ID Q73YH7_MYCPA Unreviewed; 389 AA.
AC Q73YH7;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=MAP_1979 {ECO:0000313|EMBL:AAS04296.1};
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316 {ECO:0000313|EMBL:AAS04296.1, ECO:0000313|Proteomes:UP000000580};
RN [1] {ECO:0000313|EMBL:AAS04296.1, ECO:0000313|Proteomes:UP000000580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580};
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016958; AAS04296.1; -; Genomic_DNA.
DR RefSeq; WP_003878177.1; NZ_CP106873.1.
DR AlphaFoldDB; Q73YH7; -.
DR STRING; 262316.MAP_1979; -.
DR KEGG; mpa:MAP_1979; -.
DR PATRIC; fig|262316.17.peg.2099; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_0_1_11; -.
DR Proteomes; UP000000580; 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 CDD; cd11035; P450cam-like; 1.
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:SF2; CYTOCHROME P450 130; 1.
DR PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
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 Reference proteome {ECO:0000313|Proteomes:UP000000580}.
SQ SEQUENCE 389 AA; 43529 MW; 29403DC3AF689F9D CRC64;
MTEAGGFVDQ TVTGVAEPQP MYKALRESNP VFRSTQAVVL SRLADIEMAL KHTELFSSNM
DAVDLGNVRP LIPLQIDPPD HAKYRRILDP LFTPREMARR EPLVTELVNE MIDRFAPRGE
CDFHAEFAVP LPCTVFLQLL GLPLEDLDRF LLWKDGVIRP AGDSGFDRRH ESSAGVAQQI
YEYFDKAIDE HIAVPRDDVL SAMIAADVGG QPLSREELLD ICFLFLIAGL DTVTDSLDCF
FVYLARHPQH RRQLVERPDV LPGAVEELLR WETPVPGVAR VATQDVEVGG CPISKGERVS
PLLGAANTDP AEFPDPEIVD FTRSPNRHRA FGGGPHRCLG SHLARMELRV ALREFHRRIP
DYEIRPGTQL TYTAALRSVE SLPLVFPVR
//