P5CR1_ARATH
ID P5CR1_ARATH Reviewed; 276 AA.
AC P54904;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Pyrroline-5-carboxylate reductase;
DE Short=P5C reductase;
DE Short=P5CR;
DE EC=1.5.1.2;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2772;
GN Name=PROC1; Synonyms=EMB2772; OrderedLocusNames=At5g14800;
GN ORFNames=T9L3_100;
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].
RX PubMed=8022935; DOI=10.1104/pp.103.3.771;
RA Verbruggen N., Villarroel R., van Montagu M.;
RT "Osmoregulation of a pyrroline-5-carboxylate reductase gene in Arabidopsis
RT thaliana.";
RL Plant Physiol. 103:771-781(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Landsberg erecta;
RA Verbruggen N., Villarroel R., Hua X., van Montagu M.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
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 [5]
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:14109, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:14105, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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=P54904-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M76538; AAA61346.1; -; Genomic_DNA.
DR EMBL; Y08951; CAA70148.1; -; Genomic_DNA.
DR EMBL; AL391149; CAC01879.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92078.1; -; Genomic_DNA.
DR EMBL; AF410303; AAK95289.1; -; mRNA.
DR EMBL; AY097368; AAM19884.1; -; mRNA.
DR EMBL; AY087530; AAM65072.1; -; mRNA.
DR PIR; JQ2334; JQ2334.
DR RefSeq; NP_196984.1; NM_121484.5. [P54904-1]
DR AlphaFoldDB; P54904; -.
DR SMR; P54904; -.
DR BioGRID; 16609; 2.
DR STRING; 3702.AT5G14800.1; -.
DR BindingDB; P54904; -.
DR ChEMBL; CHEMBL2242730; -.
DR iPTMnet; P54904; -.
DR PaxDb; P54904; -.
DR PRIDE; P54904; -.
DR ProteomicsDB; 248739; -. [P54904-1]
DR EnsemblPlants; AT5G14800.1; AT5G14800.1; AT5G14800. [P54904-1]
DR GeneID; 831332; -.
DR Gramene; AT5G14800.1; AT5G14800.1; AT5G14800. [P54904-1]
DR KEGG; ath:AT5G14800; -.
DR Araport; AT5G14800; -.
DR TAIR; locus:2185435; AT5G14800.
DR eggNOG; KOG3124; Eukaryota.
DR HOGENOM; CLU_042344_3_1_1; -.
DR InParanoid; P54904; -.
DR OMA; VVRVMTN; -.
DR PhylomeDB; P54904; -.
DR SABIO-RK; P54904; -.
DR UniPathway; UPA00098; UER00361.
DR PRO; PR:P54904; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P54904; baseline and differential.
DR Genevisible; P54904; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; ISS:TAIR.
DR GO; GO:0055129; P:L-proline biosynthetic process; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR HAMAP; MF_01925; P5C_reductase; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028939; P5C_Rdtase_cat_N.
DR InterPro; IPR029036; P5CR_dimer.
DR InterPro; IPR000304; Pyrroline-COOH_reductase.
DR PANTHER; PTHR11645; PTHR11645; 1.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF14748; P5CR_dimer; 1.
DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00112; proC; 1.
DR PROSITE; PS00521; P5CR; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Amino-acid biosynthesis; Cytoplasm; NADP;
KW Oxidoreductase; Proline biosynthesis; Reference proteome.
FT CHAIN 1..276
FT /note="Pyrroline-5-carboxylate reductase"
FT /id="PRO_0000187323"
SQ SEQUENCE 276 AA; 28624 MW; B577A01C92A3A28B CRC64;
MEILPIPAES FKVGFIGAGK MAESIARGVV ASGVLPPNRI CTAVHSNLNR RDVFESFGVN
VFSTSEEVVK ESDVVIFSVK PQVVKKAVTE LKSKLSKNKI LVSVAAGIKL NDLQEWSGQD
RFIRVMPNTP AAVGEAASVM SLGTGATEED GAIVAMLFGA VGKILKADEK MFDAVTGLSG
SGPAYIFLAI EALADGGVAA GLPRELALSL ASQTVLGAAT MVSKTGKHPG VLKDDVTSPG
GTTIAGVHEL EKGSFRATLM NAVVAAAKRS RELSQS