FDH_PSESR
ID FDH_PSESR Reviewed; 401 AA.
AC P33160;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Formate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000303|PubMed:8484798};
DE Short=FDH {ECO:0000255|HAMAP-Rule:MF_03210};
DE EC=1.17.1.9 {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:12144528, ECO:0000269|PubMed:8484798};
DE AltName: Full=NAD-dependent formate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000303|PubMed:1954846};
OS Pseudomonas sp. (strain 101) (Achromobacter parvulus T1).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=33067;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1954846;
RA Tishkov V.I., Galkin A.G., Egorov A.M.;
RT "NAD-dependent formate dehydrogenase of methylotrophic bacteria Pseudomonas
RT sp. 101: cloning, expression, and study of the genetic structure.";
RL Dokl. Akad. Nauk SSSR 317:745-748(1991).
RN [2]
RP PROTEIN SEQUENCE OF 2-394.
RX PubMed=2357236;
RA Popov V.O., Shumilin I.A., Ustinnikova T.B., Lamzin V.S., Egorov T.A.;
RT "NAD-dependent formate dehydrogenase from methylotrophic bacteria
RT Pseudomonas sp. 101. I. Amino acid sequence.";
RL Bioorg. Khim. 16:324-335(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=1597184; DOI=10.1111/j.1432-1033.1992.tb16945.x;
RA Lamzin V.S., Aleshin A.E., Strokopytov B.V., Yukhnevich M.G., Popov V.O.,
RA Harutyunyan E.H., Wilson K.S.;
RT "Crystal structure of NAD-dependent formate dehydrogenase.";
RL Eur. J. Biochem. 206:441-452(1992).
RN [4]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12144528; DOI=10.1042/bj20020379;
RA Serov A.E., Popova A.S., Fedorchuk V.V., Tishkov V.I.;
RT "Engineering of coenzyme specificity of formate dehydrogenase from
RT Saccharomyces cerevisiae.";
RL Biochem. J. 367:841-847(2002).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF CYS-256.
RX PubMed=8484798; DOI=10.1006/bbrc.1993.1511;
RA Tishkov V.I., Galkin A.G., Marchenko G.N., Egorova O.A., Sheluho D.V.,
RA Kulakova L.B., Dementieva L.A., Egorov A.M.;
RT "Catalytic properties and stability of a Pseudomonas sp.101 formate
RT dehydrogenase mutants containing Cys-255-Ser and Cys-255-Met
RT replacements.";
RL Biochem. Biophys. Res. Commun. 192:976-981(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-394 IN COMPLEX WITH NAD.
RX PubMed=8114093; DOI=10.1006/jmbi.1994.1188;
RA Lamzin V.S., Dauter Z., Popov V.O., Harutyunyan E.H., Wilson K.S.;
RT "High resolution structures of holo and apo formate dehydrogenase.";
RL J. Mol. Biol. 236:759-785(1994).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), AND SUBUNIT.
RX DOI=10.1134/1.2049398;
RA Filippova E.V., Polyakov K.M., Tikhonova T.V., Stekhanova T.N., Boiko K.M.,
RA Popov V.O.;
RT "Structure of a new crystal modification of the bacterial NAD-dependent
RT formate dehydrogenase with a resolution of 2.1 A.";
RL Crystallogr. Rep. 50:796-800(2005).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) IN COMPLEX WITH NAD AND FORMATE.
RX DOI=10.1134/S1063774506040146;
RA Filippova E.V., Polyakov K.M., Tikhonova T.V., Stekhanova T.N., Boiko K.M.,
RA Sadihov I.G., Tishkov V.I., Labrou N., Popov V.O.;
RT "Crystal structure of the complex of NAD-dependent formate dehydrogenase
RT from methylotrophic bacterium Pseudomonas sp.101 with formate.";
RL Crystallogr. Rep. 51:627-631(2006).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formate to carbon
CC dioxide. Formate oxidation is the final step in the methanol oxidation
CC pathway in methylotrophic microorganisms. Has a role in the
CC detoxification of exogenous formate in non-methylotrophic organisms.
CC {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:8484798}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.9; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03210, ECO:0000269|PubMed:12144528,
CC ECO:0000269|PubMed:8484798};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.5 mM for formate {ECO:0000269|PubMed:8484798};
CC KM=7.0 mM for formate {ECO:0000269|PubMed:12144528};
CC KM=0.11 mM for NAD(+) {ECO:0000269|PubMed:8484798};
CC KM=60 uM for NAD(+) {ECO:0000269|PubMed:12144528};
CC Note=kcat is 10 sec(-1) with formate as substrate.
CC {ECO:0000269|PubMed:12144528, ECO:0000269|PubMed:8484798};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03210,
CC ECO:0000269|Ref.7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03210}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. FDH subfamily. {ECO:0000255|HAMAP-Rule:MF_03210}.
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DR PIR; JU0334; JU0334.
DR PDB; 2GO1; X-ray; 2.10 A; A=1-401.
DR PDB; 2GUG; X-ray; 2.28 A; A/B/C/D=1-401.
DR PDB; 2NAC; X-ray; 1.80 A; A/B=2-394.
DR PDB; 2NAD; X-ray; 2.05 A; A/B=2-394.
DR PDB; 6JUJ; X-ray; 2.18 A; A/B=1-401.
DR PDB; 6JUK; X-ray; 2.29 A; A/B=1-401.
DR PDB; 6JWG; X-ray; 2.08 A; A/B=1-401.
DR PDB; 6JX1; X-ray; 2.23 A; A/B=1-401.
DR PDBsum; 2GO1; -.
DR PDBsum; 2GUG; -.
DR PDBsum; 2NAC; -.
DR PDBsum; 2NAD; -.
DR PDBsum; 6JUJ; -.
DR PDBsum; 6JUK; -.
DR PDBsum; 6JWG; -.
DR PDBsum; 6JX1; -.
DR AlphaFoldDB; P33160; -.
DR SMR; P33160; -.
DR BRENDA; 1.17.1.9; 5085.
DR EvolutionaryTrace; P33160; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009326; C:formate dehydrogenase complex; IEA:UniProtKB-EC.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0042183; P:formate catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd05302; FDH; 1.
DR HAMAP; MF_03210; Formate_dehydrogenase; 1.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR033689; FDH_NAD-dep.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2357236"
FT CHAIN 2..401
FT /note="Formate dehydrogenase"
FT /id="PRO_0000076027"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210,
FT ECO:0000269|Ref.8"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210,
FT ECO:0000269|Ref.8"
FT BINDING 148
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210,
FT ECO:0000269|PubMed:8114093"
FT BINDING 202..203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210,
FT ECO:0000269|PubMed:8114093"
FT BINDING 222
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210,
FT ECO:0000269|PubMed:8114093"
FT BINDING 257..261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210,
FT ECO:0000269|PubMed:8114093"
FT BINDING 283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210,
FT ECO:0000269|PubMed:8114093"
FT BINDING 309
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210,
FT ECO:0000269|PubMed:8114093"
FT BINDING 333..336
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210,
FT ECO:0000269|PubMed:8114093"
FT BINDING 381
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210,
FT ECO:0000269|PubMed:8114093"
FT SITE 285
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210,
FT ECO:0000305|PubMed:8114093"
FT SITE 333
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210,
FT ECO:0000305|PubMed:8114093"
FT MUTAGEN 256
FT /note="C->S,M: High resistance to inactivation by Hg(2+),
FT Increased stability at 25 degree Celsius and decreased
FT thermostability at 45 degree Celsius."
FT /evidence="ECO:0000269|PubMed:8484798"
FT CONFLICT 78
FT /note="D -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 139..140
FT /note="TV -> VT (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="C -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 216..217
FT /note="VH -> HV (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="N -> D (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2NAC"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2GO1"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:2NAC"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:2NAC"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:2NAC"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:2NAC"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:2NAC"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 148..163
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:2NAC"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:2NAC"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:2NAC"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:6JWG"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:2NAC"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:2NAC"
FT TURN 260..264
FT /evidence="ECO:0007829|PDB:2NAC"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:6JX1"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:2NAC"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 291..299
FT /evidence="ECO:0007829|PDB:2NAC"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:2NAC"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:2NAD"
FT HELIX 339..358
FT /evidence="ECO:0007829|PDB:2NAC"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:2NAC"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:2NAC"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:2GO1"
FT HELIX 377..381
FT /evidence="ECO:0007829|PDB:2NAD"
SQ SEQUENCE 401 AA; 44136 MW; 6B3EBA21F03A89A2 CRC64;
MAKVLCVLYD DPVDGYPKTY ARDDLPKIDH YPGGQTLPTP KAIDFTPGQL LGSVSGELGL
RKYLESNGHT LVVTSDKDGP DSVFERELVD ADVVISQPFW PAYLTPERIA KAKNLKLALT
AGIGSDHVDL QSAIDRNVTV AEVTYCNSIS VAEHVVMMIL SLVRNYLPSH EWARKGGWNI
ADCVSHAYDL EAMHVGTVAA GRIGLAVLRR LAPFDVHLHY TDRHRLPESV EKELNLTWHA
TREDMYPVCD VVTLNCPLHP ETEHMINDET LKLFKRGAYI VNTARGKLCD RDAVARALES
GRLAGYAGDV WFPQPAPKDH PWRTMPYNGM TPHISGTTLT AQARYAAGTR EILECFFEGR
PIRDEYLIVQ GGALAGTGAH SYSKGNATGG SEEAAKFKKA V