ID V5X8T7_MYCNE Unreviewed; 459 AA.
AC V5X8T7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:AHC23829.1};
GN ORFNames=D174_04120 {ECO:0000313|EMBL:AHC23829.1};
OS Mycolicibacterium neoaurum VKM Ac-1815D.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=700508 {ECO:0000313|EMBL:AHC23829.1, ECO:0000313|Proteomes:UP000018763};
RN [1] {ECO:0000313|EMBL:AHC23829.1, ECO:0000313|Proteomes:UP000018763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-1815D {ECO:0000313|EMBL:AHC23829.1,
RC ECO:0000313|Proteomes:UP000018763};
RX PubMed=24435872;
RA Shtratnikova V.Y., Bragin E.Y., Dovbnya D.V., Pekov Y.A., Schelkunov M.I.,
RA Strizhov N., Ivashina T.V., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Sterol-Transforming Mycobacterium neoaurum
RT Strain VKM Ac-1815D.";
RL Genome Announc. 2:e01177-13(2014).
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; CP006936; AHC23829.1; -; Genomic_DNA.
DR RefSeq; WP_019513419.1; NC_023036.2.
DR AlphaFoldDB; V5X8T7; -.
DR KEGG; mne:D174_04120; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_4_1_11; -.
DR Proteomes; UP000018763; 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:UP000018763}.
FT DOMAIN 41..220
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 459 AA; 48641 MW; 05E8A0A311EC02DA CRC64;
MSERGAAAEI VGELIHIVGR GHVLTDPETI ASYRTDWTGR FQGRTDVVVR PANTAEVAAV
LGVCHAHGVP VVPQGGNTGL VGGSVPMHGE LVLSTRRLDE IEHVDPVGRT LAAGAGVTVA
RAQQAARQHG LDLGVDLASR DSATLGGIVA TNAGGVRVIK NGGTRAQLLG IEAVRSDGCV
VTRWKELSKD NIGYDLPGLL AGSEGTLAVI TRVLMRLVVP VQQTVVALVA LPSVDAALVL
LDRVQRHGLR LEAAEFMTAA GVDLVCRHTG LRAPFGDDAP IYLLLEVAGA GEAENALSGL
FTEDADAVLD ATLEAGPART LWQYRERHTE SISAESRTPA VKLDVSVPLR VLTDFFTTLD
SRLRAEHPDV RAICFGHIAD GNVHVNMLDV PVEKQHAITD FVLRLVADHQ GSISAEHGIG
HAKAAWIELG RSANDIDTMK RIRAAFDPAG ILNPHVLPR
//
