AL121_ARATH
ID AL121_ARATH Reviewed; 556 AA.
AC Q8VZC3; Q93Y55; Q9FJJ2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase 12A1, mitochondrial {ECO:0000305};
DE Short=AtP5CDH {ECO:0000303|PubMed:11532180};
DE Short=P5C dehydrogenase {ECO:0000303|PubMed:11532180};
DE EC=1.2.1.88 {ECO:0000269|PubMed:11532180};
DE AltName: Full=Aldehyde dehydrogenase family 12 member A1 {ECO:0000303|PubMed:15358267};
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000305};
DE Flags: Precursor;
GN Name=ALDH12A1 {ECO:0000303|PubMed:15358267};
GN Synonyms=P5CDH {ECO:0000303|PubMed:11532180};
GN OrderedLocusNames=At5g62530 {ECO:0000312|Araport:AT5G62530};
GN ORFNames=K19B1.14 {ECO:0000312|EMBL:BAB11503.1};
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], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11532180; DOI=10.1046/j.1365-313x.2001.01101.x;
RA Deuschle K., Funck D., Hellmann H., Daeschner K., Binder S., Frommer W.B.;
RT "A nuclear gene encoding mitochondrial delta-1-pyrroline-5-carboxylate
RT dehydrogenase and its potential role in protection from proline toxicity.";
RL Plant J. 27:345-356(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [3]
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 [4]
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15548746; DOI=10.1105/tpc.104.023622;
RA Deuschle K., Funck D., Forlani G., Stransky H., Biehl A., Leister D.,
RA van der Graaff E., Kunze R., Frommer W.B.;
RT "The role of [Delta]1-pyrroline-5-carboxylate dehydrogenase in proline
RT degradation.";
RL Plant Cell 16:3413-3425(2004).
RN [6]
RP NOMENCLATURE.
RX PubMed=15358267; DOI=10.1016/j.tplants.2004.06.004;
RA Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J.;
RT "The ALDH gene superfamily of Arabidopsis.";
RL Trends Plant Sci. 9:371-377(2004).
RN [7]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19635803; DOI=10.1074/jbc.m109.009340;
RA Miller G., Honig A., Stein H., Suzuki N., Mittler R., Zilberstein A.;
RT "Unraveling delta1-pyrroline-5-carboxylate-proline cycle in plants by
RT uncoupled expression of proline oxidation enzymes.";
RL J. Biol. Chem. 284:26482-26492(2009).
RN [8]
RP FUNCTION.
RX PubMed=26284090; DOI=10.3389/fpls.2015.00572;
RA Rizzi Y.S., Monteoliva M.I., Fabro G., Grosso C.L., Larovere L.E.,
RA Alvarez M.E.;
RT "P5CDH affects the pathways contributing to Pro synthesis after ProDH
RT activation by biotic and abiotic stress conditions.";
RL Front. Plant Sci. 6:572-572(2015).
CC -!- FUNCTION: Plays a role in the inhibition of programmed cell death by
CC converting the toxic proline catabolism intermediate (s)-1-pyrroline-5-
CC carboxylate (P5C) to glutamate. {ECO:0000269|PubMed:11532180,
CC ECO:0000269|PubMed:15548746, ECO:0000269|PubMed:19635803,
CC ECO:0000269|PubMed:26284090}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-1-pyrroline-5-carboxylate + 2 H2O + NAD(+) = H(+) + L-
CC glutamate + NADH; Xref=Rhea:RHEA:16417, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17388, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.88;
CC Evidence={ECO:0000269|PubMed:11532180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16418;
CC Evidence={ECO:0000269|PubMed:11532180};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000305|PubMed:11532180}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers (PubMed:11532180).
CC Constitutively expressed at low levels in the other tissues
CC (PubMed:11532180). Highly expressed in pollen grains and tissues
CC undergoing cell death (PubMed:15548746). Expressed in old leaves,
CC mature siliques and developing embryos (PubMed:15548746).
CC {ECO:0000269|PubMed:11532180, ECO:0000269|PubMed:15548746}.
CC -!- INDUCTION: Induced by treatment with proline (PubMed:11532180,
CC PubMed:15548746). Induced by drought stress (PubMed:19635803).
CC {ECO:0000269|PubMed:11532180, ECO:0000269|PubMed:15548746,
CC ECO:0000269|PubMed:19635803}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants are hypersensitive to treatment with
CC proline (PubMed:15548746). Hypersensitivity to heat stress
CC (PubMed:19635803). {ECO:0000269|PubMed:15548746,
CC ECO:0000269|PubMed:19635803}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11503.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY039787; AAK73756.1; -; mRNA.
DR EMBL; AB015469; BAB11503.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97619.1; -; Genomic_DNA.
DR EMBL; AY065072; AAL38248.1; -; mRNA.
DR EMBL; BT000746; AAN31887.1; -; mRNA.
DR EMBL; BT010391; AAQ56834.1; -; mRNA.
DR RefSeq; NP_568955.1; NM_125647.4.
DR AlphaFoldDB; Q8VZC3; -.
DR SMR; Q8VZC3; -.
DR BioGRID; 21617; 1.
DR IntAct; Q8VZC3; 1.
DR STRING; 3702.AT5G62530.1; -.
DR PaxDb; Q8VZC3; -.
DR PRIDE; Q8VZC3; -.
DR ProteomicsDB; 245065; -.
DR EnsemblPlants; AT5G62530.1; AT5G62530.1; AT5G62530.
DR GeneID; 836373; -.
DR Gramene; AT5G62530.1; AT5G62530.1; AT5G62530.
DR KEGG; ath:AT5G62530; -.
DR Araport; AT5G62530; -.
DR TAIR; locus:2154094; AT5G62530.
DR eggNOG; KOG2451; Eukaryota.
DR HOGENOM; CLU_039242_0_0_1; -.
DR InParanoid; Q8VZC3; -.
DR OMA; VDYVAWQ; -.
DR OrthoDB; 454791at2759; -.
DR PhylomeDB; Q8VZC3; -.
DR BioCyc; ARA:AT5G62530-MON; -.
DR BRENDA; 1.2.1.88; 399.
DR UniPathway; UPA00261; UER00374.
DR PRO; PR:Q8VZC3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VZC3; baseline and differential.
DR Genevisible; Q8VZC3; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IMP:TAIR.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IMP:TAIR.
DR GO; GO:0006560; P:proline metabolic process; TAS:TAIR.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR044638; ALDH7A1-like.
DR PANTHER; PTHR43521; PTHR43521; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..556
FT /note="Delta-1-pyrroline-5-carboxylate dehydrogenase 12A1,
FT mitochondrial"
FT /id="PRO_0000256062"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 336
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 282..287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT SITE 207
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT CONFLICT 48
FT /note="A -> S (in Ref. 1; AAK73756)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="E -> D (in Ref. 1; AAK73756)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 61773 MW; 83F19E7A300D5565 CRC64;
MYRVFASRAL RAKSLCDKSS TSLASLTLSR LNHSIPFATV DAEELSGAHP AEVQSFVQGK
WIGSSNHNTL LDPLNGEPFI KVAEVDESGT QPFVDSLSQC PKHGLHNPFK SPERYLLYGD
ISTKAAHMLA LPKVADFFAR LIQRVAPKSY QQAAGEVFVT RKFLENFCGD QVRFLARSFA
IPGNHLGQQS HGYRWPYGPV TIVTPFNFPL EIPLLQLMGA LYMGNKPLLK VDSKVSIVME
QMMRLLHYCG LPAEDVDFIN SDGKTMNKIL LEANPRMTLF TGSSRVAEKL ALDLKGRIRL
EDAGFDWKVL GPDVQEVDYV AWQCDQDAYA CSGQKCSAQS MLFVHENWSK TPLVSKLKEL
AERRKLEDLT IGPVLTFTTE AMLEHMENLL QIPGSKLLFG GKELKNHSIP SIYGALEPTA
VYVPIEEILK DNKTYELVTK EIFGPFQIVT EYKKDQLPLV LEALERMHAH LTAAVVSNDP
IFLQEVIGNS VNGTTYAGLR GRTTGAPQNH WFGPAGDPRG AGIGTPEAIK LVWSCHREVI
YDYGPVPQGW ELPPST
