Reviewed, UniProtKB/Swiss-Prot P05414 (GOX_SPIOL)

Names and origin

Protein names	Recommended name:     Peroxisomal (S)-2-hydroxy-acid oxidase     EC=1.1.3.15 Alternative name(s):     Glycolate oxidase       Short name=GOX     Short chain alpha-hydroxy acid oxidase
Organism	Spinacia oleracea (Spinach)
Taxonomic identifier	3562 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	(S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2.
Cofactor	FMN.
Pathway	Photosynthesis; photorespiration; glycine from 2-phosphoglycolate: step 2/3.
Subunit structure	Homotetramer or homooctamer.
Subcellular location	Peroxisome.
Sequence similarities	Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family. Contains 1 FMN hydroxy acid dehydrogenase domain.

Ontologies

Keywords
Biological process	Glycolate pathway Photorespiration
Cellular component	Peroxisome
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxidative photosynthetic carbon pathway Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	(S)-2-hydroxy-acid oxidase activity Inferred from electronic annotation. Source: EC FMN binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 369

369

Peroxisomal (S)-2-hydroxy-acid oxidase

PRO_0000206325

Regions

Domain

1 – 359

359

FMN hydroxy acid dehydrogenase

Nucleotide binding

285 – 309

25

FMN

Motif

367 – 369

3

Microbody targeting signal Potential

Sites

Active site

254

1

Proton acceptor Ref.3

Binding site

24

1

Substrate Potential

Binding site

106

1

FMN

Binding site

127

1

FMN

Binding site

129

1

Substrate By similarity

Binding site

155

1

FMN

Binding site

164

1

Substrate By similarity

Binding site

230

1

FMN

Binding site

257

1

Substrate Potential

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.2

Secondary structure

1

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369

Helix Strand Turn

Details...

Helix

8 – 16

9

Helix

19 – 26

8

Helix

33 – 40

8

Helix

41 – 44

4

Beta strand

62 – 64

3

Beta strand

67 – 75

9

Helix

81 – 83

3

Turn

86 – 88

3

Helix

89 – 98

10

Beta strand

103 – 105

3

Helix

113 – 118

6

Beta strand

124 – 128

5

Helix

134 – 146

13

Beta strand

152 – 155

4

Turn

169 – 171

3

Helix

181 – 183

3

Beta strand

184 – 186

3

Beta strand

201 – 203

3

Helix

204 – 206

3

Helix

213 – 222

10

Beta strand

227 – 232

6

Helix

235 – 243

9

Beta strand

247 – 251

5

Turn

254 – 257

4

Helix

265 – 276

12

Beta strand

282 – 284

3

Helix

291 – 299

9

Beta strand

303 – 307

5

Helix

309 – 318

10

Helix

320 – 341

22

Helix

346 – 348

3

Helix

351 – 353

3

Sequences

	Sequence		Length	Mass (Da)
	P05414-1 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 892F1B3D0C1B48E0	FASTA	369	40,286
	10 20 30 40 50 60 MEITNVNEYE AIAKQKLPKM VYDYYASGAE DQWTLAENRN AFSRILFRPR ILIDVTNIDM 70 80 90 100 110 120 TTTILGFKIS MPIMIAPTAM QKMAHPEGEY ATARAASAAG TIMTLSSWAT SSVEEVASTG 130 140 150 160 170 180 PGIRFFQLYV YKDRNVVAQL VRRAERAGFK AIALTVDTPR LGRREADIKN RFVLPPFLTL 190 200 210 220 230 240 KNFEGIDLGK MDKANDSGLS SYVAGQIDRS LSWKDVAWLQ TITSLPILVK GVITAEDARL 250 260 270 280 290 300 AVQHGAAGII VSNHGARQLD YVPATIMALE EVVKAAQGRI PVFLDGGVRR GTDVFKALAL 310 320 330 340 350 360 GAAGVFIGRP VVFSLAAEGE AGVKKVLQMM RDEFELTMAL SGCRSLKEIS RSHIAADWDG PSSRAVARL

References

[1]	"The primary structure of spinach glycolate oxidase deduced from the DNA sequence of a cDNA clone." Volokita M., Somerville C.R. J. Biol. Chem. 262:15825-15828(1987) [PubMed: 2824469] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Primary structure of glycolate oxidase from spinach." Cederlund E., Lindqvist Y., Soederlund G., Braenden C.-I., Joernvall H. Eur. J. Biochem. 173:523-530(1988) [PubMed: 3286256] [Abstract] Cited for: PROTEIN SEQUENCE.
[3]	"The active site of spinach glycolate oxidase." Lindqvist Y., Braenden C.-I. J. Biol. Chem. 264:3624-3628(1989) [PubMed: 2644287] [Abstract] Cited for: ACTIVE SITE.
[4]	"Refined structure of spinach glycolate oxidase at 2-A resolution." Lindqvist Y. J. Mol. Biol. 209:151-166(1989) [PubMed: 2681790] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]	"Three-dimensional structures of glycolate oxidase with bound active-site inhibitors." Stenberg K., Lindqvist Y. Protein Sci. 6:1009-1015(1997) [PubMed: 9144771] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-359 IN COMPLEX WITH FMN AND INHIBITOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03492 mRNA. Translation: AAA34030.1.

PIR

OXSPH. A28496.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AL7	X-ray	2.60	A	1-359	[»]
1AL8	X-ray	2.20	A	1-359	[»]
1GOX	X-ray	2.00	A	1-369	[»]
1GYL	X-ray	3.00	A/B	1-369	[»]
2A7N	X-ray	1.80	A	176-195	[»]
2A7P	X-ray	2.20	A	176-195	[»]
2A85	X-ray	2.50	A	176-195	[»]
3GIY	X-ray	1.60	A	176-195	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.1.3.15. 286.

Family and domain databases

InterPro

IPR012133. a-Hydoxy_acid_DH_FMN.
IPR013785. Aldolase_TIM.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

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

GOX_SPIOL

Accession

Primary (citable) accession number: P05414

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	February 9, 2010
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)