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Protein

Formate dehydrogenase, mitochondrial

Gene
N/A
Organism
Hordeum vulgare (Barley)
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. Involved in the cell stress response.UniRule annotation

Catalytic activityi

Formate + NAD+ = CO2 + NADH.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei121Substrate; via amide nitrogenUniRule annotation1
Binding sitei145SubstrateUniRule annotation1
Binding sitei146NADUniRule annotation1
Binding sitei220NADUniRule annotation1
Binding sitei281NAD; via carbonyl oxygenUniRule annotation1
Sitei283Important for catalytic activityUniRule annotation1
Binding sitei307NADUniRule annotation1
Sitei331Important for catalytic activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi255 – 259NADUniRule annotation5
Nucleotide bindingi331 – 334NADUniRule annotation4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Formate dehydrogenase, mitochondrial1 PublicationUniRule annotation (EC:1.2.1.2UniRule annotation)
Short name:
FDHUniRule annotation
Alternative name(s):
NAD-dependent formate dehydrogenaseUniRule annotation
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 29MitochondrionUniRule annotationAdd BLAST29
ChainiPRO_000000719430 – 377Formate dehydrogenase, mitochondrialAdd BLAST348

Proteomic databases

PRIDEiQ9ZRI8.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiQ9ZRI8. 1 interactor.
STRINGi4513.MLOC_75288.1.

Structurei

3D structure databases

ProteinModelPortaliQ9ZRI8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 145CatalyticUniRule annotationAdd BLAST116
Regioni146 – 332Coenzyme-bindingUniRule annotationAdd BLAST187
Regioni333 – 376CatalyticUniRule annotationAdd BLAST44

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0069. Eukaryota.
COG1052. LUCA.

Family and domain databases

CDDicd05302. FDH. 1 hit.
Gene3Di3.40.50.720. 2 hits.
HAMAPiMF_03210. Formate_dehydrogenase. 1 hit.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR006140. D-isomer_DH_NAD-bd.
IPR033689. FDH_NAD-dep.
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.
PROSITEiPS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9ZRI8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAMWRAAAR QLVDRAVGSR AAHTSAGSKK IVGVFYQAGE YADKNPNFVG
60 70 80 90 100
CVEGALGIRD WLESKGHHYI VTDDKEGFNS ELEKHIEDMH VLITTPFHPA
110 120 130 140 150
YVTAEKIKKA KTPELLLTAG IGSDHIDLPA AAAAGLTVAR VTGSNTVSVA
160 170 180 190 200
EDELMRILIL LRNFLPGYQQ VVKGEWNVAG IAHRAYDLEG KTVGTVGAGR
210 220 230 240 250
YGRLLLQRLK PFNCNLLYHD RLQINPELEK EIGAKFEEDL DAMLPKCDVV
260 270 280 290 300
VINTPLTEKT RGMFNKEKIA KMKKGVIIVN NARGAIMDTQ AVADACSSGH
310 320 330 340 350
IAGYGGDVWF PQPAPKDHPW RYMPNHAMTP HISGTTIDAQ LRYAAGVKDM
360 370
LDRYFKGEEF PVENYIVKEG ELASQYK
Length:377
Mass (Da):41,546
Last modified:May 1, 1999 - v1
Checksum:iE28C1FE24E9225C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88272 mRNA. Translation: BAA36181.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88272 mRNA. Translation: BAA36181.1.

3D structure databases

ProteinModelPortaliQ9ZRI8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9ZRI8. 1 interactor.
STRINGi4513.MLOC_75288.1.

Proteomic databases

PRIDEiQ9ZRI8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0069. Eukaryota.
COG1052. LUCA.

Family and domain databases

CDDicd05302. FDH. 1 hit.
Gene3Di3.40.50.720. 2 hits.
HAMAPiMF_03210. Formate_dehydrogenase. 1 hit.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR006140. D-isomer_DH_NAD-bd.
IPR033689. FDH_NAD-dep.
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.
PROSITEiPS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFDH_HORVU
AccessioniPrimary (citable) accession number: Q9ZRI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 1, 1999
Last modified: October 5, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.