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Database: UniProt
Entry: R4Z0M9_9ACTN
LinkDB: R4Z0M9_9ACTN
Original site: R4Z0M9_9ACTN 
ID   R4Z0M9_9ACTN            Unreviewed;       400 AA.
AC   R4Z0M9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BN381_350133 {ECO:0000313|EMBL:CCM64273.1};
OS   Candidatus Microthrix parvicella RN1.
OC   Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC   Microthrixaceae; Microthrix.
OX   NCBI_TaxID=1229780 {ECO:0000313|EMBL:CCM64273.1, ECO:0000313|Proteomes:UP000018291};
RN   [1] {ECO:0000313|EMBL:CCM64273.1, ECO:0000313|Proteomes:UP000018291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RN1 {ECO:0000313|EMBL:CCM64273.1,
RC   ECO:0000313|Proteomes:UP000018291};
RX   PubMed=23446830; DOI=10.1038/ismej.2013.6;
RA   Jon McIlroy S., Kristiansen R., Albertsen M., Michael Karst S.,
RA   Rossetti S., Lund Nielsen J., Tandoi V., James Seviour R., Nielsen P.H.;
RT   "Metabolic model for the filamentous 'Candidatus Microthrix parvicella'
RT   based on genomic and metagenomic analyses.";
RL   ISME J. 7:1161-1172(2013).
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:CCM64273.1}.
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DR   EMBL; CANL01000029; CCM64273.1; -; Genomic_DNA.
DR   RefSeq; WP_012228069.1; NZ_HG422565.1.
DR   AlphaFoldDB; R4Z0M9; -.
DR   STRING; 1229780.BN381_350133; -.
DR   GeneID; 78314222; -.
DR   eggNOG; COG2124; Bacteria.
DR   HOGENOM; CLU_033716_0_0_11; -.
DR   OrthoDB; 5241086at2; -.
DR   Proteomes; UP000018291; 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; 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   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:UP000018291}.
SQ   SEQUENCE   400 AA;  44660 MW;  20B3B935F86CAF2E CRC64;
     MTTATGPLQN LNLLDPELYQ TDPQALWAEL LATDELARDV NGLWVVAQHA HLREAERRNE
     DFTSGPGYRS LLSPGENNMI ALDDPEHLRQ RHLVSSRFTP KAVRRHEDWL RATIGELLDA
     ALTGGTDGRG DLEVIDELAS QLPCRLTARL LGFPEESWRD IKEWSEALMR IDAVEHDQVA
     AQDLFNAIVA FNGVLQPLAK QRRTQPADDL VSVWANADID GFTYDSIRLY HEVGLFIAGG
     AETTRTAISH GLRTFCDHPD QWNHLAAHPE AIPTAVEEVI RWVSPLNNFF RNAAADTSLA
     GADLAEGDRL ILLYPAANRD PRVFDDPNRF DTTRSPNPHL GFGQGTHFCI GANLARYELA
     ILFEELTKRI TGLSPVTEPD VEPNIFARAV RSFHLGFTLR
//
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