ID T1JBA5_STRMM Unreviewed; 450 AA.
AC T1JBA5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=L-gulonolactone oxidase {ECO:0000256|RuleBase:RU367158};
DE Short=LGO {ECO:0000256|RuleBase:RU367158};
DE EC=1.1.3.8 {ECO:0000256|RuleBase:RU367158};
OS Strigamia maritima (European centipede) (Geophilus maritimus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR011045-PA, ECO:0000313|Proteomes:UP000014500};
RN [1] {ECO:0000313|Proteomes:UP000014500}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA Muzny D.M., Gibbs R.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:SMAR011045-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2015) to UniProtKB.
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|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|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|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}. Peroxisome
CC {ECO:0000256|ARBA:ARBA00004275}.
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; JH432010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1JBA5; -.
DR STRING; 126957.T1JBA5; -.
DR EnsemblMetazoa; SMAR011045-RA; SMAR011045-PA; SMAR011045.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_003896_4_1_1; -.
DR OMA; YPRFGEF; -.
DR OrthoDB; 53654at2759; -.
DR PhylomeDB; T1JBA5; -.
DR UniPathway; UPA00991; UER00939.
DR Proteomes; UP000014500; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; 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; IPR030654; Sugar_lactone_oxidase.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
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.
PE 3: Inferred from homology;
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|ARBA:ARBA00023136};
KW Microsome {ECO:0000256|RuleBase:RU367158};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU367158}; Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000014500}.
FT DOMAIN 22..192
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 450 AA; 51920 MW; EF7CC47507AA5556 CRC64;
MSYSIKSRGK TGILFTNWSN TFFCRPELFF VPENVHHLKE IIRLAHLENK KIRVVGCGHS
PSDIACSKDY LISLRQFDRI LHVDPERHQV KVEGGVMVVD LISYLEKHGL ALRIAGSVSS
LTLAGAICTA THGSGVNFGN LSTLVVSMEI LTSAGEIIEV SRDNDLELFQ AACCSLGALG
IIISITYQCE KAYSLELNQY PCPLHTVLEN LEVHLKSSEH FRFLWFPHTP GTVVSHINRT
TKKIVMPSRL SKWHSWFWEY LVGYYVLELS YYISTLIPSS VPFINRLFYN LLYSKPRKRV
DQSQNIFNFE CLFKQYVNEW SIPIDKTATV LIELENWFSQ NTDVRAHFPI EVRFVKGDDL
LISPSHGRDS CYINIIMYRP YGKLVDYIKY WNAYEDIMTQ NGGRPHWAKA HKVGPMQLKE
MYPMYAKFCQ IRKKLDPTDT FVNSYMERIL
//
