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P33160

- FDH_PSESR

UniProt

P33160 - FDH_PSESR

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Protein

Formate dehydrogenase

Gene
N/A
Organism
Pseudomonas sp. (strain 101) (Achromobacter parvulus T1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Formate + NAD+ = CO2 + NADH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei285 – 2851By similarity
Binding sitei309 – 3091NADBy similarity
Active sitei333 – 3331Proton donorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi202 – 2032NADBy similarity
Nucleotide bindingi283 – 2853NADBy similarity
Nucleotide bindingi333 – 3364NADBy similarity

GO - Molecular functioni

  1. formate dehydrogenase (NAD+) activity Source: UniProtKB-EC
  2. NAD binding Source: InterPro
  3. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.2.1.2. 5085.

Names & Taxonomyi

Protein namesi
Recommended name:
Formate dehydrogenase (EC:1.2.1.2)
Alternative name(s):
NAD-dependent formate dehydrogenase
Short name:
FDH
OrganismiPseudomonas sp. (strain 101) (Achromobacter parvulus T1)
Taxonomic identifieri33067 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi256 – 2561C → S or M: High resistance to inactivation by Hg(2+), Increased stability at 25 degree Celsius and decreased thermostability at 45 degree Celsius. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 401400Formate dehydrogenasePRO_0000076027Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
401
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75
Beta strandi21 – 233
Turni54 – 563
Helixi57 – 593
Helixi61 – 666
Beta strandi70 – 756
Helixi83 – 886
Beta strandi92 – 976
Helixi106 – 1116
Beta strandi117 – 1237
Helixi130 – 1356
Beta strandi139 – 1424
Turni144 – 1474
Helixi148 – 16316
Helixi166 – 1749
Helixi180 – 1845
Beta strandi194 – 1985
Helixi202 – 21110
Helixi212 – 2143
Beta strandi217 – 2215
Helixi228 – 2347
Beta strandi237 – 2415
Helixi242 – 2454
Helixi246 – 2483
Beta strandi250 – 2545
Turni260 – 2645
Helixi268 – 2714
Beta strandi278 – 2825
Helixi286 – 2883
Helixi291 – 2999
Beta strandi302 – 3098
Beta strandi312 – 3154
Helixi321 – 3233
Helixi335 – 3373
Helixi339 – 35820
Helixi364 – 3663
Beta strandi367 – 3704
Beta strandi371 – 3733
Helixi377 – 3815

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GO1X-ray2.10A1-401[»]
2GUGX-ray2.28A/B/C/D1-401[»]
2NACX-ray1.80A/B2-394[»]
2NADX-ray2.05A/B2-394[»]
ProteinModelPortaliP33160.
SMRiP33160. Positions 2-392.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33160.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 147146CatalyticAdd
BLAST
Regioni148 – 334187Coenzyme-bindingAdd
BLAST
Regioni335 – 40167CatalyticAdd
BLAST

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
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]
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.

P33160-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKVLCVLYD DPVDGYPKTY ARDDLPKIDH YPGGQTLPTP KAIDFTPGQL
60 70 80 90 100
LGSVSGELGL RKYLESNGHT LVVTSDKDGP DSVFERELVD ADVVISQPFW
110 120 130 140 150
PAYLTPERIA KAKNLKLALT AGIGSDHVDL QSAIDRNVTV AEVTYCNSIS
160 170 180 190 200
VAEHVVMMIL SLVRNYLPSH EWARKGGWNI ADCVSHAYDL EAMHVGTVAA
210 220 230 240 250
GRIGLAVLRR LAPFDVHLHY TDRHRLPESV EKELNLTWHA TREDMYPVCD
260 270 280 290 300
VVTLNCPLHP ETEHMINDET LKLFKRGAYI VNTARGKLCD RDAVARALES
310 320 330 340 350
GRLAGYAGDV WFPQPAPKDH PWRTMPYNGM TPHISGTTLT AQARYAAGTR
360 370 380 390 400
EILECFFEGR PIRDEYLIVQ GGALAGTGAH SYSKGNATGG SEEAAKFKKA

V
Length:401
Mass (Da):44,136
Last modified:January 23, 2007 - v3
Checksum:i6B3EBA21F03A89A2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781D → S(PubMed:1954846)Curated
Sequence conflicti139 – 1402TV → VT(PubMed:1954846)Curated
Sequence conflicti146 – 1461C → V(PubMed:1954846)Curated
Sequence conflicti216 – 2172VH → HV(PubMed:1954846)Curated
Sequence conflicti328 – 3281N → D(PubMed:1954846)Curated

Sequence databases

PIRiJU0334.

Cross-referencesi

Sequence databases

PIRi JU0334.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GO1 X-ray 2.10 A 1-401 [» ]
2GUG X-ray 2.28 A/B/C/D 1-401 [» ]
2NAC X-ray 1.80 A/B 2-394 [» ]
2NAD X-ray 2.05 A/B 2-394 [» ]
ProteinModelPortali P33160.
SMRi P33160. Positions 2-392.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 1.2.1.2. 5085.

Miscellaneous databases

EvolutionaryTracei P33160.

Family and domain databases

Gene3Di 3.40.50.720. 2 hits.
InterProi IPR006139. 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 ]
Pfami PF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view ]
PROSITEi PS00065. 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 ]
ProtoNeti Search...

Publicationsi

  1. "NAD-dependent formate dehydrogenase of methylotrophic bacteria Pseudomonas sp. 101: cloning, expression, and study of the genetic structure."
    Tishkov V.I., Galkin A.G., Egorov A.M.
    Dokl. Akad. Nauk SSSR 317:745-748(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "NAD-dependent formate dehydrogenase from methylotrophic bacteria Pseudomonas sp. 101. I. Amino acid sequence."
    Popov V.O., Shumilin I.A., Ustinnikova T.B., Lamzin V.S., Egorov T.A.
    Bioorg. Khim. 16:324-335(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-394.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  4. "Catalytic properties and stability of a Pseudomonas sp.101 formate dehydrogenase mutants containing Cys-255-Ser and Cys-255-Met replacements."
    Tishkov V.I., Galkin A.G., Marchenko G.N., Egorova O.A., Sheluho D.V., Kulakova L.B., Dementieva L.A., Egorov A.M.
    Biochem. Biophys. Res. Commun. 192:976-981(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-256.

Entry informationi

Entry nameiFDH_PSESR
AccessioniPrimary (citable) accession number: P33160
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3