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Database: UniProt
Entry: A0A0G3H219_9CORY
LinkDB: A0A0G3H219_9CORY
Original site: A0A0G3H219_9CORY 
ID   A0A0G3H219_9CORY        Unreviewed;       201 AA.
AC   A0A0G3H219;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Dethiobiotin synthetase {ECO:0000313|EMBL:AKK05873.1};
DE            EC=6.3.3.3 {ECO:0000313|EMBL:AKK05873.1};
GN   Name=bioD1 {ECO:0000313|EMBL:AKK05873.1};
GN   ORFNames=CMUST_07735 {ECO:0000313|EMBL:AKK05873.1};
OS   Corynebacterium mustelae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=571915 {ECO:0000313|EMBL:AKK05873.1, ECO:0000313|Proteomes:UP000035199};
RN   [1] {ECO:0000313|EMBL:AKK05873.1, ECO:0000313|Proteomes:UP000035199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45274 {ECO:0000313|EMBL:AKK05873.1,
RC   ECO:0000313|Proteomes:UP000035199};
RX   PubMed=26358597;
RA   Ruckert C., Eimer J., Winkler A., Tauch A.;
RT   "Complete Genome Sequence of the Type Strain Corynebacterium mustelae DSM
RT   45274, Isolated from Various Tissues of a Male Ferret with Lethal Sepsis.";
RL   Genome Announc. 3:e01012-15(2015).
RN   [2] {ECO:0000313|Proteomes:UP000035199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45274 {ECO:0000313|Proteomes:UP000035199};
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete genome sequence of Corynebacterium mustelae DSM 45274, isolated
RT   from various tissues of a male ferret with lethal sepsis.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP011542; AKK05873.1; -; Genomic_DNA.
DR   RefSeq; WP_047262004.1; NZ_CP011542.1.
DR   AlphaFoldDB; A0A0G3H219; -.
DR   STRING; 571915.CMUST_07735; -.
DR   KEGG; cmv:CMUST_07735; -.
DR   PATRIC; fig|571915.4.peg.1651; -.
DR   OrthoDB; 4421237at2; -.
DR   Proteomes; UP000035199; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:InterPro.
DR   CDD; cd03109; DTBS; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR004472; DTB_synth_BioD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43210; DETHIOBIOTIN SYNTHETASE; 1.
DR   PANTHER; PTHR43210:SF5; DETHIOBIOTIN SYNTHETASE; 1.
DR   Pfam; PF13500; AAA_26; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756};
KW   Ligase {ECO:0000313|EMBL:AKK05873.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035199}.
FT   DOMAIN          4..38
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
SQ   SEQUENCE   201 AA;  20797 MW;  4521211E141CC004 CRC64;
     MGIIVVSGLA SGVGKTTAAA AIVRVLQDRG RNVIPVKVAR LQKPHVQMDI GTIKKLTGIS
     GVDFSDDPSP LDRIRDLVKN GRTVVVEGSG GLSVPLRGSA TIAHIANRLD APLVVVSGMD
     PGAVDLAVAA VRFAHSCGAR VEGLLGGKLP AGADLRTRLR LMEVSKATGV PFLGSLNDGV
     GALGEEAFAQ ATRTIFLPEH W
//
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