TMOF_PSEME
ID TMOF_PSEME Reviewed; 326 AA.
AC Q03304; Q6Q8Q2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Toluene-4-monooxygenase system, ferredoxin--NAD(+) reductase component {ECO:0000303|PubMed:1429451};
DE Short=T4MO {ECO:0000303|PubMed:1429451};
DE EC=1.18.1.3 {ECO:0000269|PubMed:17964805};
DE AltName: Full=Ferredoxin--NAD(+) reductase {ECO:0000305};
DE AltName: Full=Toluene-4-monooxygenase systme, electron transfer component {ECO:0000303|PubMed:17964805};
GN Name=tmoF {ECO:0000303|PubMed:1429451};
OS Pseudomonas mendocina.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=300;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, AND FUNCTION.
RC STRAIN=KR1;
RX PubMed=1429451; DOI=10.1128/jb.174.22.7253-7261.1992;
RA Yen K.-M., Karl M.R.;
RT "Identification of a new gene, tmoF, in the Pseudomonas mendocina KR1 gene
RT cluster encoding toluene-4-monooxygenase.";
RL J. Bacteriol. 174:7253-7261(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=KR1 {ECO:0000312|EMBL:AAS66665.1};
RX PubMed=15240250; DOI=10.1128/aem.70.7.3814-3820.2004;
RA Tao Y., Fishman A., Bentley W.E., Wood T.K.;
RT "Oxidation of benzene to phenol, catechol, and 1,2,3-trihydroxybenzene by
RT toluene 4-monooxygenase of Pseudomonas mendocina KR1 and toluene 3-
RT monooxygenase of Ralstonia pickettii PKO1.";
RL Appl. Environ. Microbiol. 70:3814-3820(2004).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=17964805; DOI=10.1016/j.pep.2007.09.007;
RA Bailey L.J., Elsen N.L., Pierce B.S., Fox B.G.;
RT "Soluble expression and purification of the oxidoreductase component of
RT toluene 4-monooxygenase.";
RL Protein Expr. Purif. 57:9-16(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 2-326 IN COMPLEX WITH FAD AND
RP IRON-SULFUR (2FE-2S), COFACTOR, AND SUBUNIT.
RX PubMed=26309236; DOI=10.1021/acs.biochem.5b00692;
RA Acheson J.F., Moseson H., Fox B.G.;
RT "Structure of T4moF, the toluene 4-monooxygenase ferredoxin
RT oxidoreductase.";
RL Biochemistry 54:5980-5988(2015).
CC -!- FUNCTION: Reductase component of the toluene-4-monooxygenase
CC multicomponent enzyme system which catalyzes the O2- and NADH-dependent
CC hydroxylation of toluene to form p-cresol (PubMed:15240250,
CC PubMed:17964805). Ferredoxin reductase catalyzes the transfer of
CC electrons from NADH to ferredoxin (TmoC) (PubMed:17964805).
CC {ECO:0000269|PubMed:15240250, ECO:0000269|PubMed:17964805,
CC ECO:0000305|PubMed:1429451}.
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 Evidence={ECO:0000269|PubMed:17964805};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17964805, ECO:0000269|PubMed:26309236};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:17964805};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:17964805, ECO:0000269|PubMed:26309236};
CC Note=Binds 1 2Fe-2S cluster. {ECO:0000269|PubMed:17964805,
CC ECO:0000269|PubMed:26309236};
CC -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC {ECO:0000305|PubMed:15240250}.
CC -!- SUBUNIT: Monomer (PubMed:26309236). The alkene monooxygenase
CC multicomponent enzyme system is composed of an electron transfer
CC component and a monooxygenase component interacting with the effector
CC protein TmoD. The electron transfer component is composed of a
CC ferredoxin reductase (TmoF) and a ferredoxin (TmoC), and the
CC monooxygenase component is formed by a heterohexamer (dimer of
CC heterotrimers) of two alpha subunits (TmoA), two beta subunits (TmoE)
CC and two gamma subunits (TmoB). {ECO:0000269|PubMed:26309236}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin reductase 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; M95045; AAA26004.1; -; Genomic_DNA.
DR EMBL; AY552601; AAS66665.1; -; Genomic_DNA.
DR PIR; A47016; A47016.
DR PDB; 4WQM; X-ray; 1.62 A; A=2-326.
DR PDBsum; 4WQM; -.
DR AlphaFoldDB; Q03304; -.
DR SMR; Q03304; -.
DR KEGG; ag:AAA26004; -.
DR BioCyc; MetaCyc:MON-2501; -.
DR BRENDA; 1.14.13.236; 31258.
DR UniPathway; UPA00273; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
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; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
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; Aromatic hydrocarbons catabolism;
KW Direct protein sequencing; FAD; Flavoprotein; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..326
FT /note="Toluene-4-monooxygenase system, ferredoxin--NAD(+)
FT reductase component"
FT /id="PRO_0000167658"
FT DOMAIN 1..92
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 100..195
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 95..326
FT /note="Ferredoxin-reductase"
FT BINDING 36
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:26309236,
FT ECO:0007744|PDB:4WQM"
FT BINDING 41
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:26309236,
FT ECO:0007744|PDB:4WQM"
FT BINDING 44
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:26309236,
FT ECO:0007744|PDB:4WQM"
FT BINDING 76
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:26309236,
FT ECO:0007744|PDB:4WQM"
FT BINDING 146..149
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26309236,
FT ECO:0007744|PDB:4WQM"
FT BINDING 162..164
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26309236,
FT ECO:0007744|PDB:4WQM"
FT BINDING 170..172
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26309236,
FT ECO:0007744|PDB:4WQM"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:4WQM"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:4WQM"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4WQM"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 101..123
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:4WQM"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:4WQM"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:4WQM"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:4WQM"
FT HELIX 211..223
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:4WQM"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:4WQM"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:4WQM"
FT HELIX 281..288
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:4WQM"
FT HELIX 299..310
FT /evidence="ECO:0007829|PDB:4WQM"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:4WQM"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:4WQM"
SQ SEQUENCE 326 AA; 35983 MW; 17889D794FC092EE CRC64;
MFNIQSDDLL HHFEADSNDT LLSAALRAEL VFPYECNSGG CGACKIELLE GEVSNLWPDA
PGLAARELRK NRFLACQCKP LSDLKIKVIN RAEGRASHPP KRFSTRVVSK RFLSDEMFEL
RLEAEQKVVF SPGQYFMVDV PELGTRAYSA ANPVDGNTLT LIVKAVPNGK VSCALANETI
ETLQLDGPYG LSVLKTADET QSVFIAGGSG IAPMVSMVNT LIAQGYEKPI TVFYGSRLEA
ELEAAETLFG WKENLKLINV SSSVVGNSEK KYPTGYVHEI IPEYMEGLLG AEFYLCGPPQ
MINSVQKLLM IENKVPFEAI HFDRFF
