ID B3QXV4_CHLT3 Unreviewed; 266 AA.
AC B3QXV4;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Extradiol ring-cleavage dioxygenase class III protein subunit B {ECO:0000313|EMBL:ACF13482.1};
GN OrderedLocusNames=Ctha_1018 {ECO:0000313|EMBL:ACF13482.1};
OS Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chloroherpetonaceae;
OC Chloroherpeton.
OX NCBI_TaxID=517418 {ECO:0000313|EMBL:ACF13482.1, ECO:0000313|Proteomes:UP000001208};
RN [1] {ECO:0000313|EMBL:ACF13482.1, ECO:0000313|Proteomes:UP000001208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35110 / GB-78 {ECO:0000313|Proteomes:UP000001208};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroherpeton thalassium ATCC 35110.";
RL Submitted (JUN-2008) 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}.
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DR EMBL; CP001100; ACF13482.1; -; Genomic_DNA.
DR AlphaFoldDB; B3QXV4; -.
DR STRING; 517418.Ctha_1018; -.
DR KEGG; cts:Ctha_1018; -.
DR eggNOG; COG3384; Bacteria.
DR HOGENOM; CLU_046582_0_0_10; -.
DR OrthoDB; 9790889at2; -.
DR Proteomes; UP000001208; Chromosome.
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:ACF13482.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001208};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 31..249
FT /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT subunit B"
FT /evidence="ECO:0000259|Pfam:PF02900"
SQ SEQUENCE 266 AA; 30358 MW; 25A3EAACB7CAAA18 CRC64;
MKNKTKTILF LSHGGGPLPL LGDESHSEMV KNLKILAEEI DKPSAIILIS AHWEEEIPTI
TSAATPSLSY DYYGFPEESY QIQYPCPGEP LLANEVRRLL NKSGINTRLD EHRGFDHGLF
VPLKIMYPNA DIPCVQLSLL KSLNPAEHIR IGSALSEIKY EKLLIIGSGF SFHNMRAFFN
TQTAETKAMN ESFEQWLIDT CSNQEIGEAE RTKRLENWEN APFGRYCHPR EEHLLPLHIC
YGVAQSACKK YIELRILNKK SSFYLW
//