ID A0A0A0ELU5_9GAMM Unreviewed; 469 AA.
AC A0A0A0ELU5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KGM51966.1};
GN ORFNames=N792_06360 {ECO:0000313|EMBL:KGM51966.1};
OS Lysobacter concretionis Ko07 = DSM 16239.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1122185 {ECO:0000313|EMBL:KGM51966.1, ECO:0000313|Proteomes:UP000030017};
RN [1] {ECO:0000313|EMBL:KGM51966.1, ECO:0000313|Proteomes:UP000030017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ko07 {ECO:0000313|EMBL:KGM51966.1,
RC ECO:0000313|Proteomes:UP000030017};
RA Zhang S., Wang G.;
RT "Genome sequencing of Lysobacter.";
RL Submitted (AUG-2013) 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 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:KGM51966.1}.
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DR EMBL; AVPS01000004; KGM51966.1; -; Genomic_DNA.
DR RefSeq; WP_036193125.1; NZ_AVPS01000004.1.
DR AlphaFoldDB; A0A0A0ELU5; -.
DR STRING; 1122185.N792_06360; -.
DR eggNOG; COG0277; Bacteria.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000030017; 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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000030017}.
FT DOMAIN 36..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 469 AA; 50488 MW; 9E450A4B2A5A09CF CRC64;
MNDPRLSALL ATVPGLRLKT GPADLEYYGR DWTRRWVPAP LAIALPADAG EVQAIVRWAN
RHRVAIAPSG GRTGLSGGAV AANGELVLSL ERMNRVLAFD PIDRSLTVQP GIVLEAVHQA
ARGHGLLYPV DFAARGSCSI GGNIATNAGG IRVIRYGNTR EWVAGLKVVT GAGELLDLNR
GLVKNASGYD LRHLFIGSEG TLGIVVEATL RLTDPPPPSN VMLLALPSFE VLMQVFAVFR
ERLQLEAFEF FTDHALRHVL AHGGQAPFGE SHPYYVVAEF AAGDDARQAA ALAAFEHCLE
NGLVSDGVIS QSDAQAAQLW RLREGITESL ARHRPYKNDV SVRISAMPAF LAEAQSLLAR
EYPHFEVVWF GHIGDGNLHI NVLKPDDVDE AGFVSQCAHV TDLLAATLQR HGGSISAEHG
IGLVKKPWLD SARSAAEIEV MRGIRHVLDP LGIMNPGKLF DPPVPPGHA
//
