ID A0A150MMZ5_9BACI Unreviewed; 402 AA.
AC A0A150MMZ5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Cytochrome P450 hydroxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B4113_1508 {ECO:0000313|EMBL:KYD25837.1};
OS Geobacillus sp. B4113_201601.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1586290 {ECO:0000313|EMBL:KYD25837.1, ECO:0000313|Proteomes:UP000075654};
RN [1] {ECO:0000313|EMBL:KYD25837.1, ECO:0000313|Proteomes:UP000075654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4113_201601 {ECO:0000313|EMBL:KYD25837.1,
RC ECO:0000313|Proteomes:UP000075654};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT Foods.";
RL Submitted (JAN-2016) 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:KYD25837.1}.
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DR EMBL; LQYX01000086; KYD25837.1; -; Genomic_DNA.
DR RefSeq; WP_033842939.1; NZ_LQYX01000086.1.
DR AlphaFoldDB; A0A150MMZ5; -.
DR PATRIC; fig|1586290.3.peg.1562; -.
DR OrthoDB; 3861479at2; -.
DR Proteomes; UP000075654; 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 GO; GO:0046148; P:pigment biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR030904; CypX.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR NCBIfam; TIGR04538; P450_cycloAA_1; 1.
DR PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR46696:SF3; PULCHERRIMINIC ACID SYNTHASE; 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}.
SQ SEQUENCE 402 AA; 46147 MW; FBA25BB2BBAC19FF CRC64;
MLQQSKISIF SEAYSKDPYK FFSYFRTQEP VFYEESIDCY FVSNYEDVKY VLENEEIFTT
KMLAKRAQPV MRDRVLAQMT GKEHKEKKKM IMKGLTGENL KRLLSLFKQN AIEVLNPYLN
RGKIDLVNDF GKIFAVQSTM DMLGLDKKDQ EQIAEWHKGI AKFITSFNLS DEEIEYCFWC
SEQLEKYLLP IIESKKDSSG NDLISILKSS EFNGIKMTSQ ELLALTLNIL LAATEPVDKT
LALLFYNLLQ NPKQFEDVKN NCKLLKNAIN ETLRFKPPVQ FIPRQVSREV TIKGVLIPKN
AVIINMIGAA NRDPKAFSNP DKFDIYRSFE DNKAFTSHSQ NLAFGYGTHT CVGASLALMQ
LELVANIILN SFKNIELDES FSYEEKGLYT RGPVSLVLKF TT
//
