PROD2_ARATH
ID PROD2_ARATH Reviewed; 476 AA.
AC Q6NKX1; Q9FKR5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Proline dehydrogenase 2, mitochondrial {ECO:0000303|PubMed:20403182};
DE EC=1.5.5.2 {ECO:0000305|PubMed:20403182};
DE AltName: Full=Osmotic stress-induced proline dehydrogenase;
DE AltName: Full=Proline oxidase;
DE Flags: Precursor;
GN Name=POX2; Synonyms=PRODH2 {ECO:0000303|PubMed:20403182};
GN OrderedLocusNames=At5g38710; ORFNames=MKD10.10;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R., Kim C.J., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP INDUCTION.
RX PubMed=18088315; DOI=10.1111/j.1365-313x.2007.03385.x;
RA Hanson J., Hanssen M., Wiese A., Hendriks M.M., Smeekens S.;
RT "The sucrose regulated transcription factor bZIP11 affects amino acid
RT metabolism by regulating the expression of ASPARAGINE SYNTHETASE1 and
RT PROLINE DEHYDROGENASE2.";
RL Plant J. 53:935-949(2008).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, INDUCTION, AND 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).
CC -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC {ECO:0000305|PubMed:20403182}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + L-proline = (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:20403182};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23785;
CC Evidence={ECO:0000305|PubMed:20403182};
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 -!- TISSUE SPECIFICITY: Expressed in the vascular tissue and in the
CC abscission zone of petals, sepals, stamina, pistils and siliques. Not
CC detected in petioles. {ECO:0000269|PubMed:20403182}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in senescent leaves.
CC {ECO:0000269|PubMed:20403182}.
CC -!- INDUCTION: Down-regulated by high succrose; via the repression of
CC bZIP11. Up-regulated by proline and salt or drought stress.
CC {ECO:0000269|PubMed:17106685, ECO:0000269|PubMed:18088315,
CC ECO:0000269|PubMed:20403182}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions. No proline hypersensitivity. {ECO:0000269|PubMed:20403182}.
CC -!- SIMILARITY: Belongs to the proline oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10129.1; Type=Erroneous gene model prediction; Evidence={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; AB011478; BAB10129.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94352.1; -; Genomic_DNA.
DR EMBL; BT012572; AAS99716.1; -; mRNA.
DR EMBL; AK221601; BAD95150.1; -; mRNA.
DR RefSeq; NP_198687.1; NM_123232.3.
DR AlphaFoldDB; Q6NKX1; -.
DR SMR; Q6NKX1; -.
DR STRING; 3702.AT5G38710.1; -.
DR iPTMnet; Q6NKX1; -.
DR PaxDb; Q6NKX1; -.
DR PRIDE; Q6NKX1; -.
DR EnsemblPlants; AT5G38710.1; AT5G38710.1; AT5G38710.
DR GeneID; 833862; -.
DR Gramene; AT5G38710.1; AT5G38710.1; AT5G38710.
DR KEGG; ath:AT5G38710; -.
DR Araport; AT5G38710; -.
DR TAIR; locus:2166645; AT5G38710.
DR eggNOG; KOG0186; Eukaryota.
DR HOGENOM; CLU_018202_3_0_1; -.
DR InParanoid; Q6NKX1; -.
DR OMA; QFCAGEK; -.
DR OrthoDB; 948528at2759; -.
DR PhylomeDB; Q6NKX1; -.
DR BioCyc; ARA:AT5G38710-MON; -.
DR BioCyc; MetaCyc:AT5G38710-MON; -.
DR BRENDA; 1.5.99.B2; 399.
DR UniPathway; UPA00261; UER00373.
DR PRO; PR:Q6NKX1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6NKX1; baseline and differential.
DR Genevisible; Q6NKX1; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0004657; F:proline dehydrogenase activity; IGI:UniProtKB.
DR GO; GO:0006562; P:proline catabolic process; IGI:UniProtKB.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IBA:GO_Central.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR002872; Proline_DH_dom.
DR InterPro; IPR015659; Proline_oxidase.
DR PANTHER; PTHR13914; PTHR13914; 1.
DR Pfam; PF01619; Pro_dh; 1.
DR SUPFAM; SSF51730; SSF51730; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Proline metabolism;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..476
FT /note="Proline dehydrogenase 2, mitochondrial"
FT /id="PRO_0000394797"
SQ SEQUENCE 476 AA; 53074 MW; F15FBDF8E06A13F3 CRC64;
MANRFLRPNL IHRFSTVSPV GPPTTIIPEI LSFDQPKPEV DLDLSDQARL FASVPISTLL
RSTAILHATS IGPMVDLGSW LMSSKLMDTT VTRDLVLRIV KGTFYDHFCA GEDAAAAARR
VSSVYESTGL KGMLVYGVEH AEDGGACDEN IQKFIETVEA AKTLPSSHLS SVVVKITAIC
PMNVLKRVSD LLRWQYKNPN FKLPWKLNSF PVFSGLSPLY HTTSEPEPLT VEEERELEKA
HERLKSVCLR CQESNVPLLI DAEDTILQPA IDYMAYWSAI MFNSDKDRPI VYNTIQAYLK
DAGERLHLAL RESEKMNVPI GFKLVRGAYM SSEAKLADSL GYKSPVHDTI QNTHDCYNDC
MSFLMEKASN GSGIAVILAT HNTDSGKLGA RKASELGINK ENGKIEFAQL YGMSDALSFG
LKRAGFNVSK YMPYGPVDTA IPYLIRRAYE NRGMMSTGAL DRQLMRKELK RRVMAW
