ID Q741Y1_MYCPA Unreviewed; 560 AA.
AC Q741Y1;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=FAD dependent oxidoreductase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=MAP_0956 {ECO:0000313|EMBL:AAS03273.1};
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316 {ECO:0000313|EMBL:AAS03273.1, ECO:0000313|Proteomes:UP000000580};
RN [1] {ECO:0000313|EMBL:AAS03273.1, ECO:0000313|Proteomes:UP000000580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580};
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; AE016958; AAS03273.1; -; Genomic_DNA.
DR RefSeq; WP_010949040.1; NZ_CP106873.1.
DR AlphaFoldDB; Q741Y1; -.
DR STRING; 262316.MAP_0956; -.
DR KEGG; mpa:MAP_0956; -.
DR PATRIC; fig|262316.17.peg.998; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_008878_4_1_11; -.
DR Proteomes; UP000000580; Chromosome.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000580}.
FT DOMAIN 17..295
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 418..547
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 560 AA; 61335 MW; E456C9C6AD34DF72 CRC64;
MIRGARDFTP GMTITTDVAV VGSGPIGIVT ALELAASGVQ VVLIESGAQR PDRAAQQLAE
FDSRHDDYFH SRSGLTVRRQ VGGTSALWGG RCVKFDRIDF EHRLITEQAP WPIGYDDVEP
YLQRACDWAA CGRAVFNARD IPELAHRDLV AGLPDGAVRS TDLERWALPT RFGRHYRKAL
RRTAGLTLWT GLTCTEIVTE PAGGRVDHLV VKTLPGAQGK VVATDYVIAT GGLEATRLLL
ASDRYHPGGL GNTGGHLGRW YMAHVEGRVA RVQFSTDRVI HGYERDGDGV YVRRRFTFDP
GLLREAGMSN AAIWLVNPPI SDPSHGSGIL SGVYLTLISP LGRFLLAAAI REAHTKTDGP
PRILAHLRNI AADLPGSIGF AVAFCYARFV RRGRKAPGFF VRSADNRYLL QYHGEHLPHW
ESRVELSDER DSLGMKRIRT RMHFSDADYA SVRTAIGVID EHLRRHGAGR VEWLTDDVEA
SVRGYMRRRA GFHQAGTTRM SASPKDGVVD PQLQVHGVRG LYVAATSVLP TSSQANPTLL
GIALGVRLAE HLAASRAYPG
//
