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O13437

- FDH_CANBO

UniProt

O13437 - FDH_CANBO

Protein

Formate dehydrogenase

Gene

FDH1

Organism
Candida boidinii (Yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    NAD+-dependent enzyme which catalyzes the final step in the menthanol oxidation pathway. Involved in detoxification of formate.2 Publications

    Catalytic activityi

    Formate + NAD+ = CO2 + NADH.5 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)5 Publications
    2. KM=0.09 mM for NAD (at 30 degrees Celsius and at pH 7.5)5 Publications
    3. KM=5.6 mM for formate (at 30 degrees Celsius and at pH 7.5)5 Publications
    4. KM=0.045 mM for NAD (at 30 degrees Celsius and at pH 7.5)5 Publications
    5. KM=2.42 mM for formate (at 25 degrees Celsius and at pH 7.5)5 Publications
    6. KM=0.04 mM for NAD (at 25 degrees Celsius and at pH 7.5)5 Publications
    7. KM=2.4 mM for formate (at 25 degrees Celsius and at pH 7.6)5 Publications
    8. KM=0.04 mM for NAD (at 25 degrees Celsius and at pH 7.6)5 Publications
    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)5 Publications
    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)5 Publications
    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)5 Publications
    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)5 Publications

    Vmax=6 µM/min/mg enzyme5 Publications

    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
    Active sitei258 – 2581By similarity
    Binding sitei282 – 2821NADBy similarity
    Active sitei311 – 3111Proton donorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi159 – 1668ATPSequence Analysis
    Nucleotide bindingi174 – 1752NADBy similarity
    Nucleotide bindingi256 – 2583NADBy similarity
    Nucleotide bindingi311 – 3144NADBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. choline catabolic process Source: UniProtKB
    2. formate catabolic process Source: UniProtKB
    3. methanol oxidation Source: UniProtKB
    4. methylamine metabolic process Source: UniProtKB
    5. NADH metabolic process Source: UniProtKB
    6. NADH regeneration Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    ATP-binding, NAD, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17206.
    SABIO-RKO13437.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formate dehydrogenaseImported (EC:1.2.1.2)
    Alternative name(s):
    NAD-dependent formate dehydrogenaseImported
    Gene namesi
    Name:FDH1Imported1 Publication
    Synonyms:FDHImported, FDH3Imported
    OrganismiCandida boidinii (Yeast)
    Taxonomic identifieri5477 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    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.2 Publications

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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
    Regioni1 – 119119Catalytic1 PublicationAdd
    BLAST
    Regioni120 – 312193Coenzyme-binding1 PublicationAdd
    BLAST
    Regioni313 – 36452Catalytic1 PublicationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily.By similaritySequence Analysis

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
    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]
    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

    MKIVLVLYDA GKHAADEEKL YGCTENKLGI ANWLKDQGHE LITTSDKEGE    50
    TSELDKHIPD ADIIITTPFH PAYITKERLD KAKNLKLVVV AGVGSDHIDL 100
    DYINQTGKKI SVLEVTGSNV VSVAEHVVMT MLVLVRNFVP AHEQIINHDW 150
    EVAAIAKDAY DIEGKTIATI GAGRIGYRVL ERLLPFNPKE LLYYDYQALP 200
    KEAEEKVGAR RVENIEELVA QADIVTVNAP LHAGTKGLIN KELLSKFKKG 250
    AWLVNTARGA ICVAEDVAAA LESGQLRGYG GDVWFPQPAP KDHPWRDMRN 300
    KYGAGNAMTP HYSGTTLDAQ TRYAEGTKNI LESFFTGKFD YRPQDIILLN 350
    GEYVTKAYGK HDKK 364
    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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91D → G in strain: 2.2159. ImportedCurated
    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 varianti108 – 1081K → R in strain: 2.2159. ImportedCurated
    Natural varianti145 – 1451I → N in strain: 2.2159. ImportedCurated
    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. ImportedCurated
    Natural varianti325 – 3251E → Q in strain: 2.2159 and NCYC 1513. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF004096 Genomic DNA. Translation: AAC49766.1.
    AJ245934 Genomic DNA. Translation: CAB54834.1.
    AJ011046 Genomic DNA. Translation: CAA09466.2.
    DQ458777 Genomic DNA. Translation: ABE69165.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF004096 Genomic DNA. Translation: AAC49766.1 .
    AJ245934 Genomic DNA. Translation: CAB54834.1 .
    AJ011046 Genomic DNA. Translation: CAA09466.2 .
    DQ458777 Genomic DNA. Translation: ABE69165.2 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FSS X-ray 1.70 A/B/C/D 2-364 [» ]
    2J6I X-ray 1.55 A/B/C/D 2-364 [» ]
    ProteinModelPortali O13437.
    SMRi O13437. Positions 2-353.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi O13437.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-17206.
    SABIO-RK O13437.

    Miscellaneous databases

    EvolutionaryTracei O13437.

    Family and domain databases

    Gene3Di 3.40.50.720. 2 hits.
    InterProi IPR006139. D-isomer_2_OHA_DH_cat_dom.
    IPR006140. D-isomer_DH_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00389. 2-Hacid_dh. 1 hit.
    PF02826. 2-Hacid_dh_C. 1 hit.
    [Graphical view ]
    PROSITEi PS00065. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. "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.
    3. "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.
    4. 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.
    5. "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.
    6. "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.
    7. "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.
    8. "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, Q1PAH3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 18, 2010
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 74 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

    External Data

    Dasty 3