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Database: UniProt
Entry: A0A0Q8PSU9_9ACTN
LinkDB: A0A0Q8PSU9_9ACTN
Original site: A0A0Q8PSU9_9ACTN 
ID   A0A0Q8PSU9_9ACTN        Unreviewed;       397 AA.
AC   A0A0Q8PSU9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Hydroxyglutarate oxidase {ECO:0000313|EMBL:KRB75137.1};
GN   ORFNames=ASE01_16600 {ECO:0000313|EMBL:KRB75137.1};
OS   Nocardioides sp. Root190.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB75137.1, ECO:0000313|Proteomes:UP000050886};
RN   [1] {ECO:0000313|EMBL:KRB75137.1, ECO:0000313|Proteomes:UP000050886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root190 {ECO:0000313|EMBL:KRB75137.1,
RC   ECO:0000313|Proteomes:UP000050886};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB75137.1, ECO:0000313|Proteomes:UP000050886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root190 {ECO:0000313|EMBL:KRB75137.1,
RC   ECO:0000313|Proteomes:UP000050886};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the L2HGDH family.
CC       {ECO:0000256|ARBA:ARBA00037941}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRB75137.1}.
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DR   EMBL; LMIA01000011; KRB75137.1; -; Genomic_DNA.
DR   RefSeq; WP_056755736.1; NZ_LMIA01000011.1.
DR   AlphaFoldDB; A0A0Q8PSU9; -.
DR   STRING; 1736488.ASE01_16600; -.
DR   Proteomes; UP000050886; Unassembled WGS sequence.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR43104; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43104:SF2; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050886}.
FT   DOMAIN          7..392
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   397 AA;  42594 MW;  AEA19521DBB2B2F2 CRC64;
     MDQSFGIVGG GIVGLAVARA LLLRRPGARV LVLEKEDRVG AHQTGHNSGV VHAGIYYRPG
     SLKAELCARG RLLLRDYCAE HGLSHLECGK VVVAVDRSEL ERFEALERTA RENAVPGLRR
     LDAAGLREVE PQAAGLAALH SPQTAITDYV AIADQLAGEV VAAGGEVHTS TRATGIEQKA
     GRIRVLTDRT SYDVDRLVLC GGLQADRLGR LAGGAAAPRI VPFRGEYMAV ATGKQELVRG
     MVYPVPDPRY PFLGVHFTRR VDGGLEVGPN AVLALHRDSY RRSAVRPADV ASIASWPGTW
     QMARQHWRTG VREVRGSLST RSYMRSAQRY VPSIGAEDVV RAGFGIRAQA VDRDGSLVDD
     FRIDRDGGVV SVRNAPSPAA TSSLAIAEHV VAQILTA
//
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