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Database: UniProt
Entry: Q73SK5_MYCPA
LinkDB: Q73SK5_MYCPA
Original site: Q73SK5_MYCPA 
ID   Q73SK5_MYCPA            Unreviewed;       409 AA.
AC   Q73SK5;
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_4068c {ECO:0000313|EMBL:AAS06618.1};
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:AAS06618.1, ECO:0000313|Proteomes:UP000000580};
RN   [1] {ECO:0000313|EMBL:AAS06618.1, 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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; AE016958; AAS06618.1; -; Genomic_DNA.
DR   RefSeq; WP_003879370.1; NZ_CP106873.1.
DR   AlphaFoldDB; Q73SK5; -.
DR   STRING; 262316.MAP_4068c; -.
DR   KEGG; mpa:MAP_4068c; -.
DR   PATRIC; fig|262316.17.peg.4335; -.
DR   eggNOG; COG2124; Bacteria.
DR   HOGENOM; CLU_033716_2_0_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   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; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000000580}.
SQ   SEQUENCE   409 AA;  45246 MW;  30C2B3FAA4CAD830 CRC64;
     MTVGAAPPSV FDSDLPTLHY HSDETPAQVY PRLREAQRRA AVAIGPHGPE VLSYHLVRSV
     LRDPRFQIPP GINLLAQGID SGPLWDKVAN SLLCLEGDAH HRLRSLCSKA FTPRTVARLH
     DTMAAVMNEL VDRVAAAGRC DVVTDIARPY PVPIICALLG APREDWRRFS SWADDVFKAF
     SFTVDLREVE PVVMRAWREL DDYVDEMVAR RRHNLTDDLL SDLIRVGDEG DRLDAAELRM
     LAGGLLLAGT DTTRNQVAAS VQVLCEHPDQ WELLRQRPEL AMRAVEETMR HSPIACGTLR
     LVVEDAELDG HLFPAGTAVL VNTFAANRDP VVYNDPDRVD ITREAAPPIL TFGGGVHYCL
     GANLARREIA EALNVLANRL RNPRLAGPAP WKPMVSLSGP TSLPIEFDR
//
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