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Protein

Formate dehydrogenase

Gene

FMDH

Organism
Pichia angusta (Yeast) (Hansenula polymorpha)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 sitei93 – 931Substrate; via amide nitrogenUniRule annotation
Binding sitei119 – 1191SubstrateUniRule annotation
Binding sitei195 – 1951NADUniRule annotation
Binding sitei256 – 2561NAD; via carbonyl oxygenUniRule annotation
Sitei258 – 2581Important for catalytic activityUniRule annotation
Binding sitei282 – 2821NADUniRule annotation
Sitei311 – 3111Important for catalytic activityUniRule annotation
Binding sitei357 – 3571NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi174 – 1752NADUniRule annotation
Nucleotide bindingi230 – 2345NADUniRule annotation
Nucleotide bindingi311 – 3144NADUniRule 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:FMDH1 Publication
OrganismiPichia angusta (Yeast) (Hansenula polymorpha)
Taxonomic identifieri870730 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPichiaceaeOgataea

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCurated
Chaini2 – 362361Formate dehydrogenasePRO_0000076025Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP33677.
SMRiP33677. Positions 2-353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 119118CatalyticUniRule annotationAdd
BLAST
Regioni120 – 312193Coenzyme-bindingUniRule annotationAdd
BLAST
Regioni313 – 35846CatalyticUniRule annotationAdd
BLAST

Sequence similaritiesi

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

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.
IPR029752. D-isomer_DH_CS1.
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.
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.

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

P33677-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVVLVLYDA GKHAQDEERL YGCTENALGI RDWLEKQGHD VVVTSDKEGQ
60 70 80 90 100
NSVLEKNISD ADVIISTPFH PAYITKERID KAKKLKLLVV AGVGSDHIDL
110 120 130 140 150
DYINQSGRDI SVLEVTGSNV VSVAEHVVMT MLVLVRNFVP AHEQIISGGW
160 170 180 190 200
NVAEIAKDSF DIEGKVIATI GAGRIGYRVL ERLVAFNPKE LLYYDYQSLS
210 220 230 240 250
KEAEEKVGAR RVHDIKELVA QADIVTINCP LHAGSKGLVN AELLKHFKKG
260 270 280 290 300
AWLVNTARGA ICVAEDVAAA VKSGQLRGYG GDVWFPQPAP KDHPWRSMAN
310 320 330 340 350
KYGAGNAMTP HYSGSVIDAQ VRYAQGTKNI LESFFTQKFD YRPQDIILLN
360
GKYKTKSYGA DK
Length:362
Mass (Da):39,911
Last modified:January 23, 2007 - v2
Checksum:i0037BFD132FC055B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
A06214 Unassigned DNA. Translation: CAA00531.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
A06214 Unassigned DNA. Translation: CAA00531.1.

3D structure databases

ProteinModelPortaliP33677.
SMRiP33677. Positions 2-353.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
IPR029752. D-isomer_DH_CS1.
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.
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...

Entry informationi

Entry nameiFDH_PICAN
AccessioniPrimary (citable) accession number: P33677
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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.