ID   D3NRV6_AZOS1            Unreviewed;       495 AA.
AC   D3NRV6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=(S)-2-hydroxy-acid oxidase {ECO:0000313|EMBL:BAI71135.1};
DE            EC=1.1.3.15 {ECO:0000313|EMBL:BAI71135.1};
GN   Name=glcD {ECO:0000313|EMBL:BAI71135.1};
GN   OrderedLocusNames=AZL_004970 {ECO:0000313|EMBL:BAI71135.1};
OS   Azospirillum sp. (strain B510).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI71135.1, ECO:0000313|Proteomes:UP000002040};
RN   [1] {ECO:0000313|EMBL:BAI71135.1, ECO:0000313|Proteomes:UP000002040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B510 {ECO:0000313|EMBL:BAI71135.1,
RC   ECO:0000313|Proteomes:UP000002040};
RX   PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA   Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA   Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA   Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA   Nakayama S., Yamada M., Tabata S., Sato S.;
RT   "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT   sp. B510.";
RL   DNA Res. 17:37-50(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; AP010946; BAI71135.1; -; Genomic_DNA.
DR   RefSeq; WP_012973123.1; NC_013854.1.
DR   AlphaFoldDB; D3NRV6; -.
DR   STRING; 137722.AZL_004970; -.
DR   KEGG; azl:AZL_004970; -.
DR   HOGENOM; CLU_017779_9_2_5; -.
DR   OrthoDB; 9815648at2; -.
DR   Proteomes; UP000002040; Chromosome.
DR   GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   PANTHER; PTHR42934:SF1; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:BAI71135.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002040}.
FT   DOMAIN          48..226
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   495 AA;  53077 MW;  A4DFB0FAC7F27C1F CRC64;
     MKMPVPDSGI IARRREIVEA LRAIVPGEGV IVDENELRAY ECDGLTAFRQ LPMVAVLPGT
     VEQVSQVLKT CKAMGVKVVP RGAGTSLSGG ALPLADGVLL GMGKFKRILD IDYANRCVTV
     QPGVTNLGIS NAVAHEGFYY APDPSSQIAC TIGGNIAENS GGVHCLKYGL TTNNVLGLEM
     VLMDGTVIRL GGKHLDAGGY DLMGIVTGSE GLLGVVTEVT VRILKKPATA RAVLLGFPTS
     EQGGDCVAAI IAAGIIPGGM EMMDRPAIHA AEDFVHAGYP LDVEALLIVE LDGPAAEVDH
     LIDRVEAIAR ERGACYARVS TSEEERLAFW AGRKAAFPAV GRISPDYYCM DGTIPRKALP
     LVLRRMQEMS DRCGLRVANV FHAGDGNLHP LILYDANKPG ELEAAEEFGN DILRLCVEVG
     GVLTGEHGVG VEKRDLMTDQ FDEADLRQQQ RLKCAFDPDG LLNPGKVFPT LHRCAELGRL
     HVHQGELRFP DIPRF
//