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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
 
 
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