ID A0A1V8M371_9GAMM Unreviewed; 538 AA.
AC A0A1V8M371;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:OQK15982.1};
GN ORFNames=AU255_17210 {ECO:0000313|EMBL:OQK15982.1};
OS Methyloprofundus sedimenti.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methyloprofundus.
OX NCBI_TaxID=1420851 {ECO:0000313|EMBL:OQK15982.1, ECO:0000313|Proteomes:UP000191980};
RN [1] {ECO:0000313|EMBL:OQK15982.1, ECO:0000313|Proteomes:UP000191980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF1 {ECO:0000313|EMBL:OQK15982.1,
RC ECO:0000313|Proteomes:UP000191980};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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}.
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:OQK15982.1}.
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DR EMBL; LPUF01000003; OQK15982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8M371; -.
DR STRING; 1420851.AU255_17210; -.
DR OrthoDB; 9764248at2; -.
DR Proteomes; UP000191980; 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:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11042; CYP51-like; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24304:SF2; 24-HYDROXYCHOLESTEROL 7-ALPHA-HYDROXYLASE; 1.
DR PANTHER; PTHR24304; CYTOCHROME P450 FAMILY 7; 1.
DR Pfam; PF13370; Fer4_13; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602403-1};
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 Reference proteome {ECO:0000313|Proteomes:UP000191980}.
FT BINDING 397
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 538 AA; 61451 MW; BD84763C2CE7A22A CRC64;
MTEQPSPTNK EPEKMPGGLP LIGHMLKFGK NPFDYMTLLR SKLGEIGEFR LFHQQMVLLT
GPEGNEAFFR APDDQLDQNE AYKVMTPIFG KGVVFDAPPH IKDQQLKMLM PVLRDKPMRT
YSKVIVQEVE EAIKDWGDSG EVDILEFMKQ LTIYTSSHCL LGNEFRYELN EEFAHLYHDL
ENGMHPLAFI FPYLPIPILR RRDKARVRLQ ELVTAIIEKR AQKTEKSDDA FQMLIDVRYD
DGSPLSPHEI TGLLIGTLFA GHHTTAGTAA WITLELARNP KYMDKVLQEF DTLYGHEGEV
TFQSLREIPV FERVIKEVLR LHPPLIFLIR KVAKDLKFKD YIIKAGKYVC VSPRVSHRIP
EIFPDPEKFD PERFTKERQE DAIPFSWVAF GGGRHKCSGN AFAMLQLKAI YAILLRRYKF
ELVGTPESYQ DDYKQMVVQP GSPCMVRYTK RGNIKQTATA SKDTVANTVT KLNCFKIDID
MDLCQGHANC MAEAPEIFQV DDKGKLSILQ DTPNNTLLKK AQAAAEYCPT SAIKIIQD
//