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A5UIF3

- BIOB_HAEIG

UniProt

A5UIF3 - BIOB_HAEIG

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Protein

Biotin synthase

Gene

bioB

Organism
Haemophilus influenzae (strain PittGG)
Status
Reviewed - 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 = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.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 bindingi66 – 661Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi70 – 701Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi73 – 731Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi110 – 1101Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi141 – 1411Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi201 – 2011Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi273 – 2731Iron-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

BioCyciHINF374931:GJA4-1525-MONOMER.
UniPathwayiUPA00078; UER00162.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin synthaseUniRule annotation (EC:2.8.1.6UniRule annotation)
Gene namesi
Name:bioBUniRule annotation
Synonyms:thiP
Ordered Locus Names:CGSHiGG_08725
OrganismiHaemophilus influenzae (strain PittGG)
Taxonomic identifieri374931 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000001990: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Biotin synthasePRO_0000381416Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi374931.CGSHiGG_08725.

Structurei

3D structure databases

ProteinModelPortaliA5UIF3.
SMRiA5UIF3. Positions 19-326.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiRIMMPAS.
OrthoDBiEOG622PMP.

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.

A5UIF3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLAEKLQINS ITPHPSVEYW SVCKVEALFE TPFLELVYRA AQIHRKHFNS
60 70 80 90 100
RTIQLSTLMS IKTGGCPEDC GYCPQSARYH TGVQNQQLLD VNEIIAKAKI
110 120 130 140 150
AKARGAGRFC MGAAWRGPKP KDIEKVTEII KAVKSLGLET CGTFGLLQDG
160 170 180 190 200
MAEDLKEAGL DYYNHNLDTA PEHYAEVIGT RRFDDRLSTL GKVRKAGLKV
210 220 230 240 250
CCGGIVGMNE TRKERAGLIA SLANLDPQPE SVPINQLVKV EGTPLADAEE
260 270 280 290 300
LDWTEFVRTI AVARITMPKS YVRLSAGRSG MTEEMQAMCF MAGANSIFYG
310 320 330
DKLLVTDNPE EDGDQLLMAK LDLEPETAEN KK
Length:332
Mass (Da):36,659
Last modified:July 10, 2007 - v1
Checksum:iBC19B240D0399554
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000672 Genomic DNA. Translation: ABR00559.1.
RefSeqiWP_012055354.1. NC_009567.1.
YP_001292942.1. NC_009567.1.

Genome annotation databases

EnsemblBacteriaiABR00559; ABR00559; CGSHiGG_08725.
GeneIDi5227606.
KEGGihiq:CGSHiGG_08725.
PATRICi20187833. VBIHaeInf102487_1763.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000672 Genomic DNA. Translation: ABR00559.1 .
RefSeqi WP_012055354.1. NC_009567.1.
YP_001292942.1. NC_009567.1.

3D structure databases

ProteinModelPortali A5UIF3.
SMRi A5UIF3. Positions 19-326.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 374931.CGSHiGG_08725.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABR00559 ; ABR00559 ; CGSHiGG_08725 .
GeneIDi 5227606.
KEGGi hiq:CGSHiGG_08725.
PATRICi 20187833. VBIHaeInf102487_1763.

Phylogenomic databases

eggNOGi COG0502.
HOGENOMi HOG000239957.
KOi K01012.
OMAi RIMMPAS.
OrthoDBi EOG622PMP.

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci HINF374931:GJA4-1525-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01694. BioB.
InterProi IPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view ]
Pfami PF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF001619. Biotin_synth. 1 hit.
SMARTi SM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00433. bioB. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
    Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
    Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PittGG.

Entry informationi

Entry nameiBIOB_HAEIG
AccessioniPrimary (citable) accession number: A5UIF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 10, 2007
Last modified: November 26, 2014
This is version 53 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