ID Q090E2_STIAD Unreviewed; 436 AA.
AC Q090E2;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=P450 heme-thiolate protein {ECO:0000313|EMBL:ADO72986.1, ECO:0000313|EMBL:EAU66104.1};
GN OrderedLocusNames=STAUR_5214 {ECO:0000313|EMBL:ADO72986.1};
GN ORFNames=STIAU_7282 {ECO:0000313|EMBL:EAU66104.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU66104.1, ECO:0000313|Proteomes:UP000032702};
RN [1] {ECO:0000313|EMBL:EAU66104.1, ECO:0000313|Proteomes:UP000032702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU66104.1,
RC ECO:0000313|Proteomes:UP000032702};
RA Nierman W.C.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO72986.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO72986.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CP002271; ADO72986.1; -; Genomic_DNA.
DR EMBL; AAMD01000064; EAU66104.1; -; Genomic_DNA.
DR RefSeq; WP_002614536.1; NZ_AAMD01000064.1.
DR STRING; 378806.STAUR_5214; -.
DR KEGG; sur:STAUR_5214; -.
DR PATRIC; fig|378806.16.peg.5214; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_0_2_7; -.
DR OrthoDB; 4511384at2; -.
DR Proteomes; UP000001351; Chromosome.
DR Proteomes; UP000032702; 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 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}.
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 436 AA; 47683 MW; 0BF43F6E3B695EE3 CRC64;
MSVEPPNRSA PLGGLHGPPS TPQPLPAVLE GFDLTDQSRF SNGFPHQVFA RLRRDAPVLF
HPPGQSIDGD GFWVLSKHAD IREAAANPAF SSRGGGGRPH GGTHIDDARP ELPGVLFNMM
DDPRHQDFKD VMTPAMGRQA LATLEGKLRP YAAELVSSLL ARGNCDFATE VGATVGAHAI
SQLLGIPSQD WPLFAEWTSL LMGFDDREAG RPTERSQKIH MDIFRYGCQL LAAKRAGPSD
DLTSLLAGGK LASTSGEGPI SDLERQTCFC LMVLAGTEST RNMIAGGVLA LAENPEQWRA
LRADRSLVPS AVEEILRWTS PTPYNRRTAT RDIRIRDTQI RAGDKVTLWW TSANRDEDVF
SNPFSFDIRR KPNPHLAFGY GSHTCFGDHL GRLEMRVVLE ALLDRVEQIE LTGQVAWAGS
NKHTVLLRMP VALTGA
//