CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011502
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Hydroxyacid oxidase 2 
Protein Synonyms/Alias
 HAOX2; (S)-2-hydroxy-acid oxidase, peroxisomal; Long chain alpha-hydroxy acid oxidase; Long-chain L-2-hydroxy acid oxidase 
Gene Name
 Hao2 
Gene Synonyms/Alias
 Hao3; Haox2 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
10LVCLADFKAHAQKQLacetylation[1]
19HAQKQLSKTSWDFIEacetylation[1]
57RYLRDMSKVDTRTTIacetylation[1]
139KSDWDFNKQMVQRAEacetylation[1]
182LEANILLKDLRALKEacetylation[1]
188LKDLRALKEEKPTQSacetylation[1]
191LRALKEEKPTQSVPVacetylation[1]
229ILKGILTKEDAELAMacetylation[1]
237EDAELAMKHNVQGIVacetylation[1]
271REVVAAVKGKIEVYMacetylation[1]
273VVAAVKGKIEVYMDGacetylation[1]
290RTGTDVLKALALGARacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids. 
Sequence Annotation
 DOMAIN 2 353 FMN hydroxy acid dehydrogenase.
 NP_BIND 279 303 FMN.
 MOTIF 351 353 Microbody targeting signal (Potential).
 ACT_SITE 248 248 Proton acceptor (By similarity).
 BINDING 106 106 FMN.
 BINDING 128 128 FMN.
 BINDING 130 130 Substrate.
 BINDING 156 156 FMN.
 BINDING 165 165 Substrate.
 BINDING 224 224 FMN.
 BINDING 251 251 Substrate (By similarity).
 BINDING 303 303 FMN.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Flavoprotein; FMN; Oxidoreductase; Peroxisome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 353 AA 
Protein Sequence
MPLVCLADFK AHAQKQLSKT SWDFIEGEAD DGITYSENIA AFKRIRLRPR YLRDMSKVDT 60
RTTIQGQEIS APICISPTAF HSIAWPDGEK STARAAQEAN ICYVISSYAS YSLEDIVAAA 120
PEGFRWFQLY MKSDWDFNKQ MVQRAEALGF KALVITIDTP VLGNRRRDKR NQLNLEANIL 180
LKDLRALKEE KPTQSVPVSF PKASFCWNDL SLLQSITRLP IILKGILTKE DAELAMKHNV 240
QGIVVSNHGG RQLDEVSASI DALREVVAAV KGKIEVYMDG GVRTGTDVLK ALALGARCIF 300
LGRPILWGLA CKGEDGVKEV LDILTAELHR CMTLSGCQSV AEISPDLIQF SRL 353 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005777; C:peroxisome; IDA:HGNC.
 GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IDA:RGD.
 GO:0010181; F:FMN binding; IDA:RGD.
 GO:0052853; F:long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity; IEA:EC.
 GO:0052854; F:medium-chain-(S)-2-hydroxy-acid oxidase activity; IEA:EC.
 GO:0052852; F:very-long-chain-(S)-2-hydroxy-acid oxidase activity; IEA:EC.
 GO:0019395; P:fatty acid oxidation; IEA:Compara.
 GO:0018924; P:mandelate metabolic process; IDA:RGD.
 GO:0051260; P:protein homooligomerization; IDA:RGD. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR012133; Alpha-hydoxy_acid_DH_FMN.
 IPR000262; FMN-dep_DH.
 IPR008259; FMN_hydac_DH_AS. 
Pfam
 PF01070; FMN_dh 
SMART
  
PROSITE
 PS00557; FMN_HYDROXY_ACID_DH_1
 PS51349; FMN_HYDROXY_ACID_DH_2 
PRINTS