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
//