ID A0A240UBM8_9BURK Unreviewed; 322 AA.
AC A0A240UBM8; A0A240TR86; A0A240U027;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Phthalate 4,5-dioxygenase {ECO:0000313|EMBL:ART58462.1};
GN ORFNames=CBP33_05510 {ECO:0000313|EMBL:ART47647.1}, CBP34_05345
GN {ECO:0000313|EMBL:ART51205.1}, CBP36_05960
GN {ECO:0000313|EMBL:ART58462.1};
OS Acidovorax carolinensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=553814 {ECO:0000313|EMBL:ART58462.1, ECO:0000313|Proteomes:UP000194440};
RN [1] {ECO:0000313|Proteomes:UP000194432, ECO:0000313|Proteomes:UP000194440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA2 {ECO:0000313|EMBL:ART47647.1}, NA3
RC {ECO:0000313|EMBL:ART51205.1}, and P4 {ECO:0000313|EMBL:ART58462.1};
RA Singleton D.R., Lee J., Dickey A.N., Stroud A., Scholl E.H., Wright F.A.,
RA Aitken M.D.;
RT "Polyphasic characterization of four soil-derived phenanthrene-degrading
RT Acidovorax strains and proposal of Acidovorax phenanthrenivorans sp. nov.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP021359; ART47647.1; -; Genomic_DNA.
DR EMBL; CP021361; ART51205.1; -; Genomic_DNA.
DR EMBL; CP021366; ART58462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A240UBM8; -.
DR KEGG; acid:CBP33_05510; -.
DR KEGG; acin:CBP34_05345; -.
DR KEGG; acip:CBP36_05960; -.
DR KEGG; acis:CBP35_12985; -.
DR OrthoDB; 370747at2; -.
DR Proteomes; UP000194432; Chromosome.
DR Proteomes; UP000194440; Chromosome.
DR Proteomes; UP000194504; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06185; PDR_like; 1.
DR Gene3D; 3.10.20.30; -; 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; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Dioxygenase {ECO:0000313|EMBL:ART58462.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Oxidoreductase {ECO:0000313|EMBL:ART58462.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000194432}.
FT DOMAIN 5..107
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 239..322
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 322 AA; 34769 MW; BBB05EC83522F8D7 CRC64;
MSTDTAMLRL QVVRAEPAAR GIQLFEFRHP AGEKLPAFTA GAHIKLRTPS GATRQYSLSN
DPAERDRYVI AVKREGNGRG GSLSLVEGVK AGATLEVGAP ENLFELDTKA SSFVLIAGGI
GITPMIAMAR SLLTEGTRRF KLYYLTRDAE GTAFLDELRA PEFASHVVLH HDQGDPARGF
DLWPVLEKPG SATGQHVYCC GPKPLMDAVR DMTGHWPSSA VHFESFGGDT APHADDQPFD
VRLAHSGLTL TVPVGKSILD IVREHGVNVP SSCESGTCGS CKTRLIEGEA DHRDLVLLDE
EKTDHIMVCV SRAKSSCLVL DL
//
