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Database: UniProt
Entry: P33160
LinkDB: P33160
Original site: P33160 
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   05-DEC-2018, entry version 109.
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
RT   Pseudomonas sp. 101: cloning, expression, and study of the genetic
RT   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.,
RA   Popov V.O., 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.,
RA   Boiko K.M., Popov V.O.;
RT   "Structure of a new crystal modification of the bacterial NAD-
RT   dependent 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
RP   FORMATE.
RX   DOI=10.1134/S1063774506040146;
RA   Filippova E.V., Polyakov K.M., Tikhonova T.V., Stekhanova T.N.,
RA   Boiko K.M., Sadihov I.G., Tishkov V.I., Labrou N., Popov V.O.;
RT   "Crystal structure of the complex of NAD-dependent formate
RT   dehydrogenase from metylotrophic bacterium Pseudomonas sp.101 with
RT   formate.";
RL   Crystallogr. Rep. 51:627-631(2006).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formate to
CC       carbon dioxide. Formate oxidation is the final step in the
CC       methanol oxidation pathway in methylotrophic microorganisms. Has a
CC       role in the detoxification of exogenous formate in non-
CC       methylotrophic organisms. {ECO:0000255|HAMAP-Rule:MF_03210,
CC       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-
CC       Rule:MF_03210}.
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   PDBsum; 2GO1; -.
DR   PDBsum; 2GUG; -.
DR   PDBsum; 2NAC; -.
DR   PDBsum; 2NAD; -.
DR   ProteinModelPortal; P33160; -.
DR   SMR; P33160; -.
DR   BRENDA; 1.2.1.2; 5085.
DR   EvolutionaryTrace; P33160; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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;
KW   Oxidoreductase.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:2357236}.
FT   CHAIN         2    401       Formate dehydrogenase.
FT                                /FTId=PRO_0000076027.
FT   NP_BIND     202    203       NAD. {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000269|PubMed:8114093}.
FT   NP_BIND     257    261       NAD. {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000269|PubMed:8114093}.
FT   NP_BIND     333    336       NAD. {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000269|PubMed:8114093}.
FT   REGION        3    147       Catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210, ECO:0000305|Ref.7}.
FT   REGION      148    334       Coenzyme-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210, ECO:0000305|Ref.7}.
FT   REGION      335    382       Catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210, ECO:0000305|Ref.7}.
FT   BINDING     123    123       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000269|Ref.8}.
FT   BINDING     147    147       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210, ECO:0000269|Ref.8}.
FT   BINDING     148    148       NAD. {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000269|PubMed:8114093}.
FT   BINDING     222    222       NAD. {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000269|PubMed:8114093}.
FT   BINDING     283    283       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000269|PubMed:8114093}.
FT   BINDING     309    309       NAD. {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000269|PubMed:8114093}.
FT   BINDING     381    381       NAD. {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000269|PubMed:8114093}.
FT   SITE        285    285       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000305|PubMed:8114093}.
FT   SITE        333    333       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210,
FT                                ECO:0000305|PubMed:8114093}.
FT   MUTAGEN     256    256       C->S,M: High resistance to inactivation
FT                                by Hg(2+), Increased stability at 25
FT                                degree Celsius and decreased
FT                                thermostability at 45 degree Celsius.
FT                                {ECO:0000269|PubMed:8484798}.
FT   CONFLICT     78     78       D -> S (in Ref. 1). {ECO:0000305}.
FT   CONFLICT    139    140       TV -> VT (in Ref. 1). {ECO:0000305}.
FT   CONFLICT    146    146       C -> V (in Ref. 1). {ECO:0000305}.
FT   CONFLICT    216    217       VH -> HV (in Ref. 1). {ECO:0000305}.
FT   CONFLICT    328    328       N -> D (in Ref. 1). {ECO:0000305}.
FT   STRAND        3      7       {ECO:0000244|PDB:2NAC}.
FT   STRAND       21     23       {ECO:0000244|PDB:2GO1}.
FT   TURN         54     56       {ECO:0000244|PDB:2NAC}.
FT   HELIX        57     59       {ECO:0000244|PDB:2NAC}.
FT   HELIX        61     66       {ECO:0000244|PDB:2NAC}.
FT   STRAND       70     75       {ECO:0000244|PDB:2NAC}.
FT   HELIX        83     88       {ECO:0000244|PDB:2NAC}.
FT   STRAND       92     97       {ECO:0000244|PDB:2NAC}.
FT   HELIX       106    111       {ECO:0000244|PDB:2NAC}.
FT   STRAND      117    123       {ECO:0000244|PDB:2NAC}.
FT   HELIX       130    135       {ECO:0000244|PDB:2NAC}.
FT   STRAND      139    142       {ECO:0000244|PDB:2NAC}.
FT   TURN        144    147       {ECO:0000244|PDB:2NAC}.
FT   HELIX       148    163       {ECO:0000244|PDB:2NAC}.
FT   HELIX       166    174       {ECO:0000244|PDB:2NAC}.
FT   HELIX       180    184       {ECO:0000244|PDB:2NAC}.
FT   STRAND      194    198       {ECO:0000244|PDB:2NAC}.
FT   HELIX       202    211       {ECO:0000244|PDB:2NAC}.
FT   HELIX       212    214       {ECO:0000244|PDB:2NAC}.
FT   STRAND      217    221       {ECO:0000244|PDB:2NAC}.
FT   HELIX       228    234       {ECO:0000244|PDB:2NAC}.
FT   STRAND      237    241       {ECO:0000244|PDB:2GUG}.
FT   HELIX       242    245       {ECO:0000244|PDB:2NAC}.
FT   HELIX       246    248       {ECO:0000244|PDB:2NAC}.
FT   STRAND      250    254       {ECO:0000244|PDB:2NAC}.
FT   TURN        260    264       {ECO:0000244|PDB:2NAC}.
FT   HELIX       268    271       {ECO:0000244|PDB:2NAC}.
FT   STRAND      278    282       {ECO:0000244|PDB:2NAC}.
FT   HELIX       286    288       {ECO:0000244|PDB:2NAC}.
FT   HELIX       291    299       {ECO:0000244|PDB:2NAC}.
FT   STRAND      302    309       {ECO:0000244|PDB:2NAC}.
FT   STRAND      312    315       {ECO:0000244|PDB:2NAC}.
FT   HELIX       321    323       {ECO:0000244|PDB:2NAC}.
FT   HELIX       335    337       {ECO:0000244|PDB:2NAD}.
FT   HELIX       339    358       {ECO:0000244|PDB:2NAC}.
FT   HELIX       364    366       {ECO:0000244|PDB:2NAC}.
FT   STRAND      367    370       {ECO:0000244|PDB:2NAC}.
FT   STRAND      371    373       {ECO:0000244|PDB:2GO1}.
FT   HELIX       377    381       {ECO:0000244|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
//
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