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Protein

Formate dehydrogenase

Gene

FDH1

Organism
Candida boidinii (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NAD+-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.UniRule annotation2 Publications

Catalytic activityi

Formate + NAD+ = CO2 + NADH.UniRule annotation5 Publications

Enzyme regulationi

Cu2+, Hg and p-chloromercuribenzoate are strong inhibitors of enzyme activity and Ca2+, Mg2+, Zn2+, Mn2+, Cd2+ and Sn2+ have no effect on activity indicating a cysteine residue in the protein is essential for enzyme activity or to maintain the proper structure of the enzyme. Nitrite and nitrate inhibit some enzyme activity, however cyanide, azide, thiocyanate and cyanate are strong inhibitors of the enzymic reaction. The inhibition of cyanide is competitive with formate and reversible.1 Publication

Kineticsi

  1. KM=13 mM for formate (at 30 degrees Celsius and at pH 7.5)1 Publication
  2. KM=0.09 mM for NAD (at 30 degrees Celsius and at pH 7.5)1 Publication
  3. KM=5.6 mM for formate (at 30 degrees Celsius and at pH 7.5)1 Publication
  4. KM=0.045 mM for NAD (at 30 degrees Celsius and at pH 7.5)1 Publication
  5. KM=2.42 mM for formate (at 25 degrees Celsius and at pH 7.5)1 Publication
  6. KM=0.04 mM for NAD (at 25 degrees Celsius and at pH 7.5)1 Publication
  7. KM=2.4 mM for formate (at 25 degrees Celsius and at pH 7.6)1 Publication
  8. KM=0.04 mM for NAD (at 25 degrees Celsius and at pH 7.6)1 Publication
  9. KM=20.0 mM for formate (at 20 degrees Celsius, at pH 7.5 and after 2 weeks of storage at 4 degrees Celsius in GF buffer)1 Publication
  10. KM=0.05 mM for NAD (at 20 degrees Celsius, at pH 7.5 and after 2 weeks of storage at 4 degrees Celsius in GF buffer)1 Publication
  11. KM=35.0 mM for formate (at 20 degrees Celsius, at pH 7.5 and after 4 months of storage at 4 degrees Celsius in GF buffer)1 Publication
  12. KM=0.09 mM for NAD (at 20 degrees Celsius, at pH 7.5 and after 4 months of storage at 4 degrees Celsius in GF buffer)1 Publication
  1. Vmax=6 µM/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 7.5-8.5.5 Publications

Temperature dependencei

Broad temperature optima between 45 and 55 degrees Celsius. Reaction rate increases steeply up to 55 degrees Celsius. 50% of activity lost after incubation for 20 minutes at 57 degrees Celsius. Thermal stability increases in the presence of glycerol.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931Substrate; via amide nitrogenUniRule annotation
Binding sitei119 – 1191SubstrateUniRule annotation
Binding sitei195 – 1951NADUniRule annotation
Binding sitei256 – 2561NAD; via carbonyl oxygenUniRule annotation
Sitei258 – 2581Important for catalytic activityUniRule annotation1 Publication
Binding sitei282 – 2821NADUniRule annotation
Sitei311 – 3111Important for catalytic activityUniRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi174 – 1752NADUniRule annotation
Nucleotide bindingi230 – 2345NADUniRule annotation
Nucleotide bindingi311 – 3144NADUniRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • formate dehydrogenase (NAD+) activity Source: UniProtKB
  • NAD+ binding Source: UniProtKB
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • choline catabolic process Source: UniProtKB
  • formate catabolic process Source: UniProtKB
  • methanol oxidation Source: UniProtKB
  • methylamine metabolic process Source: UniProtKB
  • NADH metabolic process Source: UniProtKB
  • NADH regeneration Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

ATP-binding, NAD, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17206.
BRENDAi1.2.1.2. 1100.
SABIO-RKO13437.

Names & Taxonomyi

Protein namesi
Recommended name:
Formate dehydrogenaseUniRule annotationImported (EC:1.2.1.2UniRule annotation5 Publications)
Short name:
FDHUniRule annotation
Alternative name(s):
NAD-dependent formate dehydrogenaseUniRule annotationImported
Gene namesi
Name:FDH11 PublicationImported
Synonyms:FDHImported, FDH3Imported
OrganismiCandida boidinii (Yeast)
Taxonomic identifieri5477 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPichiaceaeOgataeaOgataea/Candida clade

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Biotechnological usei

Ideal catalyst for synthesizing chiral compounds of high enantiomeric purity from prochiral precursors due to a favorable thermodynamic equilibrium, the oxidation of formate to carbon dioxide while also reducing NAD to NADH. However, the necessesity for the presence of large quantities of the enzyme and its rapid inactivation under biotransformation conditions results in higher costs for the biocatalyst industry. In order to make this enzymatic reduction viable and to perform it on a larger scale a more efficient and cost effective process has been established. Site-directed mutagenesis has been effective in stabilizing this commercially important enzyme for its application in the biotransformation of trimethyl pyruvate to L-tert leucine.2 Publications

Disruption phenotypei

Is able to grow on methanol in a batch culture experiment, but its growth is greatly inhibited and a toxic level of formate accumulates in the medium. Formate is not detected in the medium in a methanol-limited chemostat culture but deletion mutant shows only one-fourth of the growth yield of the wild-type.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231C → S: Slight increase in substrate affinity for formate but no change in affinity for NAD, 9 degrees Celsius decrease in thermal stability compared to the wild-type, significantly higher stability compared to wild-type under biotransformation conditions, significantly more stable in the presence of CuCl(2); when associated with A-262. Large increase in substrate affinity for formate but no significant change in affinity for NAD, 13 degrees Celsius decrease in thermal stability compared to the wild-type, significantly more stable in the presence of CuCl(2); when associated with V-262. No significant change in affinity for formate or NAD, 5 degrees Celsius decrease in thermal stability compared to the wild-type, significantly higher stability compared to wild-type under biotransformation conditions, and significantly more stable in the presence of CuCl(2). 1 Publication
Mutagenesisi47 – 471K → E: Slight increase in substrate affinity for formate and also affinity for NAD increases by half after 2 weeks. Also after 4 months affinity for formate increases by more than half and affinity for NAD increases by more than half. Retains 84% of residual activity after incubation for 20 minutes at a thermal inactivation temperature of 55 degrees Celsius in samples stored for 2 weeks compared to wild-type which loses 50% of its activity at 55 degrees Celsius. 1 Publication
Mutagenesisi69 – 691F → A: 2-fold decrease in substrate affinity for formate, but no significant change in affinity for NAD. A significant reduction in catalytic activity compared to the wild-type. 1 Publication
Mutagenesisi119 – 1191N → A: 94-fold decrease in substrate affinity for formate and 2700-fold decrease in substrate affinity for NAD. A significant reduction in catalytic activity compared to the wild-type; when associated with A-311. 1 Publication
Mutagenesisi119 – 1191N → H: 80-fold decrease in substrate affinity for formate and a 1250-fold decrease in substrate affinity for NAD. A significant reduction in catalytic activity compared to the wild-type. 1 Publication
Mutagenesisi175 – 1751I → A: 2-fold decrease in substrate affinity for formate and a 12-fold decrease in substrate affinity for NAD. A significant reduction in catalytic activity compared to the wild-type. 1 Publication
Mutagenesisi197 – 1971Q → L: 4-fold decrease in substrate affinity for formate but no significant change in affinity for NAD compared to the wild-type. 1 Publication
Mutagenesisi258 – 2581R → A: No catalytic activity. 1 Publication
Mutagenesisi262 – 2621C → A: Slight increase in substrate affinity for formate but no change in affinity for NAD, 9 degrees Celsius decrease in thermal stability compared to the wild-type, greater stability at a higher pH compared to the wild-type; when associated with S-23. 1 Publication
Mutagenesisi262 – 2621C → V: Large increase in substrate affinity for formate but no significant change in affinity for NAD, 13 degrees Celsius decrease in thermal stability compared to the wild-type; when associated with S-23. Great increase in substrate affinity for formate and NAD and 8 degrees Celsius decrease in thermal stability compared to the wild-type. 1 Publication
Mutagenesisi287 – 2871Q → A: 2-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with A-311. 1 Publication
Mutagenesisi287 – 2871Q → E: 380-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with T-288. No significant decrease in substrate affinity for formate but a 4-fold decrease in substrate affinity for NAD and a significant reduction in catalytic activity compared to the wild-type, a more acidic pH is seen than in the wild-type, preventing formate binding by a single ionization of a group compared to that of the wild-type. 1 Publication
Mutagenesisi288 – 2881P → T: 380-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with E-287. 1 Publication
Mutagenesisi311 – 3111H → A: 2-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with A-287. 93-fold decrease in substrate affinity for formate and 2700-fold decrease in substrate affinity for NAD, and a significant reduction in catalytic activity compared to the wild-type; when associated with A-119. 1 Publication
Mutagenesisi311 – 3111H → Q: 10-fold decrease in substrate affinity for formate and significant reduction in the catalytic activity compared to the wild-type. 1 Publication
Mutagenesisi328 – 3281K → V: A 75% increase in substrate affinity for formate after 2 weeks and a 50% increase in affinity for NAD. However, after 4 months the affinity for formate increases 7-fold and affinity for NAD increases by 2 thirds. Retains 70% of residual activity after incubation for 20 minutes at a thermal inactivation temperature of 55 degrees Celsius in samples stored for 2 weeks compared to wild-type which loses 50% of its activity at 55 degrees Celsius. 1 Publication
Mutagenesisi360 – 3601K → A: Exhibits no change in substrate affinity for formate, but shows a 4-fold decrease in substrate affinity for NAD implying that L-360 side chain forms strong interactions with the cofactor. A higher reaction rate is observed at an acidic and basic pH values. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 364364Formate dehydrogenasePRO_0000393949Add
BLAST

Proteomic databases

PRIDEiO13437.

Expressioni

Inductioni

Expression is strongly induced by methanol, but is completely repressed in the presence of glucose. However, methanol induced expression is equally strong in cells grown on glucose when formate, methylamine or choline is added. No expression is detected in cells grown on glycerol. When formate, methylamine or choline is added to the culture medium of glycerol- or glucose-grown cells, they exhibit an induction of FDH1 expression.1 Publication

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Structurei

Secondary structure

1
364
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi12 – 165Combined sources
Turni24 – 263Combined sources
Helixi27 – 293Combined sources
Helixi31 – 366Combined sources
Beta strandi40 – 456Combined sources
Beta strandi49 – 524Combined sources
Helixi53 – 575Combined sources
Helixi58 – 603Combined sources
Beta strandi62 – 665Combined sources
Helixi76 – 816Combined sources
Beta strandi87 – 937Combined sources
Helixi100 – 1067Combined sources
Beta strandi111 – 1144Combined sources
Helixi120 – 13516Combined sources
Helixi138 – 1469Combined sources
Helixi152 – 1565Combined sources
Beta strandi166 – 1705Combined sources
Helixi174 – 18310Combined sources
Helixi184 – 1863Combined sources
Beta strandi189 – 1946Combined sources
Helixi201 – 2066Combined sources
Beta strandi209 – 2113Combined sources
Helixi215 – 2206Combined sources
Beta strandi223 – 2275Combined sources
Turni233 – 2375Combined sources
Helixi241 – 2444Combined sources
Beta strandi251 – 2555Combined sources
Helixi259 – 2613Combined sources
Helixi264 – 2729Combined sources
Beta strandi275 – 2828Combined sources
Beta strandi285 – 2884Combined sources
Helixi294 – 2974Combined sources
Beta strandi306 – 3083Combined sources
Helixi313 – 3153Combined sources
Helixi317 – 33519Combined sources
Helixi343 – 3453Combined sources
Beta strandi346 – 3494Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FSSX-ray1.70A/B/C/D2-364[»]
2J6IX-ray1.55A/B/C/D2-364[»]
ProteinModelPortaliO13437.
SMRiO13437. Positions 2-353.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO13437.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 119118CatalyticUniRule annotation1 PublicationAdd
BLAST
Regioni120 – 312193Coenzyme-bindingUniRule annotation1 PublicationAdd
BLAST
Regioni313 – 35846CatalyticUniRule annotation1 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily.UniRule annotation

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
HAMAPiMF_03210. Formate_dehydrogenase.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O13437-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIVLVLYDA GKHAADEEKL YGCTENKLGI ANWLKDQGHE LITTSDKEGE
60 70 80 90 100
TSELDKHIPD ADIIITTPFH PAYITKERLD KAKNLKLVVV AGVGSDHIDL
110 120 130 140 150
DYINQTGKKI SVLEVTGSNV VSVAEHVVMT MLVLVRNFVP AHEQIINHDW
160 170 180 190 200
EVAAIAKDAY DIEGKTIATI GAGRIGYRVL ERLLPFNPKE LLYYDYQALP
210 220 230 240 250
KEAEEKVGAR RVENIEELVA QADIVTVNAP LHAGTKGLIN KELLSKFKKG
260 270 280 290 300
AWLVNTARGA ICVAEDVAAA LESGQLRGYG GDVWFPQPAP KDHPWRDMRN
310 320 330 340 350
KYGAGNAMTP HYSGTTLDAQ TRYAEGTKNI LESFFTGKFD YRPQDIILLN
360
GEYVTKAYGK HDKK
Length:364
Mass (Da):40,370
Last modified:January 1, 1998 - v1
Checksum:i1B30982E0D5B77E8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 235KLYGC → EKLYG AA sequence (PubMed:11171126).Curated
Sequence conflicti23 – 231C → T AA sequence (PubMed:7557425).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91D → G in strain: 2.2159. CuratedImported
Natural varianti50 – 512ET → GN in strain: 2.2159 and NCYC 1513. 1 Publication
Natural varianti53 – 531E → V in strain: 2.2159 and NCYC 1513. 1 Publication
Natural varianti56 – 561K → Q in strain: 2.2159 and NCYC 1513. 1 Publication
Natural varianti79 – 791L → I in strain: 2.2159 and NCYC 1513. 1 Publication
Natural varianti84 – 841N → K in strain: 2.2159 and NCYC 1513. 1 Publication
Natural varianti87 – 871L → S in strain ATCC 56294 / CBS 8030 / CCRC 21757 / NRRL Y-17325. 1 Publication
Natural varianti108 – 1081K → R in strain: 2.2159. CuratedImported
Natural varianti145 – 1451I → N in strain: 2.2159. CuratedImported
Natural varianti184 – 1841L → V in strain: 2.2159 and NCYC 1513. 1 Publication
Natural varianti202 – 2021E → D in strain: 2.2159 and NCYC 1513. 1 Publication
Natural varianti308 – 3081M → T in strain: 2.2159. CuratedImported
Natural varianti325 – 3251E → Q in strain: 2.2159 and NCYC 1513. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81129 Genomic DNA. Translation: CAA57036.1.
AF004096 Genomic DNA. Translation: AAC49766.1.
AJ245934 Genomic DNA. Translation: CAB54834.1.
AJ011046 Genomic DNA. Translation: CAA09466.2.
DQ458777 Genomic DNA. Translation: ABE69165.2.
PIRiJC4252.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81129 Genomic DNA. Translation: CAA57036.1.
AF004096 Genomic DNA. Translation: AAC49766.1.
AJ245934 Genomic DNA. Translation: CAB54834.1.
AJ011046 Genomic DNA. Translation: CAA09466.2.
DQ458777 Genomic DNA. Translation: ABE69165.2.
PIRiJC4252.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FSSX-ray1.70A/B/C/D2-364[»]
2J6IX-ray1.55A/B/C/D2-364[»]
ProteinModelPortaliO13437.
SMRiO13437. Positions 2-353.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO13437.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17206.
BRENDAi1.2.1.2. 1100.
SABIO-RKO13437.

Miscellaneous databases

EvolutionaryTraceiO13437.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
HAMAPiMF_03210. Formate_dehydrogenase.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation, sequence and overexpression of the gene encoding NAD-dependent formate dehydrogenase from the methylotrophic yeast Candida methylica."
    Allen S.J., Holbrook J.J.
    Gene 162:99-104(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25.
    Strain: ATCC 56294 / CBS 8030 / CCRC 21757 / NRRL Y-17325.
  2. "Regulation of the formate dehydrogenase gene, FDH1, in the methylotrophic yeast Candida boidinii and growth characteristics of an FDH1-disrupted strain on methanol, methylamine, and choline."
    Sakai Y., Murdanoto A.P., Konishi T., Iwamatsu A., Kato N.
    J. Bacteriol. 179:4480-4485(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-45; 57-76; 87-103; 190-201; 207-236; 242-246; 292-326 AND 329-354, FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, INDUCTION.
    Strain: S2Imported.
  3. "Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues."
    Slusarczyk H., Felber S., Kula M.R., Pohl M.
    Eur. J. Biochem. 267:1280-1289(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-15, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY, MUTAGENESIS OF CYS-23 AND CYS-262.
    Strain: ATCC 32195Imported.
  4. "Active-site characterization of Candida boidinii formate dehydrogenase."
    Labrou N.E., Rigden D.J.
    Biochem. J. 354:455-463(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-30 AND 132-140, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-69; ASN-119; ILE-175; GLN-197; ARG-258; GLN-287; PRO-288 AND HIS-311.
    Strain: NCYC 1513Imported.
  5. Zhang G., Yang G., Cao Z., Liu M.
    Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 2.2159Imported.
  6. "Characterization of the NAD+ binding site of Candida boidinii formate dehydrogenase by affinity labelling and site-directed mutagenesis."
    Labrou N.E., Rigden D.J., Clonis Y.D.
    Eur. J. Biochem. 267:6657-6664(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 357-363, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-360.
  7. "Purification and properties of formaldehyde dehydrogenase and formate dehydrogenase from Candida boidinii."
    Schute H., Flossdorf J., Sahm H., Kula M.R.
    Eur. J. Biochem. 62:151-160(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  8. "Continuous computer controlled production of formate dehydrogenase (FDH) and isolation on a pilot scale."
    Weuster-Botz D., Paschold H., Striegel B., Gieren H., Kula M.R., Wandrey C.
    Chem. Eng. Technol. 17:131-137(1994)
    Cited for: BIOTECHNOLOGY.
  9. "High-resolution structures of formate dehydrogenase from Candida boidinii."
    Schirwitz K., Schmidt A., Lamzin V.S.
    Protein Sci. 16:1146-1156(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANT GLU-47 AND (1.55 ANGSTROMS) OF MUTANT VAL-328, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CATALYTIC AND COENZYME-BINDING REGIONS, MUTAGENESIS OF LYS-47 AND LYS-328.

Entry informationi

Entry nameiFDH_CANBO
AccessioniPrimary (citable) accession number: O13437
Secondary accession number(s): O93968, Q00498, Q1PAH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 1, 1998
Last modified: March 16, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.