Reviewed, UniProtKB/Swiss-Prot P32296 (P5CS_VIGAC)

Names and origin

Protein names	Recommended name:     Delta-1-pyrroline-5-carboxylate synthetase       Short name=P5CS Including the following 2 domains:     1- Recommended name:             Glutamate 5-kinase                 Short name=GK               EC=2.7.2.11         Alternative name(s):             Gamma-glutamyl kinase     2- 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
Organism	Vigna aconitifolia (Mothbean)
Taxonomic identifier	3918 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Vigna

Protein attributes

Sequence length	671 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	P5CS plays a key role in proline biosynthesis, leading to osmoregulation in plants.
Catalytic activity	ATP + L-glutamate = ADP + L-glutamate 5-phosphate. L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH.
Enzyme regulation	Feedback regulated by proline.
Pathway	Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Tissue specificity	Expressed at high levels in leaves and is inducible in roots subjected to salt stress.
Sequence similarities	In the N-terminal section; belongs to the glutamate 5-kinase family. In the C-terminal section; belongs to the gamma-glutamyl phosphate reductase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Proline biosynthesis
Ligand	ATP-binding NADP Nucleotide-binding
Molecular function	Kinase Oxidoreductase Transferase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate 5-kinase activity Inferred from electronic annotation. Source: EC 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 – 671	671	Delta-1-pyrroline-5-carboxylate synthetase		PRO_0000109778
Regions
	Region	1 – 297	297	Glutamate 5-kinase
	Region	298 – 671	374	Gamma-glutamyl phosphate reductase

Sequences

	Sequence		Length	Mass (Da)
	P32296-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 30BAE7AAF7ED1DA6	FASTA	671	73,291
	10 20 30 40 50 60 MESAVDPSRG FMKDVKRVII KVGTAVVTRE EGRLAVGRLG ALCEQIKQLN SLGYDIILVS 70 80 90 100 110 120 SGPVGIGRQR LRFRKLINSS FADLQKPQLE LDGKACAAVG QNSLMALYDT LFTQLDVTSA 130 140 150 160 170 180 QLLVTDNDFR DKDFRKQLTE TVKSLLALKV IPVFNENDAV STRKAPYEDS SGIFWDNDSL 190 200 210 220 230 240 SALLALELKA DLLVLLSDVE GLYSGPPSDP HSKLIYTYNK EKHQNEITFG DKSRVGRGGM 250 260 270 280 290 300 TAKVKAAVHA AEAGIPVVIT SGFAPENIIN VLQGQRIGTL FHKDAHEWAQ VKEVDAREMA 310 320 330 340 350 360 VAAGNVREGS RRYLQRKGNK ILLKIADALE ANEKIIRIEN EADVTAAQEA GYEKSLVARL 370 380 390 400 410 420 ALKPGKIASL ANNMRIIANM EDPIGRVLKR TELSDGLILE KTSSPLGVLL IVFESRPDAL 430 440 450 460 470 480 VQIASLAIRS GNGLLLKGGK EAKRSNAILH KVIIEAIPDN VGGKLIGLVT SREEIPELLK 490 500 510 520 530 540 LDDVIDLVIP RGSNKLVSQI KSSTKIPVLG HADGICHVYV DKSANVEMAK RIVLDAKVDY 550 560 570 580 590 600 PAACNAMETL LIHKDLIEKG WLKEIILDLR TEGVILYGGP VASSLLNIPQ AHSFHHEYSS 610 620 630 640 650 660 LACTAEIVDD VYAAIDHINL YGSAHTDSIV AEDNEVANVF LRQVDSAAVF HNASTRFSDG 670 ARFETRRRGW N

References

[1]	"A bifunctional enzyme (delta 1-pyrroline-5-carboxylate synthetase) catalyzes the first two steps in proline biosynthesis in plants." Hu C.-A.A., Delauney A.J., Verma D.P.S. Proc. Natl. Acad. Sci. U.S.A. 89:9354-9358(1992) [PubMed: 1384052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M92276 mRNA. No translation available.
PIR	A46295.
3D structure databases
HSSP	HSSP built from PDB template 1O20 based on UniProtKB Q9WYC9.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.2.1.41. 18771. 2.7.2.11. 18771.
Family and domain databases
InterPro	IPR016163. Ald_DH_C. IPR016162. Ald_DH_N. IPR001048. Asp/Glu/Uridylate_kinase. IPR000965. Gglut_pp_reduct. IPR001057. Glu_5kinase. IPR019797. Glutamate_5-kinase_CS. IPR005766. P5_carboxy_syn. IPR005715. ProB. [Graphical view]
Gene3D	G3DSA:3.40.1160.10. Aa_kinase. 1 hit. G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
Pfam	PF00696. AA_kinase. 1 hit. [Graphical view]
PIRSF	PIRSF036429. P5C_syn. 1 hit.
PRINTS	PR00474. GLU5KINASE.
TIGRFAMs	TIGR01092. P5CS. 1 hit. TIGR00407. proA. 1 hit. TIGR01027. proB. 1 hit.
PROSITE	PS00902. GLUTAMATE_5_KINASE. 1 hit. PS01223. PROA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

P5CS_VIGAC

Accession

Primary (citable) accession number: P32296

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)