ID A0A0X1SW19_PSEAA Unreviewed; 464 AA.
AC A0A0X1SW19;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:AMB84126.1};
GN ORFNames=AWM79_01920 {ECO:0000313|EMBL:AMB84126.1};
OS Pseudomonas agarici.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=46677 {ECO:0000313|EMBL:AMB84126.1, ECO:0000313|Proteomes:UP000063229};
RN [1] {ECO:0000313|EMBL:AMB84126.1, ECO:0000313|Proteomes:UP000063229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 2472 {ECO:0000313|EMBL:AMB84126.1,
RC ECO:0000313|Proteomes:UP000063229};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-2016) 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}.
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DR EMBL; CP014135; AMB84126.1; -; Genomic_DNA.
DR RefSeq; WP_060782018.1; NZ_CP014135.1.
DR AlphaFoldDB; A0A0X1SW19; -.
DR STRING; 46677.AWM79_01920; -.
DR Proteomes; UP000063229; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000063229}.
FT DOMAIN 37..216
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 464 AA; 51043 MW; F012B32E82F32BE6 CRC64;
MTNPALIDEL KTLVEPGKVL TDADSLNAYG KDWTKHFAPA PTAIVFPKTI EQVQAIVRWA
NRHGVALVPS GGRTGLSAAA VAAHGEVVVS FDYMNQILDI NLTDRTAVCQ PGVVTEQLQN
QAEEHGLYYP VDFASAGSSQ IGGNIGTNAG GIKVIRYGMT RNWVAGMKVV TGKGDVLELN
KDLIKNATGY DLRQLFIGAE GTLGFVVEAT MRLDRAPKNL TCMVLGTPDF DSIMPVLHAF
HSKLDLTAFE FFSDKALAKV LARGDVPAPF ESDCPFYALL EFEATSEEVA NDALATFEHC
VEQGWVVDGV MSQSEQQLHN LWKLREYISE TISHWTPYKN DISVTVSKVP GFLKEIEAIV
GEHYPDFEIV WFGHIGDGNL HLNILKPENL SKDEFFAKCA TVNKWVFETV EKYNGSISAE
HGVGMTKRDY LTYSRSPAEI EYMKAIKAVF DPNGIMNPGK IFAV
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