GLDH_ARATH
ID GLDH_ARATH Reviewed; 610 AA.
AC Q9SU56; B3H4I4; Q8GY16; Q9MAX4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=L-galactono-1,4-lactone dehydrogenase, mitochondrial {ECO:0000303|PubMed:18799460};
DE EC=1.3.2.3 {ECO:0000269|PubMed:18190525};
DE Flags: Precursor;
GN Name=GLDH {ECO:0000303|PubMed:18799460};
GN OrderedLocusNames=At3g47930 {ECO:0000312|Araport:AT3G47930};
GN ORFNames=T17F15.200 {ECO:0000312|EMBL:CAB41146.1};
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] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RA Tamaoki M.;
RT "Studies on gene expression of an Arabidopsis gene, involved in the
RT biosynthesis of ascorbic acid, under environmental stress.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18799460; DOI=10.1074/jbc.m805320200;
RA Pineau B., Layoune O., Danon A., De Paepe R.;
RT "L-galactono-1,4-lactone dehydrogenase is required for the accumulation of
RT plant respiratory complex I.";
RL J. Biol. Chem. 283:32500-32505(2008).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF LEU-156.
RX PubMed=18190525; DOI=10.1111/j.1742-4658.2007.06233.x;
RA Leferink N.G.H., van den Berg W.A.M., van Berkel W.J.H.;
RT "L-galactono-gamma-lactone dehydrogenase from Arabidopsis thaliana, a
RT flavoprotein involved in vitamin C biosynthesis.";
RL FEBS J. 275:713-726(2008).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) IN COMPLEX WITH THE
RP MITOCHONDRIAL COMPLEX I, AND FUNCTION.
RX PubMed=33060577; DOI=10.1038/s41467-020-18814-w;
RA Soufari H., Parrot C., Kuhn L., Waltz F., Hashem Y.;
RT "Specific features and assembly of the plant mitochondrial complex I
RT revealed by cryo-EM.";
RL Nat. Commun. 11:5195-5195(2020).
CC -!- FUNCTION: Involved in the biosynthesis of ascorbate (PubMed:18190525).
CC Catalyzes the final step of ascorbate biosynthesis (PubMed:18190525).
CC Uses L-galactono-1,4-lactone and L-gulono-1,4-lactone as substrates,
CC but not D-galactono-1,4-lactone, D-gulono-1,4-lactone, L-mannono-1,4-
CC lactone or D-galactonic acid (PubMed:18190525). Also active with
CC phenazine methosulfate and 1,4-benzoquinone as electron acceptors
CC (PubMed:18190525). Involved in the regulation of the accumulation of
CC the mitochondrial respiratory complex I (PubMed:18799460,
CC PubMed:33060577). Structural part of one of the plant-specific
CC mitochondrial complex I assembly intermediates, lacking the whole
CC distal (PD) module (PubMed:33060577). Prevents the binding of the plant
CC specific P1 protein (CPN60/HSP60), responsible for the linkage of the
CC proximal (PP) to the distal (PD) module (PubMed:33060577).
CC {ECO:0000269|PubMed:18190525, ECO:0000269|PubMed:18799460,
CC ECO:0000269|PubMed:33060577}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(III)-[cytochrome c] + L-galactono-1,4-lactone = 4 Fe(II)-
CC [cytochrome c] + 5 H(+) + L-dehydroascorbate; Xref=Rhea:RHEA:32367,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17464, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:58539; EC=1.3.2.3;
CC Evidence={ECO:0000269|PubMed:18190525};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32368;
CC Evidence={ECO:0000269|PubMed:18190525};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:18190525};
CC Note=Binds FAD non-covalently. {ECO:0000269|PubMed:18190525};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.17 mM for L-galactono-1,4-lactone {ECO:0000269|PubMed:18190525};
CC KM=13.1 mM for L-gulono-1,4-lactone as substrate
CC {ECO:0000269|PubMed:18190525};
CC KM=0.034 mM for cytochrome C as electron acceptor
CC {ECO:0000269|PubMed:18190525};
CC KM=0.026 mM for phenazine methosulfate as electron acceptor
CC {ECO:0000269|PubMed:18190525};
CC KM=0.280 mM for 1,4-benzoquinone as electron acceptor
CC {ECO:0000269|PubMed:18190525};
CC pH dependence:
CC Optimum pH is 8.8. {ECO:0000269|PubMed:18190525};
CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:18799460}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SU56-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SU56-2; Sequence=VSP_037137, VSP_037138;
CC -!- DISRUPTION PHENOTYPE: Delayed germination, chlorotic cotyledons and
CC death at the cotyledon stage. {ECO:0000269|PubMed:18799460}.
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DR EMBL; AB042279; BAA95212.1; -; mRNA.
DR EMBL; AL049658; CAB41146.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78347.1; -; Genomic_DNA.
DR EMBL; BT005925; AAO64860.1; -; mRNA.
DR EMBL; AK117924; BAC42562.1; -; mRNA.
DR PIR; T06690; T06690.
DR RefSeq; NP_190376.1; NM_114662.3. [Q9SU56-1]
DR PDB; 7A24; EM; 3.80 A; z=1-610.
DR PDBsum; 7A24; -.
DR AlphaFoldDB; Q9SU56; -.
DR SMR; Q9SU56; -.
DR BioGRID; 9268; 2.
DR IntAct; Q9SU56; 2.
DR STRING; 3702.AT3G47930.1; -.
DR PaxDb; Q9SU56; -.
DR PRIDE; Q9SU56; -.
DR ProteomicsDB; 230466; -. [Q9SU56-1]
DR EnsemblPlants; AT3G47930.1; AT3G47930.1; AT3G47930. [Q9SU56-1]
DR GeneID; 823948; -.
DR Gramene; AT3G47930.1; AT3G47930.1; AT3G47930. [Q9SU56-1]
DR KEGG; ath:AT3G47930; -.
DR Araport; AT3G47930; -.
DR TAIR; locus:2097865; AT3G47930.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_021072_0_0_1; -.
DR InParanoid; Q9SU56; -.
DR OMA; DPLNKNH; -.
DR PhylomeDB; Q9SU56; -.
DR BioCyc; ARA:AT3G47930-MON; -.
DR BRENDA; 1.3.2.3; 399.
DR SABIO-RK; Q9SU56; -.
DR UniPathway; UPA00132; -.
DR PRO; PR:Q9SU56; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SU56; baseline and differential.
DR Genevisible; Q9SU56; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016633; F:galactonolactone dehydrogenase activity; IDA:TAIR.
DR GO; GO:0080049; F:L-gulono-1,4-lactone dehydrogenase activity; IDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IDA:TAIR.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR007173; ALO_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR010031; FAD_lactone_oxidase.
DR InterPro; IPR010029; GL_DH.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR43762; PTHR43762; 1.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR PIRSF; PIRSF000136; LGO_GLO; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR TIGRFAMs; TIGR01676; GLDHase; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Membrane; Mitochondrion;
KW Oxidoreductase; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT PROPEP 36..101
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:O47881"
FT /id="PRO_0000372081"
FT CHAIN 102..610
FT /note="L-galactono-1,4-lactone dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000372082"
FT TRANSMEM 68..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 123..258
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 17..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..60
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 494..512
FT /note="KSPISPAFSTSEDDIFSWV -> WYNHVPPDSRPSPEKGHHR (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037137"
FT VAR_SEQ 513..610
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037138"
FT MUTAGEN 156
FT /note="L->A,C: No covalent flavinylation, lower affinity
FT for the substrate and lower activity."
FT /evidence="ECO:0000269|PubMed:18190525"
FT MUTAGEN 156
FT /note="L->F: No covalent flavinylation."
FT /evidence="ECO:0000269|PubMed:18190525"
FT MUTAGEN 156
FT /note="L->H: No covalent flavinylation and no change of
FT affinity for the substrate, but lower activity and
FT decreased thermostability."
FT /evidence="ECO:0000269|PubMed:18190525"
FT MUTAGEN 156
FT /note="L->I: No covalent flavinylation and higher turnover
FT rate of the substrate."
FT /evidence="ECO:0000269|PubMed:18190525"
FT CONFLICT 346
FT /note="D -> G (in Ref. 1; BAA95212)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="Q -> H (in Ref. 4; AAO64860 and 5; BAC42562)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 610 AA; 68555 MW; D49C2A13ED5F9AF7 CRC64;
MLRSLLLRRS VGHSLGTLSP SSSTIRSSFS PHRTLCTTGQ TLTPPPPPPP RPPPPPPATA
SEAQFRKYAG YAALAIFSGV ATYFSFPFPE NAKHKKAQIF RYAPLPEDLH TVSNWSGTHE
VQTRNFNQPE NLADLEALVK ESHEKKLRIR PVGSGLSPNG IGLSRSGMVN LALMDKVLEV
DKEKKRVTVQ AGIRVQQLVD AIKDYGLTLQ NFASIREQQI GGIIQVGAHG TGARLPPIDE
QVISMKLVTP AKGTIELSRE KDPELFHLAR CGLGGLGVVA EVTLQCVARH ELVEHTYVSN
LQEIKKNHKK LLSANKHVKY LYIPYTDTVV VVTCNPVSKW SGPPKDKPKY TTDEAVQHVR
DLYRESIVKY RVQDSGKKSP DSSEPDIQEL SFTELRDKLL ALDPLNDVHV AKVNQAEAEF
WKKSEGYRVG WSDEILGFDC GGQQWVSESC FPAGTLANPS MKDLEYIEEL KKLIEKEAIP
APAPIEQRWT ARSKSPISPA FSTSEDDIFS WVGIIMYLPT ADPRQRKDIT DEFFHYRHLT
QKQLWDQFSA YEHWAKIEIP KDKEELEALQ ARIRKRFPVD AYNKARRELD PNRILSNNMV
EKLFPVSTTA
