TODA_PSEP1
ID TODA_PSEP1 Reviewed; 410 AA.
AC A5W4E9; P13452;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Toluene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component;
DE EC=1.18.1.3;
GN Name=todA; OrderedLocusNames=Pput_2878;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-13.
RX PubMed=2670929; DOI=10.1016/s0021-9258(18)63793-7;
RA Zylstra G.J., Gibson D.T.;
RT "Toluene degradation by Pseudomonas putida F1. Nucleotide sequence of the
RT todC1C2BADE genes and their expression in Escherichia coli.";
RL J. Biol. Chem. 264:14940-14946(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the electron transfer component of toluene 1,2-
CC dioxygenase, transfers electrons from ferredoxin (TodB) to NADH.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16521, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.18.1.3;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC -!- SUBUNIT: This dioxygenase system consists of four proteins: the two
CC subunits of the hydroxylase component (todC1 and todC2), a ferredoxin
CC (TodB) and a ferredoxin reductase (TodA).
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin reductase family. {ECO:0000305}.
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DR EMBL; J04996; AAA26008.1; -; Genomic_DNA.
DR EMBL; CP000712; ABQ79009.1; -; Genomic_DNA.
DR PIR; D36516; D36516.
DR RefSeq; WP_012052598.1; NC_009512.1.
DR PDB; 3EF6; X-ray; 1.80 A; A=1-410.
DR PDB; 4EMI; X-ray; 1.81 A; A=1-410.
DR PDB; 4EMJ; X-ray; 2.40 A; A=1-410.
DR PDBsum; 3EF6; -.
DR PDBsum; 4EMI; -.
DR PDBsum; 4EMJ; -.
DR AlphaFoldDB; A5W4E9; -.
DR SMR; A5W4E9; -.
DR STRING; 351746.Pput_2878; -.
DR EnsemblBacteria; ABQ79009; ABQ79009; Pput_2878.
DR KEGG; ppf:Pput_2878; -.
DR eggNOG; COG1251; Bacteria.
DR HOGENOM; CLU_003291_4_0_6; -.
DR OMA; RVEHWTG; -.
DR OrthoDB; 1149616at2; -.
DR BioCyc; MetaCyc:MON-11350; -.
DR UniPathway; UPA00273; -.
DR EvolutionaryTrace; A5W4E9; -.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR028202; Reductase_C.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW FAD; Flavoprotein; NAD; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2670929"
FT CHAIN 2..410
FT /note="Toluene 1,2-dioxygenase system ferredoxin--NAD(+)
FT reductase component"
FT /id="PRO_0000314468"
FT BINDING 4..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 145..173
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3EF6"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:3EF6"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:3EF6"
FT TURN 48..53
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3EF6"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:3EF6"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3EF6"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:3EF6"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:3EF6"
FT HELIX 153..164
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:3EF6"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:3EF6"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:3EF6"
FT HELIX 244..248
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:3EF6"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:3EF6"
FT HELIX 292..306
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 334..344
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 348..357
FT /evidence="ECO:0007829|PDB:3EF6"
FT STRAND 360..368
FT /evidence="ECO:0007829|PDB:3EF6"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:3EF6"
FT HELIX 388..392
FT /evidence="ECO:0007829|PDB:3EF6"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:3EF6"
SQ SEQUENCE 410 AA; 42942 MW; 934CF2EDD2AB1450 CRC64;
MATHVAIIGN GVGGFTTAQA LRAEGFEGRI SLIGDEPHLP YDRPSLSKAV LDGSLERPPI
LAEADWYGEA RIDMLTGPEV TALDVQTRTI SLDDGTTLSA DAIVIATGSR ARTMALPGSQ
LPGVVTLRTY GDVQVLRDSW TSATRLLIVG GGLIGCEVAT TARKLGLSVT ILEAGDELLV
RVLGRRIGAW LRGLLTELGV QVELGTGVVG FSGEGQLEQV MASDGRSFVA DSALICVGAE
PADQLARQAG LACDRGVIVD HCGATLAKGV FAVGDVASWP LRAGGRRSLE TYMNAQRQAA
AVAAAILGKN VSAPQLPVSW TEIAGHRMQM AGDIEGPGDF VSRGMPGSGA ALLFRLQERR
IQAVVAVDAP RDFALATRLV EARAAIEPAR LADLSNSMRD FVRANEGDLT
