ID A0A0R3MGV0_9BRAD Unreviewed; 412 AA.
AC A0A0R3MGV0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=2-hydroxy-acid oxidase {ECO:0000313|EMBL:KRR19490.1};
GN ORFNames=CQ14_16830 {ECO:0000313|EMBL:KRR19490.1};
OS Bradyrhizobium lablabi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=722472 {ECO:0000313|EMBL:KRR19490.1, ECO:0000313|Proteomes:UP000051660};
RN [1] {ECO:0000313|EMBL:KRR19490.1, ECO:0000313|Proteomes:UP000051660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCBAU 23086 {ECO:0000313|EMBL:KRR19490.1,
RC ECO:0000313|Proteomes:UP000051660};
RA Duran D., Rey L., Navarro A., Busquets A., Imperial J., Ruiz-Argueso T.;
RT "Bradyrhizobium valentinum sp. nov., isolated from effective nodules of
RT Lupinus mariae-josephae, a lupine endemic of basic-lime soils in Eastern
RT Spain.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KRR19490.1}.
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DR EMBL; LLYB01000094; KRR19490.1; -; Genomic_DNA.
DR RefSeq; WP_057860908.1; NZ_LLYB01000094.1.
DR AlphaFoldDB; A0A0R3MGV0; -.
DR STRING; 722472.SAMN05444321_3380; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000051660; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
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; 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;
FT DOMAIN 1..181
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 412 AA; 42750 MW; 1BFED447943F6F07 CRC64;
MDTLKVRDAK DVEEVVRAAI ASEQPLEIIG HGTRRAIGHP MPTNAVLDVS ALNAVTSYEP
NELIITVQAG APLADVQSLI DSKSQQFAFE PMDTSSLLGA SGNGTIGGMI GAGLAGPRRI
RAGGARDHLL GAHAVSGFGD SFKTGGRVVK NVTGYDLCKL LTGSWGTLAV MTEVTLKVMP
KPETERTLVL SGLDDVAANR AMTAALGSPY DVSGAAHLPY QAFRPATGSL AGLAAQGRAV
TLLRLEGIAA SVADRATSLA KTLAPFGSVD TLQDAASASA WSAIRDVEPF AAGGALGAWP
VWRIVCPPAS GGVLGQALAR ESGGDMIYDW GGGLIWAALP PKPDAQAALV RQRVEAAGGH
AALIRASEQV RRHVDVFHPQ ASGLAALSER VRHSFDPRII LNRGRMLRGS AT
//