ID A0A1L9NYF2_9RHOB Unreviewed; 320 AA.
AC A0A1L9NYF2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Phthalate 4,5-dioxygenase oxygenase reductase subunit {ECO:0000313|EMBL:OJI94315.1};
DE EC=1.14.12.7 {ECO:0000313|EMBL:OJI94315.1};
GN Name=pht2 {ECO:0000313|EMBL:OJI94315.1};
GN ORFNames=PFRI_14460 {ECO:0000313|EMBL:OJI94315.1};
OS Planktotalea frisia.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Planktotalea.
OX NCBI_TaxID=696762 {ECO:0000313|EMBL:OJI94315.1, ECO:0000313|Proteomes:UP000184514};
RN [1] {ECO:0000313|EMBL:OJI94315.1, ECO:0000313|Proteomes:UP000184514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH6-1 {ECO:0000313|EMBL:OJI94315.1,
RC ECO:0000313|Proteomes:UP000184514};
RA Poehlein A., Bakenhus I., Voget S., Brinkhoff T., Simon M.;
RT "Genome sequence of Planktotalea frisia SH6-1.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OJI94315.1}.
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DR EMBL; MLCB01000106; OJI94315.1; -; Genomic_DNA.
DR RefSeq; WP_072630038.1; NZ_QKZM01000022.1.
DR AlphaFoldDB; A0A1L9NYF2; -.
DR STRING; 696762.PFRI_14460; -.
DR OrthoDB; 9792185at2; -.
DR Proteomes; UP000184514; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0018620; F:phthalate 4,5-dioxygenase activity; IEA:UniProtKB-EC.
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; 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; 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:OJI94315.1};
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:OJI94315.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184514}.
FT DOMAIN 4..109
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 233..320
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 320 AA; 35523 MW; 9419D153DD9CB67A CRC64;
MSGAEKIDVT VTEIVAVNEL VTRFKFERTD GGLLPTFSGG AHTVVEMKDG AITRMNPYSL
MSDPMDQSAY TISVRRDDEG RGGSLFMHNN VSVGDKMVIS YPVNLFSLDL RAKKQLFIAG
GIGITPFLSQ IKQMERLGGA WELHYACRNA ALGSYVDELL SAHPYEAHVY YDDEKQAIAL
EELLNGQPVG THVYVCGPKG MINWVRATTE KLGWPREAVH YEEFLAPQPG KPFEVKLAVS
NKVIQVGEDE SLLEAMERSG VDAPYLCRGG ACGQCETRVI DYSGNFIHRD HWLEDDEHAS
GEKIMPCVSR FEGKTLVLDR
//
