ID D2BC02_STRRD Unreviewed; 398 AA.
AC D2BC02;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=CYP55B1 cytochrome P450, nitric oxide reductase {ECO:0000313|EMBL:ACZ88025.1};
GN OrderedLocusNames=Sros_5256 {ECO:0000313|EMBL:ACZ88025.1};
OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS 9100).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ88025.1, ECO:0000313|Proteomes:UP000002029};
RN [1] {ECO:0000313|EMBL:ACZ88025.1, ECO:0000313|Proteomes:UP000002029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC {ECO:0000313|Proteomes:UP000002029};
RX PubMed=21304675; DOI=10.4056/sigs.631049;
RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Streptosporangium roseum type strain (NI
RT 9100).";
RL Stand. Genomic Sci. 2:29-37(2010).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CP001814; ACZ88025.1; -; Genomic_DNA.
DR RefSeq; WP_012891762.1; NC_013595.1.
DR AlphaFoldDB; D2BC02; -.
DR SMR; D2BC02; -.
DR STRING; 479432.Sros_5256; -.
DR KEGG; sro:Sros_5256; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_1_1_11; -.
DR OrthoDB; 4133219at2; -.
DR Proteomes; UP000002029; Chromosome.
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; cd11031; Cyp158A-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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002029}.
SQ SEQUENCE 398 AA; 43529 MW; A03E7D1196BA471C CRC64;
MTTEDPANFP FTFPPGIAQP PELARLREEA PVTRVTLPTG DRAWLVTRYE DVKQVLGDPR
FSRAAAELPG APQMGASNPG PDVLLGMDGP EHARLRRTAT RHFTARRVEA LRPWTRLLAE
RLMDDLISAG PPADMVSRFA LPLPLRLVLA LLGVPDEDSA RLCALTDTAF SMTRHTPQEI
LDARGRLESY MAEMIGIRRR RPTDDLLGAL VAERDKEDRL TEQQLISFAF LLVTAGYLST
SNAIASGFLT LLAHPDQLDR LRGDPELISS AAEELLRVNP SAITGALLRV ALEDVELGGV
GIRAGEGVLP AIGSANHDAL LFPDPERLDI VREDASHLAF GYGVHRCLGA HMARMELQVA
LAVLLERLPA ARLAVPEQEL VWKDHPVSRG LVALPVTW
//