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Database: UniProt
Entry: A0A0F5PDQ0_9SPHN
LinkDB: A0A0F5PDQ0_9SPHN
Original site: A0A0F5PDQ0_9SPHN 
ID   A0A0F5PDQ0_9SPHN        Unreviewed;       262 AA.
AC   A0A0F5PDQ0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Aromatic ring-opening dioxygenase LigA {ECO:0000313|EMBL:KKC26515.1};
GN   ORFNames=WP12_07980 {ECO:0000313|EMBL:KKC26515.1};
OS   Sphingomonas sp. SRS2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=133190 {ECO:0000313|EMBL:KKC26515.1, ECO:0000313|Proteomes:UP000033680};
RN   [1] {ECO:0000313|EMBL:KKC26515.1, ECO:0000313|Proteomes:UP000033680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRS2 {ECO:0000313|EMBL:KKC26515.1,
RC   ECO:0000313|Proteomes:UP000033680};
RA   Nielsen T.K., Sorensen S.R., Hansen L.H.;
RT   "Draft genome sequence of isoproturon-mineralizing Sphingomonas sp. SRS2,
RT   isolated from an agricultural field in the United Kingdom.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the DODA-type extradiol aromatic ring-opening
CC       dioxygenase family. {ECO:0000256|ARBA:ARBA00007581}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKC26515.1}.
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DR   EMBL; LARW01000072; KKC26515.1; -; Genomic_DNA.
DR   RefSeq; WP_046193187.1; NZ_LARW01000072.1.
DR   AlphaFoldDB; A0A0F5PDQ0; -.
DR   STRING; 133190.WP12_07980; -.
DR   PATRIC; fig|133190.4.peg.3456; -.
DR   OrthoDB; 9790889at2; -.
DR   Proteomes; UP000033680; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0016701; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR   CDD; cd07363; 45_DOPA_Dioxygenase; 1.
DR   Gene3D; 3.40.830.10; LigB-like; 1.
DR   InterPro; IPR014436; Extradiol_dOase_DODA.
DR   InterPro; IPR004183; Xdiol_dOase_suB.
DR   PANTHER; PTHR30096:SF0; 4,5-DOPA DIOXYGENASE EXTRADIOL-LIKE PROTEIN; 1.
DR   PANTHER; PTHR30096; UNCHARACTERIZED; 1.
DR   Pfam; PF02900; LigB; 1.
DR   PIRSF; PIRSF006157; Doxgns_DODA; 1.
DR   SUPFAM; SSF53213; LigB-like; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000313|EMBL:KKC26515.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033680};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          26..249
FT                   /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT                   subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF02900"
SQ   SEQUENCE   262 AA;  28062 MW;  3F7CB62A345CC1F3 CRC64;
     MTRQPSFYIP HGGGPCFFMD DPAGTWTGMA AFLRGLPDRL PARPSAILIV SGHWETDGFA
     FTGAPNPPLV FDYYGFPPHT YELSYPAPGD PALADRAAAL LQAAGLQAGV DAERGLDHGV
     FVPLKVAFPD ADAPVVEMSL DTRLDPGLAW RAGRALRPLR DEGVLILGAG MSFHNMRAYR
     HAEATAPSVA FDDWLANAIE GDPAAREVAL AGWADAPGGR FAHPREEHLL PLMVAAGASD
     GPGHRIYSEV VMETMISAFR FD
//
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