GLDH_BRAOL
ID GLDH_BRAOL Reviewed; 600 AA.
AC O47881;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=L-galactono-1,4-lactone dehydrogenase, mitochondrial;
DE EC=1.3.2.3;
DE Flags: Precursor;
OS Brassica oleracea (Wild cabbage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3712;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 92-104; 243-248; 340-347;
RP 364-380; 389-401; 403-412; 479-482; 534-542 AND 547-551, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=9374475; DOI=10.1074/jbc.272.48.30009;
RA Oestergaard J., Persiau G., Davey M.W., Bauw G., Van Montagu M.;
RT "Isolation of a cDNA coding for L-galactono-gamma-lactone dehydrogenase, an
RT enzyme involved in the biosynthesis of ascorbic acid in plants.
RT Purification, characterization, cDNA cloning, and expression in yeast.";
RL J. Biol. Chem. 272:30009-30016(1997).
CC -!- FUNCTION: Involved in the biosynthesis of ascorbic acid. Uses L-
CC galactono-1,4-lactone as substrate, but not L-gulono-1,4-lactone, D-
CC galactono-1,4-lactone, D-gulono-1,4-lactone, D-erythronic-1,4-lactone,
CC D-xylonic-1,4-lactone, L-mannono-1,4-lactone, D-galactonic acid, D-
CC glucuronic acid or D-gluconic acid. FAD, NAD, NADP and O(2) cannot act
CC as electron acceptor.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Inhibited by sulfhydryl-modifying agents such as
CC N-ethylmaleimide, monoiodoacetic acid and p-hydroxymercuribenzoic acid.
CC No inhibition by riboflavin and lycorine. {ECO:0000269|PubMed:9374475}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.3 mM for L-galactono-1,4-lactone {ECO:0000269|PubMed:9374475};
CC pH dependence:
CC Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:9374475};
CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: The FAD-binding PCMH-type domain does not bind FAD covalently.
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DR EMBL; Z97060; CAB09796.1; -; mRNA.
DR PIR; T14463; T14463.
DR AlphaFoldDB; O47881; -.
DR SMR; O47881; -.
DR KEGG; ag:CAB09796; -.
DR BioCyc; MetaCyc:MON-2307; -.
DR BRENDA; 1.3.2.3; 948.
DR SABIO-RK; O47881; -.
DR UniPathway; UPA00132; -.
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: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; IEA:UniProtKB-EC.
DR GO; GO:0080049; F:L-gulono-1,4-lactone dehydrogenase activity; IEA:EnsemblPlants.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-UniPathway.
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 Direct protein sequencing; Membrane; Mitochondrion; Oxidoreductase;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT PROPEP 26..91
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:9374475"
FT /id="PRO_0000372083"
FT CHAIN 92..600
FT /note="L-galactono-1,4-lactone dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000372084"
FT TRANSMEM 58..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 108..279
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 16..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..48
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 67830 MW; 0EF60046284D4C10 CRC64;
MLRSLLLRRS NARSLRPPFP PLRTLCTSGQ TLTPAPPPPP PPPPPISSSA SEKEFRKYAG
YAALALFSGA ATYFSFPFPE NAKHKKAQIF RYAPLPEDLH TVSNWSGTHE VQTRNFNQPE
TLADLEALVK EAHEKKNRIR PVGSGLSPNG IGLSRSGMVN LALMDKVLEV DKEKKRVRVQ
AGIRVQQLVD AIQEYGLTLQ NFASIREQQI GGIIQVGAHG TGARLPPIDE QVIGMKLVTP
AKGTIELSKD NDPELFHLAR CGLGGLGVVA EVTLQCVERQ ELLEHTYVST LEEIKKNHKK
LLSTNKHVKY LYIPYTDTVV VVTCNPVSKW SGAPKDKPKY TTEEALKHVR DLYRESIVKY
RVQDSSKKTP DSREPDINEL SFTELRDKLI ALDPLNDVHV GKVNQAEAEF WKKSEGYRVG
WSDEILGFDC GGQQWVSETC FPAGTLAKPS MKDLEYIEQL KELIQKEAIP APSPIEQRWT
GRSKSPMSPA FSTAEEDIFS WVGIIMYLPT ADPRQRKDIT DEFFHYRHLT QAKLWDQYSA
YEHWAKIEIP KDKEELEALQ ERLRKRFPVD AYNKARRELD PNRILSNNMV EKLFPVSKTA
