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Q2Y9Y9

- BIOB_NITMU

UniProt

Q2Y9Y9 - BIOB_NITMU

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Protein

Biotin synthase

Gene

bioB

Organism
Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849)
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 bindingi82 – 821Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi86 – 861Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi89 – 891Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi126 – 1261Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi157 – 1571Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi217 – 2171Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi289 – 2891Iron-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

BioCyciNMUL323848:GKEC-1153-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:Nmul_A1129
OrganismiNitrosospira multiformis (strain ATCC 25196 / NCIMB 11849)
Taxonomic identifieri323848 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosospira
ProteomesiUP000002718: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 342342Biotin synthasePRO_0000381504Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi323848.Nmul_A1129.

Structurei

3D structure databases

ProteinModelPortaliQ2Y9Y9.
SMRiQ2Y9Y9. Positions 35-340.
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.

Q2Y9Y9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQSASGIVN IETSSGGAVD SFADKLSGIS ADFRRWDVRR VEALLDLPFS
60 70 80 90 100
DLIHRAQLVH RQYHDPNGVQ LSTLISVKTG GCPEDCGYCP QAARYHTNVE
110 120 130 140 150
NQDMLTVEDV IAAAAAAKAQ GATRFCMGAA WRGPKERDMK SVVEMVRAVK
160 170 180 190 200
ALGLEACTTL GMLKPGQAEQ LQEAGLDYYN HNLDTSPEFY GEIITTRDYE
210 220 230 240 250
DRLDTLQKVR HAGINVCCGG IVGMGESRRA RAGLIAQLAN LDPYPESVPI
260 270 280 290 300
NHLVQVEGTP LHGTEALDPL EFVRTIAAAR ITMPKAMVRL SAGRREMPDA
310 320 330 340
VQALCFLAGA NSIFYGDKLL TTGNPEAERD KALFDRLGLH SI
Length:342
Mass (Da):37,172
Last modified:December 20, 2005 - v1
Checksum:iF1F23EA64ADA84F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000103 Genomic DNA. Translation: ABB74432.1.
RefSeqiYP_411824.1. NC_007614.1.

Genome annotation databases

EnsemblBacteriaiABB74432; ABB74432; Nmul_A1129.
GeneIDi3784242.
KEGGinmu:Nmul_A1129.
PATRICi22725486. VBINitMul110821_1311.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000103 Genomic DNA. Translation: ABB74432.1 .
RefSeqi YP_411824.1. NC_007614.1.

3D structure databases

ProteinModelPortali Q2Y9Y9.
SMRi Q2Y9Y9. Positions 35-340.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 323848.Nmul_A1129.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB74432 ; ABB74432 ; Nmul_A1129 .
GeneIDi 3784242.
KEGGi nmu:Nmul_A1129.
PATRICi 22725486. VBINitMul110821_1311.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci NMUL323848:GKEC-1153-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. "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC 25196."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25196 / NCIMB 11849.

Entry informationi

Entry nameiBIOB_NITMU
AccessioniPrimary (citable) accession number: Q2Y9Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: December 20, 2005
Last modified: November 26, 2014
This is version 67 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, Reference proteome

Documents

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

External Data

Dasty 3