CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004074
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Biotin synthase 
Protein Synonyms/Alias
  
Gene Name
 bioB 
Gene Synonyms/Alias
 b0775; JW0758 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
200VGLGETVKDRAGLLLacetylation[1]
300TPNPEEDKDLQLFRKacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 
Functional Description
 Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical- based mechanism. 
Sequence Annotation
 METAL 53 53 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
 METAL 57 57 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
 METAL 60 60 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
 METAL 97 97 Iron-sulfur 2 (2Fe-2S).
 METAL 128 128 Iron-sulfur 2 (2Fe-2S).
 METAL 188 188 Iron-sulfur 2 (2Fe-2S).
 METAL 260 260 Iron-sulfur 2 (2Fe-2S).  
Keyword
 2Fe-2S; 3D-structure; 4Fe-4S; Biotin biosynthesis; Complete proteome; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; Reference proteome; S-adenosyl-L-methionine; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 346 AA 
Protein Sequence
MAHRPRWTLS QVTELFEKPL LDLLFEAQQV HRQHFDPRQV QVSTLLSIKT GACPEDCKYC 60
PQSSRYKTGL EAERLMEVEQ VLESARKAKA AGSTRFCMGA AWKNPHERDM PYLEQMVQGV 120
KAMGLEACMT LGTLSESQAQ RLANAGLDYY NHNLDTSPEF YGNIITTRTY QERLDTLEKV 180
RDAGIKVCSG GIVGLGETVK DRAGLLLQLA NLPTPPESVP INMLVKVKGT PLADNDDVDA 240
FDFIRTIAVA RIMMPTSYVR LSAGREQMNE QTQAMCFMAG ANSIFYGCKL LTTPNPEEDK 300
DLQLFRKLGL NPQQTAVLAG DNEQQQRLEQ ALMTPDTDEY YNAAAL 346 
Gene Ontology
 GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
 GO:0004076; F:biotin synthase activity; IDA:EcoCyc.
 GO:0005506; F:iron ion binding; IEA:HAMAP.
 GO:0009102; P:biotin biosynthetic process; IMP:EcoCyc. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR010722; Biotin/thiamin_synth-assoc.
 IPR002684; Biotin_synth/BioAB.
 IPR024177; Biotin_synthase.
 IPR006638; Elp3/MiaB/NifB.
 IPR007197; rSAM. 
Pfam
 PF06968; BATS
 PF04055; Radical_SAM 
SMART
 SM00876; BATS
 SM00729; Elp3 
PROSITE
  
PRINTS