ID A0A243S6M4_9ACTN Unreviewed; 455 AA.
AC A0A243S6M4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:OUD02937.1};
GN ORFNames=CA983_12260 {ECO:0000313|EMBL:OUD02937.1};
OS Streptomyces swartbergensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=487165 {ECO:0000313|EMBL:OUD02937.1, ECO:0000313|Proteomes:UP000195105};
RN [1] {ECO:0000313|EMBL:OUD02937.1, ECO:0000313|Proteomes:UP000195105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMC13 {ECO:0000313|EMBL:OUD02937.1};
RA Le Roes-Hill M., Prins A., Durrell K.A.;
RT "Biotechnological potential of actinobacteria isolated from South African
RT environments.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR602403-1};
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:OUD02937.1}.
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DR EMBL; NGFN01000057; OUD02937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A243S6M4; -.
DR Proteomes; UP000195105; 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 Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24291:SF189; CYTOCHROME P450 4V2; 1.
DR PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
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|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
FT BINDING 395
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 455 AA; 50754 MW; 37C9E35105CC8CF7 CRC64;
MTSTAPPPIP RAAGSFPLIG HALKMRDNLG FIDSLRETRE PLVEIVLQPG TRTVVVQDPA
LIHQMLKALA PTLDKGRLYD KLGQLLGDSV VTATGRTHVR KRRQVQPAFA HYEISRYVDI
MRAEVTATVA GWEPGRTLDV REAMVGLSLD MLAKTVFSGS LDDAVFRRLR SDLSVVMNDV
GVRMMLPDWA ERLPLPFNRR FDRARAGVRA TINTAVDELQ ASGHDTGDML SMLLRAIDEE
TGEPLTGDQV CSEILTLAVA GTETTASVLS WTLYELARHP GIEARLLAEL DEVLGERPVA
FDDVTRLPYL NRVITETLRL HHPGWLVTRR TTEEIRLGEW TLPAGTELAY CQHALHRDPE
RFPDPLTFDP DRWNDAAQEP PPGAFLPFGE GKHKCMGDRF ARTEMVTALA TMLRSVRLEL
AEGQVIRQVA RLTVRPRALR MTVRPRNRPR AGVGL
//
