ID A0A0Q8XN33_9SPHN Unreviewed; 411 AA.
AC A0A0Q8XN33;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Cytochrome {ECO:0000313|EMBL:KRC81257.1};
GN ORFNames=ASE13_02285 {ECO:0000313|EMBL:KRC81257.1};
OS Sphingomonas sp. Root241.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736501 {ECO:0000313|EMBL:KRC81257.1, ECO:0000313|Proteomes:UP000051629};
RN [1] {ECO:0000313|EMBL:KRC81257.1, ECO:0000313|Proteomes:UP000051629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root241 {ECO:0000313|EMBL:KRC81257.1,
RC ECO:0000313|Proteomes:UP000051629};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC81257.1, ECO:0000313|Proteomes:UP000051629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root241 {ECO:0000313|EMBL:KRC81257.1,
RC ECO:0000313|Proteomes:UP000051629};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRC81257.1}.
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DR EMBL; LMIV01000001; KRC81257.1; -; Genomic_DNA.
DR RefSeq; WP_056610856.1; NZ_LMIV01000001.1.
DR AlphaFoldDB; A0A0Q8XN33; -.
DR STRING; 1736501.ASE13_02285; -.
DR OrthoDB; 5522954at2; -.
DR Proteomes; UP000051629; 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; cd11033; CYP142-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}.
SQ SEQUENCE 411 AA; 46987 MW; 0EB73570C3FEB0E6 CRC64;
MATLATESSP EKAMDPLDMS RAELYRDDVW QAPFRELREK APVYYTEHSA FGPYWSVSSY
KPIVQVESLP DLYSSEAGGI TIADLQEGDI KMPMFIAMDR PKHTGQRRTV APAFTPSEMV
RMNDNIRTRS AEILDSLPVG QEFDWVDTVS IELTTQMLAI LFDFPWEERR LLTYWSDWAG
DIEIAKDPVR KEERRNILFE CAAYFGNLWQ GKLGKEPTPD LISMMIHSDA MSHMDQMEFL
GNLILLIVGG NDTTRNSMSA YAWGLEQFPD ERAKLEADPA LIPNAVQEII RWQTPLAHMR
RTATQDSELE GQQICAGDKL ALWYLSANRD ESMFPNADKI IVDRGNARRH LAFGHGIHRC
VGARLAELQI GILLEEMAKR RLRVNVLREP ERVAACFVHG YRKMPVELSR Y
//
