[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2824469 [NCBI, ExPASy, EBI, Israel, Japan] Volokita M., Somerville C.R.; "The primary structure of spinach glycolate oxidase deduced from the DNA sequence of a cDNA clone."; J. Biol. Chem. 262:15825-15828(1987).
[2]	PROTEIN SEQUENCE. PubMed=3286256 [NCBI, ExPASy, EBI, Israel, Japan] Cederlund E., Lindqvist Y., Soederlund G., Braenden C.-I., Joernvall H.; "Primary structure of glycolate oxidase from spinach."; Eur. J. Biochem. 173:523-530(1988).
[3]	ACTIVE SITE. PubMed=2644287 [NCBI, ExPASy, EBI, Israel, Japan] Lindqvist Y., Braenden C.-I.; "The active site of spinach glycolate oxidase."; J. Biol. Chem. 264:3624-3628(1989).
[4]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). DOI=10.1016/0022-2836(89)90178-2; PubMed=2681790 [NCBI, ExPASy, EBI, Israel, Japan] Lindqvist Y.; "Refined structure of spinach glycolate oxidase at 2-A resolution."; J. Mol. Biol. 209:151-166(1989).
[5]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-359 IN COMPLEX WITH FMN AND INHIBITOR. PubMed=9144771 [NCBI, ExPASy, EBI, Israel, Japan] Stenberg K., Lindqvist Y.; "Three-dimensional structures of glycolate oxidase with bound active-site inhibitors."; Protein Sci. 6:1009-1015(1997).

Comments

CATALYTIC ACTIVITY: (S)-2-hydroxy acid + O₂ = 2-oxo acid + H₂O₂.
COFACTOR: FMN.
PATHWAY: Photosynthesis; photorespiration; glycine from 2-phosphoglycolic acid: step 2/3 .
SUBUNIT: Homotetramer or homooctamer.
SUBCELLULAR LOCATION: Peroxisome.
SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
SIMILARITY: Contains 1 FMN hydroxy acid dehydrogenase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J03492; AAA34030.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A28496; OXSPH.

3D structure databases

PDB

1AL7; X-ray; 2.60 A; A=1-359.	[ExPASy / RCSB / EBI]
1AL8; X-ray; 2.20 A; A=1-359.	[ExPASy / RCSB / EBI]
1GOX; X-ray; 2.00 A; A=1-369.	[ExPASy / RCSB / EBI]
1GYL; X-ray; 3.00 A; A/B=1-369.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AL7; -.
1AL8; -.
1GOX; -.
1GYL; -.

ModBase

P05414.

Family and domain databases

InterPro

IPR013785; Aldolase_TIM.
IPR012133; Alpha_OHA_DHase_FMN.
IPR008259; FMN_hydac_DHase_AS.
IPR000262; FMN_OHA_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

Pfam

PF01070; FMN_dh; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000138; Al-hdrx_acd_dh; 1.

PROSITE

PS00557; FMN_HYDROXY_ACID_DH_1; 1.
PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

P05414; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Direct protein sequencing; Flavoprotein; FMN; Glycolate pathway; Oxidoreductase; Peroxisome; Photorespiration.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 369`	`369`	`Peroxisomal (S)-2-hydroxy-acid oxidase.`	`PRO_0000206325`
`DOMAIN`	`1 359`	`359`	`FMN hydroxy acid dehydrogenase.`
`NP_BIND`	`285 309`	`25`	`FMN.`
`MOTIF`	`367 369`	`3`	`Microbody targeting signal (Potential).`
`ACT_SITE`	`254 254`		`Proton acceptor.`
`BINDING`	`24 24`		`Substrate (Potential).`
`BINDING`	`106 106`		`FMN.`
`BINDING`	`127 127`		`FMN.`
`BINDING`	`129 129`		`Substrate (By similarity).`
`BINDING`	`155 155`		`FMN.`
`BINDING`	`164 164`		`Substrate (By similarity).`
`BINDING`	`230 230`		`FMN.`
`BINDING`	`257 257`		`Substrate (Potential).`
`MOD_RES`	`1 1`		`N-acetylmethionine.`
`HELIX`	`8 16`	`9`
`HELIX`	`19 26`	`8`
`HELIX`	`33 40`	`8`
`HELIX`	`41 44`	`4`
`STRAND`	`62 64`	`3`
`STRAND`	`67 75`	`9`
`HELIX`	`81 83`	`3`
`TURN`	`86 88`	`3`
`HELIX`	`89 98`	`10`
`STRAND`	`103 105`	`3`
`HELIX`	`113 118`	`6`
`STRAND`	`124 128`	`5`
`HELIX`	`134 146`	`13`
`STRAND`	`152 155`	`4`
`TURN`	`169 171`	`3`
`HELIX`	`181 183`	`3`
`STRAND`	`184 186`	`3`
`STRAND`	`201 203`	`3`
`HELIX`	`204 206`	`3`
`HELIX`	`213 222`	`10`
`STRAND`	`227 232`	`6`
`HELIX`	`235 243`	`9`
`STRAND`	`247 251`	`5`
`TURN`	`254 257`	`4`
`HELIX`	`265 276`	`12`
`STRAND`	`282 284`	`3`
`HELIX`	`291 299`	`9`
`STRAND`	`303 307`	`5`
`HELIX`	`309 318`	`10`
`HELIX`	`320 341`	`22`
`HELIX`	`346 348`	`3`
`HELIX`	`351 353`	`3`

Sequence information

Length: 369 AA [This is the length of the unprocessed precursor]

Molecular weight: 40286 Da [This is the MW of the unprocessed precursor]

CRC64: 892F1B3D0C1B48E0 [This is a checksum on the sequence]

        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

P05414 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools