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Database: UniProt
Entry: F0MCQ6_PSEPM
LinkDB: F0MCQ6_PSEPM
Original site: F0MCQ6_PSEPM 
ID   F0MCQ6_PSEPM            Unreviewed;       199 AA.
AC   F0MCQ6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Phthalate 3,4-dioxygenase, beta subunit {ECO:0000313|EMBL:ADX75312.1};
GN   OrderedLocusNames=Asphe3_42470 {ECO:0000313|EMBL:ADX75312.1};
OS   Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG
OS   23796 / Sphe3) (Arthrobacter phenanthrenivorans).
OG   Plasmid pASPHE302 {ECO:0000313|EMBL:ADX75312.1,
OG   ECO:0000313|Proteomes:UP000008639}.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Pseudarthrobacter.
OX   NCBI_TaxID=930171 {ECO:0000313|EMBL:ADX75312.1, ECO:0000313|Proteomes:UP000008639};
RN   [1] {ECO:0000313|Proteomes:UP000008639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18606 / JCM 16027 / LMG 23796 / Sphe3
RC   {ECO:0000313|Proteomes:UP000008639};
RC   PLASMID=Plasmid pASPHE302 {ECO:0000313|Proteomes:UP000008639};
RX   PubMed=21677849; DOI=10.4056/sigs.1393494;
RA   Kallimanis A., Labutti K.M., Lapidus A., Clum A., Lykidis A.,
RA   Mavromatis K., Pagani I., Liolios K., Ivanova N., Goodwin L., Pitluck S.,
RA   Chen A., Palaniappan K., Markowitz V., Bristow J., Velentzas A.D.,
RA   Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT   "Complete genome sequence of Arthrobacter phenanthrenivorans type strain
RT   (Sphe3).";
RL   Stand. Genomic Sci. 4:123-130(2011).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       beta subunit family. {ECO:0000256|ARBA:ARBA00009570}.
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DR   EMBL; CP002381; ADX75312.1; -; Genomic_DNA.
DR   RefSeq; WP_011689784.1; NC_015147.1.
DR   AlphaFoldDB; F0MCQ6; -.
DR   KEGG; apn:Asphe3_42470; -.
DR   HOGENOM; CLU_102527_1_1_11; -.
DR   OrthoDB; 3212009at2; -.
DR   Proteomes; UP000008639; Plasmid pASPHE302.
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:ADX75312.1};
KW   Oxidoreductase {ECO:0000313|EMBL:ADX75312.1};
KW   Plasmid {ECO:0000313|EMBL:ADX75312.1}.
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   199 AA;  22584 MW;  A4B762E95ABE7A43 CRC64;
     MSVEADRNGK TLSEQSVLGG HAPRTQRTGE SLPFDDALHL QAHRWLVDEA YLLDAQDYDA
     WMSRIAEDVH YLMPVRVTTA LGAGYTTSPG MAHLDENRYS LSRRVARFAT EHAWTEDPPS
     RLRHYVTNVR TFRTDNPDEI IVDSAVLLFR SRGDVREAAT VSAGREDLLR RTGTGWELAR
     RTIMVDESVI RMQNLAIFL
//
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