P54887 (P5CS1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Including the following 2 domains:

1. Glutamate 5-kinase
   Short name=GK
   EC=2.7.2.11
   Alternative name(s):
   Gamma-glutamyl kinase
2. 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) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	717 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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	ATP-binding NADP Nucleotide-binding
Molecular function	Kinase Oxidoreductase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	L-proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway hyperosmotic salinity response Inferred from mutant phenotype PubMed 17971042. Source: TAIR pollen development Inferred from mutant phenotype PubMed 23234543. Source: TAIR proline biosynthetic process Inferred from mutant phenotype PubMed 17971042PubMed 23234543. Source: TAIR response to oxidative stress Inferred from mutant phenotype PubMed 17971042. Source: TAIR response to water deprivation Inferred from genetic interaction PubMed 21791601. Source: TAIR root development Inferred from mutant phenotype PubMed 17971042. Source: TAIR
Cellular_component	chloroplast Inferred from direct assay PubMed 17971042. Source: TAIR membrane Inferred from direct assay PubMed 17432890. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW delta1-pyrroline-5-carboxylate synthetase activity Inferred from sequence or structural similarity PubMed 10441499. Source: TAIR glutamate 5-kinase activity Inferred from electronic annotation. Source: EC glutamate-5-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

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

Note: 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 synthase A		PRO_0000109772
Regions
	Nucleotide binding	196 – 197	2	ATP By similarity
	Nucleotide binding	236 – 242	7	ATP By similarity
	Region	1 – 296	296	Glutamate 5-kinase
	Region	297 – 717	421	Gamma-glutamyl phosphate reductase
Sites
	Binding site	60	1	Substrate By similarity
	Binding site	157	1	Substrate By similarity
	Binding site	176	1	Substrate; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	79	1	Phosphoserine Ref.7
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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[7]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. CP002685 Genomic DNA. Translation: AEC09729.1. CP002685 Genomic DNA. Translation: AEC09730.1. AF424633 mRNA. Translation: AAL11626.1. AY113046 mRNA. Translation: AAM47354.1. AY150430 mRNA. Translation: AAN12972.1.
IPI	IPI00529620.
PIR	S66637. T50685.
RefSeq	NP_001189714.1. NM_001202785.1. NP_181510.1. NM_129539.2.
UniGene	At.20482.
3D structure databases
ProteinModelPortal	P54887.
SMR	P54887. Positions 13-284, 302-715.
ModBase	Search...
Protein-protein interaction databases
IntAct	P54887. 6 interactions.
STRING	3702.AT2G39800.1-P.
Proteomic databases
PaxDb	P54887.
PRIDE	P54887.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G39800.1; AT2G39800.1; AT2G39800. AT2G39800.4; AT2G39800.4; AT2G39800.
GeneID	818566.
KEGG	ath:AT2G39800.
Organism-specific databases
TAIR	At2g39800.
Phylogenomic databases
eggNOG	COG0014.
HOGENOM	HOG000246357.
InParanoid	P54887.
KO	K12657.
OMA	FEARPDC.
PhylomeDB	P54887.
ProtClustDB	PLN02418.
Enzyme and pathway databases
BioCyc	ARA:AT2G39800-MONOMER. MetaCyc:AT2G39800-MONOMER.
UniPathway	UPA00098; UER00359. UPA00098; UER00360.
Gene expression databases
ArrayExpress	P54887.
Genevestigator	P54887.
GermOnline	AT2G39800. Arabidopsis thaliana.
Family and domain databases
Gene3D	3.40.1160.10. 1 hit. 3.40.309.10. 1 hit. 3.40.605.10. 2 hits.
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. IPR001048. Asp/Glu/Uridylate_kinase. IPR000965. G-glutamylP_reductase. IPR020593. G-glutamylP_reductase_CS. IPR001057. Glu/AcGlu_kinase. IPR005715. Glu_5kinase/COase_Synthase. IPR019797. Glutamate_5-kinase_CS. IPR005766. P5_carboxy_syn. [Graphical view]
Pfam	PF00696. AA_kinase. 1 hit. PF00171. Aldedh. 1 hit. [Graphical view]
PIRSF	PIRSF036429. P5C_syn. 1 hit.
PRINTS	PR00474. GLU5KINASE.
SUPFAM	SSF53633. Aa_kinase. 1 hit. SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
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:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program