAQKDRALRA IAERLRAEAG EGKRSAVLAA 70 80 90 100 110 120 NAEDVAAARA AGVSEALVDR LVLDEARLAA IAGAVLEIAA ASDPVGQVVG MERRPNGLLV 130 140 150 160 170 180 GQVRVPLGVI AMIYESRPNV TVDAAVLCLK SGNAAILRGG KEAARSNAAL GELISDALRS 190 200 210 220 230 240 VGLPADAVQM VPSLDREATR ILLGLTGMID LAIPRGGEGL IRFVAENARV PVIQHYKGVN 250 260 270 280 290 300 HLYADAGCDL EMACRLVENG KLQRPGVCNA LECLLVHEDV AAPLLGRVAA LSERGLELRG 310 320 330 340 350 360 DAATCALVPS ARKAAEDDYG REFLAPILAV RVVRSLDEAI EHIGRYGSMH TEVICTPRYD 370 380 390 400 410 420 HAQRFLREVD ASCVLVNASS RFNDGGELGL GAEIGISTTK LHAYGPMGLA SLTTLKWIAY GEGQTR

References

[1]

"Complete genome sequence of the myxobacterium Sorangium cellulosum." Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O., Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J., Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A. , Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C., Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T., Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S., Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F., Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G., Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D., Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H., Puehler A., Mueller R. Nat. Biotechnol. 25:1281-1289(2007) [PubMed: 17965706] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: So ce56.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM746676 Genomic DNA. Translation: CAN93836.1.
RefSeq	YP_001614316.1. NC_010162.1.
3D structure databases
ProteinModelPortal	A9GVS8.
ModBase	Search...
Protein-protein interaction databases
STRING	A9GVS8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5808700.
GenomeReviews	Gene locus sce3676 in contig AM746676_GR.
KEGG	scl:sce3676.
PATRIC	23665603. VBISorCel80414_4010.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG318080.
OMA	YGICGAM.
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_SORC5

Accession

Primary (citable) accession number: A9GVS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program