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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:P96797
Protein Name:HDRD
Length:409
Molecular Weight:45055.00
Species:Methanosarcina barkeri [269797]
Location1 / Topology2 / Orientation3: Secreted1
Substrate hydron

Cross database links:

RefSeq: YP_305125.1   
Entrez Gene ID: 3624318   
Pfam: PF02754   
BioCyc: MBAR269797:MBAR_A1599-MONOMER   
KEGG: mba:Mbar_A1599   

Gene Ontology

GO:0051539 F:4 iron, 4 sulfur cluster binding
GO:0051912 F:CoB--CoM heterodisulfide reductase activity
GO:0009055 F:electron carrier activity
GO:0046872 F:metal ion binding
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:

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MAKRTPSIDT KNLTAVQLME LDACVRCGEC VKWCPTYAAS GGKPGLAPRD KILRWRQYMN 
61:	KSYGLKAKLF GPQEVSPSEL EEFKDDVHGC TTCGVCATVC EAGINTVEIW EAIRTNLVKK 
121:	GIGPYGKQSA FPKLVGQYHN PYMKDQKDRL AWVPPDVKIE DKADIVYFTG CTAGYNQLAL 
181:	AFATSRVLNK LGIKFAMLGE EEWCCGSALI RTGQVHVDDV ARELARHNVE ALQKKGAKKV 
241:	LFACAGCFRA AKIDWPRLLG KELPFEVIHI TQFLADLIQA DKIKWEKPIN KTITYHDPCH 
301:	LGRHVGVFNA PRYVLSHIPG VKFVEMDRSK EFQRCCGAGG GVKAGMPDLA VAMGESRVKD 
361:	ALETNADILS SACPFCKRNL SDGRDALKSD IVVEDIIELV AEALGLSTS