HAOX2_BOVIN
ID HAOX2_BOVIN Reviewed; 353 AA.
AC Q3ZBW2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=2-Hydroxyacid oxidase 2;
DE Short=HAOX2;
DE EC=1.1.3.15 {ECO:0000250|UniProtKB:Q9NYQ3};
DE AltName: Full=(S)-2-hydroxy-acid oxidase, peroxisomal;
GN Name=HAO2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Oxidase that catalyzes the oxidation of medium and long chain
CC hydroxyacids such as 2-hydroxyhexadecanoate and 2-hydroxyoctanoate, to
CC the correspondong 2-oxoacids. Its role in the oxidation of 2-hydroxy
CC fatty acids may contribute to the general pathway of fatty acid alpha-
CC oxidation. Active in vitro with the artificial electron acceptor 2,6-
CC dichlorophenolindophenol (DCIP), but O2 is believed to be the
CC physiological electron acceptor, leading to the production of H2O2.
CC {ECO:0000250|UniProtKB:Q9NYQ3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2S)-2-hydroxycarboxylate + O2 = a 2-oxocarboxylate + H2O2;
CC Xref=Rhea:RHEA:16789, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:35179, ChEBI:CHEBI:58123; EC=1.1.3.15;
CC Evidence={ECO:0000250|UniProtKB:Q9NYQ3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16790;
CC Evidence={ECO:0000250|UniProtKB:Q9NYQ3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyhexadecanoate + O2 = 2-oxohexadecanoate + H2O2;
CC Xref=Rhea:RHEA:67944, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:65097, ChEBI:CHEBI:176593;
CC Evidence={ECO:0000250|UniProtKB:Q9NYQ3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67945;
CC Evidence={ECO:0000250|UniProtKB:Q9NYQ3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyoctanoate + O2 = 2-oxooctanoate + H2O2;
CC Xref=Rhea:RHEA:67940, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:133514, ChEBI:CHEBI:176689;
CC Evidence={ECO:0000250|UniProtKB:Q9NYQ3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67941;
CC Evidence={ECO:0000250|UniProtKB:Q9NYQ3};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q9UJM8};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000250|UniProtKB:Q9NYQ3}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9UJM8}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q9NYQ3}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
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DR EMBL; BC103070; AAI03071.1; -; mRNA.
DR RefSeq; NP_001030243.1; NM_001035071.1.
DR RefSeq; XP_005204069.1; XM_005204012.3.
DR AlphaFoldDB; Q3ZBW2; -.
DR SMR; Q3ZBW2; -.
DR STRING; 9913.ENSBTAP00000000134; -.
DR PaxDb; Q3ZBW2; -.
DR PeptideAtlas; Q3ZBW2; -.
DR Ensembl; ENSBTAT00000000134; ENSBTAP00000000134; ENSBTAG00000000123.
DR GeneID; 509481; -.
DR KEGG; bta:509481; -.
DR CTD; 51179; -.
DR VEuPathDB; HostDB:ENSBTAG00000000123; -.
DR VGNC; VGNC:29748; HAO2.
DR eggNOG; KOG0538; Eukaryota.
DR GeneTree; ENSGT00390000018717; -.
DR HOGENOM; CLU_020639_0_0_1; -.
DR InParanoid; Q3ZBW2; -.
DR OMA; FQYEIYL; -.
DR OrthoDB; 879633at2759; -.
DR TreeFam; TF313363; -.
DR Reactome; R-BTA-390918; Peroxisomal lipid metabolism.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000000123; Expressed in adult mammalian kidney and 29 other tissues.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:Ensembl.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0019395; P:fatty acid oxidation; IEA:Ensembl.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR008259; FMN_hydac_DH_AS.
DR Pfam; PF01070; FMN_dh; 1.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 2: Evidence at transcript level;
KW Fatty acid metabolism; Flavoprotein; FMN; Lipid metabolism; Oxidoreductase;
KW Peroxisome; Reference proteome.
FT CHAIN 1..353
FT /note="2-Hydroxyacid oxidase 2"
FT /id="PRO_0000285088"
FT DOMAIN 2..353
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT MOTIF 351..353
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 77..79
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 106
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 128
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 130
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 156
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 165
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 224
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 251
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 279..283
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
FT BINDING 302..303
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q07523"
SQ SEQUENCE 353 AA; 39253 MW; E20D09034252F692 CRC64;
MPLVCLTDFR EHAREHLSKS TWDFIEGGAD DCCTRDENMA AFKKIRLRPR YLKDVSKVDM
RTTIQGAEIS APICIAPTGF HRLAWPDGEM STARAAQAAS ICYITSTYAS CSLEDIVAAA
PRGLRWFQLY VHPNRQINKQ MIQKVESLGF KALVITVDVP KVGNRRNDIT NQVDLMKKLL
LKDLGSPEMG NVMPYFQMSP IDPSICWEDL SWFQSMTRLP IILKGILTKE DAELAVKHNV
HGIIVSNHGG RQLDEVPASI DALTEVVAAV KGKVEVYLDG GIRTGNDVLK ALALGAKCVF
VGRPILWGLA YKGEHGVKEV LDILKNEFHT SMTLTGCRSV AEINQDLIQF SRL
