ID P5CS1_ARATH Reviewed; 717 AA. AC P54887; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 16-DEC-2008, entry version 69. DE RecName: Full=Delta-1-pyrroline-5-carboxylate synthetase A; DE Short=P5CS A; 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=P5CSA; Synonyms=P5CS1; OrderedLocusNames=At2g39800; GN ORFNames=T5I7.10; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=96032537; PubMed=7556633; DOI=10.1016/0014-5793(95)00935-3; RA Savoure A., Jaoua S., Hua X.J., Ardiles W., van Montagu M., RA Verbruggen N.; RT "Isolation, characterization, and chromosomal location of a gene RT encoding the delta 1-pyrroline-5-carboxylate synthetase in Arabidopsis RT thaliana."; RL FEBS Lett. 372:13-19(1995). RN [2] RP NUCLEOTIDE SEQUENCE [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 RT accumulation during salt-stress requires ABA and is regulated by ABA1, RT ABI1 and AXR2 in Arabidopsis."; RL Plant J. 12:557-569(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=95291335; PubMed=7773306; RA Yoshiba Y., Kiyosue T., Katagiri T., Ueda H., Mizoguchi T., RA Yamaguchi-Shinozaki K., Wada K., Harada Y., Shinozaki K.; RT "Correlation between the induction of a gene for delta 1-pyrroline-5- RT carboxylate synthetase and the accumulation of proline in Arabidopsis RT thaliana under osmotic stress."; RL Plant J. 7:751-760(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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 CC to osmoregulation in plants. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate = ADP + L-glutamate 5- CC phosphate. CC -!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate + CC NADP(+) = L-glutamyl 5-phosphate + NADPH. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC glutamate 5-semialdehyde from L-glutamate: step 1/2. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC glutamate 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=P54887-1; Sequence=Displayed; CC -!- SIMILARITY: In the N-terminal section; belongs to the glutamate 5- CC kinase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the gamma- CC glutamyl phosphate reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X89414; CAA61593.1; -; Genomic_DNA. DR EMBL; X86777; CAA60446.1; -; mRNA. DR EMBL; X87330; CAA60740.1; -; mRNA. DR EMBL; D32138; BAA06864.1; -; mRNA. DR EMBL; AC003000; AAB87129.1; -; Genomic_DNA. DR EMBL; AF424633; AAL11626.1; -; mRNA. DR EMBL; AY113046; AAM47354.1; -; mRNA. DR EMBL; AY150430; AAN12972.1; -; mRNA. DR PIR; S66637; S66637. DR PIR; T50685; T50685. DR RefSeq; NP_181510.1; -. DR UniGene; At.20482; -. DR HSSP; Q9WYC9; 1O20. DR PRIDE; P54887; -. DR GeneID; 818566; -. DR GenomeReviews; CT485783_GR; AT2G39800. DR KEGG; ath:AT2G39800; -. DR TAIR; At2g39800; -. DR GermOnline; AT2G39800; Arabidopsis thaliana. DR GO; GO:0009507; C:chloroplast; IDA:TAIR. DR GO; GO:0016020; C:membrane; IDA:TAIR. DR GO; GO:0004349; F:glutamate 5-kinase activity; IEA:InterPro. DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase acti...; IEA:InterPro. DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR. DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR. DR GO; GO:0048364; P:root development; IMP:TAIR. DR InterPro; IPR016163; Ald_DHase_C. DR InterPro; IPR016162; Ald_DHase_N. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR000965; Gglut_pp_reduct. DR InterPro; IPR001057; Glu_5kinase. DR InterPro; IPR005766; P5_carboxy_syn. DR InterPro; IPR005715; ProB. DR Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1. DR Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1. DR Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF036429; P5C_syn; 1. DR PRINTS; PR00474; GLU5KINASE. DR TIGRFAMs; TIGR01092; P5CS; 1. DR TIGRFAMs; TIGR00407; proA; 1. DR TIGRFAMs; TIGR01027; proB; 1. DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1. DR PROSITE; PS01223; PROA; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Amino-acid biosynthesis; Complete proteome; KW Kinase; Multifunctional enzyme; NADP; Oxidoreductase; KW Proline biosynthesis; Transferase. FT CHAIN 1 717 Delta-1-pyrroline-5-carboxylate FT synthetase A. FT /FTId=PRO_0000109772. FT REGION 1 296 Glutamate 5-kinase. FT REGION 297 717 Gamma-glutamyl phosphate reductase. FT CONFLICT 42 42 C -> F (in Ref. 3; BAA06864). FT CONFLICT 54 54 E -> K (in Ref. 3; BAA06864). FT CONFLICT 381 381 D -> E (in Ref. 3; BAA06864). FT CONFLICT 467 467 L -> F (in Ref. 3; BAA06864). FT CONFLICT 676 676 H -> Y (in Ref. 3; BAA06864). SQ SEQUENCE 717 AA; 77702 MW; DF2B296362351A78 CRC64; MEELDRSRAF ARDVKRIVVK VGTAVVTGKG GRLALGRLGA LCEQLAELNS DGFEVILVSS GAVGLGRQRL RYRQLVNSSF ADLQKPQTEL DGKACAGVGQ SSLMAYYETM FDQLDVTAAQ LLVNDSSFRD KDFRKQLNET VKSMLDLRVI PIFNENDAIS TRRAPYQDSS GIFWDNDSLA ALLALELKAD LLILLSDVEG LYTGPPSDPN SKLIHTFVKE KHQDEITFGD KSRLGRGGMT AKVKAAVNAA YAGIPVIITS GYSAENIDKV LRGLRVGTLF HQDARLWAPI TDSNARDMAV AARESSRKLQ ALSSEDRKKI LLDIADALEA NVTTIKAENE LDVASAQEAG LEESMVARLV MTPGKISSLA ASVRKLADME DPIGRVLKKT EVADGLVLEK TSSPLGVLLI VFESRPDALV QIASLAIRSG NGLLLKGGKE ARRSNAILHK VITDAIPETV GGKLIGLVTS REEIPDLLKL DDVIDLVIPR GSNKLVTQIK NTTKIPVLGH ADGICHVYVD KACDTDMAKR IVSDAKLDYP AACNAMETLL VHKDLEQNAV LNELIFALQS NGVTLYGGPR ASKILNIPEA RSFNHEYCAK ACTVEVVEDV YGAIDHIHRH GSAHTDCIVT EDHEVAELFL RQVDSAAVFH NASTRFSDGF RFGLGAEVGV STGRIHARGP VGVEGLLTTR WIMRGKGQVV DGDNGIVYTH QDIPIQA //