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Database: UniProt
Entry: A0A1V2THQ2_9NOCA
LinkDB: A0A1V2THQ2_9NOCA
Original site: A0A1V2THQ2_9NOCA 
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}.
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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
//
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