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Reviewed, UniProtKB/Swiss-Prot O27434 (HDRA_METTH)

Last modified November 25, 2008. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    CoB--CoM heterodisulfide reductase iron-sulfur subunit A
    EC=1.8.98.1
Gene names
Name: hdrA
Ordered Locus Names: MTH_1381
OrganismMethanobacterium thermoautotrophicum [Complete proteome] [HAMAP]
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length659 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B). May act as the catalytic subunit By similarity.

Catalytic activity

Coenzyme B + coenzyme M + methanophenazine = N-(7-((2-sulfoethyl)dithio)heptanoyl)-O(3)-phospho-L-threonine + dihydromethanophenazine.

Cofactor

Binds 4 4Fe-4S clusters per subunit By similarity.

FAD By similarity.

Pathway

Cofactor metabolism; coenzyme B/coenzyme M regeneration; coenzyme B and coenzyme M from CoB-CoM heterodisulfide: step 1/1.

Subunit structure

The heterodisulfide reductase is composed of three subunits; hdrA, hdrB and hdrC. It forms a complex with the F420-non-reducing hydrogenase (Mvh), which provides the reducing equivalents to the heterodisulfide reductase By similarity.

Sequence similarities

Belongs to the hdrA family.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 659659CoB--CoM heterodisulfide reductase iron-sulfur subunit A
PRO_0000150061

Regions

Domain245 – 275314Fe-4S ferredoxin-type 1
Domain293 – 322304Fe-4S ferredoxin-type 2
Domain582 – 611304Fe-4S ferredoxin-type 3
Domain612 – 641304Fe-4S ferredoxin-type 4
Nucleotide binding159 – 18224FAD Potential

Sites

Metal binding2551Iron-sulfur 1 (4Fe-4S) Potential
Metal binding2581Iron-sulfur 1 (4Fe-4S) Potential
Metal binding2611Iron-sulfur 1 (4Fe-4S) Potential
Metal binding2651Iron-sulfur 2 (4Fe-4S) Potential
Metal binding3021Iron-sulfur 2 (4Fe-4S) Potential
Metal binding3051Iron-sulfur 2 (4Fe-4S) Potential
Metal binding3081Iron-sulfur 2 (4Fe-4S) Potential
Metal binding3121Iron-sulfur 1 (4Fe-4S) Potential
Metal binding5921Iron-sulfur 3 (4Fe-4S) Potential
Metal binding5951Iron-sulfur 3 (4Fe-4S) Potential
Metal binding5981Iron-sulfur 3 (4Fe-4S) Potential
Metal binding6021Iron-sulfur 4 (4Fe-4S) Potential
Metal binding6211Iron-sulfur 4 (4Fe-4S) Potential
Metal binding6241Iron-sulfur 4 (4Fe-4S) Potential
Metal binding6271Iron-sulfur 4 (4Fe-4S) Potential
Metal binding6311Iron-sulfur 3 (4Fe-4S) Potential

Sequences

Sequence LengthMass (Da)Tools
O27434-1 [UniParc].

Last modified January 16, 2004. Version 2.
Checksum: ED517077EC5B6CBD

FASTA65972,392
        10         20         30         40         50         60 
MAEEKKEETM EEPRIGVYVC HCGVNIGGVV DIEAVRDYAA KLPNVVVSKD YKYYCSDPGQ 

        70         80         90        100        110        120 
LEIQKDIKEL GLNRVVVAAC SPRLHEPTFR RCVEEAGLNQ FLFEFANLRE QDSWVHMDDP 

       130        140        150        160        170        180 
EGATEKAKDL VRMAVAKARL LEPLEASKVS VDDKALVIGG GVAGIQTALD LADMGFKTYM 

       190        200        210        220        230        240 
VEKRPSISGR MGQLDKTFPT LDCSMCILAP KMVDVGKHDN IELITYAEVK EVDGYIGNFK 

       250        260        270        280        290        300 
VKIEKKPRYI DEDLCTGCGS CVEVCPIEMP NYFDEGIGMT KAVYIPFPQA VPLCATIDKD 

       310        320        330        340        350        360 
YCIECMLCDE ICERGAVKHD QEPEEIEIEV GTIIVATGYD AYDPTEKLEY GYGRHTNVIT 

       370        380        390        400        410        420 
GLELERMINA SGPTDGKVIK PSDGEKPKRV AFIHCVGSRD EQIGKPYCSR VCCMYIMKNA 

       430        440        450        460        470        480 
QLIKDKMPDT EVTLYYMDIR AFGKGFEEFY KRSQEKYGIK FIRGRPAEIL ENPDLTLTVR 

       490        500        510        520        530        540 
SEDTLLGKVT EYDYDMVVLG VGLVPPEGSE KLRQTIGLSK SADGFLMEAH PKLRPVDTLT 

       550        560        570        580        590        600 
DGVYLAGVAQ GPKDIPDAVA QASGAAARAA IPMVKGEVEI EPIVAVTDSD VCGGCEVCIE 

       610        620        630        640        650 
LCPFGAISIE EGHANVNVAL CKGCGTCVAA CPSGAMDQQH FRTEQIMAQI EAALNEQAK 

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References

[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Delta H.

Cross-references

Sequence databases

AE000666 Genomic DNA. Translation: AAB85858.1. Different initiation.
PIRG69050.
RefSeqNP_276497.1.

3D structure databases

HSSPHSSP built from PDB template 1DWL based on UniProtKB P07485.
ModBaseSearch...

Genome annotation databases

GeneID1471098.
GenomeReviewsGene locus MTH_1381 in contig AE000666_GR.
KEGGmth:MTH1381.
NMPDRfig|187420.1.peg.1352.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO27434.

Enzyme and pathway databases

BioCycMTHE187420:MTH1381-MON.

Family and domain databases

InterProIPR001450. 4Fe4S_Fe_S_bd.
IPR006076. FAD-dep_OxRdtase.
IPR001100. Pyr_nuc-diS_OxRdtase.
[Graphical view]
PfamPF01266. DAO. 1 hit.
PF00037. Fer4. 4 hits.
[Graphical view]
PRINTSPR00353. 4FE4SFRDOXIN.
PR00411. PNDRDTASEI.
PROSITEPS00198. 4FE4S_FER_1. 4 hits.
PS51379. 4FE4S_FER_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubO27434.

Entry information

Entry nameHDRA_METTH
AccessionPrimary (citable) accession number: O27434
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: November 25, 2008
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents