L-gulonolactone oxidase - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot P10867 (GGLO_RAT)

Last modified June 16, 2009. Version 87. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    L-gulonolactone oxidase
      Short name=LGO
    EC=1.1.3.8
Alternative name(s):
    L-gulono-gamma-lactone oxidase
      Short name=GLO

Gene names

Name:

Gulo

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length	440 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate. Ref.6
Catalytic activity	L-gulono-1,4-lactone + O₂ = L-xylo-hex-2-ulono-1,4-lactone + H₂O₂. L-xylo-hex-2-ulono-1,4-lactone = L-ascorbate.
Cofactor	FAD.
Pathway	Cofactor biosynthesis; L-ascorbic acid biosynthesis.
Subcellular location	Microsome membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence similarities	Belongs to the oxygen-dependent FAD-linked oxidoreductase family. Contains 1 FAD-binding PCMH-type domain.

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Ontologies

Keywords
Biological process	Ascorbate biosynthesis
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	L-ascorbic acid biosynthetic process Ref.1 Traceable author statement. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Ref.1 Traceable author statement. Source: RGD
Molecular function	D-arabinono-1,4-lactone oxidase activity Inferred from electronic annotation. Source: InterPro FAD binding Inferred from electronic annotation. Source: InterPro L-gulonolactone oxidase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 440

439

L-gulonolactone oxidase

PRO_0000128161

Regions

Transmembrane

251 – 273

Potential

Domain

17 – 187

171

FAD-binding PCMH-type

Amino acid modifications

Modified residue

Tele-8alpha-FAD histidine By similarity

Experimental info

Sequence conflict

I → V in AAH89803. Ref.4

Sequence conflict

189

H → Q in AAA41164. Ref.1

Sequence conflict

404

Q → R Ref.2

Sequence conflict

404

Q → R Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

P10867-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D63AD580A6F591F8
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FASTA

440

50,615

        10         20         30         40         50         60 
MVHGYKGVQF QNWAKTYGCS PEVYYQPTSV EEVREVLALA REQKKKVKVV GGGHSPSDIA 

        70         80         90        100        110        120 
CTDGFMIHMG KMNRVLQVDK EKKQITVEAG ILLADLHPQL DEHGLAMSNL GAVSDVTVAG 

       130        140        150        160        170        180 
VIGSGTHNTG IKHGILATQV VALTLMTADG EVLECSESRN ADVFQAARVH LGCLGIILTV 

       190        200        210        220        230        240 
TLQCVPQFHL QETSFPSTLK EVLDNLDSHL KRSEYFRFLW FPHTENVSII YQDHTNKAPS 

       250        260        270        280        290        300 
SASNWFWDYA IGFYLLEFLL WTSTYLPCLV GWINRFFFWM LFNCKKESSN LSHKIFTYEC 

       310        320        330        340        350        360 
RFKQHVQDWA IPREKTKEAL LELKAMLEAH PKVVAHYPVE VRFTRGDDIL LSPCFQRDSC 

       370        380        390        400        410        420 
YMNIIMYRPY GKDVPRLDYW LAYETIMKKF GGRPHWAKAH NCTQKDFEEM YPTFHKFCDI 

       430        440 
REKLDPTGMF LNSYLEKVFY

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3338984] [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: 1400507] [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: 1962571] [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: 15489334] [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: 3214183] [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: 8459881] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-41, FUNCTION.

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Cross-references

Sequence databases
	J03536 Genomic DNA. Translation: AAA41164.1. D12754 Genomic DNA. Translation: BAA02232.1. D00526 Genomic DNA. Translation: BAA33497.1. BC089803 mRNA. Translation: AAH89803.1.
IPI	IPI00555278.
PIR	OXRTGU. A45123.
RefSeq	NP_071556.2.
UniGene	Rn.115212
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	P10867.
Genome annotation databases
Ensembl	ENSRNOG00000016648. Rattus norvegicus. [Contig view]
GeneID	60671.
KEGG	rno:60671.
Organism-specific databases
RGD	620701. Gulo.
Phylogenomic databases
HOVERGEN	P10867.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-13235.
BRENDA	1.1.3.8. 248.
Gene expression databases
ArrayExpress	P10867.
GermOnline	ENSRNOG00000016648. Rattus norvegicus.
Family and domain databases
InterPro	IPR007173. ALO. IPR016166. FAD-bd_2. IPR016168. FAD-linked_Oxase_FAD-bd_sub2. IPR010031. FAD_lactone_oxidase. IPR006094. Oxid_FAD_bind_N. IPR006093. Oxy_OxRdtase_FAD_BS. [Graphical view]
Gene3D	G3DSA:3.30.465.20. FAD-linked_oxidase_FAD-bd_sub2. 1 hit.
Pfam	PF04030. ALO. 1 hit. PF01565. FAD_binding_4. 1 hit. [Graphical view]
TIGRFAMs	TIGR01678. FAD_lactone_ox. 1 hit.
PROSITE	PS51387. FAD_PCMH. 1 hit. PS00862. OX2_COVAL_FAD. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	612407.

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Entry information

Entry name

GGLO_RAT

Accession

Primary (citable) accession number: P10867
Secondary accession number(s): Q5EBC1, Q64597, Q9QWR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents