ID C4RBG5_MICS3 Unreviewed; 234 AA.
AC C4RBG5;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=p-cumate dioxygenase small subunit {ECO:0000313|EMBL:EEP69728.1};
GN ORFNames=MCAG_00055 {ECO:0000313|EMBL:EEP69728.1};
OS Micromonospora sp. (strain ATCC 39149 / NRRL 15099 / SCC 1413).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=219305 {ECO:0000313|EMBL:EEP69728.1, ECO:0000313|Proteomes:UP000010307};
RN [1] {ECO:0000313|Proteomes:UP000010307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39149 / NRRL 15099 / SCC 1413
RC {ECO:0000313|Proteomes:UP000010307};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Galagan J., Nusbaum C., Birren B.;
RT "The genome sequence of Micromonospora carbonacea var. africana strain ATCC
RT 39149.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC beta subunit family. {ECO:0000256|ARBA:ARBA00009570}.
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DR EMBL; GG657738; EEP69728.1; -; Genomic_DNA.
DR AlphaFoldDB; C4RBG5; -.
DR STRING; 219305.MCAG_00055; -.
DR eggNOG; COG5517; Bacteria.
DR HOGENOM; CLU_102527_1_1_11; -.
DR Proteomes; UP000010307; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR CDD; cd00667; ring_hydroxylating_dioxygenases_beta; 1.
DR Gene3D; 3.10.450.50; -; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR000391; Rng_hydr_dOase-bsu.
DR PANTHER; PTHR41534:SF2; 3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE SUBUNIT BETA; 1.
DR PANTHER; PTHR41534; BLR3401 PROTEIN; 1.
DR Pfam; PF00866; Ring_hydroxyl_B; 1.
DR SUPFAM; SSF54427; NTF2-like; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000313|EMBL:EEP69728.1};
KW Oxidoreductase {ECO:0000313|EMBL:EEP69728.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010307}.
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 234 AA; 26705 MW; 1C52D7669E2C069A CRC64;
MPAGLSQPHG PLLGSVTRHE QAGPGDDRRA SRPRVLAAVG PTDARRRRSP RGRSPRRDAR
GRTAMTIELT VDEAAQVRLW HRVSQFLFRE ARLLDEWRLL EWYDEMLTDD IRYSVPATDV
RGETVDALGL IDDDAARLRQ RIEQLLNGEV WCENPRSRTN RTISNVEILT DRGTHLDVAA
NVIVYRFGHG RSDAFVGKCR LELVVEGESF RVRRRVVVLD HETLYEHGKL SIIL
//
