ID F6EK23_HOYSD Unreviewed; 486 AA.
AC F6EK23;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:AEF41381.1};
GN OrderedLocusNames=AS9A_2934 {ECO:0000313|EMBL:AEF41381.1};
OS Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS (Amycolicicoccus subflavus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC Hoyosella.
OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF41381.1, ECO:0000313|Proteomes:UP000009235};
RN [1] {ECO:0000313|EMBL:AEF41381.1, ECO:0000313|Proteomes:UP000009235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX PubMed=21725023; DOI=10.1128/JB.05388-11;
RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA Wu X.L.;
RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT actinomycete isolated from crude oil-polluted soil.";
RL J. Bacteriol. 193:4538-4539(2011).
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}.
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DR EMBL; CP002786; AEF41381.1; -; Genomic_DNA.
DR RefSeq; WP_013807730.1; NC_015564.1.
DR AlphaFoldDB; F6EK23; -.
DR STRING; 443218.AS9A_2934; -.
DR KEGG; asd:AS9A_2934; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_001570_15_0_11; -.
DR OrthoDB; 9764248at2; -.
DR Proteomes; UP000009235; 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; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1.
DR PANTHER; PTHR24291:SF191; STEROL 14-DEMETHYLASE; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009235}.
FT BINDING 434
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 486 AA; 54940 MW; B1DCDC30A8802089 CRC64;
MSTLVNPKNI KHAVARHKPT IATLPGTRLI ADTLEHHHRR AEPFATPPAD SGLKPVLGDA
GLPVLGHTFE LMRLGPEYQM RRYNQLGPVS WANVFGRRGV AIAGPEATQA VLVNRDNTYT
QGGWRYLIDA FFHRGLMLLD ADEHRYHRRI MQAAFTKERL EGYVAVADEV VDAQVWKFTR
GGDVELYPTL KQLTLEVATR VFMDAGKQSD DVVTKLNDAF IACVRGGTAI VRYPVPGGRW
ARGLRGRRTL ESYFREHLPA KRRENSRDLF AALCHATSED GETFSDDDIV NHMIFLMMAA
HDTATITATA TAYHLAKHPE WQEKVRAEVA AHDGPVSPSY LDGLMTLDNV ISESLRLVAP
VPAFMRETTK DTEILGFYIP KGTFLLVDPW VNHLLPEYWT EPTRFDPERF APHRREDKQH
PFLFVPFGGG AHRCIGMKFG MLEVKTILHY LLRTYRLELK PGYDVHWDTS SLPFPTDGLP
ITLTRI
//
