ID Q13GG9_PARXL Unreviewed; 410 AA.
AC Q13GG9;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:ABE36820.1};
GN ORFNames=Bxe_C0945 {ECO:0000313|EMBL:ABE36820.1};
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36820.1, ECO:0000313|Proteomes:UP000001817};
RN [1] {ECO:0000313|EMBL:ABE36820.1, ECO:0000313|Proteomes:UP000001817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400 {ECO:0000313|EMBL:ABE36820.1,
RC ECO:0000313|Proteomes:UP000001817};
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CP000272; ABE36820.1; -; Genomic_DNA.
DR RefSeq; WP_011494067.1; NZ_CP008761.1.
DR AlphaFoldDB; Q13GG9; -.
DR STRING; 266265.Bxe_C0945; -.
DR KEGG; bxb:DR64_7505; -.
DR KEGG; bxe:Bxe_C0945; -.
DR PATRIC; fig|266265.5.peg.8709; -.
DR eggNOG; COG2124; Bacteria.
DR OrthoDB; 4168525at2; -.
DR Proteomes; UP000001817; Chromosome 3.
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 CDD; cd11030; CYP105-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR46696:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 46361 MW; 85651DB0B4568AAD CRC64;
MTSAINDVRP QTTSTFPFAR TGSPLHPPAE YARYRDGQPV TRVQMWDGRY AWIFTRMEDV
KAVLSSPHFS VVPSKPGYPF LTPARAATVK SYQTFITMDP PDHTRFRRML TRDFTQKRME
ELRPQIAAYV NRLIDEMLAR GSPGDLVSAL ALKLPVTVVS MLVGVPYEDH EDLVKWSGQR
LDLEQNPTVS ESAADNMLAY FDGLLQRKER DPGDGADMLS RLVIEQIKPG HLSRLEAIHM
VNLLYFAGHE TTANQIALGT LSFLLDPRQR ALLENNPGLL KNAIEEMLRF HTISHYNSCR
VATADVEVGG TLIREGEGAY ALIMAANRDP AAFPAPDRFD IERPNSQEHV AFSYGLHMCL
GQPLARLELQ VCFEALFRRL PRLRLAVPLE ELPFKREMYV YGLHALPVTW
//
