ID A1TDI9_MYCVP Unreviewed; 453 AA.
AC A1TDI9;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ABM15239.1};
GN OrderedLocusNames=Mvan_4464 {ECO:0000313|EMBL:ABM15239.1};
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM15239.1, ECO:0000313|Proteomes:UP000009159};
RN [1] {ECO:0000313|EMBL:ABM15239.1, ECO:0000313|Proteomes:UP000009159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000511; ABM15239.1; -; Genomic_DNA.
DR RefSeq; WP_011781617.1; NZ_JACKSD010000141.1.
DR AlphaFoldDB; A1TDI9; -.
DR STRING; 350058.Mvan_4464; -.
DR KEGG; mva:Mvan_4464; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_1_11; -.
DR Proteomes; UP000009159; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 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; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009159}.
FT DOMAIN 35..213
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 453 AA; 47139 MW; F6D3E5F31C4AA339 CRC64;
MQPLASLIAE LPDGTVVTDP DIVASYRQDR AADPSAGTPI AVVRPRRTEE VQATLRWATA
HRIAVVPRGM GTGLSGGATA LDGGIVLSTE KMRDITVDPV TRTAVAQPGL LNAEVKKAVA
EYGLWYPPDP SSFEICSIGG NIATNAGGLC CVKYGVTTDY VLGLQVVLAD GTAVRLGGPR
LKDVAGLSLT KLFVGSEGTL GVVTEVTLKL LPAQSGACTV VATFDSVEDA ANAVVTITGK
IRPSMLEFMD SAAINAVEDK LKMGLDRSAA AMMVAASDDR GPSGAQDAEF MAGVFTEHGA
REVFSTSDPD EGEAFVAARR FAIPAVEARG ALLLEDVGVP LPALAELVGG VEKIAGHHEL
MISVIAHAGD GNTHPLIVFD PDDPDMERRA QQAFGEIMDL AIGLGGTITG EHGVGRLKRP
WLAGQLGPEA MELNRRIKQA LDPDGILNPG AAI
//
