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Protein
Submitted name:

BirA bifunctional protein

Gene

birA

Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

  • biotin metabolic process Source: MTBBASE
  • protein biotinylation Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

LigaseImported

Enzyme and pathway databases

BioCyciMTBRV:RV3279C-MONOMER.
BRENDAi6.3.4.15. 3445.

Names & Taxonomyi

Protein namesi
Submitted name:
BirA bifunctional proteinImported (EC:6.3.4.15Imported)
Gene namesi
Name:birAImported
Ordered Locus Names:MT3379Imported
OrganismiMycobacterium tuberculosis (strain CDC 1551 / Oshkosh)Imported
Taxonomic identifieri83331 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001020 Componenti: Chromosome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3102688.

Interactioni

Chemistry

BindingDBiP96884.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CGHX-ray1.80A/B1-266[»]
3L1AX-ray2.69A/B1-266[»]
3L2ZX-ray2.80A/B1-266[»]
3RUXX-ray1.70A/B2-266[»]
ProteinModelPortaliP96884.
SMRiP96884. Positions 2-265.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 14791BPL/LPL catalyticInterPro annotationAdd
BLAST
Domaini218 – 26447BPL_CInterPro annotationAdd
BLAST

Phylogenomic databases

HOGENOMiHOG000041813.
KOiK03524.
OrthoDBiEOG6DNTBX.

Family and domain databases

InterProiIPR004408. Biotin_CoA_COase_ligase.
IPR003142. BPL_C.
IPR004143. BPL_LPL_catalytic.
[Graphical view]
PANTHERiPTHR12835. PTHR12835. 1 hit.
PfamiPF02237. BPL_C. 1 hit.
PF03099. BPL_LplA_LipB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00121. birA_ligase. 1 hit.

Sequencei

Sequence statusi: Complete.

P96884-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDRDRLRPP LDERSLRDQL IGAGSGWRQL DVVAQTGSTN ADLLARAASG
60 70 80 90 100
ADIDGVVLIA EHQTAGRGRH GRGWAATARA QIILSVGVRV VDVPVQAWGW
110 120 130 140 150
LSLAAGLAVL DSVAPLIAVP PAETGLKWPN DVLARGGKLA GILAEVAQPF
160 170 180 190 200
VVLGVGLNVT QAPEEVDPDA TSLLDLGVAA PDRNRIASRL LRELEARIIQ
210 220 230 240 250
WRNANPQLAA DYRARSLTIG SRVRVELPGG QDVVGIARDI DDQGRLCLDV
260
GGRTVVVSAG DVVHLR
Length:266
Mass (Da):28,121
Last modified:July 1, 1997 - v2
Checksum:i3DE5CE48830F070F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000516 Genomic DNA. Translation: AAK47721.1.
PIRiH70979.
RefSeqiWP_003899999.1. NZ_KK341227.1.

Genome annotation databases

EnsemblBacteriaiAAK47721; AAK47721; MT3379.
KEGGimtc:MT3379.
PATRICi18129182. VBIMycTub22151_3687.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000516 Genomic DNA. Translation: AAK47721.1.
PIRiH70979.
RefSeqiWP_003899999.1. NZ_KK341227.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CGHX-ray1.80A/B1-266[»]
3L1AX-ray2.69A/B1-266[»]
3L2ZX-ray2.80A/B1-266[»]
3RUXX-ray1.70A/B2-266[»]
ProteinModelPortaliP96884.
SMRiP96884. Positions 2-265.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP96884.
ChEMBLiCHEMBL3102688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK47721; AAK47721; MT3379.
KEGGimtc:MT3379.
PATRICi18129182. VBIMycTub22151_3687.

Phylogenomic databases

HOGENOMiHOG000041813.
KOiK03524.
OrthoDBiEOG6DNTBX.

Enzyme and pathway databases

BioCyciMTBRV:RV3279C-MONOMER.
BRENDAi6.3.4.15. 3445.

Family and domain databases

InterProiIPR004408. Biotin_CoA_COase_ligase.
IPR003142. BPL_C.
IPR004143. BPL_LPL_catalytic.
[Graphical view]
PANTHERiPTHR12835. PTHR12835. 1 hit.
PfamiPF02237. BPL_C. 1 hit.
PF03099. BPL_LplA_LipB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00121. birA_ligase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CDC 1551 / OshkoshImported.
  2. "Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration."
    Gupta V., Gupta R.K., Khare G., Salunke D.M., Surolia A., Tyagi A.K.
    PLoS ONE 5:e9222-e9222(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS).
  3. "Bisubstrate adenylation inhibitors of biotin protein ligase from Mycobacterium tuberculosis."
    Duckworth B.P., Geders T.W., Tiwari D., Boshoff H.I., Sibbald P.A., Barry C.E., Schnappinger D., Finzel B.C., Aldrich C.C.
    Chem. Biol. 18:1432-1441(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-266.
  4. "Active site conformational changes upon reaction intermediate biotinyl-5'-AMP binding in biotin protein ligase from Mycobacterium tuberculosis."
    Ma Q., Akhter Y., Wilmanns M., Ehebauer M.T.
    Protein Sci. 23:932-939(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).

Entry informationi

Entry nameiP96884_MYCTO
AccessioniPrimary (citable) accession number: P96884
Secondary accession number(s): F2GKV2, Q7D5S4
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1997
Last sequence update: July 1, 1997
Last modified: June 8, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteomeImported

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 one 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.