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1,8-cineole 2-endo-monooxygenase (EC 1.14.13.156) (cytochrome P450) (CYP176A1) (P450cin)

 CINA_CITBR              Reviewed;         404 AA.
Q8VQF6;
26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
25-OCT-2017, entry version 80.
RecName: Full=1,8-cineole 2-endo-monooxygenase;
EC=1.14.13.156;
AltName: Full=cytochrome P450;
Short=CYP176A1;
Short=P450cin;
Name=cinA;
Citrobacter braakii.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
NCBI_TaxID=57706;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 171-195,
FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
PubMed=12016226; DOI=10.1074/jbc.M203382200;
Hawkes D.B., Adams G.W., Burlingame A.L., Ortiz de Montellano P.R.,
De Voss J.J.;
"Cytochrome P450(cin) (CYP176A), isolation, expression, and
characterization.";
J. Biol. Chem. 277:27725-27732(2002).
[2]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 8-404 IN COMPLEX WITH HEME
AND SUBSTRATE, COFACTOR, AND SUBUNIT.
PubMed=15260491; DOI=10.1021/bi049293p;
Meharenna Y.T., Li H., Hawkes D.B., Pearson A.G., De Voss J.,
Poulos T.L.;
"Crystal structure of P450cin in a complex with its substrate, 1,8-
cineole, a close structural homologue to D-camphor, the substrate for
P450cam.";
Biochemistry 43:9487-9494(2004).
[3]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 8-404 OF MUTANT ALA-242 IN
COMPLEX WITH HEME AND SUBSTRATE, SUBSTRATE SPECIFICITY, MUTAGENESIS OF
ASN-242, AND SUBUNIT.
PubMed=18270198; DOI=10.1074/jbc.M709722200;
Meharenna Y.T., Slessor K.E., Cavaignac S.M., Poulos T.L.,
De Voss J.J.;
"The critical role of substrate-protein hydrogen bonding in the
control of regioselective hydroxylation in p450cin.";
J. Biol. Chem. 283:10804-10812(2008).
[4]
X-RAY CRYSTALLOGRAPHY (1.37 ANGSTROMS) OF 8-404 IN COMPLEX WITH HEME
AND SUBSTRATE, AND SUBUNIT.
PubMed=22775403; DOI=10.1021/bi300666u;
Madrona Y., Tripathi S., Li H., Poulos T.L.;
"Crystal structures of substrate-free and nitrosyl cytochrome P450cin:
implications for O(2) activation.";
Biochemistry 51:6623-6631(2012).
-!- FUNCTION: Involved in the degradation of cineol (eucalyptol).
Catalyzes the initial hydroxylation of cineole exclusively at the
pro-R carbon to give the (S)-6beta-hydroxycineole. Cineole is the
natural substrate of CinA. {ECO:0000269|PubMed:12016226}.
-!- CATALYTIC ACTIVITY: 1,8-cineole + NADPH + O(2) = 2-endo-hydroxy-
1,8-cineole + NADP(+) + H(2)O. {ECO:0000269|PubMed:12016226}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:15260491};
-!- PATHWAY: Terpene metabolism; 1,8-cineol degradation.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15260491,
ECO:0000269|PubMed:18270198, ECO:0000269|PubMed:22775403}.
-!- MISCELLANEOUS: It lacks the conserved threonine believed to be
involved in dioxygen activation and instead contains an asparagine
at position 242. It is the first isolated P450 using the
flavoprotein cindoxin (CinC) as its natural redox partner
(PubMed:12016226). {ECO:0000305|PubMed:12016226}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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EMBL; AF456128; AAL57614.1; -; Genomic_DNA.
PDB; 1T2B; X-ray; 1.70 A; A/B=8-404.
PDB; 3BDZ; X-ray; 2.00 A; A/B=8-404.
PDB; 3BE0; X-ray; 3.05 A; A/B=8-404.
PDB; 4FB2; X-ray; 1.37 A; A/B/C/D=8-404.
PDB; 4FMX; X-ray; 1.55 A; A/B=8-404.
PDB; 4FYZ; X-ray; 2.32 A; A/B=8-404.
PDB; 4L6G; X-ray; 1.37 A; A/B=8-404.
PDB; 4L77; X-ray; 1.38 A; A/B=8-404.
PDB; 4LHT; X-ray; 2.14 A; A/B=8-404.
PDBsum; 1T2B; -.
PDBsum; 3BDZ; -.
PDBsum; 3BE0; -.
PDBsum; 4FB2; -.
PDBsum; 4FMX; -.
PDBsum; 4FYZ; -.
PDBsum; 4L6G; -.
PDBsum; 4L77; -.
PDBsum; 4LHT; -.
ProteinModelPortal; Q8VQF6; -.
SMR; Q8VQF6; -.
KEGG; ag:AAL57614; -.
KO; K21120; -.
BioCyc; MetaCyc:MONOMER-17202; -.
BRENDA; 1.14.13.156; 6880.
UniPathway; UPA01032; -.
EvolutionaryTrace; Q8VQF6; -.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
GO; GO:0046232; P:carbazole catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR002397; Cyt_P450_B.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00359; BP450.
SUPFAM; SSF48264; SSF48264; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
Monooxygenase; NADP; Oxidoreductase.
CHAIN 1 404 1,8-cineole 2-endo-monooxygenase.
/FTId=PRO_0000422738.
METAL 347 347 Iron (heme axial ligand).
BINDING 73 73 Heme. {ECO:0000269|PubMed:15260491,
ECO:0000269|PubMed:18270198,
ECO:0000269|PubMed:22775403}.
BINDING 98 98 Heme. {ECO:0000269|PubMed:15260491,
ECO:0000269|PubMed:18270198,
ECO:0000269|PubMed:22775403}.
BINDING 102 102 Heme. {ECO:0000269|PubMed:15260491,
ECO:0000269|PubMed:18270198,
ECO:0000269|PubMed:22775403}.
BINDING 242 242 Substrate. {ECO:0000269|PubMed:15260491}.
BINDING 289 289 Heme. {ECO:0000269|PubMed:15260491,
ECO:0000269|PubMed:18270198,
ECO:0000269|PubMed:22775403}.
BINDING 345 345 Heme. {ECO:0000269|PubMed:15260491,
ECO:0000269|PubMed:18270198,
ECO:0000269|PubMed:22775403}.
SITE 242 242 Controls regioselective substrate
oxidation.
MUTAGEN 242 242 N->A: Has only a modest effect on
monooxygenase activity. The substrate is
free to adopt an alternate conformation
which places the ethereal oxygen in an
optimal position for polar interactions
with solvent.
{ECO:0000269|PubMed:18270198}.
TURN 10 13 {ECO:0000244|PDB:4FB2}.
STRAND 16 18 {ECO:0000244|PDB:3BE0}.
STRAND 25 27 {ECO:0000244|PDB:4FB2}.
HELIX 28 38 {ECO:0000244|PDB:4FB2}.
STRAND 42 46 {ECO:0000244|PDB:4FB2}.
HELIX 48 50 {ECO:0000244|PDB:4FB2}.
STRAND 52 55 {ECO:0000244|PDB:4FB2}.
HELIX 58 65 {ECO:0000244|PDB:4FB2}.
STRAND 69 72 {ECO:0000244|PDB:4FB2}.
HELIX 73 75 {ECO:0000244|PDB:4FB2}.
STRAND 77 79 {ECO:0000244|PDB:4FB2}.
TURN 89 92 {ECO:0000244|PDB:4FB2}.
HELIX 97 106 {ECO:0000244|PDB:4FB2}.
TURN 107 109 {ECO:0000244|PDB:4FB2}.
HELIX 111 115 {ECO:0000244|PDB:4FB2}.
HELIX 118 130 {ECO:0000244|PDB:4FB2}.
TURN 131 135 {ECO:0000244|PDB:4FB2}.
STRAND 136 139 {ECO:0000244|PDB:4FB2}.
HELIX 140 143 {ECO:0000244|PDB:4FB2}.
TURN 144 147 {ECO:0000244|PDB:4FB2}.
HELIX 148 156 {ECO:0000244|PDB:4FB2}.
HELIX 161 163 {ECO:0000244|PDB:4FB2}.
HELIX 164 176 {ECO:0000244|PDB:4FB2}.
HELIX 180 203 {ECO:0000244|PDB:4FB2}.
HELIX 209 215 {ECO:0000244|PDB:4FB2}.
HELIX 225 256 {ECO:0000244|PDB:4FB2}.
HELIX 258 266 {ECO:0000244|PDB:4FB2}.
HELIX 268 270 {ECO:0000244|PDB:4FB2}.
HELIX 271 282 {ECO:0000244|PDB:4FB2}.
STRAND 287 291 {ECO:0000244|PDB:4FB2}.
STRAND 295 297 {ECO:0000244|PDB:4FB2}.
STRAND 300 302 {ECO:0000244|PDB:4FB2}.
STRAND 307 310 {ECO:0000244|PDB:4FB2}.
HELIX 312 315 {ECO:0000244|PDB:4FB2}.
TURN 319 321 {ECO:0000244|PDB:4FB2}.
STRAND 322 324 {ECO:0000244|PDB:4FB2}.
HELIX 343 345 {ECO:0000244|PDB:4L77}.
HELIX 350 367 {ECO:0000244|PDB:4FB2}.
STRAND 380 382 {ECO:0000244|PDB:4FB2}.
STRAND 384 386 {ECO:0000244|PDB:4FB2}.
STRAND 388 391 {ECO:0000244|PDB:4FB2}.
STRAND 393 395 {ECO:0000244|PDB:4FB2}.
SEQUENCE 404 AA; 45266 MW; 1EA334C5CF1B8243 CRC64;
MTATVASTSL FTTADHYHTP LGPDGTPHAF FEALRDEAET TPIGWSEAYG GHWVVAGYKE
IQAVIQNTKA FSNKGVTFPR YETGEFELMM AGQDDPVHKK YRQLVAKPFS PEATDLFTEQ
LRQSTNDLID ARIELGEGDA ATWLANEIPA RLTAILLGLP PEDGDTYRRW VWAITHVENP
EEGAEIFAEL VAHARTLIAE RRTNPGNDIM SRVIMSKIDG ESLSEDDLIG FFTILLLGGI
DNTARFLSSV FWRLAWDIEL RRRLIAHPEL IPNAVDELLR FYGPAMVGRL VTQEVTVGDI
TMKPGQTAML WFPIASRDRS AFDSPDNIVI ERTPNRHLSL GHGIHRCLGA HLIRVEARVA
ITEFLKRIPE FSLDPNKECE WLMGQVAGML HVPIIFPKGK RLSE


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