Reviewed, UniProtKB/Swiss-Prot P54887 (P5CS1_ARATH)

Names and origin

Protein names

Recommended name:
    Delta-1-pyrroline-5-carboxylate synthetase A
      Short name=P5CS A
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

Gene names

Name:	P5CSA
Synonyms:	P5CS1
Ordered Locus Names:	At2g39800
ORF Names:	T5I7.10

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	717 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.
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.
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
Coding sequence diversity	Alternative splicing
Ligand	NADP
Molecular function	Kinase Oxidoreductase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW proline biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	glutamate 5-kinase activity Inferred from electronic annotation. Source: InterPro glutamate-5-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Notes: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P54887-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 717	717	Delta-1-pyrroline-5-carboxylate synthetase A		PRO_0000109772
Regions
	Region	1 – 296	296	Glutamate 5-kinase
	Region	297 – 717	421	Gamma-glutamyl phosphate reductase
Experimental info
	Sequence conflict	42	1	C → F in BAA06864. Ref.3
	Sequence conflict	54	1	E → K in BAA06864. Ref.3
	Sequence conflict	381	1	D → E in BAA06864. Ref.3
	Sequence conflict	467	1	L → F in BAA06864. Ref.3
	Sequence conflict	676	1	H → Y in BAA06864. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: DF2B296362351A78	FASTA	717	77,702
	10 20 30 40 50 60 MEELDRSRAF ARDVKRIVVK VGTAVVTGKG GRLALGRLGA LCEQLAELNS DGFEVILVSS 70 80 90 100 110 120 GAVGLGRQRL RYRQLVNSSF ADLQKPQTEL DGKACAGVGQ SSLMAYYETM FDQLDVTAAQ 130 140 150 160 170 180 LLVNDSSFRD KDFRKQLNET VKSMLDLRVI PIFNENDAIS TRRAPYQDSS GIFWDNDSLA 190 200 210 220 230 240 ALLALELKAD LLILLSDVEG LYTGPPSDPN SKLIHTFVKE KHQDEITFGD KSRLGRGGMT 250 260 270 280 290 300 AKVKAAVNAA YAGIPVIITS GYSAENIDKV LRGLRVGTLF HQDARLWAPI TDSNARDMAV 310 320 330 340 350 360 AARESSRKLQ ALSSEDRKKI LLDIADALEA NVTTIKAENE LDVASAQEAG LEESMVARLV 370 380 390 400 410 420 MTPGKISSLA ASVRKLADME DPIGRVLKKT EVADGLVLEK TSSPLGVLLI VFESRPDALV 430 440 450 460 470 480 QIASLAIRSG NGLLLKGGKE ARRSNAILHK VITDAIPETV GGKLIGLVTS REEIPDLLKL 490 500 510 520 530 540 DDVIDLVIPR GSNKLVTQIK NTTKIPVLGH ADGICHVYVD KACDTDMAKR IVSDAKLDYP 550 560 570 580 590 600 AACNAMETLL VHKDLEQNAV LNELIFALQS NGVTLYGGPR ASKILNIPEA RSFNHEYCAK 610 620 630 640 650 660 ACTVEVVEDV YGAIDHIHRH GSAHTDCIVT EDHEVAELFL RQVDSAAVFH NASTRFSDGF 670 680 690 700 710 RFGLGAEVGV STGRIHARGP VGVEGLLTTR WIMRGKGQVV DGDNGIVYTH QDIPIQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation, characterization, and chromosomal location of a gene encoding the delta 1-pyrroline-5-carboxylate synthetase in Arabidopsis thaliana." Savoure A., Jaoua S., Hua X.J., Ardiles W., van Montagu M., Verbruggen N. FEBS Lett. 372:13-19(1995) [PubMed: 7556633] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: cv. Columbia.
[2]	"Differential expression of two P5CS genes controlling proline accumulation during salt-stress requires ABA and is regulated by ABA1, ABI1 and AXR2 in Arabidopsis." Strizhov N., Abraham E., Oekresz L., Blickling S., Zilberstein A., Schell J., Koncz C., Szabados L. Plant J. 12:557-569(1997) [PubMed: 9351242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[3]	"Correlation between the induction of a gene for delta 1-pyrroline-5-carboxylate synthetase and the accumulation of proline in Arabidopsis thaliana under osmotic stress." Yoshiba Y., Kiyosue T., Katagiri T., Ueda H., Mizoguchi T., Yamaguchi-Shinozaki K., Wada K., Harada Y., Shinozaki K. Plant J. 7:751-760(1995) [PubMed: 7773306] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[4]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X89414 Genomic DNA. Translation: CAA61593.1. X86777 mRNA. Translation: CAA60446.1. X87330 mRNA. Translation: CAA60740.1. D32138 mRNA. Translation: BAA06864.1. AC003000 Genomic DNA. Translation: AAB87129.1. AF424633 mRNA. Translation: AAL11626.1. AY113046 mRNA. Translation: AAM47354.1. AY150430 mRNA. Translation: AAN12972.1.
PIR	S66637. T50685.
RefSeq	NP_181510.1.
UniGene	At.20482
3D structure databases
HSSP	HSSP built from PDB template 1O20 based on UniProtKB Q9WYC9.
ModBase	Search...
Genome annotation databases
GeneID	818566.
GenomeReviews	Gene locus AT2G39800 in contig CT485783_GR.
KEGG	ath:AT2G39800.
Organism-specific databases
TAIR	At2g39800.
Gene expression databases
GermOnline	AT2G39800. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR016163. Ald_DHase_C. IPR016162. Ald_DHase_N. IPR001048. Asp/Glu/Uridylate_kinase. IPR000965. Gglut_pp_reduct. IPR001057. Glu_5kinase. 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

P5CS1_ARATH

Accession

Primary (citable) accession number: P54887

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)