ID A0A244EC89_9BURK Unreviewed; 384 AA.
AC A0A244EC89;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Cytochrome {ECO:0000313|EMBL:OUM02080.1};
GN ORFNames=A8M77_13320 {ECO:0000313|EMBL:OUM02080.1};
OS Variovorax sp. JS1663.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1851577 {ECO:0000313|EMBL:OUM02080.1, ECO:0000313|Proteomes:UP000195166};
RN [1] {ECO:0000313|EMBL:OUM02080.1, ECO:0000313|Proteomes:UP000195166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1663 {ECO:0000313|EMBL:OUM02080.1};
RX PubMed=28526789;
RA Mahan K.M., Zheng H., Fida T.T., Parry R.J., Graham D.E., Spain J.C.;
RT "A novel, iron-dependent enzyme that catalyzes the initial step in the
RT biodegradation of N-nitroglycine by Variovorax sp. strain JS1663.";
RL Appl. Environ. Microbiol. 83:0-0(2017).
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:OUM02080.1}.
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DR EMBL; LYMK01000013; OUM02080.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A244EC89; -.
DR OrthoDB; 4168525at2; -.
DR Proteomes; UP000195166; 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 CDD; cd11036; AknT-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; 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:UP000195166}.
SQ SEQUENCE 384 AA; 40150 MW; C43FA4AC85C0C7C2 CRC64;
MNDSLAPPAD AIAAVTHPDP YPWYARLREG PALVRDEGLR LWVASRAEVM REVLAHPAMR
VRPAAEPVPR AIAGTPAGEL FGRLVRMNDG APHAAHKPVL QRALAGLDLG IARAGMRRIA
PQLPAATAAE ACFTWPVAGV AHLLGFDDEA LPPLAAWTRD FVACLSPLSS EAQLQAASEA
AAALMARFEA LVAARPARED SLLAAVRGQA PDDGSRALLA NLVGLLSQTC EATAGLMGNS
LVVLAREPGL HAQITAQPLL LEALVAETAR HDPSVQNTRR FAAEPLTVAG TALAAGDAVL
LVLGAAHRDP ALNPAPDRFD LQRAERRMLG FGHGLHACPG QALACTLAAA GVEALLAGGL
DPAGLAERGW DYRPSANARI PVFR
//
