ID D6V2Y2_9BRAD Unreviewed; 402 AA.
AC D6V2Y2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:EFI52312.1};
GN ORFNames=AfiDRAFT_0298 {ECO:0000313|EMBL:EFI52312.1};
OS Afipia sp. 1NLS2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=666684 {ECO:0000313|EMBL:EFI52312.1, ECO:0000313|Proteomes:UP000004041};
RN [1] {ECO:0000313|EMBL:EFI52312.1, ECO:0000313|Proteomes:UP000004041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLS2 {ECO:0000313|EMBL:EFI52312.1,
RC ECO:0000313|Proteomes:UP000004041};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Prakah O.,
RA Elkins J.G., Brown S.D., Palumbo A.V., Hemme C., Zhou J., Watson D.B.,
RA Jardine P.M., Kostka J.E., Green S.J., Woyke T.J.;
RT "The draft genome of Afipia sp. 1NLS2.";
RL Submitted (MAY-2010) 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:EFI52312.1}.
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DR EMBL; ADVZ01000001; EFI52312.1; -; Genomic_DNA.
DR RefSeq; WP_009337184.1; NZ_ADVZ01000001.1.
DR AlphaFoldDB; D6V2Y2; -.
DR eggNOG; COG0579; Bacteria.
DR Proteomes; UP000004041; 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}.
FT DOMAIN 6..392
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 402 AA; 43619 MW; 7BAA2CDB7C241841 CRC64;
MSYTHCVIGG GIVGLATATE IMRRDSKARV VLVEKENGFA FHQTGHNSGV IHAGIYYAPG
SMKAQLCREG EMATKEFCTA RNIPFETCGK LIVATDAAEM ERMQALIGRA EQNNISIEEI
SATRLRQLEP NITGDGAILV HATGIVDYRQ ICAAMAEELR QNGARVVTGT AVTQIEESER
GVSVMLDSGE RLTADRLIAC AGLQSDRIAR MGGLKPTHRI VPFRGEYFTL PPSRSSIVKH
LIYPVPDPDL QFLGIHLTRM IDGRITIGPN AVLGFHREGY DKGSMNLPDI ISMASFGGFW
KLILQHSRAA LSEFGNSISR RRYLDLCRKY CPGLTLADMG QPGAGIRAQA VMADGSLLQD
FLFLNTSRQV HVCNAPSPAA TSAIPIARKI VDQLDHAIGA SA
//
