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Biotin biosynthesis cytochrome P450 (EC 1.14.14.46)

 BIOI_BACSU              Reviewed;         395 AA.
P53554;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 129.
RecName: Full=Biotin biosynthesis cytochrome P450;
EC=1.14.14.46 {ECO:0000269|PubMed:11368323};
Name=bioI; Synonyms=CYP107H; OrderedLocusNames=BSU30190;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=8763940; DOI=10.1128/jb.178.14.4122-4130.1996;
Bower S., Perkins J.B., Yocum R.R., Howitt C.L., Rahaim P., Pero J.;
"Cloning, sequencing, and characterization of the Bacillus subtilis
biotin biosynthetic operon.";
J. Bacteriol. 178:4122-4130(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
"Sequencing and functional annotation of the Bacillus subtilis genes
in the 200 kb rrnB-dnaB region.";
Microbiology 143:3431-3441(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
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., 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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[4]
PROTEIN SEQUENCE OF 2-9, FUNCTION AS BIOTIN BIOSYNTHESIS CYTOCHROME
P450, CATALYTIC ACTIVITY, MASS SPECTROMETRY, AND SUBSTRATE
SPECIFICITY.
PubMed=11368323; DOI=10.1006/abbi.2000.2067;
Stok J.E., De Voss J.;
"Expression, purification, and characterization of BioI: a carbon-
carbon bond cleaving cytochrome P450 involved in biotin biosynthesis
in Bacillus subtilis.";
Arch. Biochem. Biophys. 384:351-360(2000).
[5]
PROTEIN SEQUENCE OF 2-11, MASS SPECTROMETRY, AND SUBSTRATE
SPECIFICITY.
PubMed=11472016; DOI=10.1007/s007750100229;
Green A.J., Rivers S.L., Cheeseman M., Reid G.A., Quaroni L.G.,
Macdonald I.D.G., Chapman S.K., Munro A.W.;
"Expression, purification and characterization of cytochrome P450
Biol: a novel P450 involved in biotin synthesis in Bacillus
subtilis.";
J. Biol. Inorg. Chem. 6:523-533(2001).
[6]
SUBSTRATE SPECIFICITY, AND DISULFIDE BOND.
PubMed=15449931; DOI=10.1021/bi049132l;
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.;
"Thermodynamic and biophysical characterization of cytochrome P450
BioI from Bacillus subtilis.";
Biochemistry 43:12410-12426(2004).
[7]
REACTION MECHANISM.
PubMed=14737344; DOI=10.1039/b311652b;
Cryle M.J., De Voss J.J.;
"Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1).";
Chem. Commun. (Camb.) 7:86-87(2004).
[8]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-395 IN COMPLEX WITH
SUBSTRATE ANALOGS AND HEME, AND COFACTOR.
PubMed=18838690; DOI=10.1073/pnas.0805983105;
Cryle M.J., Schlichting I.;
"Structural insights from a P450 Carrier Protein complex reveal how
specificity is achieved in the P450(BioI) ACP complex.";
Proc. Natl. Acad. Sci. U.S.A. 105:15696-15701(2008).
-!- 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.
{ECO:0000269|PubMed:11368323, ECO:0000269|PubMed:8763940}.
-!- CATALYTIC ACTIVITY: A long-chain acyl-[acyl-carrier protein] + 2
reduced flavodoxin + 3 O(2) = pimeloyl-[acyl-carrier protein] + an
n-alkanal + 2 oxidized flavodoxin + 3 H(2)O.
{ECO:0000269|PubMed:11368323}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:18838690};
Note=Binds 1 heme group covalently per subunit.
{ECO:0000269|PubMed:18838690};
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
-!- MASS SPECTROMETRY: Mass=44732; Method=Electrospray; Range=2-395;
Evidence={ECO:0000269|PubMed:11472016};
-!- MASS SPECTROMETRY: Mass=45348; Method=Electrospray; Range=2-395;
Evidence={ECO:0000269|PubMed:11368323};
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U51868; AAB17462.1; -; Genomic_DNA.
EMBL; AF008220; AAC00266.1; -; Genomic_DNA.
EMBL; AL009126; CAB14997.1; -; Genomic_DNA.
PIR; G69594; G69594.
RefSeq; NP_390897.1; NC_000964.3.
RefSeq; WP_004398783.1; NZ_JNCM01000036.1.
PDB; 3EJB; X-ray; 2.00 A; B/D/F/H=2-395.
PDB; 3EJD; X-ray; 2.10 A; B/D/F/H=2-395.
PDB; 3EJE; X-ray; 2.10 A; B/D/F/H=2-395.
PDBsum; 3EJB; -.
PDBsum; 3EJD; -.
PDBsum; 3EJE; -.
ProteinModelPortal; P53554; -.
SMR; P53554; -.
DIP; DIP-46307N; -.
IntAct; P53554; 1.
STRING; 224308.Bsubs1_010100016446; -.
DrugBank; DB04450; Heptyl 1-Thiohexopyranoside.
PaxDb; P53554; -.
EnsemblBacteria; CAB14997; CAB14997; BSU30190.
GeneID; 935928; -.
KEGG; bsu:BSU30190; -.
PATRIC; fig|224308.179.peg.3275; -.
eggNOG; ENOG4106A3M; Bacteria.
eggNOG; COG2124; LUCA.
HOGENOM; HOG000243678; -.
InParanoid; P53554; -.
KO; K16593; -.
OMA; DGIMRYP; -.
PhylomeDB; P53554; -.
BioCyc; BSUB:BSU30190-MONOMER; -.
BioCyc; MetaCyc:BSU30190-MONOMER; -.
BRENDA; 1.14.15.12; 658.
UniPathway; UPA00078; -.
EvolutionaryTrace; P53554; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
GO; GO:0009102; P:biotin biosynthetic process; IDA:UniProtKB.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR002397; Cyt_P450_B.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00359; BP450.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
3D-structure; Biotin biosynthesis; Complete proteome;
Direct protein sequencing; Disulfide bond; Heme; Iron; Metal-binding;
Monooxygenase; Oxidoreductase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:11368323,
ECO:0000269|PubMed:11472016}.
CHAIN 2 395 Biotin biosynthesis cytochrome P450.
/FTId=PRO_0000052260.
REGION 89 93 Heme binding.
REGION 169 173 Substrate binding.
REGION 285 287 Heme binding.
REGION 343 345 Heme binding.
METAL 345 345 Iron (heme axial ligand).
BINDING 60 60 Substrate.
BINDING 307 307 Substrate.
DISULFID 250 275 {ECO:0000269|PubMed:15449931}.
HELIX 11 14 {ECO:0000244|PDB:3EJB}.
HELIX 16 26 {ECO:0000244|PDB:3EJB}.
STRAND 28 34 {ECO:0000244|PDB:3EJB}.
STRAND 37 42 {ECO:0000244|PDB:3EJB}.
HELIX 45 53 {ECO:0000244|PDB:3EJB}.
HELIX 71 78 {ECO:0000244|PDB:3EJB}.
HELIX 81 83 {ECO:0000244|PDB:3EJB}.
HELIX 88 97 {ECO:0000244|PDB:3EJB}.
HELIX 98 100 {ECO:0000244|PDB:3EJB}.
HELIX 102 106 {ECO:0000244|PDB:3EJB}.
HELIX 109 121 {ECO:0000244|PDB:3EJB}.
TURN 122 126 {ECO:0000244|PDB:3EJB}.
STRAND 127 130 {ECO:0000244|PDB:3EJB}.
HELIX 131 134 {ECO:0000244|PDB:3EJB}.
HELIX 136 148 {ECO:0000244|PDB:3EJB}.
HELIX 152 154 {ECO:0000244|PDB:3EJB}.
HELIX 155 166 {ECO:0000244|PDB:3EJB}.
HELIX 167 169 {ECO:0000244|PDB:3EJB}.
HELIX 175 201 {ECO:0000244|PDB:3EJB}.
HELIX 207 213 {ECO:0000244|PDB:3EJB}.
HELIX 222 252 {ECO:0000244|PDB:3EJB}.
HELIX 255 263 {ECO:0000244|PDB:3EJB}.
HELIX 265 267 {ECO:0000244|PDB:3EJB}.
HELIX 268 278 {ECO:0000244|PDB:3EJB}.
STRAND 284 291 {ECO:0000244|PDB:3EJB}.
STRAND 293 295 {ECO:0000244|PDB:3EJB}.
STRAND 298 300 {ECO:0000244|PDB:3EJB}.
STRAND 305 309 {ECO:0000244|PDB:3EJB}.
HELIX 310 313 {ECO:0000244|PDB:3EJB}.
TURN 317 319 {ECO:0000244|PDB:3EJB}.
STRAND 320 322 {ECO:0000244|PDB:3EJB}.
HELIX 341 343 {ECO:0000244|PDB:3EJE}.
HELIX 348 365 {ECO:0000244|PDB:3EJB}.
STRAND 382 384 {ECO:0000244|PDB:3EJB}.
STRAND 391 393 {ECO:0000244|PDB:3EJB}.
SEQUENCE 395 AA; 44865 MW; E4AC3AF2637ACE1A CRC64;
MTIASSTASS EFLKNPYSFY DTLRAVHPIY KGSFLKYPGW YVTGYEETAA ILKDARFKVR
TPLPESSTKY QDLSHVQNQM MLFQNQPDHR RLRTLASGAF TPRTTESYQP YIIETVHHLL
DQVQGKKKME VISDFAFPLA SFVIANIIGV PEEDREQLKE WAASLIQTID FTRSRKALTE
GNIMAVQAMA YFKELIQKRK RHPQQDMISM LLKGREKDKL TEEEAASTCI LLAIAGHETT
VNLISNSVLC LLQHPEQLLK LRENPDLIGT AVEECLRYES PTQMTARVAS EDIDICGVTI
RQGEQVYLLL GAANRDPSIF TNPDVFDITR SPNPHLSFGH GHHVCLGSSL ARLEAQIAIN
TLLQRMPSLN LADFEWRYRP LFGFRALEEL PVTFE


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