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Protein

Formate dehydrogenase subunit beta

Gene

fdhB

Organism
Desulfovibrio gigas
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Beta chain of the formate dehydrogenase (FDH) catalyzes the reversible two-electron oxidation of formate to carbon dioxide. FDH loses activity in the presence of air, but this activity can be restored. This chain is an electron transfer unit.2 Publications

Cofactori

[4Fe-4S] cluster1 PublicationNote: Binds 3 [4Fe-4S] clusters.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi12Iron-sulfur 1 (4Fe-4S)1 Publication1
Metal bindingi15Iron-sulfur 1 (4Fe-4S)1 Publication1
Metal bindingi18Iron-sulfur 1 (4Fe-4S)1 Publication1
Metal bindingi22Iron-sulfur 2 (4Fe-4S)1 Publication1
Metal bindingi73Iron-sulfur 3 (4Fe-4S)1 Publication1
Metal bindingi76Iron-sulfur 3 (4Fe-4S)1 Publication1
Metal bindingi81Iron-sulfur 3 (4Fe-4S)1 Publication1
Metal bindingi121Iron-sulfur 3 (4Fe-4S)1 Publication1
Metal bindingi138Iron-sulfur 2 (4Fe-4S)1 Publication1
Metal bindingi141Iron-sulfur 2 (4Fe-4S)1 Publication1
Metal bindingi153Iron-sulfur 2 (4Fe-4S)1 Publication1
Metal bindingi157Iron-sulfur 1 (4Fe-4S)1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Formate dehydrogenase subunit beta
Short name:
FDH subunit beta
Alternative name(s):
Formate dehydrogenase small subunit
Gene namesi
Name:fdhBImported
OrganismiDesulfovibrio gigasImported
Taxonomic identifieri879 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001592212 – 215Formate dehydrogenase subunit betaAdd BLAST214

Interactioni

Subunit structurei

Heterodimer of alpha (FdhA) and beta (FdhB) subunits.4 Publications

Structurei

Secondary structure

1215
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Helixi9 – 11Combined sources3
Helixi17 – 26Combined sources10
Beta strandi42 – 44Combined sources3
Beta strandi52 – 60Combined sources9
Beta strandi63 – 71Combined sources9
Helixi80 – 85Combined sources6
Turni86 – 88Combined sources3
Beta strandi92 – 95Combined sources4
Turni97 – 99Combined sources3
Beta strandi102 – 104Combined sources3
Helixi106 – 110Combined sources5
Helixi114 – 120Combined sources7
Helixi142 – 145Combined sources4
Turni146 – 148Combined sources3
Helixi152 – 156Combined sources5
Beta strandi158 – 160Combined sources3
Beta strandi162 – 166Combined sources5
Helixi167 – 181Combined sources15
Turni182 – 184Combined sources3
Beta strandi189 – 192Combined sources4
Turni193 – 195Combined sources3
Beta strandi197 – 204Combined sources8
Helixi206 – 208Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H0HX-ray1.80B/L2-215[»]
ProteinModelPortaliQ8GC87.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GC87.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 324Fe-4S ferredoxin-type 1Add BLAST30
Domaini129 – 1684Fe-4S ferredoxin-type 2Add BLAST40

Sequence similaritiesi

Contains 2 4Fe-4S ferredoxin-type domains.Curated

Keywords - Domaini

Repeat

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8GC87-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKGFFVDTT RCTACRGCQV ACKQWHGNPA TPTENTGFHQ NPPDFNFHTY
60 70 80 90 100
KLVRMHEQEI DGRIDWLFFP DQCRHCIAPP CKATADMEDE SAIIHDDATG
110 120 130 140 150
CVLFTPKTKD LEDYESVISA CPYDVPRKVA ESNQMAKCDM CIDRITNGLR
160 170 180 190 200
PACVTSCPTG AMNFGDLSEM EAMASARLAE IKAAYSDAKL CDPDDVRVIF
210
LTAHNPKLYH EYAVA
Length:215
Mass (Da):23,983
Last modified:January 23, 2007 - v3
Checksum:i01A18C18901FEA2F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ427412 Genomic DNA. Translation: CAD20557.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ427412 Genomic DNA. Translation: CAD20557.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H0HX-ray1.80B/L2-215[»]
ProteinModelPortaliQ8GC87.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GC87.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFDHB_DESGI
AccessioniPrimary (citable) accession number: Q8GC87
Secondary accession number(s): P83237
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: October 5, 2016
This is version 67 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

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.