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ATP-dependent dethiobiotin synthetase BioD (EC 6.3.3.3) (DTB synthetase) (DTBS) (Dethiobiotin synthase)

 A0A0A8WVA7_9DELT        Unreviewed;       240 AA.
A0A0A8WVA7;
04-MAR-2015, integrated into UniProtKB/TrEMBL.
04-MAR-2015, sequence version 1.
27-SEP-2017, entry version 18.
RecName: Full=ATP-dependent dethiobiotin synthetase BioD {ECO:0000256|HAMAP-Rule:MF_00336};
EC=6.3.3.3 {ECO:0000256|HAMAP-Rule:MF_00336};
AltName: Full=DTB synthetase {ECO:0000256|HAMAP-Rule:MF_00336};
Short=DTBS {ECO:0000256|HAMAP-Rule:MF_00336};
AltName: Full=Dethiobiotin synthase {ECO:0000256|HAMAP-Rule:MF_00336};
Name=bioD {ECO:0000256|HAMAP-Rule:MF_00336,
ECO:0000313|EMBL:GAM09971.1};
ORFNames=OR1_02256 {ECO:0000313|EMBL:GAM09971.1};
Geobacter sp. OR-1.
Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
Geobacteraceae; Geobacter.
NCBI_TaxID=1266765 {ECO:0000313|EMBL:GAM09971.1, ECO:0000313|Proteomes:UP000030972};
[1] {ECO:0000313|EMBL:GAM09971.1, ECO:0000313|Proteomes:UP000030972}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR-1 {ECO:0000313|EMBL:GAM09971.1,
ECO:0000313|Proteomes:UP000030972};
PubMed=23668621; DOI=10.1021/es400231x;
Ohtsuka T., Yamaguchi N., Makino T., Sakurai K., Kimura K., Kudo K.,
Homma E., Dong DT., Amachi S.;
"Arsenic dissolution from Japanese paddy soil by a dissimilatory
arsenate-reducing bacterium Geobacter sp. OR-1.";
Environ. Sci. Technol. 47:6263-6271(2013).
[2] {ECO:0000313|EMBL:GAM09971.1, ECO:0000313|Proteomes:UP000030972}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR-1 {ECO:0000313|EMBL:GAM09971.1,
ECO:0000313|Proteomes:UP000030972};
Ehara A., Suzuki H., Amachi S.;
"Draft Genome Sequence of Geobacter sp. Strain OR-1, an Arsenate-
Respiring Bacterium Isolated from Japanese Paddy Soil.";
Genome Announc. 3:e01478-14(2015).
-!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-
dependent insertion of CO2 between the N7 and N8 nitrogen atoms of
7,8-diaminopelargonic acid (DAPA) to form an ureido ring.
{ECO:0000256|HAMAP-Rule:MF_00336, ECO:0000256|SAAS:SAAS00385301}.
-!- CATALYTIC ACTIVITY: ATP + 7,8-diaminononanoate + CO(2) = ADP +
phosphate + dethiobiotin. {ECO:0000256|HAMAP-Rule:MF_00336,
ECO:0000256|SAAS:SAAS00385333}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00336,
ECO:0000256|SAAS:SAAS00385353};
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from
7,8-diaminononanoate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00336,
ECO:0000256|SAAS:SAAS00385290}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336,
ECO:0000256|SAAS:SAAS00701772}.
-!- SIMILARITY: Belongs to the dethiobiotin synthetase family.
{ECO:0000256|HAMAP-Rule:MF_00336, ECO:0000256|SAAS:SAAS00701766}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00336}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:GAM09971.1}.
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EMBL; BAZF01000009; GAM09971.1; -; Genomic_DNA.
RefSeq; WP_041971915.1; NZ_BAZF01000009.1.
EnsemblBacteria; GAM09971; GAM09971; OR1_02256.
UniPathway; UPA00078; UER00161.
Proteomes; UP000030972; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
HAMAP; MF_00336; BioD; 1.
InterPro; IPR004472; DTB_synth_BioD.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR43210; PTHR43210; 1.
PIRSF; PIRSF006755; DTB_synth; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00347; bioD; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00336,
ECO:0000256|SAAS:SAAS00089817};
Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00336,
ECO:0000256|SAAS:SAAS00089830};
Complete proteome {ECO:0000313|Proteomes:UP000030972};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336,
ECO:0000256|SAAS:SAAS00701761};
Ligase {ECO:0000256|HAMAP-Rule:MF_00336,
ECO:0000256|SAAS:SAAS00089835};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00336,
ECO:0000256|SAAS:SAAS00089822};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00336,
ECO:0000256|SAAS:SAAS00462117};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00336,
ECO:0000256|SAAS:SAAS00089817};
Reference proteome {ECO:0000313|Proteomes:UP000030972}.
NP_BIND 176 177 ATP. {ECO:0000256|HAMAP-Rule:MF_00336}.
METAL 17 17 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00336}.
METAL 55 55 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00336}.
METAL 116 116 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00336}.
BINDING 42 42 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00336}.
BINDING 55 55 ATP. {ECO:0000256|HAMAP-Rule:MF_00336}.
SEQUENCE 240 AA; 25357 MW; 2CF6DBC81D712BFE CRC64;
MAKGVFITGT DTGVGKTVAA AAIARLLKRR GIDVGVMKPV TSGCRDCNGK LVSDDAELLA
WSAGIPDVTW EIAPYLLRNP VAPSEAASQD GVRIDFSVIK DAFNSLASRH EFIIVEGAGG
LMVPLAGGFL IADLITYLDL PALVVSRPNL GTINHTLLTT FSARQMDIQV SGIVINSFPA
EPNDAELSAP HLLGSLASAP ILGVFPKIEE TDLHLVVEQL TDAITDHPLT PFLLKELGIV


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