ID K0NHF1_DESTT Unreviewed; 477 AA.
AC K0NHF1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=GlcD: (S)-2-hydroxy-acid oxidase (Glycolate oxidase), delta subunit {ECO:0000313|EMBL:CCK79298.1};
DE EC=1.1.3.15 {ECO:0000313|EMBL:CCK79298.1};
GN Name=glcD {ECO:0000313|EMBL:CCK79298.1};
GN OrderedLocusNames=TOL2_C11340 {ECO:0000313|EMBL:CCK79298.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK79298.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK79298.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FO203503; CCK79298.1; -; Genomic_DNA.
DR RefSeq; WP_014956645.1; NC_018645.1.
DR AlphaFoldDB; K0NHF1; -.
DR STRING; 651182.TOL2_C11340; -.
DR KEGG; dto:TOL2_C11340; -.
DR HOGENOM; CLU_017779_9_2_7; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000007347; 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:SF2; 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:CCK79298.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347}.
FT DOMAIN 35..214
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 477 AA; 51775 MW; FEA47AAAA1ACC3F0 CRC64;
MKKIDEARLK NIVGERNIKT DPCDLYVYGS DSSVHHALPW AVVRPQTTAQ VQEIMRYANE
NIIPVIARGG GSGMCGQTVP IQGGIVLDMK GMNKILEINP QDVYCRVQPG VVDDDLNLAL
KPYGVFYPPT PASSRIATIG GEIANNASGV RSVKYGATRD AVLGMKVVMA NGELVTLGSH
TRVEASGYQI HKLMVGSEGT LGIVVEATLS FVPLPEFRCM GVANFDSLKD AGEAIGSIMA
SGAIPSMLEL VDSVAIKAVN KTMNLGLKEV AAALIFEADG MVKEAVDYEI NNMRTICERH
NGQDIYSSYD PKEREKIFLG RKKLFPALSK YDDNLASTAL ADDMAVPYSK MAQMAEKIHE
IADKNNIIMT AYGHCGSGCM HTKILMDTKR KDQWASAKKA ISEVYDYVRS VNGTTSAEHG
IGLSKAQAFK LEKSDSLTLL ACIKKALDPN NILNPGKLMQ APENWVTATN LRYSVNC
//
