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CANBO:FDH

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Species (Taxon ID) Candida boidinii (Yeast). (5477)
Gene Name(s) FDH1 (ECO:0000303 with PMID:9226256[1], ECO:0000312 with EMBL:AAC49766.1)
Protein Name(s) Formate dehydrogenase (ECO:0000312 with EMBL:CAB54834.1)

NAD-dependent formate dehydrogenase (ECO:0000312 with EMBL:AAC49766.1)

External Links
UniProt O13437
EMBL AF004096
AJ245934
AJ011046
DQ458777
PDB 2FSS
2J6I
PDBsum 2FSS
2J6I
ProteinModelPortal O13437
SMR O13437
PRIDE O13437
BioCyc MetaCyc:MONOMER-17206
SABIO-RK O13437
EvolutionaryTrace O13437
GO GO:0005829
GO:0005524
GO:0008863
GO:0070403
GO:0016616
GO:0042803
GO:0042426
GO:0042183
GO:0015946
GO:0030416
GO:0006734
GO:0006735
Gene3D 3.40.50.720
InterPro IPR006139
IPR029753
IPR029752
IPR006140
IPR016040
Pfam PF00389
PF02826
PROSITE PS00065
PS00670
PS00671

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0070403

NAD+ binding

PMID:1248477[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0070403

NAD+ binding

PMID:10691964[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042803

protein homodimerization activity

PMID:17525463[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042803

protein homodimerization activity

PMID:1248477[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0042426

choline catabolic process

PMID:9226256[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042183

formate catabolic process

PMID:1248477[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042183

formate catabolic process

PMID:11171126[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042183

formate catabolic process

PMID:10691964[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0030416

methylamine metabolic process

PMID:9226256[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0015946

methanol oxidation

PMID:9226256[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008863

formate dehydrogenase (NAD+) activity

PMID:9226256[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008863

formate dehydrogenase (NAD+) activity

PMID:17525463[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008863

formate dehydrogenase (NAD+) activity

PMID:1248477[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008863

formate dehydrogenase (NAD+) activity

PMID:11171126[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008863

formate dehydrogenase (NAD+) activity

PMID:10691964[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006735

NADH regeneration

PMID:17525463[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006735

NADH regeneration

PMID:10691964[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006734

NADH metabolic process

PMID:9226256[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q08911

C

Seeded From UniProt

complete

enables

GO:0008863

formate dehydrogenase (NAD+) activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR033689

F

Seeded From UniProt

complete

enables

GO:0016616

oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006139

F

Seeded From UniProt

complete

enables

GO:0051287

NAD binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006139
InterPro:IPR006140

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006139
InterPro:IPR006140

P

Seeded From UniProt

complete

involved_in

GO:0042183

formate catabolic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000371006

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000371006

C

Seeded From UniProt

complete

enables

GO:0008863

formate dehydrogenase (NAD+) activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000371006

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

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Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Sakai, Y et al. (1997) 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 4480-5 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 2.3 Schüte, H et al. (1976) Purification and properties of formaldehyde dehydrogenase and formate dehydrogenase from Candida boidinii. Eur. J. Biochem. 62 151-60 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 3.3 Slusarczyk, H et al. (2000) Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues. Eur. J. Biochem. 267 1280-9 PubMed GONUTS page
  4. ↑ 4.0 4.1 4.2 Schirwitz, K et al. (2007) High-resolution structures of formate dehydrogenase from Candida boidinii. Protein Sci. 16 1146-56 PubMed GONUTS page
  5. ↑ 5.0 5.1 Labrou, NE & Rigden, DJ (2001) Active-site characterization of Candida boidinii formate dehydrogenase. Biochem. J. 354 455-63 PubMed GONUTS page
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