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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi12 – 121Iron-sulfur 1 (4Fe-4S)1 Publication
Metal bindingi15 – 151Iron-sulfur 1 (4Fe-4S)1 Publication
Metal bindingi18 – 181Iron-sulfur 1 (4Fe-4S)1 Publication
Metal bindingi22 – 221Iron-sulfur 2 (4Fe-4S)1 Publication
Metal bindingi73 – 731Iron-sulfur 3 (4Fe-4S)1 Publication
Metal bindingi76 – 761Iron-sulfur 3 (4Fe-4S)1 Publication
Metal bindingi81 – 811Iron-sulfur 3 (4Fe-4S)1 Publication
Metal bindingi121 – 1211Iron-sulfur 3 (4Fe-4S)1 Publication
Metal bindingi138 – 1381Iron-sulfur 2 (4Fe-4S)1 Publication
Metal bindingi141 – 1411Iron-sulfur 2 (4Fe-4S)1 Publication
Metal bindingi153 – 1531Iron-sulfur 2 (4Fe-4S)1 Publication
Metal bindingi157 – 1571Iron-sulfur 1 (4Fe-4S)1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 215214Formate dehydrogenase subunit betaPRO_0000159221Add
BLAST

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi9 – 113Combined sources
Helixi17 – 2610Combined sources
Beta strandi42 – 443Combined sources
Beta strandi52 – 609Combined sources
Beta strandi63 – 719Combined sources
Helixi80 – 856Combined sources
Turni86 – 883Combined sources
Beta strandi92 – 954Combined sources
Turni97 – 993Combined sources
Beta strandi102 – 1043Combined sources
Helixi106 – 1105Combined sources
Helixi114 – 1207Combined sources
Helixi142 – 1454Combined sources
Turni146 – 1483Combined sources
Helixi152 – 1565Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi162 – 1665Combined sources
Helixi167 – 18115Combined sources
Turni182 – 1843Combined sources
Beta strandi189 – 1924Combined sources
Turni193 – 1953Combined sources
Beta strandi197 – 2048Combined sources
Helixi206 – 2083Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H0HX-ray1.80B/L2-215[»]
ProteinModelPortaliQ8GC87.
SMRiQ8GC87. Positions 2-215.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GC87.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 32304Fe-4S ferredoxin-type 1Add
BLAST
Domaini129 – 168404Fe-4S ferredoxin-type 2Add
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1H0HX-ray1.80B/L2-215[»]
ProteinModelPortaliQ8GC87.
SMRiQ8GC87. Positions 2-215.
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...

Publicationsi

  1. "Gene sequence and the 1.8 A crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas."
    Raaijmakers H., Macieira S.I.M.G., Dias J.M., Teixeira S., Bursakov S., Huber R., Moura J.J.G., Moura I., Romao M.J.
    Structure 10:1261-1272(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156, PROTEIN SEQUENCE OF 157-215, SUBUNIT, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FDHA.
    Strain: ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759.
  2. Cited for: PROTEIN SEQUENCE OF 157-215, METAL-BINDING, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759.
  3. "Properties of formate dehydrogenase from Desulfivibrio gigas."
    Riederer-Henderson M.A., Peck H.D. Jr.
    Can. J. Microbiol. 32:430-435(1986)
    Cited for: FUNCTION.
  4. "Purification and characterization of a tungsten-containing formate dehydrogenase from Desulfovibrio gigas."
    Almendra M.J., Brondino C.D., Gavel O., Pereira A.S., Tavares P., Bursakov S., Duarte R., Caldeira J., Moura J.J.G., Moura I.
    Biochemistry 38:16366-16372(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, FUNCTION.
    Strain: ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759.
  5. "Tungsten-containing formate dehydrogenase from Desulfovibrio gigas: metal identification and preliminary structural data by multi-wavelength crystallography."
    Raaijmakers H., Teixeira S., Dias J.M., Almendra M.J., Brondino C.D., Moura I., Moura J.J.G., Romao M.J.
    J. Biol. Inorg. Chem. 6:398-404(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: METAL-BINDING, SUBUNIT.

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: December 9, 2015
This is version 66 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.