ID A0A221W0Q8_9PSEU Unreviewed; 493 AA.
AC A0A221W0Q8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Cytochrome P450 116 {ECO:0000313|EMBL:ASO19366.1};
DE EC=1.14.-.- {ECO:0000313|EMBL:ASO19366.1};
GN Name=thcB {ECO:0000313|EMBL:ASO19366.1};
GN ORFNames=AHOG_08605 {ECO:0000313|EMBL:ASO19366.1};
OS Actinoalloteichus hoggarensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinoalloteichus.
OX NCBI_TaxID=1470176 {ECO:0000313|EMBL:ASO19366.1, ECO:0000313|Proteomes:UP000204221};
RN [1] {ECO:0000313|EMBL:ASO19366.1, ECO:0000313|Proteomes:UP000204221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45943 {ECO:0000313|EMBL:ASO19366.1,
RC ECO:0000313|Proteomes:UP000204221};
RA Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA Kalinowski J., Zotchev S.B.;
RT "Complete genome sequence of Actinoalloteichus hoggarensis DSM 45943, type
RT strain of Actinoalloteichus hoggarensis.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CP022521; ASO19366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221W0Q8; -.
DR KEGG; ahg:AHOG_08605; -.
DR Proteomes; UP000204221; Chromosome.
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; 2.
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,
KW ECO:0000313|EMBL:ASO19366.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000204221}.
SQ SEQUENCE 493 AA; 52455 MW; A4EB566AC09515B4 CRC64;
MHAASSASGS PGDIAIGMGD RPFAPYRRLV VDDAMLWAAD GTAPSTDPGD LFPRLWDPPS
VDAATPSVWY SEETDLWLVR RAADIRRVLA DVDTFRPDNA LDAFTPLSVP ALRTLARAGF
SLPPTLANNG TETHAGLRGV VASFVTPRRV EAAVPTIRRL VRSWLDDAVP DLRGGAVLDL
AVPLARDLPA RVLLHLLRVE GVDLAVLKAW SSASLELFWG VPDERRQRDL AVLAGDFHRW
LRGRLAAADP SGSDLFAALR RHRLPDGSPL STPAAVGVCY FLFIAGQETT TQLLAGLLHR
MLGEPRRWGE IAAGAPGAAE ACVEEFLRLA PPVPTWRRIT AAPTVIDGVT VPAGARLLLL
LGAAGTDGAT SPHAGCPVPS TVLEGRPLGS AGGVAAPPAD ETGRRGPVLR VEPAGPGEFH
PGRPNPRRHL AFGHGPHFCL GANLARTEAA VVLRTVASAL PRLRRVEDDP PQLRLLSFRA
PRRVLVTEAP PKG
//
