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Database: UniProt
Entry: Q6NKI8_CORDI
LinkDB: Q6NKI8_CORDI
Original site: Q6NKI8_CORDI 
ID   Q6NKI8_CORDI            Unreviewed;       362 AA.
AC   Q6NKI8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=Thiamine biosynthesis oxidoreductase {ECO:0000313|EMBL:CAE48542.1};
GN   Name=thiO {ECO:0000313|EMBL:CAE48542.1};
GN   OrderedLocusNames=DIP0031 {ECO:0000313|EMBL:CAE48542.1};
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=257309 {ECO:0000313|EMBL:CAE48542.1, ECO:0000313|Proteomes:UP000002198};
RN   [1] {ECO:0000313|EMBL:CAE48542.1, ECO:0000313|Proteomes:UP000002198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis
RC   {ECO:0000313|Proteomes:UP000002198};
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.,
RA   Bentley S.D., Besra G.S., Churcher C., James K.D., De Zoysa A.,
RA   Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S.,
RA   Jagels K., Moule S., Quail M.A., Rabbinowitsch E., Rutherford K.,
RA   Thomson N.R., Unwin L., Whitehead S., Barrell B.G.Parkhill.J.;
RT   "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT   NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(2003).
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
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DR   EMBL; BX248354; CAE48542.1; -; Genomic_DNA.
DR   RefSeq; WP_010933963.1; NC_002935.2.
DR   AlphaFoldDB; Q6NKI8; -.
DR   STRING; 257309.DIP0031; -.
DR   KEGG; cdi:DIP0031; -.
DR   HOGENOM; CLU_007884_4_5_11; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000002198; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012727; Gly_oxidase_ThiO.
DR   NCBIfam; TIGR02352; thiamin_ThiO; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR13847:SF293; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN MNMC; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002198}.
FT   DOMAIN          2..331
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   362 AA;  38789 MW;  1F207B4628C559D1 CRC64;
     MKIAVVGGGI VGLSTAFELS SRGHSVHVFD PNPASGASHF AGGMLAPAAE VQFQQDPLFP
     LMKRAGKLWP DMVRRVAQRT NLPTGYRTEG TLVVAADRAD AEHLKQLRAT QEAAGMDVRP
     ITTRQARGLE PALGPRLSAA VHIPNDTQVA PRVFLTALLD ALDDCGVGVI KEKITDLEPL
     YQQFDVVVLA AGLGAQHLSP IPLALRPVRG DILRVQTEPG AVNMVVRGWV NDRPIYIIPR
     ANGEIAIGAT SREDERDLPS VEGIYDLLRD AIRVVPGIVD SSLIEANVGV RPGTPDDLPY
     LGWASDRLII STGYFRHGIL LSALGAHVTA CLIDGTDPGI DLTACAPDRH HNERGTTHGH
     LH
//
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