ID A0A345D8G5_9BURK Unreviewed; 449 AA.
AC A0A345D8G5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Terephthalate 1,2-dioxygenase, reductase component 2 {ECO:0000313|EMBL:AXF84653.1};
DE EC=1.14.12.15 {ECO:0000313|EMBL:AXF84653.1};
GN Name=tphA1II {ECO:0000313|EMBL:AXF84653.1};
GN ORFNames=DTO96_100363 {ECO:0000313|EMBL:AXF84653.1};
OS Ephemeroptericola cinctiostellae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ephemeroptericola.
OX NCBI_TaxID=2268024 {ECO:0000313|EMBL:AXF84653.1, ECO:0000313|Proteomes:UP000252182};
RN [1] {ECO:0000313|Proteomes:UP000252182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F02 {ECO:0000313|Proteomes:UP000252182};
RA Kim H.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP031124; AXF84653.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345D8G5; -.
DR KEGG; hyf:DTO96_100363; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000252182; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0018628; F:terephthalate 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR CDD; cd06198; FNR_like_3; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000313|EMBL:AXF84653.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AXF84653.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000252182};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 226..325
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 449 AA; 50189 MW; 57C36E927C38B973 CRC64;
MRKIKPFFIG FLVTLSGLWL LSDQSLFNPP YQFLPMRNVL MNYTGIIAMG VMSISMLLAV
RPARFEPFFG GLDKMYRLHK WLGITGLVFS IVHWAIKESP GWLSGLGLIA LPNRPKGPHA
GSQQATGSSI EQFFQSLKHP AESVGEWAFY IAVVLLALAL IKKFPYRYFF QTHRLMPLVY
LALVFHSTFT MNFSYYSQVV GPVMAVLMMS GTVAAIIVLF RKVGVQRKVV GVIEGIERYT
ESSVVRVNIK IKDRWAGHEA GQFAFVNFDD KEAAHPFTIS SGWKGDGHLF FLIKELGDYT
KTLASQLKAG QAVTLEGPYG QFTFKSDKPR QTWVAGGIGI TPFIARMHAL AAEPSQQKVD
LFFCVPHVDE PGFAKARADA QAAGIHLHIM AEPLDGRLDA NRLCTMVPDW QDGDVWFCGP
AGFGDSLSEA LIKKGLRPED FHRELFEMR
//
