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0  structures 20  species 0  interactions 20  sequences 1  architecture

Family: NiFe_hyd_3_EhaA (PF17367)

Summary: NiFe-hydrogenase-type-3 Eha complex subunit A

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NiFe-hydrogenase-type-3 Eha complex subunit A Provide feedback

Energy-converting [NiFe] hydrogenases are membrane-bound enzymes with a six-subunit core: the large and small hydrogenase subunits, plus two hydrophilic proteins and two integral membrane proteins. Their large and small subunits show little sequence similarity to other [NiFe] hydrogenases, except for key conserved residues coordinating the active site and [FeS] cluster. Energy-converting [NiFe] hydrogenases function as ion pumps, catalyzing the reduction of ferredoxin with H2 driven by the proton-motive force or the sodium-ion-motive force [1]. Eha and Ehb hydrogenases contain extra subunits in addition to those shared by other energy-converting [NiFe] hydrogenases (or [NiFe]-hydrogenase-3-type). Eha contains a 6[4Fe-4S] polyferredoxin, a 10[4F-4S] polyferredoxin, ten other predicted integral membrane proteins (EhaA, EhaB, EhaC, EhaD, EhaE, EhaF, EhaG, EhaI, EhaK, EhaL) and four hydrophobic subunits (EhaM, EhaR, EhS, EhT) [2]. Eha and Ehb catalyse the reduction of low-potential redox carriers (e.g. ferredoxins or polyferredoxins), which then might function as electron donors to oxidoreductases [3]. Based on sequence similarity and genome context analysis, other organisms such as Methanopyrus kandleri, Methanocaldococcus jannaschii, and Methanothermobacter marburgensis also encode Eha-like [NiFe]-hydrogenase-3-type complexes and have very similar eha operon structure [3]. This domain family can be found on the small membrane proteins that are predicted to be the EhaA trans-membrane subunits of multisubunit membrane-bound [NiFe]-hydrogenase Eha complexes.

Literature references

  1. Kaster AK, Goenrich M, Seedorf H, Liesegang H, Wollherr A, Gottschalk G, Thauer RK;, Archaea. 2011;2011:973848.: More than 200 genes required for methane formation from H(2) and CO(2) and energy conservation are present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus. PUBMED:21559116 EPMC:21559116

  2. Tersteegen A, Hedderich R;, Eur J Biochem. 1999;264:930-943.: Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins. PUBMED:10491142 EPMC:10491142

  3. Nikolskaya AN, Arighi CN, Huang H, Barker WC, Wu CH;, Evol Bioinform Online. 2007;2:197-209.: PIRSF family classification system for protein functional and evolutionary analysis. PUBMED:19455212 EPMC:19455212


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Domain organisation

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(9)
Full
(20)
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(45)
NCBI
(61)
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(3)
RP35
(8)
RP55
(21)
RP75
(29)
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  Seed
(9)
Full
(20)
Representative proteomes UniProt
(45)
NCBI
(61)
Meta
(0)
RP15
(3)
RP35
(8)
RP55
(21)
RP75
(29)
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  Seed
(9)
Full
(20)
Representative proteomes UniProt
(45)
NCBI
(61)
Meta
(0)
RP15
(3)
RP35
(8)
RP55
(21)
RP75
(29)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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Curation and family details

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This family is new in this Pfam release.

Seed source: PRODOM:PD029748
Previous IDs: none
Type: Family
Author: El-Gebali S
Number in seed: 9
Number in full: 20
Average length of the domain: 93.00 aa
Average identity of full alignment: 41 %
Average coverage of the sequence by the domain: 89.95 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.5 25.5
Trusted cut-off 25.6 54.7
Noise cut-off 25.4 25.4
Model length: 97
Family (HMM) version: 1
Download: download the raw HMM for this family

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