E8QXT0 (E8QXT0_ISOPI) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00412
Short name=GPR HAMAP-Rule MF_00412
EC=1.2.1.41 HAMAP-Rule MF_00412

Alternative name(s):
Glutamate-5-semialdehyde dehydrogenase HAMAP-Rule MF_00412
Glutamyl-gamma-semialdehyde dehydrogenase HAMAP-Rule MF_00412

Gene names

Name:	proA HAMAP-Rule MF_00412
Ordered Locus Names:	Isop_3560 EMBL ADV64117.1

Organism

Isosphaera pallida (strain ATCC 43644 / DSM 9630 / IS1B) [Complete proteome] [HAMAP] EMBL ADV64117.1

Taxonomic identifier

575540 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Planctomycetes › Planctomycetia › Planctomycetales › Planctomycetaceae › Isosphaera › Isosphaera pallida

Protein attributes

Sequence length	440 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-Rule MF_00412 SAAS SAAS020593
Catalytic activity	L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP-Rule MF_00412 SAAS SAAS020593
Pathway	Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. HAMAP-Rule MF_00412 SAAS SAAS020593
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00412 SAAS SAAS020593.
Sequence similarities	Belongs to the gamma-glutamyl phosphate reductase family. HAMAP-Rule MF_00412

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Proline biosynthesis HAMAP-Rule MF_00412 SAAS SAAS020593
Cellular component	Cytoplasm HAMAP-Rule MF_00412 SAAS SAAS020593
Ligand	NADP HAMAP-Rule MF_00412 SAAS SAAS020593
Molecular function	Oxidoreductase HAMAP-Rule MF_00412 SAAS SAAS020593 EMBL ADV64117.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	L-proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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: HAMAP
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	E8QXT0 [UniParc]. Last modified April 5, 2011. Version 1. Checksum: 09DDB62A47D81CFA	FASTA	440	46,712
	10 20 30 40 50 60 MIPDPHAHAS ADAATSADAL SPDELKTICD HMADAAQRAA RKLMTASGAA KDAWLKASAR 70 80 90 100 110 120 GLIAQTEAIL AANARDLDHA QNAGLSRAAI DRLRLDSNRI AEIAHALEEI AALPDPLGET 130 140 150 160 170 180 LASSIRPNGL EVRKVRVPLG VVFMIYESRP NVTADAAALC VKSGNAVILR GGSEAFHSNH 190 200 210 220 230 240 ALHRVLADAL EPAGLPREAV QLVPVTDRAA VGHLLTRSDA IDLAIPRGGA GLIRRVVAEA 250 260 270 280 290 300 RMPVLKHYDG NCHVYIDQYA DPDMAEAIIL NAKVQRPGVC NAAETLLIHR AIAATMLPRI 310 320 330 340 350 360 AERLLAHGVE LRGDPEACAL VPAMTPATPE DWDTEYLDLT LAVAVVDSLD AAIEHINRHG 370 380 390 400 410 420 SKHTDAIVSR DLESVRRFAA RVDTAAVMIN ASTRFNDGGQ LGLGAEIGIS TDKLHARGPC 430 440 GLRELTTTKW IVTGSGHIRA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete sequence of chromosome of Isophaera pallida ATCC 43644." US DOE Joint Genome Institute (JGI-PGF) Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders E., Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V. , Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Eisen J.A. Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC 43644.
[2]	"Complete genome sequence of Isosphaera pallida type strain (IS1B)." US DOE Joint Genome Institute (JGI-PGF) Goker M., Cleland D., Saunders E., Lapidus A., Nolan M., Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A. , Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Beck B., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P. Stand. Genomic Sci. 4:63-71(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43644 / DSM 9630 / IS1B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002353 Genomic DNA. Translation: ADV64117.1.
RefSeq	YP_004180666.1. NC_014962.1.
3D structure databases
ProteinModelPortal	E8QXT0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADV64117; ADV64117; Isop_3560.
GeneID	10157714.
KEGG	ipa:Isop_3560.
PATRIC	46962190. VBIIsoPal14453_4555.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000246356.
KO	K00147.
Enzyme and pathway databases
BioCyc	IPAL575540:GI5T-3615-MONOMER.
UniPathway	UPA00098; UER00360.
Family and domain databases
Gene3D	3.40.309.10. 1 hit. 3.40.605.10. 2 hits.
HAMAP	MF_00412. ProA.
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]
PANTHER	PTHR11063:SF1. PTHR11063:SF1. 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

E8QXT0_ISOPI

Accession

Primary (citable) accession number: E8QXT0

Entry history

Integrated into UniProtKB/TrEMBL:	April 5, 2011
Last sequence update:	April 5, 2011
Last modified:	May 1, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)