GenomeNet

Database: UniProt
Entry: A1T2B1_MYCVP
LinkDB: A1T2B1_MYCVP
Original site: A1T2B1_MYCVP 
ID   A1T2B1_MYCVP            Unreviewed;       198 AA.
AC   A1T2B1;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Phthalate 3,4-dioxygenase, beta subunit {ECO:0000313|EMBL:ABM11311.1};
GN   OrderedLocusNames=Mvan_0464 {ECO:0000313|EMBL:ABM11311.1};
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM11311.1, ECO:0000313|Proteomes:UP000009159};
RN   [1] {ECO:0000313|EMBL:ABM11311.1, ECO:0000313|Proteomes:UP000009159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       beta subunit family. {ECO:0000256|ARBA:ARBA00009570}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000511; ABM11311.1; -; Genomic_DNA.
DR   RefSeq; WP_011777783.1; NZ_JACKSD010000013.1.
DR   AlphaFoldDB; A1T2B1; -.
DR   STRING; 350058.Mvan_0464; -.
DR   KEGG; mva:Mvan_0464; -.
DR   eggNOG; COG5517; Bacteria.
DR   HOGENOM; CLU_102527_1_1_11; -.
DR   Proteomes; UP000009159; Chromosome.
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:ABM11311.1};
KW   Oxidoreductase {ECO:0000313|EMBL:ABM11311.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009159}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   198 AA;  22485 MW;  8CC942EAFC63E82C CRC64;
     MTVDDQRTGR PMAPSVLGAH AARAQRVGDP LPFDDSRHLE AHRFLVNEAY LLDAQDYDRW
     LGVLTEDIHY YMPVRITTAA GAGFDSSPGM AHFDENKYSL ERRVARFATE HAWTEDPPSR
     LRHFITNVRT FLTDDADHLV VDSAELLFRS RGDVNESTLL SCGREDLLRR DGNALKLARR
     TICVDESVLR MQNLAVFL
//
DBGET integrated database retrieval system