ID R7XTD1_9ACTN Unreviewed; 468 AA.
AC R7XTD1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=FAD linked oxidase domain-containing protein {ECO:0000313|EMBL:EON22612.1};
GN ORFNames=CF8_3467 {ECO:0000313|EMBL:EON22612.1};
OS Nocardioides sp. CF8.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=110319 {ECO:0000313|EMBL:EON22612.1, ECO:0000313|Proteomes:UP000015971};
RN [1] {ECO:0000313|EMBL:EON22612.1, ECO:0000313|Proteomes:UP000015971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF8 {ECO:0000313|EMBL:EON22612.1,
RC ECO:0000313|Proteomes:UP000015971};
RX PubMed=23833136;
RA Kimbrel J.A., Chang J., Arp D.J., Sayavedra-Soto L.A.;
RT "The Draft Genome Sequence of Nocardioides sp. Strain CF8 Reveals the Scope
RT of Its Metabolic Capabilities.";
RL Genome Announc. 1:e00439-e00439(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:EON22612.1}.
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DR EMBL; ASEP01000101; EON22612.1; -; Genomic_DNA.
DR RefSeq; WP_010834280.1; NZ_CM001852.1.
DR AlphaFoldDB; R7XTD1; -.
DR STRING; 110319.CF8_3467; -.
DR PATRIC; fig|110319.3.peg.52; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_4_1_11; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000015971; 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 Reference proteome {ECO:0000313|Proteomes:UP000015971}.
FT DOMAIN 35..216
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 468 AA; 47825 MW; 90F06D427D1EEEFA CRC64;
MTHLLSDLRA AIGDAHVLTD PADLSPYAAD WRGAYRGTPL AVVRPASTSE VAEVVRLAHA
AGVAIVPQGG NTGMCGGAIP SGDGSQLVLS LGRLRQVREV DAAGGTITVE AGVILADVQA
AAQAVDRLFP LSLGAEGSCT VGGNIATNAG GTAVLRYGMM RSLVLGLEVV LPDGRVWDGL
RSLRKDNTGY DLTQLFIGAE GTLGIVTAAV LTLHPATPAR ATAWVALPSV AAAATLLPLL
REYAAERLTT WELVSRPALE LVLAAGLADP LASDAEWFGL IEIAGPAGAS VDDDLERALA
AAVEAGLVLD AAVAGSPAQR SGLWALRERV SEAQESLGPT IKHDVSVPIT SLDDLVARLG
PALESALPGI RPIVYGHVGD GNLHYNLSRP ASLSGDHFVA QAAMLSTIVH DCTVELGGSI
SAEHGLGSGK AAAAAAYKSD VEVDLMRAVK NALDPAGLMN PGKVLAPD
//
