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Protein

Biotin synthase

Gene

bioB

Organism
Methanococcus maripaludis (strain C6 / ATCC BAA-1332)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi67 – 671Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi71 – 711Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi74 – 741Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi110 – 1101Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi142 – 1421Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi201 – 2011Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi277 – 2771Iron-sulfur 2 (2Fe-2S)UniRule annotation

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. biotin synthase activity Source: UniProtKB-HAMAP
  4. iron ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. biotin biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Biotin biosynthesis

Keywords - Ligandi

2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMMAR444158:GHN2-1481-MONOMER.
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:MmarC6_1435
OrganismiMethanococcus maripaludis (strain C6 / ATCC BAA-1332)
Taxonomic identifieri444158 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
ProteomesiUP000000791 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327Biotin synthasePRO_0000381464Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi444158.MmarC6_1435.

Structurei

3D structure databases

ProteinModelPortaliA9AA75.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiCAQSSHH.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB.
InterProiIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view]
PfamiPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF001619. Biotin_synth. 1 hit.
SMARTiSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00433. bioB. 1 hit.

Sequencei

Sequence statusi: Complete.

A9AA75-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIKLNPDS LEIYEKSDSG KLNRNDLIDL WNLDLNDLLN ISCALKKLFN
60 70 80 90 100
KDKIDLCSIM NAKSGICPEN CIFCSQSKHN TSKIDTYELK SKEEILKNAK
110 120 130 140 150
SVEKYSNRFS IVVSGKTVTD LEFEKIIESI EEIQNKTKLK VCVSLGLLNK
160 170 180 190 200
DKLKALKEKN VRIHNNLETS ENYFKNICTS HDYNDKVKVI LEAKKIGLEM
210 220 230 240 250
CSGGIFGMGE SIEDRVDLFL DLKKLGVDSV ALNLLNPIYG TKIYEKIKFG
260 270 280 290 300
VISPINSIDA LKSICIARIA LPDKVIRLCG GREHVLKDMQ KYSLFALDGL
310 320
MIGNYLTTNG QNIQSDLKMI KEMGFER
Length:327
Mass (Da):37,032
Last modified:January 15, 2008 - v1
Checksum:i7127DE8003048ECA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000867 Genomic DNA. Translation: ABX02248.1.
RefSeqiYP_001549480.1. NC_009975.1.

Genome annotation databases

EnsemblBacteriaiABX02248; ABX02248; MmarC6_1435.
GeneIDi5737476.
KEGGimmx:MmarC6_1435.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000867 Genomic DNA. Translation: ABX02248.1.
RefSeqiYP_001549480.1. NC_009975.1.

3D structure databases

ProteinModelPortaliA9AA75.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi444158.MmarC6_1435.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX02248; ABX02248; MmarC6_1435.
GeneIDi5737476.
KEGGimmx:MmarC6_1435.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiCAQSSHH.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciMMAR444158:GHN2-1481-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB.
InterProiIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view]
PfamiPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF001619. Biotin_synth. 1 hit.
SMARTiSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00433. bioB. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C6 / ATCC BAA-1332.

Entry informationi

Entry nameiBIOB_METM6
AccessioniPrimary (citable) accession number: A9AA75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: January 15, 2008
Last modified: March 4, 2015
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.