FDM_PSEPU
ID FDM_PSEPU Reviewed; 399 AA.
AC Q52078;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Formaldehyde dismutase {ECO:0000303|PubMed:3514215};
DE EC=1.2.98.1 {ECO:0000269|PubMed:3514215};
GN Name=fdm {ECO:0000312|EMBL:AAA25818.1};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA25818.1, ECO:0000312|PIR:JC2516}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, AND COFACTOR.
RC STRAIN=JCM 9045 / F61;
RX PubMed=7766017; DOI=10.1271/bbb.59.197;
RA Yanase H., Noda H., Aoki K., Kita K., Kato N.;
RT "Cloning, sequence analysis, and expression of the gene encoding
RT formaldehyde dismutase from Pseudomonas putida F61.";
RL Biosci. Biotechnol. Biochem. 59:197-202(1995).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=JCM 9045 / F61;
RX PubMed=3514215; DOI=10.1111/j.1432-1033.1986.tb09548.x;
RA Kato N., Yamagami T., Shimao M., Sakazawa C.;
RT "Formaldehyde dismutase, a novel NAD-binding oxidoreductase from
RT Pseudomonas putida F61.";
RL Eur. J. Biochem. 156:59-64(1986).
RN [3] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 2-399, AND SUBUNIT.
RA Hasegawa T., Yamano A., Miura K., Katsube Y., Yanase H., Kato N.;
RT "The X-ray crystal structure of formaldehyde dismutase at 2.3 A
RT resolution.";
RL Acta Crystallogr. A 58:C102-C102(2002).
CC -!- FUNCTION: Active against a range of primary alcohols as well as some
CC secondary alcohols. Exhibits higher activity against alcohols with
CC longer carbon chains. {ECO:0000269|PubMed:3514215}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 formaldehyde + H2O = formate + H(+) + methanol;
CC Xref=Rhea:RHEA:19221, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16842, ChEBI:CHEBI:17790; EC=1.2.98.1;
CC Evidence={ECO:0000269|PubMed:3514215};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:3514215, ECO:0000269|PubMed:7766017};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:3514215,
CC ECO:0000269|PubMed:7766017};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:3514215, ECO:0000269|PubMed:7766017};
CC Name=NADH; Xref=ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:3514215, ECO:0000269|PubMed:7766017};
CC Note=Binds 1 molecule of NAD(+) or NADH per subunit.
CC {ECO:0000269|PubMed:3514215, ECO:0000269|PubMed:7766017};
CC -!- ACTIVITY REGULATION: Inhibited by the substrate analog pyrazole but not
CC by NAD analogs such as AMP, ADP, ATP or N-methylnicotinamide chloride.
CC {ECO:0000269|PubMed:3514215}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=275 nm {ECO:0000269|PubMed:3514215};
CC Note=Exhibits a small and broad shoulder at 320 nm as the
CC characteristic absorption spectrum of the reduced form of the
CC coenzyme. {ECO:0000269|PubMed:3514215};
CC Kinetic parameters:
CC KM=40 mM for ethanol (at 30 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:3514215};
CC KM=20 mM for 1-propanol (at 30 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:3514215};
CC KM=3.2 mM for 1-butanol (at 30 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:3514215};
CC KM=1.4 mM for 1-pentanol (at 30 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:3514215};
CC KM=330 mM for cyclohexanol (at 30 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:3514215};
CC Note=Does not catalyze oxidation of methanol at pH 7.0.;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000255}.
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DR EMBL; L25862; AAA25818.1; -; Genomic_DNA.
DR PIR; JC2516; JC2516.
DR RefSeq; WP_016974636.1; NZ_MCBJ01000007.1.
DR PDB; 2DPH; X-ray; 2.27 A; A/B=2-399.
DR PDBsum; 2DPH; -.
DR AlphaFoldDB; Q52078; -.
DR SMR; Q52078; -.
DR KEGG; ag:AAA25818; -.
DR EvolutionaryTrace; Q52078; -.
DR GO; GO:0047895; F:formaldehyde dismutase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; NAD;
KW Nucleotide-binding; Oxidoreductase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7766017"
FT CHAIN 2..399
FT /note="Formaldehyde dismutase"
FT /evidence="ECO:0000269|PubMed:7766017"
FT /id="PRO_0000413582"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 47..51
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 197..198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 218..219
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 299..301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 336..338
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2DPH"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2DPH"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:2DPH"
FT TURN 166..170
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:2DPH"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 281..289
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 323..328
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 344..352
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 358..363
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:2DPH"
FT HELIX 373..381
FT /evidence="ECO:0007829|PDB:2DPH"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:2DPH"
SQ SEQUENCE 399 AA; 42981 MW; E953AA05A1404EFB CRC64;
MAGNKSVVYH GTRDLRVETV PYPKLEHNNR KLEHAVILKV VSTNICGSDQ HIYRGRFIVP
KGHVLGHEIT GEVVEKGSDV ELMDIGDLVS VPFNVACGRC RNCKEARSDV CENNLVNPDA
DLGAFGFDLK GWSGGQAEYV LVPYADYMLL KFGDKEQAME KIKDLTLISD ILPTGFHGCV
SAGVKPGSHV YIAGAGPVGR CAAAGARLLG AACVIVGDQN PERLKLLSDA GFETIDLRNS
APLRDQIDQI LGKPEVDCGV DAVGFEAHGL GDEANTETPN GALNSLFDVV RAGGAIGIPG
IYVGSDPDPV NKDAGSGRLH LDFGKMWTKS IRIMTGMAPV TNYNRHLTEA ILWDQMPYLS
KVMNIEVITL DQAPDGYAKF DKGSPAKFVI DPHGMLKNK
