Reviewed, UniProtKB/Swiss-Prot Q8HXW0 (GGLO_PIG)

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

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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 transcript level.

General annotation (Comments)

Function	Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate By similarity. UniProtKB P10867
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 By similarity. UniProtKB P10867
Pathway	Cofactor biosynthesis; L-ascorbic acid biosynthesis.
Subcellular location	Microsome membrane; Single-pass membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass membrane protein By similarity.
Sequence similarities	Belongs to the oxygen-dependent FAD-linked oxidoreductase family. Contains 1 FAD-binding PCMH-type domain.

Ontologies

Keywords
Biological process	Ascorbate biosynthesis
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	L-ascorbic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW 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 Inferred from electronic annotation. Source: UniProtKB-SubCell
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity UniProtKB P10867
	Chain	2 – 440	439	L-gulonolactone oxidase		PRO_0000128160
Regions
	Transmembrane	253 – 273	21	Potential
	Domain	17 – 187	171	FAD-binding PCMH-type
Amino acid modifications
	Modified residue	54	1	Tele-8alpha-FAD histidine By similarity UniProtKB P08159

Sequences

	Sequence		Length	Mass (Da)
	Q8HXW0-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 81BC3E0873627201	FASTA	440	50,352
	10 20 30 40 50 60 MVHGHKGVKF QNWAKTYGCC PEMYYQPTSV EEIREVLALA RQQNKRVKVV GGGHSPSDIA 70 80 90 100 110 120 CTDGFMIHMG KMNRVLKVDM EKKQVTVEAG ILLADLHPQL DKHGLALSNL GAVSDVTAGG 130 140 150 160 170 180 VIGSGTHNTG IKHGILATQV VELTLLTPDG TVLVCSESSN AEVFQAARVH LGCLGVILTV 190 200 210 220 230 240 TLQCVPQFHL QETTFPSTLK EVLDNLDSHL KKSEYFRFLW FPHSENVSVI YQDHTNKPPS 250 260 270 280 290 300 SSANWFWDYA IGFYLLEFLL WISTFVPGLV GWINRFFFWL LFNGKKENCN LSHKIFTYEC 310 320 330 340 350 360 RFKQHVQDWA IPREKTKEAL LELKAMLEAH PKVVAHYPVE VRFTRADDIL LSPCFQRDSC 370 380 390 400 410 420 YMNIIMYRPY GKDVPRLDYW LAYETIMKKV GGRPHWAKAH NCTRKDFEKM YPAFRKFCAI 430 440 REKLDPTGMF LNAYLEKVFY

References

[1]	"Intragenic deletion in the gene encoding L-gulonolactone oxidase causes vitamin C deficiency in pigs." Hasan L., Voegeli P., Stoll P., Kramer S.S., Stranzinger G., Neuenschwander S. Mamm. Genome 15:323-333(2004) [PubMed: 15112110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF440259 mRNA. Translation: AAN63634.1. AF136938 mRNA. Translation: AAF61429.1.
RefSeq	NP_001123420.1.
UniGene	Ssc.16369
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	396759.
KEGG	ssc:396759.
Phylogenomic databases
HOVERGEN	Q8HXW0.
Enzyme and pathway databases
BRENDA	1.1.3.8. 249.
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...

Entry information

Entry name

GGLO_PIG

Accession

Primary (citable) accession number: Q8HXW0
Secondary accession number(s): Q9N1U4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 47 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)