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Protein

Biotin synthase

Gene

bioB

Organism
Chlamydia pneumoniae (Chlamydophila pneumoniae)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.UniRule annotation

Catalytic activityi

Dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation
  • [2Fe-2S] clusterUniRule annotationNote: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.UniRule annotation

Pathwayi: biotin biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes biotin from 7,8-diaminononanoate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. ATP-dependent dethiobiotin synthetase BioD (bioD)
  2. Biotin synthase (bioB), Biotin synthase (bioB), Biotin synthase (bioB)
This subpathway is part of the pathway biotin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes biotin from 7,8-diaminononanoate, the pathway biotin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi54Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi58Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi61Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi98Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi130Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi190Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi262Iron-sulfur 2 (2Fe-2S)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processBiotin biosynthesis
Ligand2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin synthaseUniRule annotation (EC:2.8.1.6UniRule annotation)
Gene namesi
Name:bioBUniRule annotation
Ordered Locus Names:CPn_1044, CP_0808, CpB1084
OrganismiChlamydia pneumoniae (Chlamydophila pneumoniae)
Taxonomic identifieri83558 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
Proteomesi
  • UP000000583 Componenti: Chromosome
  • UP000000801 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003813031 – 331Biotin synthaseAdd BLAST331

Proteomic databases

PRIDEiQ9Z6L5

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi182082.CpB1084

Structurei

3D structure databases

ProteinModelPortaliQ9Z6L5
SMRiQ9Z6L5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Biotin synthase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107QSQ Bacteria
COG0502 LUCA
HOGENOMiHOG000239957
KOiK01012
OMAiADRFCMG
OrthoDBiPOG091H01DF

Family and domain databases

Gene3Di3.20.20.70, 1 hit
HAMAPiMF_01694 BioB, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR010722 BATS_dom
IPR034416 BATS_domain_containing
IPR002684 Biotin_synth/BioAB
IPR024177 Biotin_synthase
IPR006638 Elp3/MiaB/NifB
IPR007197 rSAM
PANTHERiPTHR22976 PTHR22976, 1 hit
PfamiView protein in Pfam
PF06968 BATS, 1 hit
PF04055 Radical_SAM, 1 hit
PIRSFiPIRSF001619 Biotin_synth, 1 hit
SFLDiSFLDF00272 biotin_synthase, 1 hit
SFLDG01060 BATS_domain_containing, 1 hit
SFLDG01278 biotin_synthase_like, 1 hit
SFLDS00029 Radical_SAM, 1 hit
SMARTiView protein in SMART
SM00876 BATS, 1 hit
SM00729 Elp3, 1 hit
TIGRFAMsiTIGR00433 bioB, 1 hit

Sequencei

Sequence statusi: Complete.

Q9Z6L5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREETVSWSL EDIREIYHTP VFELIHKANA ILRSNFLHSE LQTCYLISIK
60 70 80 90 100
TGGCVEDCAY CAQSSRYHTH VTPEPMMKIV DVVERAKRAV ELGATRVCLG
110 120 130 140 150
AAWRNAKDDR YFDRVLAMVK SITDLGAEVC CALGMLSEEQ AKKLYDAGLY
160 170 180 190 200
AYNHNLDSSP EFYETIITTR SYEDRLNTLD VVNKSGISTC CGGIVGMGES
210 220 230 240 250
EEDRIKLLHV LATRDHIPES VPVNLLWPID GTPLQDQPPI SFWEVLRTIA
260 270 280 290 300
TARVVFPRSM VRLAAGRAFL TVEQQTLCFL AGANSIFYGD KLLTVENNDI
310 320 330
DEDAEMIKLL GLIPRPSFGI ERGNPCYANN S
Length:331
Mass (Da):37,075
Last modified:May 1, 1999 - v1
Checksum:i7ADA2C0E732C1370
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001363 Genomic DNA Translation: AAD19181.1
AE002161 Genomic DNA Translation: AAF38605.1
AE009440 Genomic DNA Translation: AAP99013.1
BA000008 Genomic DNA Translation: BAA99251.1
PIRiA86621
H72004
RefSeqiNP_225238.1, NC_000922.1
WP_010883677.1, NZ_LN847257.1

Genome annotation databases

EnsemblBacteriaiAAD19181; AAD19181; CPn_1044
AAF38605; AAF38605; CP_0808
AAP99013; AAP99013; CpB1084
BAA99251; BAA99251; BAA99251
GeneIDi895651
KEGGicpa:CP_0808
cpj:bioB
cpn:CPn1044
cpt:CpB1084
PATRICifig|115713.3.peg.1143

Similar proteinsi

Entry informationi

Entry nameiBIOB_CHLPN
AccessioniPrimary (citable) accession number: Q9Z6L5
Secondary accession number(s): Q7AHW6, Q7BWK9, Q7DE82
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 1, 1999
Last modified: March 28, 2018
This is version 124 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health