ID   HDRE_METMA              Reviewed;         259 AA.
AC   Q8PVW4;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 40.
DE   RecName: Full=CoB--CoM heterodisulfide reductase 2 subunit E;
DE            EC=1.8.98.1;
GN   Name=hdrE; OrderedLocusNames=MM_1843;
OS   Methanosarcina mazei (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2209;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
RX   MEDLINE=22120827; PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene
RT   transfer between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN   [2]
RP   FUNCTION, AND SOURCE OF ELECTRONS.
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
RX   PubMed=9654152; DOI=10.1016/S0014-5793(98)00555-9;
RA   Baeumer S., Murakami E., Brodersen J., Gottschalk G., Ragsdale S.W.,
RA   Deppenmeier U.;
RT   "The F420H2:heterodisulfide oxidoreductase system from Methanosarcina
RT   species. 2-Hydroxyphenazine mediates electron transfer from F420H2
RT   dehydrogenase to heterodisulfide reductase.";
RL   FEBS Lett. 428:295-298(1998).
CC   -!- FUNCTION: Part of a complex that catalyzes the reversible
CC       reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme
CC       M) and H-S-CoB (coenzyme B). HdrE may be responsible for anchoring
CC       the complex to the membrane.
CC   -!- CATALYTIC ACTIVITY: Coenzyme B + coenzyme M + methanophenazine =
CC       N-(7-((2-sulfoethyl)dithio)heptanoyl)-O(3)-phospho-L-threonine +
CC       dihydromethanophenazine.
CC   -!- PATHWAY: Cofactor metabolism; coenzyme B/coenzyme M regeneration;
CC       coenzyme B and coenzyme M from CoB-CoM heterodisulfide: step 1/1.
CC   -!- SUBUNIT: The heterodisulfide reductase 2 is composed of two
CC       subunits; hdrD and hdrE (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- MISCELLANEOUS: Methanophenazine seems to mediate electron transfer
CC       from a F420-non-reducing hydrogenase to the heterodisulfide
CC       reductase 2.
CC   -!- SIMILARITY: Belongs to the hdrE family.
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DR   EMBL; AE008384; AAM31539.1; -; Genomic_DNA.
DR   RefSeq; NP_633867.1; -.
DR   GeneID; 1480185; -.
DR   GenomeReviews; AE008384_GR; MM_1843.
DR   KEGG; mma:MM_1843; -.
DR   NMPDR; fig|192952.1.peg.1843; -.
DR   HOGENOM; Q8PVW4; -.
DR   OMA; Q8PVW4; REASIMY.
DR   BioCyc; MMAZ192952:MM1843-MON; -.
DR   BRENDA; 1.8.98.1; 261165.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IEA:EC.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Membrane; Methanogenesis;
KW   Oxidoreductase; Transmembrane.
FT   CHAIN         1    259       CoB--CoM heterodisulfide reductase 2
FT                                subunit E.
FT                                /FTId=PRO_0000150084.
FT   TRANSMEM     15     35       Potential.
FT   TRANSMEM    104    124       Potential.
FT   TRANSMEM    147    167       Potential.
FT   TRANSMEM    180    200       Potential.
FT   TRANSMEM    218    238       Potential.
SQ   SEQUENCE   259 AA;  28989 MW;  A328ADE9E99406F9 CRC64;
     MAYFSGLSDA LRLTFVQIMI LSAIAVVIFL YGMIGNFQKW GAGVTGYALE PPTGKKGSAI
     RFLKTWWAQV RAESHHHGKP ILEVLILDIF FQRRILKRSP IRWFMHFTIF AGWMSLFALS
     GLMFAVEMTE KIGIELPFTP AEFREMLSLP NYIFGYILLI GVMIAVVRRL FVSEVREASI
     MYDWVLLGGV FIVTISGFIA DGIRTGIIWG FGLDPVTAPP AALFHSVISL LFCIAYIPYS
     KYIHVIATPL AILANKGGE
//