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Protein

L-gulonolactone oxidase

Gene

Gulo

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate.1 Publication

Catalytic activityi

L-gulono-1,4-lactone + O2 = L-ascorbate + H2O2.

Cofactori

Pathwayi: L-ascorbate biosynthesis via UDP-alpha-D-glucuronate pathway

This protein is involved in step 4 of the subpathway that synthesizes L-ascorbate from UDP-alpha-D-glucuronate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. Regucalcin (Rgn)
  4. L-gulonolactone oxidase (Gulo)
This subpathway is part of the pathway L-ascorbate biosynthesis via UDP-alpha-D-glucuronate pathway, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-ascorbate from UDP-alpha-D-glucuronate, the pathway L-ascorbate biosynthesis via UDP-alpha-D-glucuronate pathway and in Cofactor biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Ascorbate biosynthesis

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13235.
UniPathwayiUPA00991; UER00939.

Names & Taxonomyi

Protein namesi
Recommended name:
L-gulonolactone oxidase (EC:1.1.3.8)
Short name:
LGO
Alternative name(s):
L-gulono-gamma-lactone oxidase
Short name:
GLO
Gene namesi
Name:Gulo
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620701. Gulo.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei251 – 27323HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 440439L-gulonolactone oxidasePRO_0000128161Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541Pros-8alpha-FAD histidineBy similarity

Proteomic databases

PaxDbiP10867.
PRIDEiP10867.

PTM databases

iPTMnetiP10867.
PhosphoSiteiP10867.

Interactioni

Protein-protein interaction databases

MINTiMINT-4564517.
STRINGi10116.ENSRNOP00000022703.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 187171FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4730. Eukaryota.
COG0277. LUCA.
HOGENOMiHOG000252847.
HOVERGENiHBG005834.
InParanoidiP10867.
KOiK00103.
OrthoDBiEOG7N8ZV8.
PhylomeDBiP10867.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR007173. ALO.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR010031. FAD_lactone_oxidase.
IPR006094. Oxid_FAD_bind_N.
IPR006093. Oxy_OxRdtase_FAD_BS.
IPR030654. Sugar_lactone_oxidase.
[Graphical view]
PfamiPF04030. ALO. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
PIRSFiPIRSF000136. LGO_GLO. 1 hit.
SUPFAMiSSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR01678. FAD_lactone_ox. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10867-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHGYKGVQF QNWAKTYGCS PEVYYQPTSV EEVREVLALA REQKKKVKVV
60 70 80 90 100
GGGHSPSDIA CTDGFMIHMG KMNRVLQVDK EKKQITVEAG ILLADLHPQL
110 120 130 140 150
DEHGLAMSNL GAVSDVTVAG VIGSGTHNTG IKHGILATQV VALTLMTADG
160 170 180 190 200
EVLECSESRN ADVFQAARVH LGCLGIILTV TLQCVPQFHL QETSFPSTLK
210 220 230 240 250
EVLDNLDSHL KRSEYFRFLW FPHTENVSII YQDHTNKAPS SASNWFWDYA
260 270 280 290 300
IGFYLLEFLL WTSTYLPCLV GWINRFFFWM LFNCKKESSN LSHKIFTYEC
310 320 330 340 350
RFKQHVQDWA IPREKTKEAL LELKAMLEAH PKVVAHYPVE VRFTRGDDIL
360 370 380 390 400
LSPCFQRDSC YMNIIMYRPY GKDVPRLDYW LAYETIMKKF GGRPHWAKAH
410 420 430 440
NCTQKDFEEM YPTFHKFCDI REKLDPTGMF LNSYLEKVFY
Length:440
Mass (Da):50,615
Last modified:January 23, 2007 - v3
Checksum:iD63AD580A6F591F8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851I → V in AAH89803 (PubMed:15489334).Curated
Sequence conflicti189 – 1891H → Q in AAA41164 (PubMed:3338984).Curated
Sequence conflicti404 – 4041Q → R (PubMed:1400507).Curated
Sequence conflicti404 – 4041Q → R (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03536 Genomic DNA. Translation: AAA41164.1.
D12754 Genomic DNA. Translation: BAA02232.1.
D00526 Genomic DNA. Translation: BAA33497.1.
BC089803 mRNA. Translation: AAH89803.1.
PIRiA45123. OXRTGU.
RefSeqiNP_071556.2. NM_022220.2.
UniGeneiRn.115212.

Genome annotation databases

GeneIDi60671.
KEGGirno:60671.
UCSCiRGD:620701. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03536 Genomic DNA. Translation: AAA41164.1.
D12754 Genomic DNA. Translation: BAA02232.1.
D00526 Genomic DNA. Translation: BAA33497.1.
BC089803 mRNA. Translation: AAH89803.1.
PIRiA45123. OXRTGU.
RefSeqiNP_071556.2. NM_022220.2.
UniGeneiRn.115212.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4564517.
STRINGi10116.ENSRNOP00000022703.

PTM databases

iPTMnetiP10867.
PhosphoSiteiP10867.

Proteomic databases

PaxDbiP10867.
PRIDEiP10867.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi60671.
KEGGirno:60671.
UCSCiRGD:620701. rat.

Organism-specific databases

CTDi268756.
RGDi620701. Gulo.

Phylogenomic databases

eggNOGiKOG4730. Eukaryota.
COG0277. LUCA.
HOGENOMiHOG000252847.
HOVERGENiHBG005834.
InParanoidiP10867.
KOiK00103.
OrthoDBiEOG7N8ZV8.
PhylomeDBiP10867.

Enzyme and pathway databases

UniPathwayiUPA00991; UER00939.
BioCyciMetaCyc:MONOMER-13235.

Miscellaneous databases

NextBioi612407.
PROiP10867.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR007173. ALO.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR010031. FAD_lactone_oxidase.
IPR006094. Oxid_FAD_bind_N.
IPR006093. Oxy_OxRdtase_FAD_BS.
IPR030654. Sugar_lactone_oxidase.
[Graphical view]
PfamiPF04030. ALO. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
PIRSFiPIRSF000136. LGO_GLO. 1 hit.
SUPFAMiSSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR01678. FAD_lactone_ox. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequence analysis of a complementary DNA encoding rat liver L-gulono-gamma-lactone oxidase, a key enzyme for L-ascorbic acid biosynthesis."
    Koshizaka T., Nishikimi M., Ozawa T., Yagi K.
    J. Biol. Chem. 263:1619-1621(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "Guinea pigs possess a highly mutated gene for L-gulono-gamma-lactone oxidase, the key enzyme for L-ascorbic acid biosynthesis missing in this species."
    Nishikimi M., Kawai T., Yagi K.
    J. Biol. Chem. 267:21967-21972(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  3. "Molecular basis for the deficiency in humans of gulonolactone oxidase, a key enzyme for ascorbic acid biosynthesis."
    Nishikimi M., Yagi K.
    Am. J. Clin. Nutr. 54:1203S-1208S(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  5. "Occurrence in humans and guinea pigs of the gene related to their missing enzyme L-gulono-gamma-lactone oxidase."
    Nishikimi M., Koshizaka T., Ozawa T., Yagi K.
    Arch. Biochem. Biophys. 267:842-846(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-237.
  6. "L-gulono-gamma-lactone oxidase is the enzyme responsible for the production of methylguanidine in the rat liver."
    Fujitsuka N., Yokozawa T., Oura H., Akao T., Kobashi K., Ienaga K., Nakamura K.
    Nephron 63:445-451(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-41, FUNCTION.

Entry informationi

Entry nameiGGLO_RAT
AccessioniPrimary (citable) accession number: P10867
Secondary accession number(s): Q5EBC1, Q64597, Q9QWR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.