PDR_BURCE
ID PDR_BURCE Reviewed; 322 AA.
AC P33164; Q9ZFR3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Phthalate dioxygenase reductase;
DE Short=PDR;
DE EC=1.-.-.-;
GN Name=ophA1;
OS Burkholderia cepacia (Pseudomonas cepacia).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29424 / DBO1;
RX PubMed=9851995; DOI=10.1128/jb.180.24.6529-6537.1998;
RA Chang H.K., Zylstra G.J.;
RT "Novel organization of the genes for phthalate degradation from
RT Burkholderia cepacia DBO1.";
RL J. Bacteriol. 180:6529-6537(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FMN AND IRON-SULFUR
RP (2FE-2S), AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 29424 / DBO1;
RX PubMed=1280857; DOI=10.1126/science.1280857;
RA Correll C.C., Batie C.J., Ballou D.P., Ludwig M.L.;
RT "Phthalate dioxygenase reductase: a modular structure for electron transfer
RT from pyridine nucleotides to [2Fe-2S].";
RL Science 258:1604-1610(1992).
CC -!- FUNCTION: Component of the electron transfer chain involved in pyridine
CC nucleotide-dependent dihydroxylation of phthalate. Utilizes FMN to
CC mediate electron transfer from the two-electron donor, NADH, to the
CC one-electron acceptor, (2Fe-2S).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:1280857};
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the PDR/VanB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF095748; AAD03550.1; -; Genomic_DNA.
DR PIR; A44230; A44230.
DR PDB; 2PIA; X-ray; 2.00 A; A=2-322.
DR PDBsum; 2PIA; -.
DR AlphaFoldDB; P33164; -.
DR SMR; P33164; -.
DR EvolutionaryTrace; P33164; -.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 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; IPR000951; Ph_dOase_redase.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Electron transport;
KW Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..322
FT /note="Phthalate dioxygenase reductase"
FT /id="PRO_0000189398"
FT DOMAIN 7..109
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT DOMAIN 239..322
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 56..57
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:1280857,
FT ECO:0007744|PDB:2PIA"
FT BINDING 73..75
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:1280857,
FT ECO:0007744|PDB:2PIA"
FT BINDING 81..84
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:1280857,
FT ECO:0007744|PDB:2PIA"
FT BINDING 125
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:1280857,
FT ECO:0007744|PDB:2PIA"
FT BINDING 226
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:1280857,
FT ECO:0007744|PDB:2PIA"
FT BINDING 273
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:1280857,
FT ECO:0007744|PDB:2PIA"
FT BINDING 275
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:1280857,
FT ECO:0007744|PDB:2PIA"
FT BINDING 278
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:1280857,
FT ECO:0007744|PDB:2PIA"
FT BINDING 281
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:1280857,
FT ECO:0007744|PDB:2PIA"
FT BINDING 309
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:1280857,
FT ECO:0007744|PDB:2PIA"
FT TURN 4..8
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 10..21
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:2PIA"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:2PIA"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2PIA"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 139..149
FT /evidence="ECO:0007829|PDB:2PIA"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:2PIA"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:2PIA"
FT TURN 163..168
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:2PIA"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:2PIA"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:2PIA"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:2PIA"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:2PIA"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:2PIA"
FT TURN 299..304
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:2PIA"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:2PIA"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:2PIA"
SQ SEQUENCE 322 AA; 35665 MW; A550988FF80059A6 CRC64;
MTTPQEDGFL RLKIASKEKI ARDIWSFELT DPQGAPLPPF EAGANLTVAV PNGSRRTYSL
CNDSQERNRY VIAVKRDSNG RGGSISFIDD TSEGDAVEVS LPRNEFPLDK RAKSFILVAG
GIGITPMLSM ARQLRAEGLR SFRLYYLTRD PEGTAFFDEL TSDEWRSDVK IHHDHGDPTK
AFDFWSVFEK SKPAQHVYCC GPQALMDTVR DMTGHWPSGT VHFESFGATN TNARENTPFT
VRLSRSGTSF EIPANRSILE VLRDANVRVP SSCESGTCGS CKTALCSGEA DHRDMVLRDD
EKGTQIMVCV SRAKSAELVL DL
