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Formate dehydrogenase (FDH) (EC 1.17.1.9) (NAD-dependent formate dehydrogenase)

 FDH_CANBO               Reviewed;         364 AA.
O13437; O93968; Q00498; Q1PAH3;
18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 90.
RecName: Full=Formate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000312|EMBL:CAB54834.1};
Short=FDH {ECO:0000255|HAMAP-Rule:MF_03210};
EC=1.17.1.9 {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:10691964, ECO:0000269|PubMed:11171126, ECO:0000269|PubMed:1248477, ECO:0000269|PubMed:17525463, ECO:0000269|PubMed:9226256};
AltName: Full=NAD-dependent formate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000312|EMBL:AAC49766.1};
Name=FDH1 {ECO:0000303|PubMed:9226256, ECO:0000312|EMBL:AAC49766.1};
Synonyms=FDH {ECO:0000312|EMBL:CAA09466.2},
FDH3 {ECO:0000312|EMBL:CAB54834.1};
Candida boidinii (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Pichiaceae; Ogataea;
Ogataea/Candida clade.
NCBI_TaxID=5477;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-25.
STRAIN=ATCC 56294 / CBS 8030 / CCRC 21757 / NRRL Y-17325;
PubMed=7557425; DOI=10.1016/0378-1119(95)00347-9;
Allen S.J., Holbrook J.J.;
"Isolation, sequence and overexpression of the gene encoding NAD-
dependent formate dehydrogenase from the methylotrophic yeast Candida
methylica.";
Gene 162:99-104(1995).
[2]
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, AND INDUCTION.
STRAIN=S2 {ECO:0000312|EMBL:AAC49766.1};
PubMed=9226256; DOI=10.1128/jb.179.14.4480-4485.1997;
Sakai Y., Murdanoto A.P., Konishi T., Iwamatsu A., Kato N.;
"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.";
J. Bacteriol. 179:4480-4485(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-15, CATALYTIC
ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY, AND
MUTAGENESIS OF CYS-23 AND CYS-262.
STRAIN=ATCC 32195 {ECO:0000312|EMBL:CAB54834.1};
PubMed=10691964; DOI=10.1046/j.1432-1327.2000.01123.x;
Slusarczyk H., Felber S., Kula M.R., Pohl M.;
"Stabilization of NAD-dependent formate dehydrogenase from Candida
boidinii by site-directed mutagenesis of cysteine residues.";
Eur. J. Biochem. 267:1280-1289(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-30 AND 132-140,
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
PHE-69; ASN-119; ILE-175; GLN-197; ARG-258; GLN-287; PRO-288 AND
HIS-311.
STRAIN=NCYC 1513 {ECO:0000312|EMBL:CAA09466.2};
PubMed=11171126; DOI=10.1042/0264-6021:3540455;
Labrou N.E., Rigden D.J.;
"Active-site characterization of Candida boidinii formate
dehydrogenase.";
Biochem. J. 354:455-463(2001).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=2.2159 {ECO:0000312|EMBL:ABE69165.2};
Zhang G., Yang G., Cao Z., Liu M.;
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 357-363, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF LYS-360.
PubMed=11054119; DOI=10.1046/j.1432-1327.2000.01761.x;
Labrou N.E., Rigden D.J., Clonis Y.D.;
"Characterization of the NAD+ binding site of Candida boidinii formate
dehydrogenase by affinity labelling and site-directed mutagenesis.";
Eur. J. Biochem. 267:6657-6664(2000).
[7]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND SUBUNIT.
PubMed=1248477; DOI=10.1111/j.1432-1033.1976.tb10108.x;
Schute H., Flossdorf J., Sahm H., Kula M.R.;
"Purification and properties of formaldehyde dehydrogenase and formate
dehydrogenase from Candida boidinii.";
Eur. J. Biochem. 62:151-160(1976).
[8]
BIOTECHNOLOGY.
DOI=10.1002/ceat.270170211;
Weuster-Botz D., Paschold H., Striegel B., Gieren H., Kula M.R.,
Wandrey C.;
"Continuous computer controlled production of formate dehydrogenase
(FDH) and isolation on a pilot scale.";
Chem. Eng. Technol. 17:131-137(1994).
[9]
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, AND
MUTAGENESIS OF LYS-47 AND LYS-328.
PubMed=17525463; DOI=10.1110/ps.062741707;
Schirwitz K., Schmidt A., Lamzin V.S.;
"High-resolution structures of formate dehydrogenase from Candida
boidinii.";
Protein Sci. 16:1146-1156(2007).
-!- FUNCTION: 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. {ECO:0000255|HAMAP-Rule:MF_03210,
ECO:0000269|PubMed:1248477, ECO:0000269|PubMed:9226256}.
-!- CATALYTIC ACTIVITY: Formate + NAD(+) = CO(2) + NADH.
{ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:10691964,
ECO:0000269|PubMed:11171126, ECO:0000269|PubMed:1248477,
ECO:0000269|PubMed:17525463, ECO:0000269|PubMed:9226256}.
-!- ENZYME REGULATION: Cu(2+), Hg and p-chloromercuribenzoate are
strong inhibitors of enzyme activity and Ca(2+), Mg(2+), Zn(2+),
Mn(2+), Cd(2+) and Sn(2+) 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. {ECO:0000269|PubMed:1248477}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=13 mM for formate (at 30 degrees Celsius and at pH 7.5)
{ECO:0000269|PubMed:1248477};
KM=0.09 mM for NAD (at 30 degrees Celsius and at pH 7.5)
{ECO:0000269|PubMed:1248477};
KM=5.6 mM for formate (at 30 degrees Celsius and at pH 7.5)
{ECO:0000269|PubMed:10691964};
KM=0.045 mM for NAD (at 30 degrees Celsius and at pH 7.5)
{ECO:0000269|PubMed:10691964};
KM=2.42 mM for formate (at 25 degrees Celsius and at pH 7.5)
{ECO:0000269|PubMed:11171126};
KM=0.04 mM for NAD (at 25 degrees Celsius and at pH 7.5)
{ECO:0000269|PubMed:11171126};
KM=2.4 mM for formate (at 25 degrees Celsius and at pH 7.6)
{ECO:0000269|PubMed:11054119};
KM=0.04 mM for NAD (at 25 degrees Celsius and at pH 7.6)
{ECO:0000269|PubMed:11054119};
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)
{ECO:0000269|PubMed:17525463};
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)
{ECO:0000269|PubMed:17525463};
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)
{ECO:0000269|PubMed:17525463};
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)
{ECO:0000269|PubMed:17525463};
Vmax=6 uM/min/mg enzyme {ECO:0000269|PubMed:10691964};
pH dependence:
Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:10691964,
ECO:0000269|PubMed:11054119, ECO:0000269|PubMed:11171126,
ECO:0000269|PubMed:1248477, ECO:0000269|PubMed:17525463};
Temperature dependence:
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. {ECO:0000269|PubMed:10691964,
ECO:0000269|PubMed:11054119, ECO:0000269|PubMed:11171126,
ECO:0000269|PubMed:1248477, ECO:0000269|PubMed:17525463};
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03210,
ECO:0000269|PubMed:1248477, ECO:0000269|PubMed:17525463}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03210}.
-!- INDUCTION: 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.
{ECO:0000269|PubMed:9226256}.
-!- DISRUPTION PHENOTYPE: 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. {ECO:0000269|PubMed:9226256}.
-!- BIOTECHNOLOGY: 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.
{ECO:0000269|PubMed:10691964, ECO:0000269|Ref.8}.
-!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
dehydrogenase family. FDH subfamily. {ECO:0000255|HAMAP-
Rule:MF_03210}.
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EMBL; X81129; CAA57036.1; -; Genomic_DNA.
EMBL; AF004096; AAC49766.1; -; Genomic_DNA.
EMBL; AJ245934; CAB54834.1; -; Genomic_DNA.
EMBL; AJ011046; CAA09466.2; -; Genomic_DNA.
EMBL; DQ458777; ABE69165.2; -; Genomic_DNA.
PIR; JC4252; JC4252.
PDB; 2FSS; X-ray; 1.70 A; A/B/C/D=2-364.
PDB; 2J6I; X-ray; 1.55 A; A/B/C/D=2-364.
PDBsum; 2FSS; -.
PDBsum; 2J6I; -.
ProteinModelPortal; O13437; -.
SMR; O13437; -.
PRIDE; O13437; -.
BioCyc; MetaCyc:MONOMER-17206; -.
BRENDA; 1.2.1.2; 1100.
SABIO-RK; O13437; -.
EvolutionaryTrace; O13437; -.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IDA:UniProtKB.
GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0042426; P:choline catabolic process; IMP:UniProtKB.
GO; GO:0042183; P:formate catabolic process; IDA:UniProtKB.
GO; GO:0015946; P:methanol oxidation; IMP:UniProtKB.
GO; GO:0030416; P:methylamine metabolic process; IMP:UniProtKB.
GO; GO:0006734; P:NADH metabolic process; IMP:UniProtKB.
GO; GO:0006735; P:NADH regeneration; IDA:UniProtKB.
CDD; cd05302; FDH; 1.
HAMAP; MF_03210; Formate_dehydrogenase; 1.
InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
InterPro; IPR029753; D-isomer_DH_CS.
InterPro; IPR029752; D-isomer_DH_CS1.
InterPro; IPR006140; D-isomer_DH_NAD-bd.
InterPro; IPR033689; FDH_NAD-dep.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF00389; 2-Hacid_dh; 1.
Pfam; PF02826; 2-Hacid_dh_C; 1.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; NAD;
Nucleotide-binding; Oxidoreductase.
CHAIN 1 364 Formate dehydrogenase.
/FTId=PRO_0000393949.
NP_BIND 174 175 NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
NP_BIND 230 234 NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
NP_BIND 311 314 NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
REGION 2 119 Catalytic. {ECO:0000255|HAMAP-
Rule:MF_03210,
ECO:0000269|PubMed:17525463}.
REGION 120 312 Coenzyme-binding. {ECO:0000255|HAMAP-
Rule:MF_03210,
ECO:0000269|PubMed:17525463}.
REGION 313 358 Catalytic. {ECO:0000255|HAMAP-
Rule:MF_03210,
ECO:0000269|PubMed:17525463}.
BINDING 93 93 Substrate; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_03210}.
BINDING 119 119 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03210}.
BINDING 195 195 NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
BINDING 256 256 NAD; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03210}.
BINDING 282 282 NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
SITE 258 258 Important for catalytic activity.
{ECO:0000255|HAMAP-Rule:MF_03210,
ECO:0000305|PubMed:17525463}.
SITE 311 311 Important for catalytic activity.
{ECO:0000255|HAMAP-Rule:MF_03210,
ECO:0000305|PubMed:17525463}.
VARIANT 9 9 D -> G (in strain: 2.2159). {ECO:0000305,
ECO:0000312|EMBL:ABE69165.2}.
VARIANT 50 51 ET -> GN (in strain: 2.2159 and NCYC
1513). {ECO:0000269|PubMed:11171126}.
VARIANT 53 53 E -> V (in strain: 2.2159 and NCYC 1513).
{ECO:0000269|PubMed:11171126}.
VARIANT 56 56 K -> Q (in strain: 2.2159 and NCYC 1513).
{ECO:0000269|PubMed:11171126}.
VARIANT 79 79 L -> I (in strain: 2.2159 and NCYC 1513).
{ECO:0000269|PubMed:11171126}.
VARIANT 84 84 N -> K (in strain: 2.2159 and NCYC 1513).
{ECO:0000269|PubMed:11171126}.
VARIANT 87 87 L -> S (in strain ATCC 56294 / CBS 8030 /
CCRC 21757 / NRRL Y-17325).
{ECO:0000269|PubMed:7557425}.
VARIANT 108 108 K -> R (in strain: 2.2159). {ECO:0000305,
ECO:0000312|EMBL:ABE69165.2}.
VARIANT 145 145 I -> N (in strain: 2.2159). {ECO:0000305,
ECO:0000312|EMBL:ABE69165.2}.
VARIANT 184 184 L -> V (in strain: 2.2159 and NCYC 1513).
{ECO:0000269|PubMed:11171126}.
VARIANT 202 202 E -> D (in strain: 2.2159 and NCYC 1513).
{ECO:0000269|PubMed:11171126}.
VARIANT 308 308 M -> T (in strain: 2.2159). {ECO:0000305,
ECO:0000312|EMBL:ABE69165.2}.
VARIANT 325 325 E -> Q (in strain: 2.2159 and NCYC 1513).
{ECO:0000269|PubMed:11171126}.
MUTAGEN 23 23 C->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).
{ECO:0000269|PubMed:10691964}.
MUTAGEN 47 47 K->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.
{ECO:0000269|PubMed:17525463}.
MUTAGEN 69 69 F->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.
{ECO:0000269|PubMed:11171126}.
MUTAGEN 119 119 N->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.
{ECO:0000269|PubMed:11171126}.
MUTAGEN 119 119 N->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.
{ECO:0000269|PubMed:11171126}.
MUTAGEN 175 175 I->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.
{ECO:0000269|PubMed:11171126}.
MUTAGEN 197 197 Q->L: 4-fold decrease in substrate
affinity for formate but no significant
change in affinity for NAD compared to
the wild-type.
{ECO:0000269|PubMed:11171126}.
MUTAGEN 258 258 R->A: No catalytic activity.
{ECO:0000269|PubMed:11171126}.
MUTAGEN 262 262 C->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.
{ECO:0000269|PubMed:10691964}.
MUTAGEN 262 262 C->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.
{ECO:0000269|PubMed:10691964}.
MUTAGEN 287 287 Q->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. {ECO:0000269|PubMed:11171126}.
MUTAGEN 287 287 Q->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.
{ECO:0000269|PubMed:11171126}.
MUTAGEN 288 288 P->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. {ECO:0000269|PubMed:11171126}.
MUTAGEN 311 311 H->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.
{ECO:0000269|PubMed:11171126}.
MUTAGEN 311 311 H->Q: 10-fold decrease in substrate
affinity for formate and significant
reduction in the catalytic activity
compared to the wild-type.
{ECO:0000269|PubMed:11171126}.
MUTAGEN 328 328 K->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.
{ECO:0000269|PubMed:17525463}.
MUTAGEN 360 360 K->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.
{ECO:0000269|PubMed:11054119}.
CONFLICT 19 23 KLYGC -> EKLYG (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 23 23 C -> T (in Ref. 1; AA sequence).
{ECO:0000305}.
STRAND 2 6 {ECO:0000244|PDB:2J6I}.
HELIX 12 16 {ECO:0000244|PDB:2J6I}.
TURN 24 26 {ECO:0000244|PDB:2J6I}.
HELIX 27 29 {ECO:0000244|PDB:2J6I}.
HELIX 31 36 {ECO:0000244|PDB:2J6I}.
STRAND 40 45 {ECO:0000244|PDB:2J6I}.
STRAND 49 52 {ECO:0000244|PDB:2FSS}.
HELIX 53 57 {ECO:0000244|PDB:2J6I}.
HELIX 58 60 {ECO:0000244|PDB:2J6I}.
STRAND 62 66 {ECO:0000244|PDB:2J6I}.
HELIX 76 81 {ECO:0000244|PDB:2J6I}.
STRAND 87 93 {ECO:0000244|PDB:2J6I}.
HELIX 100 106 {ECO:0000244|PDB:2J6I}.
STRAND 111 114 {ECO:0000244|PDB:2J6I}.
HELIX 120 135 {ECO:0000244|PDB:2J6I}.
HELIX 138 146 {ECO:0000244|PDB:2J6I}.
HELIX 152 156 {ECO:0000244|PDB:2J6I}.
STRAND 166 170 {ECO:0000244|PDB:2J6I}.
HELIX 174 183 {ECO:0000244|PDB:2J6I}.
HELIX 184 186 {ECO:0000244|PDB:2J6I}.
STRAND 189 194 {ECO:0000244|PDB:2J6I}.
HELIX 201 206 {ECO:0000244|PDB:2J6I}.
STRAND 209 211 {ECO:0000244|PDB:2J6I}.
HELIX 215 220 {ECO:0000244|PDB:2J6I}.
STRAND 223 227 {ECO:0000244|PDB:2J6I}.
TURN 233 237 {ECO:0000244|PDB:2J6I}.
HELIX 241 244 {ECO:0000244|PDB:2J6I}.
STRAND 251 255 {ECO:0000244|PDB:2J6I}.
HELIX 259 261 {ECO:0000244|PDB:2J6I}.
HELIX 264 272 {ECO:0000244|PDB:2J6I}.
STRAND 275 282 {ECO:0000244|PDB:2J6I}.
STRAND 285 288 {ECO:0000244|PDB:2J6I}.
HELIX 294 297 {ECO:0000244|PDB:2J6I}.
STRAND 306 308 {ECO:0000244|PDB:2J6I}.
HELIX 313 315 {ECO:0000244|PDB:2J6I}.
HELIX 317 335 {ECO:0000244|PDB:2J6I}.
HELIX 343 345 {ECO:0000244|PDB:2J6I}.
STRAND 346 349 {ECO:0000244|PDB:2J6I}.
SEQUENCE 364 AA; 40370 MW; 1B30982E0D5B77E8 CRC64;
MKIVLVLYDA GKHAADEEKL YGCTENKLGI ANWLKDQGHE LITTSDKEGE TSELDKHIPD
ADIIITTPFH PAYITKERLD KAKNLKLVVV AGVGSDHIDL DYINQTGKKI SVLEVTGSNV
VSVAEHVVMT MLVLVRNFVP AHEQIINHDW EVAAIAKDAY DIEGKTIATI GAGRIGYRVL
ERLLPFNPKE LLYYDYQALP KEAEEKVGAR RVENIEELVA QADIVTVNAP LHAGTKGLIN
KELLSKFKKG AWLVNTARGA ICVAEDVAAA LESGQLRGYG GDVWFPQPAP KDHPWRDMRN
KYGAGNAMTP HYSGTTLDAQ TRYAEGTKNI LESFFTGKFD YRPQDIILLN GEYVTKAYGK
HDKK


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