P54888 (P5CS2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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:	P5CSB
Synonyms:	P5CS2
Ordered Locus Names:	At3g55610
ORF Names:	F1I16_20

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	726 AA.
Sequence status	Complete.
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.
Sequence caution	The sequence CAB81586.1 differs from that shown. Reason: Erroneous gene model prediction.

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
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	L-proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway embryo development ending in seed dormancy 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
Cellular_component	chloroplast Inferred from direct assay PubMed 17971042. Source: TAIR cytosol Inferred from direct assay PubMed 21166475. Source: TAIR plasmodesma Inferred from direct assay PubMed 21533090. Source: TAIR
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...

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: P54888-1)

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 – 726	726	Delta-1-pyrroline-5-carboxylate synthase B		PRO_0000109773
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

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: E01446A6659021FF	FASTA	726	78,871
	10 20 30 40 50 60 MTEIDRSRAF AKDVKRIVVK VGTAVVTGKG GRLALGRLGA ICEQLAELNS DGFEVILVSS 70 80 90 100 110 120 GAVGLGRQRL RYRQLVNSSF ADLQKPQMEL DGKACAGVGQ SSLMAYYETM FDQLDVTVAQ 130 140 150 160 170 180 MLVTDSSFRD KDFRKQLSET VKAMLRMRVI PVFNENDAIS TRRAPYKDST GIFWDNDSLA 190 200 210 220 230 240 ALLSLELKAD LLILLSDVEG LYTGPPSDST SKLIHTFIKE KHQDEITFGE KSKLGRGGMT 250 260 270 280 290 300 AKVKAAVNAA YGGVPVIITS GYAAENISKV LRGLRVGTLF HQDAHLWAPV VDTTSRDMAV 310 320 330 340 350 360 AARESSRKLQ ALSSEDRKQI LHDIANALEV NEKTIKAEND LDVAAAQEAG YEESLVARLV 370 380 390 400 410 420 MKPGKISSLA ASVRQLAEME DPIGRVLKKT QVADDLILEK TSSPIGVLLI VFESRPDALV 430 440 450 460 470 480 QIASLAIRSG NGLLLKGGKE ARRSNAILHK VITDAIPETV GGKLIGLVTS REEIPDLLKL 490 500 510 520 530 540 DDVIDLVIPR GSNKLVSQIK NSTKIPVLGH ADGICHVYVD KSGKLDMAKR IVSDAKLDYP 550 560 570 580 590 600 AACNAMETLL VHKDLEQNGF LDDLIYVLQT KGVTLYGGPR ASAKLNIPET KSFHHEYSSK 610 620 630 640 650 660 ACTVEIVEDV YGAIDHIHQH GSAHTDCIVT EDSEVAEIFL RQVDSAAVFH NASTRFSDGF 670 680 690 700 710 720 RFGLGAEVGI STSRIHARGP VGVEGLLTTR WIMRGKGQVV DGDNGIVYTH KDLPVLQRTE AVENGI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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 [GENOMIC DNA / MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X86778 Genomic DNA. Translation: CAA60447.1. Y09355 mRNA. Translation: CAA70527.1. AL161667 Genomic DNA. Translation: CAB81586.1. Sequence problems. CP002686 Genomic DNA. Translation: AEE79408.1. AY091766 mRNA. Translation: AAM10314.1.
IPI	IPI00542239.
PIR	T47700. T50684. T50682.
RefSeq	NP_191120.2. NM_115419.4.
UniGene	At.25196.
3D structure databases
ProteinModelPortal	P54888.
SMR	P54888. Positions 13-284, 302-718.
ModBase	Search...
Protein-protein interaction databases
IntAct	P54888. 2 interactions.
Proteomic databases
PaxDb	P54888.
PRIDE	P54888.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G55610.1; AT3G55610.1; AT3G55610.
GeneID	824727.
KEGG	ath:AT3G55610.
Organism-specific databases
TAIR	At3g55610.
Phylogenomic databases
eggNOG	COG0014.
HOGENOM	HOG000246357.
InParanoid	P54888.
KO	K12657.
OMA	LLPWVQS.
PhylomeDB	P54888.
ProtClustDB	PLN02418.
Enzyme and pathway databases
UniPathway	UPA00098; UER00359. UPA00098; UER00360.
Gene expression databases
Genevestigator	P54888.
GermOnline	AT3G55610. 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. 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. [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

P5CS2_ARATH

Accession

Primary (citable) accession number: P54888
Secondary accession number(s): Q9M061

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program