ID A0A0N0D7Q6_9RHOB Unreviewed; 387 AA.
AC A0A0N0D7Q6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Cytochrome P450-pinF2, plant-inducible {ECO:0000313|EMBL:KPA19931.1};
DE EC=1.14.-.- {ECO:0000313|EMBL:KPA19931.1};
GN ORFNames=shim_38900 {ECO:0000313|EMBL:KPA19931.1};
OS Shimia sp. SK013.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA19931.1, ECO:0000313|Proteomes:UP000037951};
RN [1] {ECO:0000313|EMBL:KPA19931.1, ECO:0000313|Proteomes:UP000037951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK013 {ECO:0000313|EMBL:KPA19931.1,
RC ECO:0000313|Proteomes:UP000037951};
RA Voget S., Kanukollu S., Daniel R., Engelen B.;
RT "Genome Sequence of Shimia sp. SK013.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPA19931.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LAJH01000028; KPA19931.1; -; Genomic_DNA.
DR RefSeq; WP_054004297.1; NZ_LAJH01000028.1.
DR AlphaFoldDB; A0A0N0D7Q6; -.
DR STRING; 1389006.shim_38900; -.
DR PATRIC; fig|1389006.3.peg.4015; -.
DR OrthoDB; 9801155at2; -.
DR Proteomes; UP000037951; Unassembled WGS sequence.
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 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 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,
KW ECO:0000313|EMBL:KPA19931.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037951}.
SQ SEQUENCE 387 AA; 42247 MW; 90B02378EAFF41AF CRC64;
MSNAPIYEID PKAFWADPYP DLARMRETTP IAYVPQLGAT LITRRDDIFE NEKKTDIFSS
DQPDGLMTVL MGQNMMRKDG AAHQAERRAI FPTVSPKTVQ RVWKAHFETA TADILDRVQP
NGQADMVADI ARPISGEALK AMTGLTNMTW QEMDRVSQGM IDGCANYAGD PNITATCHNC
TASIDAHIAQ RKPALHDAPD SSLLSVMMQA ELSDAQISAN IKLAISGGQN EPRDAIAGAA
WALLTHPDQL AKITNGDATW LAAFEEYARW MSPIGMSPRR IVKPHETKGV TFDLEDRVFL
MFSSGNRDAA CFTNPDAFDL SQNASKAISF GAGPHFCAGA WASKCLIAEV ALPMIFDRLA
GLTLAGDTPF GGWAFRGPLS MPVRWQI
//
