(data stored in ACNUC7421 zone)

SWISSPROT: B4SIG5_STRM5

ID   B4SIG5_STRM5            Unreviewed;       230 AA.
AC   B4SIG5;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 81.
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=Smal_0465 {ECO:0000313|EMBL:ACF50170.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50170.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50170.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50170.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-
CC       dependent insertion of CO2 between the N7 and N8 nitrogen atoms of
CC       7,8-diaminopelargonic acid (DAPA) to form an ureido ring.
CC       {ECO:0000256|HAMAP-Rule:MF_00336, ECO:0000256|SAAS:SAAS00297567}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7,8-diaminononanoate + ATP + CO2 = ADP + dethiobiotin + 3
CC         H(+) + phosphate; Xref=Rhea:RHEA:15805, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57861, ChEBI:CHEBI:58500, ChEBI:CHEBI:456216;
CC         EC=6.3.3.3; Evidence={ECO:0000256|HAMAP-Rule:MF_00336,
CC         ECO:0000256|SAAS:SAAS01124672};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00336, ECO:0000256|SAAS:SAAS00173485};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from
CC       7,8-diaminononanoate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00336,
CC       ECO:0000256|SAAS:SAAS00089826}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336,
CC       ECO:0000256|SAAS:SAAS00701772}.
CC   -!- SIMILARITY: Belongs to the dethiobiotin synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00336, ECO:0000256|SAAS:SAAS00701766}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00336}.
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DR   EMBL; CP001111; ACF50170.1; -; Genomic_DNA.
DR   RefSeq; WP_012509947.1; NC_011071.1.
DR   STRING; 391008.Smal_0465; -.
DR   EnsemblBacteria; ACF50170; ACF50170; Smal_0465.
DR   KEGG; smt:Smal_0465; -.
DR   eggNOG; ENOG4105E78; Bacteria.
DR   eggNOG; COG0132; LUCA.
DR   HOGENOM; HOG000275032; -.
DR   KO; K01935; -.
DR   OMA; SPHWAAE; -.
DR   OrthoDB; 1739932at2; -.
DR   BioCyc; SMAL391008:SMAL_RS02390-MONOMER; -.
DR   UniPathway; UPA00078; UER00161.
DR   Proteomes; UP000001867; 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   HAMAP; MF_00336; BioD; 1.
DR   InterPro; IPR004472; DTB_synth_BioD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43210; PTHR43210; 1.
DR   PIRSF; PIRSF006755; DTB_synth; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00347; bioD; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4SIG5.
DR   SWISS-2DPAGE; B4SIG5.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00462044};
KW   Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00462056};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00701761};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00462072, ECO:0000313|EMBL:ACF50170.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00462077};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00297566};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00462110}.
FT   NP_BIND     122    125       ATP. {ECO:0000256|HAMAP-Rule:MF_00336}.
FT   NP_BIND     182    183       ATP. {ECO:0000256|HAMAP-Rule:MF_00336}.
FT   NP_BIND     211    213       ATP. {ECO:0000256|HAMAP-Rule:MF_00336}.
FT   METAL        19     19       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00336}.
FT   METAL        23     23       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00336}.
FT   METAL        61     61       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00336}.
FT   METAL       122    122       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00336}.
FT   BINDING      48     48       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00336}.
FT   BINDING      61     61       ATP. {ECO:0000256|HAMAP-Rule:MF_00336}.
SQ   SEQUENCE   230 AA;  24362 MW;  830260502CF1DD23 CRC64;
     MPLPATLPPA LFVTGTDTEI GKTAASTALL HALRRRGLRA VGMKPVASGS EDLGQGLRNE
     DALALQAASW PVPDYADLNP YALRQPLAPE LAAAEDGVQV ELAPIVAAFE RLRAQADIVV
     VEGVGGWLAP VSATLDQLDL VRALHLPVVL VVGMRLGCVN HARLTAQSLQ ASGVECLGWI
     GNHIDPAMQR QEENIATLQQ RLSMPCWGRL PHLPGANGEA LSANLHADLR
//

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