ID L2EDK6_9BURK Unreviewed; 483 AA.
AC L2EDK6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:EKZ97420.1};
GN ORFNames=D769_20334 {ECO:0000313|EMBL:EKZ97420.1};
OS Cupriavidus sp. HMR-1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1249621 {ECO:0000313|EMBL:EKZ97420.1, ECO:0000313|Proteomes:UP000010442};
RN [1] {ECO:0000313|EMBL:EKZ97420.1, ECO:0000313|Proteomes:UP000010442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR-1 {ECO:0000313|EMBL:EKZ97420.1,
RC ECO:0000313|Proteomes:UP000010442};
RX PubMed=23409271;
RA Li L.G., Cai L., Zhang T.;
RT "Genome of Cupriavidus sp. HMR-1, a Heavy Metal-Resistant Bacterium.";
RL Genome Announc. 1:E00202-E00212(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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:EKZ97420.1}.
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DR EMBL; ANKP01000193; EKZ97420.1; -; Genomic_DNA.
DR RefSeq; WP_008648851.1; NZ_ANKP01000193.1.
DR AlphaFoldDB; L2EDK6; -.
DR PATRIC; fig|1249621.3.peg.4024; -.
DR Proteomes; UP000010442; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; IPR016167; FAD-bd_PCMH_sub1.
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; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 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 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827}.
FT DOMAIN 41..222
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 483 AA; 51582 MW; 51B96ADBA812EC47 CRC64;
MTALPSQDVL LQAMQAIVGP HGCLTAAADT EPFVTDYRRI YVGKSPVVVM PSTTEQVSQV
MTWCYQHDVP VVPQGGNTSL MGGAVPDDSG TAVVISLRKM HRVLAIDTVN DTMTVEAGVT
LSAARQAAED SKRLFPLRIG SEGSCQIGGN LSTNAGGTAV LRYGNMRDLV LGIEAVLPDG
RVFSSLRGLR KDNTGYDLKH LFIGAEGTLG IITGAVLKLM PQPRSSAVAF VAVQSPEAAV
KLLGEARALS GQAVTAFELI SAPALDLVLE YLGNEPSPLE GRHDWMVLIE LTSGADEESL
NTTLMEILEA GLGQGWVVDA AVASSLTDAQ KFWRIREEIS DAQTRTGGSI KCDISVPVSR
IADFIGKASA GVLALEPATR MVIYGHMGDG NVHFNPLRPK DRPARDFLAQ WYKPVSDLVD
GLAHAENGSI SAEHGIGVAK RDDLTRYKST VELELMWQVK RALDPKNLLN PGRVLPRIAG
PAD
//
