ID   P5CS2_ARATH             Reviewed;         726 AA.
AC   P54888; Q9M061;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 173.
DE   RecName: Full=Delta-1-pyrroline-5-carboxylate synthase B;
DE            Short=P5CS B;
DE   Includes:
DE     RecName: Full=Glutamate 5-kinase;
DE              Short=GK;
DE              EC=2.7.2.11;
DE     AltName: Full=Gamma-glutamyl kinase;
DE   Includes:
DE     RecName: Full=Gamma-glutamyl phosphate reductase;
DE              Short=GPR;
DE              EC=1.2.1.41;
DE     AltName: Full=Glutamate-5-semialdehyde dehydrogenase;
DE     AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase;
GN   Name=P5CSB; Synonyms=P5CS2; OrderedLocusNames=At3g55610;
GN   ORFNames=F1I16_20;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9351242; DOI=10.1046/j.1365-313x.1997.00557.x;
RA   Strizhov N., Abraham E., Oekresz L., Blickling S., Zilberstein A.,
RA   Schell J., Koncz C., Szabados L.;
RT   "Differential expression of two P5CS genes controlling proline accumulation
RT   during salt-stress requires ABA and is regulated by ABA1, ABI1 and AXR2 in
RT   Arabidopsis.";
RL   Plant J. 12:557-569(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: P5CS plays a key role in proline biosynthesis, leading to
CC       osmoregulation in plants.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate;
CC         Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-
CC         glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:19541,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58066, ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-glutamate: step 1/2.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-glutamate: step 2/2.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=P54888-1; Sequence=Displayed;
CC   -!- SIMILARITY: In the N-terminal section; belongs to the glutamate 5-
CC       kinase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the gamma-glutamyl
CC       phosphate reductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB81586.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X86778; CAA60447.1; -; Genomic_DNA.
DR   EMBL; Y09355; CAA70527.1; -; mRNA.
DR   EMBL; AL161667; CAB81586.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE79408.1; -; Genomic_DNA.
DR   EMBL; AY091766; AAM10314.1; -; mRNA.
DR   PIR; T47700; T47700.
DR   PIR; T50682; T50684.
DR   RefSeq; NP_191120.2; NM_115419.5. [P54888-1]
DR   AlphaFoldDB; P54888; -.
DR   SMR; P54888; -.
DR   BioGRID; 10043; 4.
DR   IntAct; P54888; 3.
DR   STRING; 3702.P54888; -.
DR   iPTMnet; P54888; -.
DR   MetOSite; P54888; -.
DR   PaxDb; 3702-AT3G55610-1; -.
DR   ProteomicsDB; 236352; -. [P54888-1]
DR   EnsemblPlants; AT3G55610.1; AT3G55610.1; AT3G55610. [P54888-1]
DR   GeneID; 824727; -.
DR   Gramene; AT3G55610.1; AT3G55610.1; AT3G55610. [P54888-1]
DR   KEGG; ath:AT3G55610; -.
DR   Araport; AT3G55610; -.
DR   TAIR; AT3G55610; P5CS2.
DR   eggNOG; KOG1154; Eukaryota.
DR   eggNOG; KOG4165; Eukaryota.
DR   HOGENOM; CLU_016144_0_0_1; -.
DR   InParanoid; P54888; -.
DR   OrthoDB; 314297at2759; -.
DR   PhylomeDB; P54888; -.
DR   BioCyc; ARA:AT3G55610-MONOMER; -.
DR   UniPathway; UPA00098; UER00359.
DR   UniPathway; UPA00098; UER00360.
DR   PRO; PR:P54888; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; P54888; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004349; F:glutamate 5-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009555; P:pollen development; IMP:TAIR.
DR   GO; GO:0006561; P:proline biosynthetic process; IMP:TAIR.
DR   CDD; cd04256; AAK_P5CS_ProBA; 1.
DR   CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   HAMAP; MF_00412; ProA; 1.
DR   HAMAP; MF_00456; ProB; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR020593; G-glutamylP_reductase_CS.
DR   InterPro; IPR041744; G5K_ProBA.
DR   InterPro; IPR001057; Glu/AcGlu_kinase.
DR   InterPro; IPR005715; Glu_5kinase/COase_Synthase.
DR   InterPro; IPR019797; Glutamate_5-kinase_CS.
DR   InterPro; IPR000965; GPR_dom.
DR   InterPro; IPR005766; P5_carboxy_syn.
DR   NCBIfam; TIGR01092; P5CS; 1.
DR   NCBIfam; TIGR00407; proA; 1.
DR   NCBIfam; TIGR01027; proB; 1.
DR   PANTHER; PTHR11063:SF8; DELTA-1-PYRROLINE-5-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11063; GLUTAMATE SEMIALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036429; P5C_syn; 1.
DR   PRINTS; PR00474; GLU5KINASE.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR   PROSITE; PS01223; PROA; 1.
DR   Genevisible; P54888; AT.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Amino-acid biosynthesis; ATP-binding; Kinase;
KW   Multifunctional enzyme; NADP; Nucleotide-binding; Oxidoreductase;
KW   Proline biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..726
FT                   /note="Delta-1-pyrroline-5-carboxylate synthase B"
FT                   /id="PRO_0000109773"
FT   REGION          1..296
FT                   /note="Glutamate 5-kinase"
FT   REGION          297..717
FT                   /note="Gamma-glutamyl phosphate reductase"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         196..197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         236..242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   726 AA;  78871 MW;  E01446A6659021FF CRC64;
     MTEIDRSRAF AKDVKRIVVK VGTAVVTGKG GRLALGRLGA ICEQLAELNS DGFEVILVSS
     GAVGLGRQRL RYRQLVNSSF ADLQKPQMEL DGKACAGVGQ SSLMAYYETM FDQLDVTVAQ
     MLVTDSSFRD KDFRKQLSET VKAMLRMRVI PVFNENDAIS TRRAPYKDST GIFWDNDSLA
     ALLSLELKAD LLILLSDVEG LYTGPPSDST SKLIHTFIKE KHQDEITFGE KSKLGRGGMT
     AKVKAAVNAA YGGVPVIITS GYAAENISKV LRGLRVGTLF HQDAHLWAPV VDTTSRDMAV
     AARESSRKLQ ALSSEDRKQI LHDIANALEV NEKTIKAEND LDVAAAQEAG YEESLVARLV
     MKPGKISSLA ASVRQLAEME DPIGRVLKKT QVADDLILEK TSSPIGVLLI VFESRPDALV
     QIASLAIRSG NGLLLKGGKE ARRSNAILHK VITDAIPETV GGKLIGLVTS REEIPDLLKL
     DDVIDLVIPR GSNKLVSQIK NSTKIPVLGH ADGICHVYVD KSGKLDMAKR IVSDAKLDYP
     AACNAMETLL VHKDLEQNGF LDDLIYVLQT KGVTLYGGPR ASAKLNIPET KSFHHEYSSK
     ACTVEIVEDV YGAIDHIHQH GSAHTDCIVT EDSEVAEIFL RQVDSAAVFH NASTRFSDGF
     RFGLGAEVGI STSRIHARGP VGVEGLLTTR WIMRGKGQVV DGDNGIVYTH KDLPVLQRTE
     AVENGI
//