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Database: UniProt
Entry: A7MJ00_CROS8
LinkDB: A7MJ00_CROS8
Original site: A7MJ00_CROS8 
ID   A7MJ00_CROS8            Unreviewed;       227 AA.
AC   A7MJ00;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   24-JAN-2024, entry version 103.
DE   RecName: Full=ATP-dependent dethiobiotin synthetase BioD {ECO:0000256|HAMAP-Rule:MF_00336};
DE            EC=6.3.3.3 {ECO:0000256|HAMAP-Rule:MF_00336};
DE   AltName: Full=DTB synthetase {ECO:0000256|HAMAP-Rule:MF_00336};
DE            Short=DTBS {ECO:0000256|HAMAP-Rule:MF_00336};
DE   AltName: Full=Dethiobiotin synthase {ECO:0000256|HAMAP-Rule:MF_00336};
GN   Name=bioD {ECO:0000256|HAMAP-Rule:MF_00336};
GN   OrderedLocusNames=ESA_02569 {ECO:0000313|EMBL:ABU77814.1};
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339 {ECO:0000313|EMBL:ABU77814.1, ECO:0000313|Proteomes:UP000000260};
RN   [1] {ECO:0000313|EMBL:ABU77814.1, ECO:0000313|Proteomes:UP000000260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894 {ECO:0000313|EMBL:ABU77814.1,
RC   ECO:0000313|Proteomes:UP000000260};
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
CC   -!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-
CC       dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-
CC       diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to
CC       form a ureido ring. {ECO:0000256|HAMAP-Rule:MF_00336}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-
CC         dethiobiotin + ADP + 3 H(+) + phosphate; Xref=Rhea:RHEA:15805,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:149469, ChEBI:CHEBI:149473,
CC         ChEBI:CHEBI:456216; EC=6.3.3.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00336};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00336};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC       diaminononanoate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00336}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00336}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336}.
CC   -!- SIMILARITY: Belongs to the dethiobiotin synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00336}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00336}.
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DR   EMBL; CP000783; ABU77814.1; -; Genomic_DNA.
DR   RefSeq; WP_012125304.1; NC_009778.1.
DR   AlphaFoldDB; A7MJ00; -.
DR   KEGG; esa:ESA_02569; -.
DR   PATRIC; fig|290339.8.peg.2290; -.
DR   HOGENOM; CLU_072551_0_0_6; -.
DR   OMA; SPHWAAE; -.
DR   UniPathway; UPA00078; UER00161.
DR   Proteomes; UP000000260; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03109; DTBS; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00336; BioD; 1.
DR   InterPro; IPR004472; DTB_synth_BioD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00347; bioD; 1.
DR   PANTHER; PTHR43210:SF5; ATP-DEPENDENT DETHIOBIOTIN SYNTHETASE BIOD 1; 1.
DR   PANTHER; PTHR43210; DETHIOBIOTIN SYNTHETASE; 1.
DR   Pfam; PF13500; AAA_26; 1.
DR   PIRSF; PIRSF006755; DTB_synth; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00336};
KW   Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756, ECO:0000256|HAMAP-
KW   Rule:MF_00336}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00336};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00336};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00336};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00336};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000260}.
FT   ACT_SITE        38
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         13..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         55
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         116..119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         176..177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT   BINDING         205..207
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
SQ   SEQUENCE   227 AA;  24403 MW;  49B687EC47D6C083 CRC64;
     MTERWFITGT DTEVGKTIAS CALLEAAKAA GFSTAGYKPV ASGSDITPQG LRNSDALALQ
     RHSSVALRYE QVNPLTFEEP TSPHIVSQEQ GLPIDFTVMS AGLRALEPLA DWVQVEGAGG
     WFTPLSDDAT FADWVKQERL PVILVVGVKL GCINHALLTA QAVQAAGLRL AGWVANDVQP
     PGRRHQEYLA TLEQLLPAPM LGEIPWLGAE PDVTPAAQWI DLSKLAR
//
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