Q54E41 (HAOX_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hydroxyacid oxidase
Short name=HAOX
EC=1.1.3.15

Alternative name(s):
Glycolate oxidase
Short name=GOX

Gene names

Name:	haox
ORF Names:	DDB_G0291814

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	388 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Has 2-hydroxyacid oxidase activity By similarity.
Catalytic activity	(S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2.
Cofactor	FMN By similarity.
Pathway	Organic acid metabolism; glycolate degradation; 3-phospho-D-glycerate from glycolate: step 1/4.
Sequence similarities	Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family. Contains 1 FMN hydroxy acid dehydrogenase domain.

Ontologies

Keywords
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycolate catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	FMN binding Inferred from electronic annotation. Source: InterPro long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity Inferred from electronic annotation. Source: EC medium-chain-(S)-2-hydroxy-acid oxidase activity Inferred from electronic annotation. Source: EC very-long-chain-(S)-2-hydroxy-acid oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 388	388	Hydroxyacid oxidase		PRO_0000328260
Regions
	Domain	26 – 384	359	FMN hydroxy acid dehydrogenase
	Nucleotide binding	310 – 334	25	FMN By similarity
	Compositional bias	7 – 10	4	Poly-Asn
Sites
	Active site	279	1	Proton acceptor By similarity
	Binding site	52	1	Substrate Potential
	Binding site	134	1	FMN By similarity
	Binding site	156	1	FMN By similarity
	Binding site	158	1	Substrate By similarity
	Binding site	184	1	FMN By similarity
	Binding site	193	1	Substrate By similarity
	Binding site	255	1	FMN By similarity
	Binding site	282	1	Substrate Potential

Sequences

	Sequence		Length	Mass (Da)
	Q54E41 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: C42C59FFE992395D	FASTA	388	42,877
	10 20 30 40 50 60 MENQFKNNNN SSSIETSNQF SNKKTNRLDS FVSVSELHEE AKRLLPKMAY DYYASGSNDQ 70 80 90 100 110 120 ITLAENENAF SRIKLVPRSL VDVSKVNTKT RIFGRDISTP ILIAPWAMQR MASQRGELDT 130 140 150 160 170 180 VEASKEFNTI MTLSSLSTTS VEDLSSATNG NPGWFQLYVF KDRKVSEELV KRAESIGYSA 190 200 210 220 230 240 LVLTVDTPFL GKRTADFKNS FKLPNGLSLK IFEKLMLSNL DGGLNQYIAT MIDPSLTWND 250 260 270 280 290 300 LKWLKSITKL PILVKGIMCP KDAELALQYG ADGIIVSNHG GRQLDTCPST IEVLPYISKV 310 320 330 340 350 360 VRGRVPLILD GGIRRGTDVL KALAFGANAV CIGRPIIWGL STGGKDGVLK VLNLLNSELQ 370 380 LAMALTGITN ISDINNSIIW DQNKYIKL

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000185 Genomic DNA. Translation: EAL61528.1.
RefSeq	XP_629946.1. XM_629944.1.
3D structure databases
ProteinModelPortal	Q54E41.
SMR	Q54E41. Positions 31-381.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDBDRAFT_0184082.
Proteomic databases
PRIDE	Q54E41.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0267054; DDB0267054; DDB_G0291814.
GeneID	8628352.
KEGG	ddi:DDB_G0291814.
Organism-specific databases
dictyBase	DDB_G0291814. hao.
Phylogenomic databases
eggNOG	COG1304.
KO	K11517.
OMA	IGTRQVF.
ProtClustDB	CLSZ2429507.
Enzyme and pathway databases
UniPathway	UPA00864; UER00830.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR012133. Alpha-hydoxy_acid_DH_FMN. IPR000262. FMN-dep_DH. IPR008259. FMN_hydac_DH_AS. [Graphical view]
Pfam	PF01070. FMN_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITE	PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit. PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HAOX_DICDI

Accession

Primary (citable) accession number: Q54E41

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	May 29, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)