SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P54888

- P5CS2_ARATH

UniProt

P54888 - P5CS2_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Delta-1-pyrroline-5-carboxylate synthase B

Gene
P5CSB, P5CS2, At3g55610, F1I16_20
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

P5CS plays a key role in proline biosynthesis, leading to osmoregulation in plants.

Catalytic activityi

ATP + L-glutamate = ADP + L-glutamate 5-phosphate.
L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601Substrate By similarity
Binding sitei157 – 1571Substrate By similarity
Binding sitei176 – 1761Substrate; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi196 – 1972ATP By similarity
Nucleotide bindingi236 – 2427ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate 5-kinase activity Source: UniProtKB-EC
  3. glutamate-5-semialdehyde dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. embryo development ending in seed dormancy Source: TAIR
  2. L-proline biosynthetic process Source: UniProtKB-UniPathway
  3. pollen development Source: TAIR
  4. proline biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Oxidoreductase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Proline biosynthesis

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:GQT-931-MONOMER.
UniPathwayiUPA00098; UER00359.
UPA00098; UER00360.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-1-pyrroline-5-carboxylate synthase B
Short name:
P5CS B
Including the following 2 domains:
Glutamate 5-kinase (EC:2.7.2.11)
Short name:
GK
Alternative name(s):
Gamma-glutamyl kinase
Gamma-glutamyl phosphate reductase (EC:1.2.1.41)
Short name:
GPR
Alternative name(s):
Glutamate-5-semialdehyde dehydrogenase
Glutamyl-gamma-semialdehyde dehydrogenase
Gene namesi
Name:P5CSB
Synonyms:P5CS2
Ordered Locus Names:At3g55610
ORF Names:F1I16_20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G55610.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. cytoplasm Source: TAIR
  3. cytosol Source: TAIR
  4. plasmodesma Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 726726Delta-1-pyrroline-5-carboxylate synthase BPRO_0000109773Add
BLAST

Proteomic databases

PaxDbiP54888.
PRIDEiP54888.

Expressioni

Gene expression databases

GenevestigatoriP54888.

Interactioni

Protein-protein interaction databases

BioGridi10043. 2 interactions.
IntActiP54888. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP54888.
SMRiP54888. Positions 13-284, 302-718.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 296296Glutamate 5-kinaseAdd
BLAST
Regioni297 – 717421Gamma-glutamyl phosphate reductaseAdd
BLAST

Sequence similaritiesi

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.

Phylogenomic databases

eggNOGiCOG0014.
HOGENOMiHOG000246357.
InParanoidiP54888.
KOiK12657.
OMAiLLPWVQS.
PhylomeDBiP54888.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPiMF_00412. ProA.
MF_00456. ProB.
InterProiIPR016161. 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]
PfamiPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFiPIRSF036429. P5C_syn. 1 hit.
PRINTSiPR00474. GLU5KINASE.
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01092. P5CS. 1 hit.
TIGR00407. proA. 1 hit.
TIGR01027. proB. 1 hit.
PROSITEiPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS01223. PROA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. Align

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

Isoform 1 (identifier: P54888-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MTEIDRSRAF AKDVKRIVVK VGTAVVTGKG GRLALGRLGA ICEQLAELNS    50
DGFEVILVSS GAVGLGRQRL RYRQLVNSSF ADLQKPQMEL DGKACAGVGQ 100
SSLMAYYETM FDQLDVTVAQ MLVTDSSFRD KDFRKQLSET VKAMLRMRVI 150
PVFNENDAIS TRRAPYKDST GIFWDNDSLA ALLSLELKAD LLILLSDVEG 200
LYTGPPSDST SKLIHTFIKE KHQDEITFGE KSKLGRGGMT AKVKAAVNAA 250
YGGVPVIITS GYAAENISKV LRGLRVGTLF HQDAHLWAPV VDTTSRDMAV 300
AARESSRKLQ ALSSEDRKQI LHDIANALEV NEKTIKAEND LDVAAAQEAG 350
YEESLVARLV MKPGKISSLA ASVRQLAEME DPIGRVLKKT QVADDLILEK 400
TSSPIGVLLI VFESRPDALV QIASLAIRSG NGLLLKGGKE ARRSNAILHK 450
VITDAIPETV GGKLIGLVTS REEIPDLLKL DDVIDLVIPR GSNKLVSQIK 500
NSTKIPVLGH ADGICHVYVD KSGKLDMAKR IVSDAKLDYP AACNAMETLL 550
VHKDLEQNGF LDDLIYVLQT KGVTLYGGPR ASAKLNIPET KSFHHEYSSK 600
ACTVEIVEDV YGAIDHIHQH GSAHTDCIVT EDSEVAEIFL RQVDSAAVFH 650
NASTRFSDGF RFGLGAEVGI STSRIHARGP VGVEGLLTTR WIMRGKGQVV 700
DGDNGIVYTH KDLPVLQRTE AVENGI 726
Length:726
Mass (Da):78,871
Last modified:October 1, 1996 - v1
Checksum:iE01446A6659021FF
GO

Sequence cautioni

The sequence CAB81586.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiT47700.
T50682. T50684.
RefSeqiNP_191120.2. NM_115419.4. [P54888-1]
UniGeneiAt.25196.

Genome annotation databases

EnsemblPlantsiAT3G55610.1; AT3G55610.1; AT3G55610. [P54888-1]
GeneIDi824727.
KEGGiath:AT3G55610.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi T47700.
T50682. T50684.
RefSeqi NP_191120.2. NM_115419.4. [P54888-1 ]
UniGenei At.25196.

3D structure databases

ProteinModelPortali P54888.
SMRi P54888. Positions 13-284, 302-718.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 10043. 2 interactions.
IntActi P54888. 2 interactions.

Proteomic databases

PaxDbi P54888.
PRIDEi P54888.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G55610.1 ; AT3G55610.1 ; AT3G55610 . [P54888-1 ]
GeneIDi 824727.
KEGGi ath:AT3G55610.

Organism-specific databases

TAIRi AT3G55610.

Phylogenomic databases

eggNOGi COG0014.
HOGENOMi HOG000246357.
InParanoidi P54888.
KOi K12657.
OMAi LLPWVQS.
PhylomeDBi P54888.

Enzyme and pathway databases

UniPathwayi UPA00098 ; UER00359 .
UPA00098 ; UER00360 .
BioCyci ARA:GQT-931-MONOMER.

Gene expression databases

Genevestigatori P54888.

Family and domain databases

Gene3Di 3.40.1160.10. 1 hit.
3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPi MF_00412. ProA.
MF_00456. ProB.
InterProi 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 ]
Pfami PF00696. AA_kinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036429. P5C_syn. 1 hit.
PRINTSi PR00474. GLU5KINASE.
SUPFAMi SSF53633. SSF53633. 1 hit.
SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR01092. P5CS. 1 hit.
TIGR00407. proA. 1 hit.
TIGR01027. proB. 1 hit.
PROSITEi PS00902. GLUTAMATE_5_KINASE. 1 hit.
PS01223. PROA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiP5CS2_ARATH
AccessioniPrimary (citable) accession number: P54888
Secondary accession number(s): Q9M061
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi