(data stored in ACNUC7421 zone)

SWISSPROT: D4YXM4_SPHJU

ID   D4YXM4_SPHJU            Unreviewed;       204 AA.
AC   D4YXM4;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 54.
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   ECO:0000313|EMBL:BAI95106.1};
GN   OrderedLocusNames=SJA_C1-02720 {ECO:0000313|EMBL:BAI95106.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95106.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95106.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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:SAAS00385301}.
CC   -!- CATALYTIC ACTIVITY: ATP + 7,8-diaminononanoate + CO(2) = ADP +
CC       phosphate + dethiobiotin. {ECO:0000256|HAMAP-Rule:MF_00336,
CC       ECO:0000256|SAAS:SAAS00385333}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00336, ECO:0000256|SAAS:SAAS00385353};
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:SAAS00385290}.
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; AP010803; BAI95106.1; -; Genomic_DNA.
DR   RefSeq; WP_013038907.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-02720; -.
DR   EnsemblBacteria; BAI95106; BAI95106; SJA_C1-02720.
DR   GeneID; 29271975; -.
DR   KEGG; sjp:SJA_C1-02720; -.
DR   eggNOG; ENOG4105E78; Bacteria.
DR   eggNOG; COG0132; LUCA.
DR   HOGENOM; HOG000275033; -.
DR   KO; K01935; -.
DR   OMA; DYWKPIQ; -.
DR   OrthoDB; POG091H004W; -.
DR   UniPathway; UPA00078; UER00161.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP.
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; D4YXM4.
DR   SWISS-2DPAGE; D4YXM4.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00089817};
KW   Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00089830};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
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:SAAS00089835, ECO:0000313|EMBL:BAI95106.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00089822};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00462117};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00336,
KW   ECO:0000256|SAAS:SAAS00089833};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   NP_BIND      12     17       ATP. {ECO:0000256|HAMAP-Rule:MF_00336}.
FT   METAL        12     12       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00336}.
FT   METAL        16     16       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00336}.
FT   METAL        43     43       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00336}.
FT   METAL        99     99       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00336}.
FT   BINDING      43     43       ATP. {ECO:0000256|HAMAP-Rule:MF_00336}.
SQ   SEQUENCE   204 AA;  21429 MW;  8BA22E721F3B3636 CRC64;
     MSVFIVTGTD TDIGKTVFAA GLAGALGAYY WKPVQAGVDP EGDKERVASL SGLPASHILP
     EAYRLTTPAS PHLAARIDGV EIALDRLALP QVDGPLVVEG AGGLMVPVSE TLLMIDLFAH
     WGAPVILCAR TGLGTINHSL LSLEALRARA IPVAGIAFIG EPHEENERIV PLLGKVPSLG
     RLPHLDPLDA DTLKTAFKTS IRLP
//

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