BIOI_BACSU
ID BIOI_BACSU Reviewed; 395 AA.
AC P53554;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Biotin biosynthesis cytochrome P450;
DE EC=1.14.14.46 {ECO:0000269|PubMed:11368323};
GN Name=bioI; Synonyms=CYP107H; OrderedLocusNames=BSU30190;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8763940; DOI=10.1128/jb.178.14.4122-4130.1996;
RA Bower S., Perkins J.B., Yocum R.R., Howitt C.L., Rahaim P., Pero J.;
RT "Cloning, sequencing, and characterization of the Bacillus subtilis biotin
RT biosynthetic operon.";
RL J. Bacteriol. 178:4122-4130(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP PROTEIN SEQUENCE OF 2-9, FUNCTION AS BIOTIN BIOSYNTHESIS CYTOCHROME P450,
RP CATALYTIC ACTIVITY, MASS SPECTROMETRY, AND SUBSTRATE SPECIFICITY.
RX PubMed=11368323; DOI=10.1006/abbi.2000.2067;
RA Stok J.E., De Voss J.;
RT "Expression, purification, and characterization of BioI: a carbon-carbon
RT bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus
RT subtilis.";
RL Arch. Biochem. Biophys. 384:351-360(2000).
RN [5]
RP PROTEIN SEQUENCE OF 2-11, MASS SPECTROMETRY, AND SUBSTRATE SPECIFICITY.
RX PubMed=11472016; DOI=10.1007/s007750100229;
RA Green A.J., Rivers S.L., Cheeseman M., Reid G.A., Quaroni L.G.,
RA Macdonald I.D.G., Chapman S.K., Munro A.W.;
RT "Expression, purification and characterization of cytochrome P450 Biol: a
RT novel P450 involved in biotin synthesis in Bacillus subtilis.";
RL J. Biol. Inorg. Chem. 6:523-533(2001).
RN [6]
RP SUBSTRATE SPECIFICITY, AND DISULFIDE BOND.
RX PubMed=15449931; DOI=10.1021/bi049132l;
RA Lawson R.J., Leys D., Sutcliffe M.J., Kemp C.A., Cheesman M.R., Smith S.J.,
RA Clarkson J., Smith W.E., Haq I., Perkins J.B., Munro A.W.;
RT "Thermodynamic and biophysical characterization of cytochrome P450 BioI
RT from Bacillus subtilis.";
RL Biochemistry 43:12410-12426(2004).
RN [7]
RP REACTION MECHANISM.
RX PubMed=14737344; DOI=10.1039/b311652b;
RA Cryle M.J., De Voss J.J.;
RT "Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1).";
RL Chem. Commun. (Camb.) 7:86-87(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-395 IN COMPLEX WITH SUBSTRATE
RP ANALOGS AND HEME, AND COFACTOR.
RX PubMed=18838690; DOI=10.1073/pnas.0805983105;
RA Cryle M.J., Schlichting I.;
RT "Structural insights from a P450 Carrier Protein complex reveal how
RT specificity is achieved in the P450(BioI) ACP complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15696-15701(2008).
CC -!- FUNCTION: Catalyzes the C-C bond cleavage of fatty acid linked to acyl
CC carrier protein (ACP) to generate pimelic acid for biotin biosynthesis.
CC It has high affinity for long-chain fatty acids with the greatest
CC affinity for myristic acid. {ECO:0000269|PubMed:11368323,
CC ECO:0000269|PubMed:8763940}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a C2-C8-saturated long-chain fatty acyl-[ACP] + 3 O2 + 2
CC reduced [flavodoxin] = 6-carboxyhexanoyl-[ACP] + a fatty aldehyde + 3
CC H(+) + 3 H2O + 2 oxidized [flavodoxin]; Xref=Rhea:RHEA:52852,
CC Rhea:RHEA-COMP:9955, Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:10623,
CC Rhea:RHEA-COMP:13382, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:35746, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:78846, ChEBI:CHEBI:136878;
CC EC=1.14.14.46; Evidence={ECO:0000269|PubMed:11368323};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:18838690};
CC Note=Binds 1 heme group covalently per subunit.
CC {ECO:0000269|PubMed:18838690};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC -!- MASS SPECTROMETRY: Mass=44732; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11472016};
CC -!- MASS SPECTROMETRY: Mass=45348; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11368323};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; U51868; AAB17462.1; -; Genomic_DNA.
DR EMBL; AF008220; AAC00266.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14997.1; -; Genomic_DNA.
DR PIR; G69594; G69594.
DR RefSeq; NP_390897.1; NC_000964.3.
DR RefSeq; WP_004398783.1; NZ_JNCM01000036.1.
DR PDB; 3EJB; X-ray; 2.00 A; B/D/F/H=2-395.
DR PDB; 3EJD; X-ray; 2.10 A; B/D/F/H=2-395.
DR PDB; 3EJE; X-ray; 2.10 A; B/D/F/H=2-395.
DR PDBsum; 3EJB; -.
DR PDBsum; 3EJD; -.
DR PDBsum; 3EJE; -.
DR AlphaFoldDB; P53554; -.
DR SMR; P53554; -.
DR DIP; DIP-46307N; -.
DR IntAct; P53554; 1.
DR STRING; 224308.BSU30190; -.
DR DrugBank; DB04450; Heptyl 1-Thiohexopyranoside.
DR PaxDb; P53554; -.
DR PRIDE; P53554; -.
DR EnsemblBacteria; CAB14997; CAB14997; BSU_30190.
DR GeneID; 935928; -.
DR KEGG; bsu:BSU30190; -.
DR PATRIC; fig|224308.179.peg.3275; -.
DR eggNOG; COG2124; Bacteria.
DR InParanoid; P53554; -.
DR OMA; RPELWPN; -.
DR PhylomeDB; P53554; -.
DR BioCyc; BSUB:BSU30190-MON; -.
DR BioCyc; MetaCyc:BSU30190-MON; -.
DR BRENDA; 1.14.14.46; 658.
DR UniPathway; UPA00078; -.
DR EvolutionaryTrace; P53554; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biotin biosynthesis; Direct protein sequencing;
KW Disulfide bond; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11368323,
FT ECO:0000269|PubMed:11472016"
FT CHAIN 2..395
FT /note="Biotin biosynthesis cytochrome P450"
FT /id="PRO_0000052260"
FT BINDING 60
FT /ligand="substrate"
FT BINDING 89..93
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT BINDING 169..173
FT /ligand="substrate"
FT BINDING 285..287
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT BINDING 307
FT /ligand="substrate"
FT BINDING 343..345
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT BINDING 345
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT DISULFID 250..275
FT /evidence="ECO:0000269|PubMed:15449931"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:3EJB"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:3EJB"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:3EJB"
FT TURN 122..126
FT /evidence="ECO:0007829|PDB:3EJB"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 155..166
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 175..201
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 222..252
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:3EJB"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:3EJB"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:3EJB"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:3EJB"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:3EJB"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:3EJB"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:3EJB"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:3EJE"
FT HELIX 348..365
FT /evidence="ECO:0007829|PDB:3EJB"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:3EJB"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:3EJB"
SQ 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
