ID   PROD1_ARATH             Reviewed;         499 AA.
AC   P92983; P92945; Q8VXV1; Q944L2; Q96281;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   02-SEP-2026, entry version 170.
DE   RecName: Full=Proline dehydrogenase 1, mitochondrial;
DE            EC=1.5.5.2 {ECO:0000305|PubMed:8776899};
DE   AltName: Full=Osmotic stress-induced proline dehydrogenase;
DE   AltName: Full=Proline oxidase;
DE   AltName: Full=Protein EARLY RESPONSIVE TO DEHYDRATION 5;
DE   Flags: Precursor;
GN   Name=POX1; Synonyms=ERD5, PRO1, PRODH1; OrderedLocusNames=At3g30775;
GN   ORFNames=MIF6.16, MIF6.19;
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 [MRNA], AND INDUCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=9003320; DOI=10.1007/pl00008600;
RA   Peng Z., Lu Q., Verma D.P.S.;
RT   "Reciprocal regulation of delta 1-pyrroline-5-carboxylate synthetase and
RT   proline dehydrogenase genes controls proline levels during and after
RT   osmotic stress in plants.";
RL   Mol. Gen. Genet. 253:334-341(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Root;
RX   PubMed=8710950; DOI=10.1073/pnas.93.16.8787;
RA   Verbruggen N., Hua X.J., May M., van Montagu M.;
RT   "Environmental and developmental signals modulate proline homeostasis:
RT   evidence for a negative transcriptional regulator.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:8787-8791(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=8776899; DOI=10.1105/tpc.8.8.1323;
RA   Kiyosue T., Yoshiba Y., Yamaguchi-Shinozaki K., Shinozaki K.;
RT   "A nuclear gene encoding mitochondrial proline dehydrogenase, an enzyme
RT   involved in proline metabolism, is upregulated by proline but downregulated
RT   by dehydration in Arabidopsis.";
RL   Plant Cell 8:1323-1335(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [6]
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   [7]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [8]
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   [9]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=9847097; DOI=10.1104/pp.118.4.1233;
RA   Nakashima K., Satoh R., Kiyosue T., Yamaguchi-Shinozaki K., Shinozaki K.;
RT   "A gene encoding proline dehydrogenase is not only induced by proline and
RT   hypoosmolarity, but is also developmentally regulated in the reproductive
RT   organs of Arabidopsis.";
RL   Plant Physiol. 118:1233-1241(1998).
RN   [10]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=12773641; DOI=10.1093/pcp/pcg066;
RA   Nanjo T., Fujita M., Seki M., Kato T., Tabata S., Shinozaki K.;
RT   "Toxicity of free proline revealed in an arabidopsis T-DNA-tagged mutant
RT   deficient in proline dehydrogenase.";
RL   Plant Cell Physiol. 44:541-548(2003).
RN   [11]
RP   INDUCTION BY BZIP53.
RC   STRAIN=cv. Columbia;
RX   PubMed=16810321; DOI=10.1038/sj.emboj.7601206;
RA   Weltmeier F., Ehlert A., Mayer C.S., Dietrich K., Wang X., Schuetze K.,
RA   Alonso R., Harter K., Vicente-Carbajosa J., Droege-Laser W.;
RT   "Combinatorial control of Arabidopsis proline dehydrogenase transcription
RT   by specific heterodimerisation of bZIP transcription factors.";
RL   EMBO J. 25:3133-3143(2006).
RN   [12]
RP   INDUCTION.
RX   PubMed=17106685; DOI=10.1007/s00425-006-0429-3;
RA   Ribarits A., Abdullaev A., Tashpulatov A., Richter A., Heberle-Bors E.,
RA   Touraev A.;
RT   "Two tobacco proline dehydrogenases are differentially regulated and play a
RT   role in early plant development.";
RL   Planta 225:1313-1324(2007).
RN   [13]
RP   FUNCTION, INDUCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=20403182; DOI=10.1186/1471-2229-10-70;
RA   Funck D., Eckard S., Mueller G.;
RT   "Non-redundant functions of two proline dehydrogenase isoforms in
RT   Arabidopsis.";
RL   BMC Plant Biol. 10:70-70(2010).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP   PHE-72.
RX   PubMed=25732537; DOI=10.1093/jxb/erv064;
RA   Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT   "Identification of cleavage sites and substrate proteins for two
RT   mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL   J. Exp. Bot. 66:2691-2708(2015).
CC   -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC       {ECO:0000269|PubMed:20403182, ECO:0000269|PubMed:9847097}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a
CC         quinol + H(+); Xref=Rhea:RHEA:23784, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17388, ChEBI:CHEBI:24646, ChEBI:CHEBI:60039,
CC         ChEBI:CHEBI:132124; EC=1.5.5.2;
CC         Evidence={ECO:0000305|PubMed:8776899};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20403182,
CC       ECO:0000269|PubMed:9847097, ECO:0000305|PubMed:25732537}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in pollen grains, in
CC       the stigma and in developing embryos. {ECO:0000269|PubMed:20403182,
CC       ECO:0000269|PubMed:9847097}.
CC   -!- INDUCTION: Down-regulated by salt or drought stress. Up-regulated by
CC       proline, hypoosmolarity or rehydration (PubMed:17106685,
CC       PubMed:20403182, PubMed:9003320, PubMed:9847097). Activated by BZIP53
CC       (PubMed:16810321). {ECO:0000269|PubMed:16810321,
CC       ECO:0000269|PubMed:17106685, ECO:0000269|PubMed:20403182,
CC       ECO:0000269|PubMed:9003320, ECO:0000269|PubMed:9847097}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC       conditions. Proline hypersensitivity. {ECO:0000269|PubMed:12773641,
CC       ECO:0000269|PubMed:20403182}.
CC   -!- SIMILARITY: Belongs to the proline oxidase family. {ECO:0000305}.
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DR   EMBL; U59508; AAB40615.1; -; mRNA.
DR   EMBL; X97075; CAA65783.1; -; mRNA.
DR   EMBL; D83025; BAA11682.1; -; mRNA.
DR   EMBL; AB028614; BAB02917.1; -; Genomic_DNA.
DR   EMBL; AP001296; BAB02917.1; JOINED; Genomic_DNA.
DR   EMBL; CP002686; AEE77659.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM65921.1; -; Genomic_DNA.
DR   EMBL; OZ408685; CAO7042943.1; -; Genomic_DNA.
DR   EMBL; AF428306; AAL16138.1; -; mRNA.
DR   EMBL; AY074571; AAL67111.1; -; mRNA.
DR   RefSeq; NP_001319672.1; NM_001339059.1.
DR   RefSeq; NP_189701.3; NM_113981.6.
DR   AlphaFoldDB; P92983; -.
DR   SMR; P92983; -.
DR   BioGRID; 8159; 1.
DR   FunCoup; P92983; 887.
DR   IntAct; P92983; 2.
DR   STRING; 3702.P92983; -.
DR   iPTMnet; P92983; -.
DR   PaxDb; 3702-P92983; -.
DR   ProteomicsDB; 226217; -.
DR   DNASU; 822833; -.
DR   GeneID; 822833; -.
DR   KEGG; ath:AT3G30775; -.
DR   Araport; AT3G30775; -.
DR   TAIR; AT3G30775; ERD5.
DR   eggNOG; KOG0186; Eukaryota.
DR   HOGENOM; CLU_018202_3_0_1; -.
DR   InParanoid; P92983; -.
DR   OMA; WMQDAAD; -.
DR   PhylomeDB; P92983; -.
DR   BioCyc; ARA:AT3G30775-MONOMER; -.
DR   BioCyc; MetaCyc:AT3G30775-MONOMER; -.
DR   BRENDA; 1.5.5.2; 399.
DR   UniPathway; UPA00261; UER00373.
DR   PRO; PR:P92983; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IMP:TAIR.
DR   GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR   GO; GO:0006562; P:L-proline catabolic process; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IGI:TAIR.
DR   Gene3D; 3.20.20.220; -; 1.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR002872; Proline_DH_dom.
DR   InterPro; IPR015659; Proline_oxidase.
DR   PANTHER; PTHR13914:SF0; PROLINE DEHYDROGENASE 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13914; PROLINE OXIDASE; 1.
DR   Pfam; PF01619; Pro_dh; 1.
DR   SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Proline metabolism;
KW   Reference proteome; Stress response; Transit peptide.
FT   TRANSIT         1..72
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:25732537"
FT   CHAIN           73..499
FT                   /note="Proline dehydrogenase 1, mitochondrial"
FT                   /id="PRO_0000025804"
FT   CONFLICT        30
FT                   /note="A -> V (in Ref. 1; AAB40615)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        46
FT                   /note="P -> T (in Ref. 1; AAB40615)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="H -> Q (in Ref. 1; AAB40615)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="A -> P (in Ref. 2; CAA65783)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        355
FT                   /note="A -> R (in Ref. 3; BAA11682)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        361
FT                   /note="L -> V (in Ref. 2; CAA65783)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        398
FT                   /note="V -> A (in Ref. 8; AAL67111)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        425
FT                   /note="K -> R (in Ref. 8; AAL16138)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        477
FT                   /note="A -> P (in Ref. 1; AAB40615)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   499 AA;  54956 MW;  1428611A40EFC824 CRC64;
     MATRLLRTNF IRRSYRLPAF SPVGPPTVTA STAVVPEILS FGQQAPEPPL HHPKPTEQSH
     DGLDLSDQAR LFSSIPTSDL LRSTAVLHAA AIGPMVDLGT WVMSSKLMDA SVTRGMVLGL
     VKSTFYDHFC AGEDADAAAE RVRSVYEATG LKGMLVYGVE HADDAVSCDD NMQQFIRTIE
     AAKSLPTSHF SSVVVKITAI CPISLLKRVS DLLRWEYKSP NFKLSWKLKS FPVFSESSPL
     YHTNSEPEPL TAEEERELEA AHGRIQEICR KCQESNVPLL IDAEDTILQP AIDYMAYSSA
     IMFNADKDRP IVYNTIQAYL RDAGERLHLA VQNAEKENVP MGFKLVRGAY MSSEASLADS
     LGCKSPVHDT IQDTHSCYND CMTFLMEKAS NGSGFGVVLA THNADSGRLA SRKASDLGID
     KQNGKIEFAQ LYGMSDALSF GLKRAGFNVS KYMPFGPVAT AIPYLLRRAY ENRGMMATGA
     HDRQLMRMEL KRRLIAGIA
//