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Protein

Delta-1-pyrroline-5-carboxylate synthase B

Gene

P5CSB

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: 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 – 601SubstrateBy similarity
Binding sitei157 – 1571SubstrateBy similarity
Binding sitei176 – 1761Substrate; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi196 – 1972ATPBy similarity
Nucleotide bindingi236 – 2427ATPBy 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: GO_Central

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.
ReactomeiREACT_232680. Amino acid synthesis and interconversion (transamination).
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

ExpressionAtlasiP54888. baseline and differential.
GenevestigatoriP54888.

Interactioni

Protein-protein interaction databases

BioGridi10043. 2 interactions.
IntActiP54888. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP54888.
SMRiP54888. Positions 8-284, 302-718.
ModBaseiSearch...
MobiDBiSearch...

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.Curated
In the C-terminal section; belongs to the gamma-glutamyl phosphate reductase family.Curated

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP54888.
SMRiP54888. Positions 8-284, 302-718.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi10043. 2 interactions.
IntActiP54888. 2 interactions.

Proteomic databases

PaxDbiP54888.
PRIDEiP54888.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT3G55610.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00098; UER00359.
UPA00098; UER00360.
BioCyciARA:GQT-931-MONOMER.
ReactomeiREACT_232680. Amino acid synthesis and interconversion (transamination).

Gene expression databases

ExpressionAtlasiP54888. baseline and differential.
GenevestigatoriP54888.

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]
ProtoNetiSearch...

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: February 4, 2015
This is version 125 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.