(data stored in SCRATCH917 zone)

HOGENOM: YERPD_1_PE1005

ID   YERPD_1_PE1005                       STANDARD;      PRT;   240 AA.
AC   YERPD_1_PE1005; D0JHR0;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATP-dependent dethiobiotin synthetase BioD 1; EC=6.3.3
DE   3;AltName: Full=DTB synthetase 1;AltName: Full=Dethiobiotin synthase 1;
DE   (YERPD_1.PE1005).
GN   Name=bioD; Synonyms=bioD1; OrderedLocusNames=YPD4_1005;
OS   YERSINIA PESTIS D106004.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=637382;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS YERPD_1.PE1005.
CC       Yersinia pestis (strain D106004) chromosome, complete sequence.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:D0JHR0_YERPD
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 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + 7,8-diaminononanoate + CO(2) = ADP +
CC       phosphate + dethiobiotin.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from
CC       7,8-diaminononanoate: step 1/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the dethiobiotin synthetase family.
CC   -!- GENE_FAMILY: HOG000275032 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D0JHR0; -.
DR   EMBL; CP001585; ACY57914.1; -; Genomic_DNA.
DR   ProteinModelPortal; D0JHR0; -.
DR   SMR; D0JHR0; 2-230.
DR   GenomeReviews; CP001585_GR; YPD4_1005.
DR   OMA; PQMERIE; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004141; F:dethiobiotin synthase activity; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00336; BioD; 1; -.
DR   InterPro; IPR004472; BioD_synth.
DR   InterPro; IPR002586; CbiA_P_synth.
DR   Pfam; PF01656; CbiA; 1.
DR   PIRSF; PIRSF006755; DTB_synth; 1.
DR   TIGRFAMs; TIGR00347; BioD; 1.
DR   HOGENOMDNA; YERPD_1.PE1005; -.
KW   ACY57914.100026476820036002503210000011;
KW   Dethiobiotin synthetase 1 ;
KW   ATP-binding; Biotin biosynthesis; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding.
SQ   SEQUENCE   240 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTKRWFITGT DTDVGKTVAS CALLQAATAQ GYRTAGYKPV ASGSQMTADG LRNSDALALQ
     ANSSQRLGYS QVNPFTFLEA TSPHIASESE GRAIPLTALS QGLRQLEPSA DWILIEGAGG
     WFTPLSPQAT FADWVQQEQL PVIMVVGVKL GCINHALLTA QAIQHAGLTL AGWVANEVTP
     AGRRQAEYQA TLTRMITAPL LGIIPYLSDI EENPVTTRRD LGHYLDLTVL RAAEREAVNM
//

If you have problems or comments...

PBIL Back to PBIL home page