ID A0A1V2THQ2_9NOCA Unreviewed; 444 AA.
AC A0A1V2THQ2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:ONM49050.1};
GN ORFNames=B0T46_08925 {ECO:0000313|EMBL:ONM49050.1};
OS Nocardia donostiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1538463 {ECO:0000313|EMBL:ONM49050.1, ECO:0000313|Proteomes:UP000188836};
RN [1] {ECO:0000313|EMBL:ONM49050.1, ECO:0000313|Proteomes:UP000188836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X1655 {ECO:0000313|EMBL:ONM49050.1,
RC ECO:0000313|Proteomes:UP000188836};
RX PubMed=26914251; DOI=10.1007/s10482-016-0667-8;
RA Ercibengoa M., Bell M., Marimon J.M., Humrighouse B., Klenk H.P.,
RA Potter G., Perez-Trallero E.;
RT "Nocardia donostiensis sp. nov., isolated from human respiratory
RT specimens.";
RL Antonie Van Leeuwenhoek 109:653-660(2016).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {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:ONM49050.1}.
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; MUMY01000006; ONM49050.1; -; Genomic_DNA.
DR RefSeq; WP_077116042.1; NZ_MUMY01000006.1.
DR AlphaFoldDB; A0A1V2THQ2; -.
DR STRING; 1538463.B0T36_16095; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000188836; 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 CDD; cd11053; CYP110-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF166; CYTOCHROME P450 12A4, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000188836}.
SQ SEQUENCE 444 AA; 48319 MW; 37ACFC03C058E683 CRC64;
MGVVPRRSGE AAPRAPRPAL AHAIAAGIGF ERYFRWRRER DGDPFRLRFP GLGAVLFTGI
QEGAREVFRS PVHTVEPPRP NPIEPLVGTA SLILTNGDRH RQDRALLAPA FHPAQLQHYG
TVIQEAALRE MSGRWHPGGR IDARTAATAI TLQVILTAVF GVAKERHAAY TAAIADFLGS
FTGPLMLAPA LRHGVLGRAP WDRFVTARDR LDQLLLADIA RRRRRGAVTP DILTLLLSCR
YDDGTAITDA DLCDQLRTLL VAGHDTTANT LAWAMWRVYG DPAVSAQLRA ELRSAGPVAQ
TAPAGLPYLN AVCRETLRLH PAVPIVLRRV AAPTLLRGAP LAAGEVMGVA LPLLHSDPAV
WAEPELFRPA RFLRHRYSPF EFAPFGGGHR RCLGAAFAEF ELRVALATIA AGANLRPVPG
RAPRSRPHGI ATRPSRPLLF DVIS
//