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Protein

Formate dehydrogenase

Gene

fdh

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 annotation

Catalytic activityi

Formate + NAD+ = CO2 + NADH.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei94 – 941Substrate; via amide nitrogenUniRule annotation
Binding sitei120 – 1201SubstrateUniRule annotation
Binding sitei196 – 1961NADUniRule annotation
Binding sitei257 – 2571NAD; via carbonyl oxygenUniRule annotation
Sitei259 – 2591Important for catalytic activityUniRule annotation
Binding sitei283 – 2831NADUniRule annotation
Sitei312 – 3121Important for catalytic activityUniRule annotation
Binding sitei358 – 3581NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi175 – 1762NADUniRule annotation
Nucleotide bindingi231 – 2355NADUniRule annotation
Nucleotide bindingi312 – 3154NADUniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Formate dehydrogenase1 PublicationUniRule annotation (EC:1.2.1.2UniRule annotation)
Short name:
FDHUniRule annotation
Alternative name(s):
NAD-dependent formate dehydrogenaseUniRule annotation
Gene namesi
Name:fdh1 Publication
ORF Names:99H12.160, NCU03813
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805 Componenti: Chromosome 2, Linkage Group V

Organism-specific databases

EuPathDBiFungiDB:NCU03813.

Subcellular locationi

  • Cytoplasm UniRule annotation

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Formate dehydrogenasePRO_0000076026Add
BLAST

Proteomic databases

PRIDEiQ07103.

Expressioni

Developmental stagei

Developmentally regulated. Expressed only during conidiation and early germination.1 Publication

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ07103.
SMRiQ07103. Positions 3-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni3 – 120118CatalyticUniRule annotationAdd
BLAST
Regioni121 – 313193Coenzyme-bindingUniRule annotationAdd
BLAST
Regioni314 – 35946CatalyticUniRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi364 – 37411Ala-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000136703.
InParanoidiQ07103.
KOiK00122.
OMAiEVTYCNS.
OrthoDBiEOG769ZV3.

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.

Q07103-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKVLAVLYD GGKHGEEVPE LLGTIQNELG LRKWLEDQGH TLVTTCDKDG
60 70 80 90 100
ENSTFDKELE DAEIIITTPF HPGYLTAERL ARAKKLKLAV TAGIGSDHVD
110 120 130 140 150
LNAANKTNGG ITVAEVTGSN VVSVAEHVLM TILVLVRNFV PAHEQIQEGR
160 170 180 190 200
WDVAEAAKNE FDLEGKVVGT VGVGRIGERV LRRLKPFDCK ELLYYDYQPL
210 220 230 240 250
SAEKEAEIGC RRVADLEEML AQCDVVTINC PLHEKTQGLF NKELISKMKK
260 270 280 290 300
GSWLVNTARG AIVVKEDVAE ALKSGHLRGY GGDVWFPQPA PQDHPLRYAK
310 320 330 340 350
NPFGGGNAMV PHMSGTSLDA QKRYAAGTKA IIESYLSGKH DYRPEDLIVY
360 370
GGDYATKSYG ERERAKAAAA AAKSA
Length:375
Mass (Da):40,957
Last modified:February 1, 1995 - v1
Checksum:i3073CB95FB204968
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13964 Genomic DNA. Translation: AAA99900.1.
AL451018 Genomic DNA. Translation: CAC18252.1.
CM002240 Genomic DNA. Translation: EAA31966.1.
PIRiA47117.
RefSeqiXP_961202.1. XM_956109.3.

Genome annotation databases

EnsemblFungiiEFNCRT00000003500; EFNCRP00000003500; EFNCRG00000003496.
GeneIDi3877330.
KEGGincr:NCU03813.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13964 Genomic DNA. Translation: AAA99900.1.
AL451018 Genomic DNA. Translation: CAC18252.1.
CM002240 Genomic DNA. Translation: EAA31966.1.
PIRiA47117.
RefSeqiXP_961202.1. XM_956109.3.

3D structure databases

ProteinModelPortaliQ07103.
SMRiQ07103. Positions 3-354.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ07103.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000003500; EFNCRP00000003500; EFNCRG00000003496.
GeneIDi3877330.
KEGGincr:NCU03813.

Organism-specific databases

EuPathDBiFungiDB:NCU03813.

Phylogenomic databases

HOGENOMiHOG000136703.
InParanoidiQ07103.
KOiK00122.
OMAiEVTYCNS.
OrthoDBiEOG769ZV3.

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

« Hide 'large scale' publications
  1. "Developmental regulation of the gene for formate dehydrogenase in Neurospora crassa."
    Chow C.M., RajBhandary U.L.
    J. Bacteriol. 175:3703-3709(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE.
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  2. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
    Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
    Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  3. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Entry informationi

Entry nameiFDH_NEUCR
AccessioniPrimary (citable) accession number: Q07103
Secondary accession number(s): Q7RVC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 20, 2016
This is version 128 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

Complete proteome, Reference proteome

Documents

  1. 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.