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Database: UniProt
Entry: Q0JG21_ORYSJ
LinkDB: Q0JG21_ORYSJ
Original site: Q0JG21_ORYSJ 
ID   Q0JG21_ORYSJ            Unreviewed;       285 AA.
AC   Q0JG21;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|RuleBase:RU003903};
DE            EC=1.5.1.2 {ECO:0000256|RuleBase:RU003903};
GN   OrderedLocusNames=Os01g0948400 {ECO:0000313|EMBL:BAS76215.1};
GN   ORFNames=OSNPB_010948400 {ECO:0000313|EMBL:BAS76215.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947 {ECO:0000313|EMBL:BAS76215.1, ECO:0000313|Proteomes:UP000059680};
RN   [1] {ECO:0000313|Proteomes:UP000059680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RA   Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N.,
RA   Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y.,
RA   Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N.,
RA   Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M.,
RA   Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M.,
RA   Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K.,
RA   Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N.,
RA   Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H.,
RA   Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M.,
RA   Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S.,
RA   Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y.,
RA   Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H.,
RA   Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K.,
RA   Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M.,
RA   Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A.,
RA   Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S.,
RA   Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R.,
RA   Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J.,
RA   Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X.,
RA   Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S.,
RA   Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A.,
RA   Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R.,
RA   Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S.,
RA   Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M.,
RA   Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S.,
RA   Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H.,
RA   Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C.,
RA   Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S.,
RA   Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S.,
RA   Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K.,
RA   Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A.,
RA   Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R.,
RA   Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S.,
RA   Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K.,
RA   Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D.,
RA   Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I.,
RA   Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A.,
RA   Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H.,
RA   Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S.,
RA   Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T.,
RA   Kadowaki K., Sugiura M., Burr B., Sasaki T.;
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2] {ECO:0000313|EMBL:BAS76215.1, ECO:0000313|Proteomes:UP000059680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
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         Evidence={ECO:0000256|RuleBase:RU003903};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC       from L-glutamate 5-semialdehyde: step 1/1.
CC       {ECO:0000256|RuleBase:RU003903}.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000256|ARBA:ARBA00005525, ECO:0000256|RuleBase:RU003903}.
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DR   EMBL; AP014957; BAS76215.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0JG21; -.
DR   SMR; Q0JG21; -.
DR   EnsemblPlants; Os01t0948400-01; Os01t0948400-01; Os01g0948400.
DR   Gramene; Os01t0948400-01; Os01t0948400-01; Os01g0948400.
DR   eggNOG; KOG3124; Eukaryota.
DR   HOGENOM; CLU_042344_3_1_1; -.
DR   OMA; VVRVMTN; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000059680; Chromosome 1.
DR   ExpressionAtlas; Q0JG21; baseline and differential.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009408; P:response to heat; IEA:EnsemblPlants.
DR   GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 1.10.3730.10; ProC C-terminal domain-like; 1.
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   NCBIfam; TIGR00112; proC; 1.
DR   PANTHER; PTHR11645; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR   PANTHER; PTHR11645:SF0; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF14748; P5CR_dimer; 1.
DR   PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00521; P5CR; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003903};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000193-1};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003903};
KW   Proline biosynthesis {ECO:0000256|RuleBase:RU003903};
KW   Proteomics identification {ECO:0007829|ProteomicsDB:Q0JG21};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059680};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..285
FT                   /note="Pyrroline-5-carboxylate reductase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013530596"
FT   DOMAIN          22..116
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          178..282
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
FT   BINDING         25..30
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         74
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAS76215.1"
SQ   SEQUENCE   285 AA;  30062 MW;  C39A3E4ABA38DA45 CRC64;
     ASKPTFHIHA ILLRLLLLLL LLGFIGPGNL AESIARGVAA SGVLPATAIR TAPHRRPERA
     EAFSSIGAHI LETNAQVVDD SDVIVISVKP QIVRQVLVEL KPLLSEEKLL VSIAAGIKME
     DLQGWSGHRR FIRVMPNTPS AVGQAASVMC LGEMATENDE NRVRSLFSAI GKVWTAEEKY
     FDAVTGLSGS GPAYIFLAIE AMADGGVAAG LPRDLALGLA SQTVLGAATM VNKTGKHPGQ
     LKDMVTSPAG TTITGIQELE KGAFRGTLIN AVVAATKRCR ELSQS
//
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