ID Q8YB39_BRUME Unreviewed; 344 AA.
AC Q8YB39;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=(S)-2-hydroxy-acid oxidase subunit glce {ECO:0000313|EMBL:AAL54304.1};
DE EC=1.1.3.15 {ECO:0000313|EMBL:AAL54304.1};
GN OrderedLocusNames=BMEII1062 {ECO:0000313|EMBL:AAL54304.1};
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914 {ECO:0000313|EMBL:AAL54304.1, ECO:0000313|Proteomes:UP000000419};
RN [1] {ECO:0000313|EMBL:AAL54304.1, ECO:0000313|Proteomes:UP000000419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094
RC {ECO:0000313|Proteomes:UP000000419};
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.J.,
RA Haselkorn R., Kyrpides N., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; AE008918; AAL54304.1; -; Genomic_DNA.
DR PIR; AE3642; AE3642.
DR AlphaFoldDB; Q8YB39; -.
DR KEGG; bme:BMEII1062; -.
DR eggNOG; COG0277; Bacteria.
DR PhylomeDB; Q8YB39; -.
DR Proteomes; UP000000419; Chromosome II.
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 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 PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 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:AAL54304.1}.
FT DOMAIN 1..119
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 344 AA; 37254 MW; 7F235FC14B2E07CF CRC64;
MLSARAGTPM AEIQKLLADH NQCFHFEPMD YGPLLGAEPG RGTIGGTLAA NLAGPRRLKA
GAARDHVLGV RVVSGRGEVF KSGGRVVKNV TGYDLSKGMA NSWGTLGVAT EVTFKVLPAP
ETVATLAVRG LDDEQAARVM ALAMGSREEV SSAAHLPPTV AWRFLDGKLG GDAATILRLE
GFAPSVAHRS RQLQDLLGRT GTIDVLDDSQ SRQLWREVRD VLPYAQAGDG RAVWRVSMAP
MQGWRMVDEF RRHAGVDAYY DWQGGLIWMR MEAEPEADVL RKLIARHGGG HATLIRAPER
VRGSVDVFQP QPAALAALSA RLKQQFDPEN ILNPGRMYPH QAGA
//
