ID L7KNK0_9ACTN Unreviewed; 412 AA.
AC L7KNK0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative cytochrome P450 {ECO:0000313|EMBL:GAC49288.1};
GN ORFNames=GOACH_11_00830 {ECO:0000313|EMBL:GAC49288.1};
OS Gordonia aichiensis NBRC 108223.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1220583 {ECO:0000313|EMBL:GAC49288.1, ECO:0000313|Proteomes:UP000010988};
RN [1] {ECO:0000313|EMBL:GAC49288.1, ECO:0000313|Proteomes:UP000010988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108223 {ECO:0000313|EMBL:GAC49288.1,
RC ECO:0000313|Proteomes:UP000010988};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia aichiensis NBRC 108223.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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|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:GAC49288.1}.
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DR EMBL; BANR01000011; GAC49288.1; -; Genomic_DNA.
DR RefSeq; WP_005175316.1; NZ_BANR01000011.1.
DR AlphaFoldDB; L7KNK0; -.
DR STRING; 1220583.GOACH_11_00830; -.
DR eggNOG; COG2124; Bacteria.
DR OrthoDB; 9801155at2; -.
DR Proteomes; UP000010988; 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; cd11037; CYP199A2-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 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:UP000010988}.
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 45387 MW; 52BBB6D5F258089F CRC64;
MTLTHSDTHT SGVGSGLPET DADPFGSEIL EDPGQFHAAL RDAGPLVHLT RYDVYAMGRY
EEVHAALTDW QSFQSGAGVG LSNFRFEKPW RPPSLLLESD PPVHDAPRSV LSSILSPRAL
RRLREHWFAD AEDFVESLPD GELDAITDIA QKFPLRVFPD AVGVGVDGRE NLLPYGDHLF
NAFGPSNELV QKGLPRIGEV SAWVNEQCVR ESLSATVYDG EATFGGQIWA AADRGDITAE
QAPTIVRSLL SAGVDTTVLG IGAVLASFAT HPDQWEMLRH NPSLARIAFD EAVRLESPVQ
TFFRTATHPV MVGDHLVPDG KKILMFLGSA NRDPRRWRNP DTFDLSRDPS GHVGFGMGIH
QCVGQHVARL EAEAVLTALV RRFRRLDVVG VPRRHHNNTL RAWEHFPIAL VS
//