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Q8TYP4 (HDRA1_METKA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CoB--CoM heterodisulfide reductase iron-sulfur subunit A 1

EC=1.8.98.1
Gene names
Name:hdrA1
Synonyms:hdrA_1
Ordered Locus Names:MK0249
OrganismMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) [Reference proteome] [HAMAP]
Taxonomic identifier190192 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus

Protein attributes

Sequence length669 AA.
Sequence statusComplete.
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 M-coenzyme B heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B 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.

Ontologies

Keywords
   Biological processMethanogenesis
   Coding sequence diversitySelenocysteine
   DomainRepeat
   Ligand4Fe-4S
FAD
Flavoprotein
Iron
Iron-sulfur
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmethanogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

CoB--CoM heterodisulfide reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 669669CoB--CoM heterodisulfide reductase iron-sulfur subunit A 1
PRO_0000150058

Regions

Domain239 – 270324Fe-4S ferredoxin-type 1
Domain287 – 318324Fe-4S ferredoxin-type 2
Domain584 – 613304Fe-4S ferredoxin-type 3
Domain617 – 646304Fe-4S ferredoxin-type 4
Nucleotide binding153 – 17624FAD Potential

Sites

Metal binding2491Iron-sulfur 1 (4Fe-4S) Potential
Metal binding2521Iron-sulfur 1 (4Fe-4S) Potential
Metal binding2551Iron-sulfur 1 (4Fe-4S) Potential
Metal binding2591Iron-sulfur 2 (4Fe-4S) Potential
Metal binding2961Iron-sulfur 2 (4Fe-4S) Potential
Metal binding2991Iron-sulfur 2 (4Fe-4S) Potential
Metal binding3021Iron-sulfur 2 (4Fe-4S) Potential
Metal binding3061Iron-sulfur 1 (4Fe-4S) Potential
Metal binding5931Iron-sulfur 3 (4Fe-4S) Potential
Metal binding5961Iron-sulfur 3 (4Fe-4S) Potential
Metal binding5991Iron-sulfur 3 (4Fe-4S) Potential
Metal binding6031Iron-sulfur 4 (4Fe-4S) Potential
Metal binding6261Iron-sulfur 4 (4Fe-4S) Potential
Metal binding6291Iron-sulfur 4 (4Fe-4S) Potential
Metal binding6321Iron-sulfur 4 (4Fe-4S) Potential
Metal binding6361Iron-sulfur 3 (4Fe-4S) Potential

Amino acid modifications

Non-standard residue2001Selenocysteine Probable

Sequences

Sequence LengthMass (Da)Tools
Q8TYP4 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: C2D8D120157026E5

FASTA66973,742
        10         20         30         40         50         60 
MGDKDDVRIG VFVCHCGVNI KASVDVEEVV EYAKKLPGVV YATDYPFFCA DPGQEIIQEA 

        70         80         90        100        110        120 
IKEHDLDRVV VAACTPKIHE NTFRNCVKEA GLSPYYMEMV NIREHCSFVH MQEPEKATEK 

       130        140        150        160        170        180 
AKDLIRAAVE RAKRLEDVPT KEVEVENSVL IIGGGIAGIQ AALDLADQGF KVYLVEKEPT 

       190        200        210        220        230        240 
IGGNMARLAK TFPTDDCAMU ILAPKMVQVG NHPNIEMITY AEVKDVDGYI GNFEVTIEKK 

       250        260        270        280        290        300 
PRYVDEDACT GCGVCAEVCP IEVPNEFDLG IGTRKAIYVP FPQAMPLVYT IDMEHCIQCG 

       310        320        330        340        350        360 
LCEEACPQDP PAIDFDQEPE EIRLKVGTII VATGYEEFDA SKLEEYGYGK YDNVITTLEL 

       370        380        390        400        410        420 
ERMINPAGPT EGHVIRPSDG KEPHRIVFIH CVGSRCPGKE EKGEAYCSRI CCMFILKNAQ 

       430        440        450        460        470        480 
LIKQHEPDAE VYCCYMDVRA FGKGYEEYYE RAQKQFGVRF IRGRPAEIVE DPETKNLIVR 

       490        500        510        520        530        540 
VEDTLTGEPM EIEADLVVLG CGLVAPEETY SKLADILGID RSPDGFFKEL HPKLEPVSTK 

       550        560        570        580        590        600 
VRGVQIAGVA QGPKDIPDTV AQAKGAASEA SIPMSQGKVE IELITATVDE DVCGGCGACA 

       610        620        630        640        650        660 
QVCPFDAIEM VEKDGKRVAE VQDVACQGCG QCAAACPSGA MQLRYYRDEQ LMPQIEALLA 


EALEEEEEE 

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References

[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009439 Genomic DNA. Translation: AAM01466.1.
RefSeqNP_613536.1. NC_003551.1.

3D structure databases

ProteinModelPortalQ8TYP4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190192.MK0249.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM01466; AAM01466; MK0249.
GeneID1477552.
KEGGmka:MK0249.

Phylogenomic databases

eggNOGCOG1148.
HOGENOMHOG000230698.
KOK03388.
OMACTPKIHE.
ProtClustDBCLSK876667.

Enzyme and pathway databases

UniPathwayUPA00647; UER00700.

Family and domain databases

InterProIPR001450. 4Fe4S-bd_dom.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
[Graphical view]
PfamPF00037. Fer4. 2 hits.
PF12838. Fer4_7. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PROSITEPS00198. 4FE4S_FER_1. 4 hits.
PS51379. 4FE4S_FER_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHDRA1_METKA
AccessionPrimary (citable) accession number: Q8TYP4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: February 26, 2008
Last modified: December 11, 2013
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways