(data stored in SCRATCH917 zone)

HOGENOM: YERPD_1_PE1002

ID   YERPD_1_PE1002                       STANDARD;      PRT;   345 AA.
AC   YERPD_1_PE1002; D0JHQ7;
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=Biotin synthase; EC=2.8.1 6; (YERPD_1.PE1002).
GN   Name=bioB; OrderedLocusNames=YPD4_1002;
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.PE1002.
CC       Yersinia pestis (strain D106004) chromosome, complete sequence.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:D0JHQ7_YERPD
CC   -!- FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin
CC       by the insertion of a sulfur atom into dethiobiotin via a radical-
CC       based mechanism (By similarity).
CC   -!- CATALYTIC ACTIVITY: Dethiobiotin + sulfur + 2 S-adenosyl-L-
CC       methionine = biotin + 2 L-methionine + 2 5'-deoxyadenosine.
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster. The cluster is coordinated with
CC       3 cysteines and 1 arginine (By similarity).
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster. The cluster is coordinated with
CC       3 cysteines and an exchangeable S-adenosyl-L-methionine (By
CC       similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from
CC       7,8-diaminononanoate: step 2/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin
CC       synthase family.
CC   -!- GENE_FAMILY: HOG000239957 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D0JHQ7; -.
DR   EMBL; CP001585; ACY57911.1; -; Genomic_DNA.
DR   ProteinModelPortal; D0JHQ7; -.
DR   GenomeReviews; CP001585_GR; YPD4_1002.
DR   OMA; MGMETCM; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004076; F:biotin synthase activity; IEA:HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01694; BioB; 1; -.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR010722; Biotin/thiamin_synth-assoc.
DR   InterPro; IPR002684; Biotin_synth.
DR   InterPro; IPR024177; Biotin_synthase-like.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR007197; rSAM.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF06968; BATS; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF001619; Biotin_synth; 1.
DR   SMART; SM00876; BATS; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00433; BioB; 1.
DR   HOGENOMDNA; YERPD_1.PE1002; -.
KW   ACY57911.100026476820036002503210000011;
KW   Biotin synthase;
KW   2Fe-2S; 4Fe-4S; Biotin biosynthesis; Complete proteome; Iron;
KW   Iron-sulfur; Metal-binding; S-adenosyl-L-methionine; Transferase.
SQ   SEQUENCE   345 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MATYHHWTVG QALALFDKPL LELLFEAQQV HRQHFDPRQV QVSTLLSIKT GACPEDCKYC
     PQSSRYKTGL ESERLMQVEQ VLESAKKAKA AGSTRFCMGA AWKNPHERDM PYLAKMVEGV
     KALGMETCMT LGSLSKQQAH RLADAGLDYY NHNLDTSPEF YGSIITTRSY QERLDTLNEV
     RDAGIKVCSG GIVGLGETVR DRAGLLVQLA NLPKPPESVP INMLVKVKGT PLENNAEVDA
     FEFIRTIAVA RIMMPSSYVR LSAGREQMNE QTQAMCFMAG ANSIFYGCKL LTTPNPDEDK
     DLQLFRKLGL NPQQTATSHG DREQQQALTE QLLHGDTAQF YNAAV
//

If you have problems or comments...

PBIL Back to PBIL home page