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Protein
Submitted name:

F420-reducing hydrogenase, subunit beta

Gene

frhB

Organism
Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei48 – 481FAD; via amide nitrogenCombined sources
Metal bindingi103 – 1031Iron-sulfur (4Fe-4S) 1Combined sources
Metal bindingi103 – 1031Iron-sulfur (4Fe-4S) 2Combined sources
Metal bindingi104 – 1041Iron-sulfur (4Fe-4S) 1Combined sources
Metal bindingi104 – 1041Iron-sulfur (4Fe-4S) 2Combined sources
Metal bindingi134 – 1341Iron-sulfur (4Fe-4S) 1Combined sources
Metal bindingi134 – 1341Iron-sulfur (4Fe-4S) 2Combined sources
Metal bindingi192 – 1921Iron-sulfur (4Fe-4S) 1Combined sources
Metal bindingi195 – 1951Iron-sulfur (4Fe-4S) 1Combined sources
Binding sitei198 – 1981FADCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 307FADCombined sources
Nucleotide bindingi73 – 775FADCombined sources
Nucleotide bindingi133 – 1353FADCombined sources
Nucleotide bindingi207 – 2104FADCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseImported

Keywords - Ligandi

4Fe-4SCombined sources, FADCombined sources, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciMMAR79929:GH5J-1689-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
F420-reducing hydrogenase, subunit betaImported (EC:1.12.98.1Imported)
Gene namesi
Name:frhBImported
Ordered Locus Names:MTBMA_c16830Imported
OrganismiMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)Imported
Taxonomic identifieri79929 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
ProteomesiUP000000345 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi79929.MTBMA_c16830.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZFSelectron microscopy4.00C1-281[»]
4CI0electron microscopy3.36C1-281[»]
4OMFX-ray1.71B1-281[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000223731.
KOiK00441.
OMAiREYGCEK.

Family and domain databases

InterProiIPR007516. Co_F420_Hydgase/DH_bsu_N.
IPR017679. Coenz_F420_hydrogenase_bsu.
IPR007525. FrhB_FdhB_C.
[Graphical view]
PfamiPF04432. FrhB_FdhB_C. 1 hit.
PF04422. FrhB_FdhB_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03289. frhB. 1 hit.

Sequencei

Sequence statusi: Complete.

D9PYF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLGTYKEIV SARSTDREIQ KLAQDGGIVT GLLAYALDEG IIEGAVVAGP
60 70 80 90 100
GEEFWKPQPM VAMSSDELKA AAGTKYTFSP NVMMLKKAVR QYGIEKLGTV
110 120 130 140 150
AIPCQTMGIR KMQTYPFGVR FLADKIKLLV GIYCMENFPY TSLQTFICEK
160 170 180 190 200
LGVSMELVEK MDIGKGKFWV YTQDDVLTLP LKETHGYEQA GCKICKDYVA
210 220 230 240 250
ELADVSTGSV GSPDGWSTVI TRTDAGDSIF KQAVEAGLFE TKPIEEVKPG
260 270 280
LGLLEKLAAQ KKEKAEKNIA ARKEMGLPTP F
Length:281
Mass (Da):30,744
Last modified:October 5, 2010 - v1
Checksum:i1E981B4ADF3B1A16
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001710 Genomic DNA. Translation: ADL59254.1.
RefSeqiWP_013296464.1. NC_014408.1.
YP_003850567.1. NC_014408.1.

Genome annotation databases

EnsemblBacteriaiADL59254; ADL59254; MTBMA_c16830.
GeneIDi9705394.
KEGGimmg:MTBMA_c16830.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001710 Genomic DNA. Translation: ADL59254.1.
RefSeqiWP_013296464.1. NC_014408.1.
YP_003850567.1. NC_014408.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZFSelectron microscopy4.00C1-281[»]
4CI0electron microscopy3.36C1-281[»]
4OMFX-ray1.71B1-281[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi79929.MTBMA_c16830.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADL59254; ADL59254; MTBMA_c16830.
GeneIDi9705394.
KEGGimmg:MTBMA_c16830.

Phylogenomic databases

HOGENOMiHOG000223731.
KOiK00441.
OMAiREYGCEK.

Enzyme and pathway databases

BioCyciMMAR79929:GH5J-1689-MONOMER.

Family and domain databases

InterProiIPR007516. Co_F420_Hydgase/DH_bsu_N.
IPR017679. Coenz_F420_hydrogenase_bsu.
IPR007525. FrhB_FdhB_C.
[Graphical view]
PfamiPF04432. FrhB_FdhB_C. 1 hit.
PF04422. FrhB_FdhB_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03289. frhB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Methanothermobacter marburgensis."
    Kaster A., Seedorf H., Goenrich M., Wiezer A., Liesegang H., Thauer R., Gottschalk G.
    Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Marburg.
  2. "Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism."
    Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K.
    J. Bacteriol. 192:5850-5851(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / MarburgImported.
  3. "De novo modeling of the F(420)-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy."
    Mills D.J., Vitt S., Strauss M., Shima S., Vonck J.
    Elife 2:e00218-e00218(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS) IN COMPLEX WITH FAD AND IRON-SULFUR (4FE-4S).
  4. "Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector."
    Allegretti M., Mills D.J., McMullan G., Kuhlbrandt W., Vonck J.
    Elife 3:e01963-e01963(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.36 ANGSTROMS) IN COMPLEX WITH FAD AND IRON-SULFUR (4FE-4S).
  5. "The F-reducing [NiFe]-hydrogenase complex from Methanothermobacter marburgensis, the first X-ray structure of a group 3 family member."
    Vitt S., Ma K., Warkentin E., Moll J., Pierik A.J., Shima S., Ermler U.
    J. Mol. Biol. 426:2813-2826(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH FAD AND IRON-SULFUR (4FE-4S).

Entry informationi

Entry nameiD9PYF6_METTM
AccessioniPrimary (citable) accession number: D9PYF6
Entry historyi
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: July 22, 2015
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteomeImported

External Data

Dasty 3

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 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.