P74935 (PROA_TREPA) 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:	TP_0350

Organism

Treponema pallidum (strain Nichols) [Complete proteome] [HAMAP]

Taxonomic identifier

243276 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Treponema

Protein attributes

Sequence length	428 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 – 428	428	Gamma-glutamyl phosphate reductase HAMAP MF_00412		PRO_0000189806
Experimental info
	Sequence conflict	153	1	P → A in AAB39980. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P74935 [UniParc]. Last modified December 15, 1998. Version 3. Checksum: B4E2BC5BE46D5C45	FASTA	428	46,608
	10 20 30 40 50 60 MVEVYARLRA AVARLAVCSA AEKDGALRAV RDALHAQRED ILRANAQDLA RAREAGLAAP 70 80 90 100 110 120 LVARLALSEH LLEDMLRSLT VLSLQRDPIG EIIEGYTLAN GLEIRKVRVP LGVVAVIYES 130 140 150 160 170 180 RPNVTVDAFA LAYKSGNAVL LRAGSAASYS NAPLLRAIHV GLKKAHGVVD AVAVPPVLEE 190 200 210 220 230 240 KYGDVDHILR ARGFIDAVFP RGGAALIRRV VEGAHVPVIE TGCGVCHLYV DESANIDVAL 250 260 270 280 290 300 QIAENAKLQK PAACNSVETL LVHRAVARPF LHRVQEIFAT CEETTRKPGG VDFFCDAESF 310 320 330 340 350 360 SLLTERGARK NVFHAQAETW DREYLDYQVS VRVVPNLEEA LRHIARHSTK HSEVIVTRDR 370 380 390 400 410 420 ARARRFHQEV DAACVYVNAS SRFTDGGQFG MGAEIGVSTQ KLHARGPMGL CALTTSKYLI DGEGQVRP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequences of the proA and proB genes of Treponema pallidum, the syphilis agent." Stamm L.V., Barnes N.Y. DNA Seq. 8:63-70(1997) [PubMed: 9522123] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Nichols.
[2]	"Complete genome sequence of Treponema pallidum, the syphilis spirochete." Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A., Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D., Khalak H.G., Richardson D.L., Howell J.K. , Chidambaram M., Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O., Venter J.C. Science 281:375-388(1998) [PubMed: 9665876] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nichols.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U61535 Genomic DNA. Translation: AAB39980.1. AE000520 Genomic DNA. Translation: AAC65335.1.
PIR	E71336.
RefSeq	NP_218790.1. NC_000919.1.
3D structure databases
ProteinModelPortal	P74935.
ModBase	Search...
Protein-protein interaction databases
IntAct	P74935. 2 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2611456.
GenomeReviews	Gene locus TP_0350 in contig AE000520_GR.
KEGG	tpa:TP0350.
NMPDR	fig|243276.1.peg.349.
PATRIC	20530693. VBITrePal57110_0367.
TIGR	TP_0350.
Phylogenomic databases
HOGENOM	HBG318080.
OMA	YGICGAM.
ProtClustDB	PRK00197.
Enzyme and pathway databases
BioCyc	TPAL243276:TP_0350-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_TREPA

Accession

Primary (citable) accession number: P74935
Secondary accession number(s): O83370

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 15, 1998
Last modified:	January 25, 2012
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program