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Database: UniProt
Entry: D1C8S6_SPHTD
LinkDB: D1C8S6_SPHTD
Original site: D1C8S6_SPHTD 
ID   D1C8S6_SPHTD            Unreviewed;       337 AA.
AC   D1C8S6;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=3,4-dihydroxyphenylacetate 2,3-dioxygenase {ECO:0000313|EMBL:ACZ40219.1};
GN   OrderedLocusNames=Sthe_2806 {ECO:0000313|EMBL:ACZ40219.1};
OS   Sphaerobacter thermophilus (strain DSM 20745 / S 6022).
OC   Bacteria; Thermomicrobiota; Thermomicrobia; Sphaerobacterales;
OC   Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter.
OX   NCBI_TaxID=479434 {ECO:0000313|EMBL:ACZ40219.1, ECO:0000313|Proteomes:UP000002027};
RN   [1] {ECO:0000313|Proteomes:UP000002027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC   {ECO:0000313|Proteomes:UP000002027};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., LaButti K.M., Clum A., Sun H.I., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA   Hugenholtz P., Woyke T., Wu D., Steenblock K., Schneider S., Pukall R.,
RA   Goeker M., Klenk H.P., Eisen J.A.;
RT   "The complete chromosome 2 of Sphaerobacter thermophilus DSM 20745.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ40219.1, ECO:0000313|Proteomes:UP000002027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC   {ECO:0000313|Proteomes:UP000002027};
RX   PubMed=21304676;
RA   Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA   Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Munk C., Kiss H., Chain P., Han C.,
RA   Brettin T., Detter J.C., Schuler E., Goker M., Rohde M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Desulfohalobium retbaense type strain
RT   (HR(100)).";
RL   Stand. Genomic Sci. 2:38-48(2010).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954,
CC         ECO:0000256|RuleBase:RU000683};
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC       {ECO:0000256|ARBA:ARBA00008784, ECO:0000256|RuleBase:RU000683}.
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DR   EMBL; CP001824; ACZ40219.1; -; Genomic_DNA.
DR   RefSeq; WP_012873255.1; NC_013524.1.
DR   AlphaFoldDB; D1C8S6; -.
DR   STRING; 479434.Sthe_2806; -.
DR   KEGG; sti:Sthe_2806; -.
DR   eggNOG; COG0346; Bacteria.
DR   HOGENOM; CLU_052361_3_0_0; -.
DR   InParanoid; D1C8S6; -.
DR   OrthoDB; 317332at2; -.
DR   Proteomes; UP000002027; Chromosome 2.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 2.
DR   InterPro; IPR011981; DHPA_dOase_Mn/Fe.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR018146; Glyoxalase_1_CS.
DR   InterPro; IPR037523; VOC.
DR   InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2.
DR   NCBIfam; TIGR02295; HpaD; 1.
DR   PANTHER; PTHR21366:SF27; BLL2967 PROTEIN; 1.
DR   PANTHER; PTHR21366; GLYOXALASE FAMILY PROTEIN; 1.
DR   Pfam; PF00903; Glyoxalase; 2.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR   PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR   PROSITE; PS00934; GLYOXALASE_I_1; 1.
DR   PROSITE; PS51819; VOC; 2.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797,
KW   ECO:0000256|RuleBase:RU000683};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU000683};
KW   Iron {ECO:0000256|RuleBase:RU000683};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000683};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002027}.
FT   DOMAIN          15..129
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   DOMAIN          150..272
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
SQ   SEQUENCE   337 AA;  38538 MW;  EC7B7BAE4065DBC8 CRC64;
     MGASMPPTPD FTILKTGHVE LRVTDLERAC AFYDGLLGFV ETERDDDRVY LRCLEDWEHH
     SLILTRADAP GLGHIAYRVA SERDLDALHR LATERGLPTR WVEPGEERGQ GRALRIQDPL
     GFPVEFYHAV ERVPRMLQRF HEYRGPHVMR VDHVNLQVPD VDAGTSWYRD TLGFYCSEYT
     ETEDTPPRLW AVWLHRKQNV HDVALMTGPG PRLHHVGFWL PESSNVLRAA DILSAAGYEA
     SIERGPGRHG ISNAMFLYLR DPDGNRVELY TCDYLIADPD FEPIRWRLND PKRQTYWGHP
     APPSWFNDAS HVATFDGDGY MPIQAPAMAD RPSYVGH
//
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