Skip Header

Contribute Send feedback
Read comments (?) or add your own

P53554 (BIOI_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biotin biosynthesis cytochrome P450
EC=1.14.-.-
Gene names
Name:bioI
Synonyms:CYP107H
Ordered Locus Names:BSU30190
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. It has high affinity for long-chain fatty acids with the greatest affinity for myristic acid. Ref.1 Ref.4

Cofactor

Binds 1 heme group covalently per subunit. Ref.8

Pathway

Cofactor biosynthesis; biotin biosynthesis.

Sequence similarities

Belongs to the cytochrome P450 family.

Mass spectrometry

Molecular mass is 44732 Da from positions 2 - 395. Determined by ESI. Ref.5

Molecular mass is 45348 Da from positions 2 - 395. Determined by ESI. Ref.4

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.5
Chain2 – 395394Biotin biosynthesis cytochrome P450
PRO_0000052260

Regions

Region89 – 935Heme binding
Region169 – 1735Substrate binding
Region285 – 2873Heme binding
Region343 – 3453Heme binding

Sites

Metal binding3451Iron (heme axial ligand)
Binding site601Substrate
Binding site3071Substrate

Amino acid modifications

Disulfide bond250 ↔ 275 Ref.6

Secondary structure

1 ......................................................... 395
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53554 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: E4AC3AF2637ACE1A

FASTA39544,865
        10         20         30         40         50         60 
MTIASSTASS EFLKNPYSFY DTLRAVHPIY KGSFLKYPGW YVTGYEETAA ILKDARFKVR 

        70         80         90        100        110        120 
TPLPESSTKY QDLSHVQNQM MLFQNQPDHR RLRTLASGAF TPRTTESYQP YIIETVHHLL 

       130        140        150        160        170        180 
DQVQGKKKME VISDFAFPLA SFVIANIIGV PEEDREQLKE WAASLIQTID FTRSRKALTE 

       190        200        210        220        230        240 
GNIMAVQAMA YFKELIQKRK RHPQQDMISM LLKGREKDKL TEEEAASTCI LLAIAGHETT 

       250        260        270        280        290        300 
VNLISNSVLC LLQHPEQLLK LRENPDLIGT AVEECLRYES PTQMTARVAS EDIDICGVTI 

       310        320        330        340        350        360 
RQGEQVYLLL GAANRDPSIF TNPDVFDITR SPNPHLSFGH GHHVCLGSSL ARLEAQIAIN 

       370        380        390 
TLLQRMPSLN LADFEWRYRP LFGFRALEEL PVTFE

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing, and characterization of the Bacillus subtilis biotin biosynthetic operon."
Bower S., Perkins J.B., Yocum R.R., Howitt C.L., Rahaim P., Pero J.
J. Bacteriol. 178:4122-4130(1996) [PubMed: 8763940] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
Microbiology 143:3431-3441(1997) [PubMed: 9387221] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Expression, purification, and characterization of BioI: a carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis."
Stok J.E., De Voss J.
Arch. Biochem. Biophys. 384:351-360(2000) [PubMed: 11368323] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-9, FUNCTION AS BIOTIN BIOSYNTHESIS CYTOCHROME P450, MASS SPECTROMETRY, SUBSTRATE SPECIFICITY.
[5]"Expression, purification and characterization of cytochrome P450 Biol: a novel P450 involved in biotin synthesis in Bacillus subtilis."
Green A.J., Rivers S.L., Cheeseman M., Reid G.A., Quaroni L.G., Macdonald I.D.G., Chapman S.K., Munro A.W.
J. Biol. Inorg. Chem. 6:523-533(2001) [PubMed: 11472016] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11, MASS SPECTROMETRY, SUBSTRATE SPECIFICITY.
[6]"Thermodynamic and biophysical characterization of cytochrome P450 BioI from Bacillus subtilis."
Lawson R.J., Leys D., Sutcliffe M.J., Kemp C.A., Cheesman M.R., Smith S.J., Clarkson J., Smith W.E., Haq I., Perkins J.B., Munro A.W.
Biochemistry 43:12410-12426(2004) [PubMed: 15449931] [Abstract]
Cited for: SUBSTRATE SPECIFICITY, DISULFIDE BOND.
[7]"Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1)."
Cryle M.J., De Voss J.J.
Chem. Commun. (Camb.) 7:86-87(2004) [PubMed: 14737344] [Abstract]
Cited for: REACTION MECHANISM.
[8]"Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex."
Cryle M.J., Schlichting I.
Proc. Natl. Acad. Sci. U.S.A. 105:15696-15701(2008) [PubMed: 18838690] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-395 IN COMPLEX WITH ANALOGS SUBSTRATE AND HEME, COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U51868 Genomic DNA. Translation: AAB17462.1.
AF008220 Genomic DNA. Translation: AAC00266.1.
AL009126 Genomic DNA. Translation: CAB14997.1.
PIRG69594.
RefSeqNP_390897.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EJBX-ray2.00B/D/F/H2-395[»]
3EJDX-ray2.10B/D/F/H2-395[»]
3EJEX-ray2.10B/D/F/H2-395[»]
ProteinModelPortalP53554.
SMRP53554. Positions 7-394.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-46307N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000003521; EBBACP00000003521; EBBACG00000003514.
GeneID935928.
GenomeReviewsGene locus BSU30190 in contig AL009126_GR.
KEGGbsu:BSU30190.
NMPDRfig|224308.1.peg.3022.
PATRIC18977940. VBIBacSub10457_3158.

Organism-specific databases

GenoListBSU30190. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000001046.
HOGENOMHBG695262.
OMAELSTIRW.
PhylomeDBP53554.
ProtClustDBCLSK887747.

Enzyme and pathway databases

BioCycBSUB:BSU30190-MONOMER.

Family and domain databases

InterProIPR000794. Beta-ketoacyl_synthase.
IPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
IPR017972. Cyt_P450_CS.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
KOK00517.
PANTHERPTHR11712. Ketoacyl_synth. 1 hit.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00359. BP450.
PR00385. P450.
SUPFAMSSF48264. Cytochrome_P450. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBIOI_BACSU
AccessionPrimary (citable) accession number: P53554
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 25, 2012
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents