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Reviewed, UniProtKB/Swiss-Prot P96801 (HDRA2_METKA)

Last modified November 25, 2008. Version 61. 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

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Names and origin

Protein namesRecommended name:
    CoB--CoM heterodisulfide reductase iron-sulfur subunit A 2
    EC=1.8.98.1
Gene names
Name: hdrA2
Synonyms: hdrA_2
Ordered Locus Names: MK0265
OrganismMethanopyrus kandleri [Complete proteome] [HAMAP]
Taxonomic identifier2320 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus

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Protein attributes

Sequence length656 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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 By similarity.

Sequence similarities

Belongs to the hdrA family.

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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 656656CoB--CoM heterodisulfide reductase iron-sulfur subunit A 2
PRO_0000150059

Regions

Domain238 – 269324Fe-4S ferredoxin-type 1
Domain286 – 315304Fe-4S ferredoxin-type 2
Domain577 – 606304Fe-4S ferredoxin-type 3
Domain610 – 639304Fe-4S ferredoxin-type 4
Nucleotide binding152 – 17524FAD Potential

Sites

Metal binding2481Iron-sulfur 1 (4Fe-4S) Potential
Metal binding2511Iron-sulfur 1 (4Fe-4S) Potential
Metal binding2541Iron-sulfur 1 (4Fe-4S) Potential
Metal binding2581Iron-sulfur 2 (4Fe-4S) Potential
Metal binding2951Iron-sulfur 2 (4Fe-4S) Potential
Metal binding2981Iron-sulfur 2 (4Fe-4S) Potential
Metal binding3011Iron-sulfur 2 (4Fe-4S) Potential
Metal binding3051Iron-sulfur 1 (4Fe-4S) Potential
Metal binding5861Iron-sulfur 3 (4Fe-4S) Potential
Metal binding5891Iron-sulfur 3 (4Fe-4S) Potential
Metal binding5921Iron-sulfur 3 (4Fe-4S) Potential
Metal binding5961Iron-sulfur 4 (4Fe-4S) Potential
Metal binding6191Iron-sulfur 4 (4Fe-4S) Potential
Metal binding6221Iron-sulfur 4 (4Fe-4S) Potential
Metal binding6251Iron-sulfur 4 (4Fe-4S) Potential
Metal binding6291Iron-sulfur 3 (4Fe-4S) Potential

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Sequences

Sequence LengthMass (Da)Tools
P96801-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: C7CF218545ACEA7C

FASTA65671,925
        10         20         30         40         50         60 
MAEEEPRIGV YVCHCGVNIA GVVDVKEVAE FAKTLKNVVV ARDYKYVCSD PGQEIIQRDI 

        70         80         90        100        110        120 
EKYDLNRVVV AACSPRLHEP TFRRCVEEAG LNPYCFEMAN IREHCSWVHM DDPARATEKA 

       130        140        150        160        170        180 
KDLVRMAVAK ARLLESLETI KVDVTDRALV IGGGVSGIQA ALDLADMGFE VILVEKEPSI 

       190        200        210        220        230        240 
GGRMAQLDKT FPTNDCSICI LAPKMVDVSK HPNIKMYTYA EVVEVDGYVG NFTVKIEKKP 

       250        260        270        280        290        300 
RYVDEDACTG CGACAEVCPI EVPNEFDEGL GMRKAIYKPF PQAVPSVFTI DEEHCIRCGL 

       310        320        330        340        350        360 
CEEVCDADAI DFDQEPEIVE EEVGAIICAI GYDTCDPTER EEYGYGVYDN VITSIELERL 

       370        380        390        400        410        420 
INASGPTGGK VVRPSDGKKP KRIAFIQCVG SRDPHRTNPY CSNVCCMYAM KLAQLIREKY 

       430        440        450        460        470        480 
PETQIDIYYM DVRAFGKGYE EYYERSQKQY GIRFIRGRPA EIVEDPETKN LIVRAEDTLL 

       490        500        510        520        530        540 
GDVVEREYDL VVLSVGMVPR DSADVIQEVL SISRSPDGFF MEAHPKLRPV DTAIDGIFLA 

       550        560        570        580        590        600 
GACQGPKDIP SSVAQGSAAA ARAATALAAG EVAVEPIVSE VDEEICGGCG TCVELCPYGA 

       610        620        630        640        650 
IELVEKDGKL VAEVTAALCK GCGTCAAACP SGAMEQNHFK TEQLYKQIEG AFRDPA

« Hide

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References

« Hide 'large scale' references
[1]"Heterodisulfide reductase from methanol-grown cells of Methanosarcina barkeri is not a flavoenzyme."
Kuenkel A., Vaupel M., Heim S., Thauer R.K., Hedderich R.
Eur. J. Biochem. 244:226-234(1997) [PubMed: 9063468] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed: 11930014] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

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Cross-references

Sequence databases

Y09871 Genomic DNA. Translation: CAA70999.1.
AE010324 Genomic DNA. Translation: AAM01482.1.
RefSeqNP_613552.1.

3D structure databases

HSSPHSSP built from PDB template 1CLF based on UniProtKB P00195.
ModBaseSearch...

Genome annotation databases

GeneID1477568.
GenomeReviewsGene locus MK0265 in contig AE009439_GR.
KEGGmka:MK0265.
NMPDRfig|190192.1.peg.265.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP96801.

Enzyme and pathway databases

BioCycMKAN190192:MK0265-MON.

Family and domain databases

InterProIPR001450. 4Fe4S_Fe_S_bd.
IPR006076. FAD-dep_OxRdtase.
IPR016040. NAD(P)-bd.
IPR001100. Pyr_nuc-diS_OxRdtase.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF01266. DAO. 1 hit.
PF00037. Fer4. 4 hits.
[Graphical view]
PRINTSPR00353. 4FE4SFRDOXIN.
PR00411. PNDRDTASEI.
PROSITEPS00198. 4FE4S_FER_1. 3 hits.
PS51379. 4FE4S_FER_2. 4 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameHDRA2_METKA
AccessionPrimary (citable) accession number: P96801
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: May 1, 1997
Last modified: November 25, 2008
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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