ID A3RG68_TRISC Unreviewed; 440 AA.
AC A3RG68;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=L-gulonolactone oxidase {ECO:0000256|ARBA:ARBA00017520, ECO:0000256|RuleBase:RU367158};
DE Short=LGO {ECO:0000256|RuleBase:RU367158};
DE EC=1.1.3.8 {ECO:0000256|ARBA:ARBA00013121, ECO:0000256|RuleBase:RU367158};
GN Name=GLO {ECO:0000313|EMBL:ABO15547.1};
OS Triakis scyllium (Banded houndshark) (Hemigaleus pingi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Triakidae;
OC Triakis.
OX NCBI_TaxID=30494 {ECO:0000313|EMBL:ABO15547.1};
RN [1] {ECO:0000313|EMBL:ABO15547.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17317254; DOI=10.1016/j.cbpb.2007.01.001;
RA Cho Y.S., Douglas S.E., Gallant J.W., Kim K.Y., Kim D.S., Nam Y.K.;
RT "Isolation and characterization of cDNA sequences of L-gulono-gamma-lactone
RT oxidase, a key enzyme for biosynthesis of ascorbic acid, from extant
RT primitive fish groups.";
RL Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 147:178-190(2007).
CC -!- FUNCTION: Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and L-
CC xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate.
CC {ECO:0000256|ARBA:ARBA00003303, ECO:0000256|RuleBase:RU367158}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-gulono-1,4-lactone + O2 = H(+) + H2O2 + L-ascorbate;
CC Xref=Rhea:RHEA:32363, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17587, ChEBI:CHEBI:38290; EC=1.1.3.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001630,
CC ECO:0000256|RuleBase:RU367158};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU367158};
CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis via UDP-alpha-
CC D-glucuronate pathway; L-ascorbate from UDP-alpha-D-glucuronate: step
CC 4/4. {ECO:0000256|ARBA:ARBA00004764, ECO:0000256|RuleBase:RU367158}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000256|RuleBase:RU367158}; Single-pass membrane protein
CC {ECO:0000256|RuleBase:RU367158}. Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU367158}; Single-pass membrane protein
CC {ECO:0000256|RuleBase:RU367158}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466, ECO:0000256|RuleBase:RU367158}.
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DR EMBL; EF397519; ABO15547.1; -; mRNA.
DR AlphaFoldDB; A3RG68; -.
DR UniPathway; UPA00991; UER00939.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071949; F:FAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050105; F:L-gulonolactone oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2520; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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-like.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR InterPro; IPR030654; Sugar_lactone_oxidase.
DR NCBIfam; TIGR01678; FAD_lactone_ox; 1.
DR PANTHER; PTHR43762; L-GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR43762:SF1; L-GULONOLACTONE OXIDASE; 1.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR PIRSF; PIRSF000136; LGO_GLO; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE 2: Evidence at transcript level;
KW Ascorbate biosynthesis {ECO:0000256|RuleBase:RU367158};
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU367158};
KW FAD {ECO:0000256|RuleBase:RU367158};
KW Flavoprotein {ECO:0000256|RuleBase:RU367158};
KW Membrane {ECO:0000256|RuleBase:RU367158};
KW Microsome {ECO:0000256|RuleBase:RU367158};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU367158};
KW Transmembrane {ECO:0000256|RuleBase:RU367158};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367158}.
FT TRANSMEM 245..266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367158"
FT DOMAIN 17..187
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 440 AA; 51217 MW; 30ACA353F8006D64 CRC64;
MVQGTMGYQF QNWATTYSSE PELYFEPTTV EEIRQILELA KQRKKRVKIV GCGHSPSDIA
CTDDYLIRLN KFNRILQVDK ERKQVTVEAG MVLSDLNEKL DELGLALSNI GAVSDVALGG
VIGTGTHNTG IQHGILATQI VAMTLMTAAG DTIECSYTVN RELFQATRLH LGSLGVVLNV
TIQCVPAFKL HLQQFPKTLT EVLNDLDTHL KASEYFRFFW FPHTDKVTVF YADRTDKPIK
TSSSWFWNYA IGYYLLEFLL WISAFFPRLV PWINRLFYWL LYSTKVEQVK RSDKAFNFDC
LFKQHVSDWA VPIKQTRAAL EQLKDWLDNN PNVRVHFPVE VRFVRADDIL LSPCYKQDSC
YINIIMYRPY GKEVPRERYW AMYEEIMKRN GGRPHWAKAH SFLRQDFEKT YSAFHKFCSI
REELDPSGMF LNNYLEKTFF
//
