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3.D.7.1.1
H2:heterodisulfide oxidoreductase, HHO. Two protons are consumed in the cytoplasm while two protons are released in the periplasm, contributing to the pmf (Simon et al., 2008; Welte and Deppenmeier 2013).  The HdrD/E-type heterodisulfide reductase probably can function independently of the other subunits.

Accession Number:P96796
Protein Name:HDRE
Length:263
Molecular Weight:29734.00
Species:Methanosarcina barkeri [269797]
Number of TMSs:5
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate hydron

Cross database links:

RefSeq: YP_305124.1   
Entrez Gene ID: 3624317   
Pfam: PF02665   
BioCyc: MBAR269797:MBAR_A1598-MONOMER   
KEGG: mba:Mbar_A1598   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0009325 C:nitrate reductase complex
GO:0005886 C:plasma membrane
GO:0051912 F:CoB--CoM heterodisulfide reductase activity
GO:0008940 F:nitrate reductase activity
GO:0015948 P:methanogenesis
GO:0055114 P:oxidation reduction

References (3)

[1] “Heterodisulfide reductase from methanol-grown cells of Methanosarcina barkeri is not a flavoenzyme.”  Kuenkel A.et.al.   9063468
[2] “The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.”  Maeder D.L.et.al.   16980466
[3] “Purification of a two-subunit cytochrome-b-containing heterodisulfide reductase from methanol-grown Methanosarcina barkeri.”  Heiden S.et.al.   8174566

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence
1:	MSEEMLYFSG LSDVLRMTFV QIMIFSTIAI VIFLYGLISN FQKWGTGVTG YALEPQEGKK 
61:	GSAITFLKTW WSQVTAESHH RGESILEILI LDILFQRRIL KRSPFRWVMH LFIFGGWMTL 
121:	FALSGMMFAV EMTEKIGIAL PFTPAEFRDF LSIPNYIFGY ILLIGVLVAL VRRLFVSEVR 
181:	EASIMYDWVL IGIVFLVTIS GFIADGIRTG FIWSFGLDPS VAPPAALFHS IFSLLFCIAF 
241:	IPYSKYIHII AIPLALLANK GGE