(data stored in SCRATCH zone)

HOGENOM: SYNS3_1_PE1005

ID   SYNS3_1_PE1005                       STANDARD;      PRT;   322 AA.
AC   SYNS3_1_PE1005; Q0IBC8;
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; (SYNS3_1.PE1005).
GN   Name=bioB; OrderedLocusNames=sync_1032;
OS   SYNECHOCOCCUS SP. CC9311.
OC   Bacteria; Cyanobacteria; Chroococcales; Synechococcus.
OX   NCBI_TaxID=64471;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SYNS3_1.PE1005.
CC       Synechococcus sp. CC9311, complete genome.
CC       1..88329 annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:BIOB_SYNS3
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 4Fe-4S cluster. The cluster is coordinated with
CC       3 cysteines and an exchangeable S-adenosyl-L-methionine (By
CC       similarity).
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster. The cluster is coordinated with
CC       3 cysteines and 1 arginine (By 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   -!- SEQUENCE CAUTION:
CC       Sequence=ABI46705.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000239957 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q0IBC8; -.
DR   EMBL; CP000435; ABI46705.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_730244.1; NC_008319.1.
DR   STRING; Q0IBC8; -.
DR   GeneID; 4259028; -.
DR   GenomeReviews; CP000435_GR; sync_1032.
DR   KEGG; syg:sync_1032; -.
DR   TIGR; sync_1032; -.
DR   eggNOG; COG0502; -.
DR   ProtClustDB; CLSK2316849; -.
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:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-KW.
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; SYNS3_1.PE1005; -.
KW   2Fe-2S; 4Fe-4S; Biotin biosynthesis; Complete proteome; Iron;
KW   Iron-sulfur; Metal-binding; S-adenosyl-L-methionine; Transferase.
SQ   SEQUENCE   322 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRHDWTRSEI EALLDLPLMD LLWRAQGVHR ASNPGYHVQL ASLLSVKTGG CEEDCAYCPQ
     SMHHSSDVTG QPELQVAPVL ERAKAAKQAG ADRFCMGWAW REIRDGAPFE AMLQMVSGVR
     ALGMEACVTA GMLTDGQAQR LAKAGLTAYN HNLDTSPEHY DKIITTRTFQ ERLETLERVR
     QAGVTLCCGG IIGMGETIGD RASMLQVLAS INPHPESVPI NALVAVEGTP LEELPPIDPI
     ELVRMIAVTR ILMPGSRVRL SAGREQLSKE AQILCLQAGA DSIFYGETLL TTGNPAVEAD
     RELLRTAGVQ ANWLSASEKL AA
//

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