Reviewed, UniProtKB/Swiss-Prot Q8Q0T0 (HDRA_METMA)

Names and origin

Protein names

Recommended name:
    CoB--CoM heterodisulfide reductase 1 iron-sulfur subunit A
    EC=1.8.98.1

Gene names

Name:	hdrA
Ordered Locus Names:	MM_0056

Organism

Methanosarcina mazei (Methanosarcina frisia) [Complete proteome] [HAMAP]

Taxonomic identifier

2209 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	793 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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 B/coenzyme M regeneration; coenzyme B and coenzyme M from CoB-CoM heterodisulfide: step 1/1.
Subunit structure	The heterodisulfide reductase 1 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 process	Methanogenesis
Domain	Repeat
Ligand	4Fe-4S FAD Flavoprotein Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	methanogenesis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tRNA processing Inferred from electronic annotation. Source: InterPro
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW CoB--CoM heterodisulfide reductase activity Inferred from electronic annotation. Source: EC FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 793	793	CoB--CoM heterodisulfide reductase 1 iron-sulfur subunit A		PRO_0000150060
Regions
	Domain	233 – 264	32	4Fe-4S ferredoxin-type 1
	Domain	282 – 311	30	4Fe-4S ferredoxin-type 2
	Domain	571 – 600	30	4Fe-4S ferredoxin-type 3
	Domain	601 – 629	29	4Fe-4S ferredoxin-type 4
	Nucleotide binding	147 – 170	24	FAD Potential
Sites
	Metal binding	243	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	246	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	250	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	254	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	291	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	294	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	297	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	301	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	580	1	Iron-sulfur 3 (4Fe-4S) Potential
	Metal binding	583	1	Iron-sulfur 3 (4Fe-4S) Potential
	Metal binding	586	1	Iron-sulfur 3 (4Fe-4S) Potential
	Metal binding	590	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	609	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	612	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	615	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	619	1	Iron-sulfur 3 (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8Q0T0-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: F34517E61FD4B362	FASTA	793	86,803
	10 20 30 40 50 60 MRIGVYVCHC GLNIAGVIDV SALEEMAGEL EDVVLAREVQ FLCSDSGQEG IIKDIKDNKI 70 80 90 100 110 120 DRVVIAACSP RLHEKTFRHV MEKADLNPYL MEMVNIREQC SWVHADDPQM ATQKAFDLIR 130 140 150 160 170 180 MGVAKARFLR ELSATSSKAS RNVLIIGGGV AGIEAALNLA EAGFPVTMVE RESTIGGKMA 190 200 210 220 230 240 LMNEVFPTND CSICVLAPKM TEVQNHPNIT LYTYSEVTDI SGSVGKFHVR VTRKPRFVLE 250 260 270 280 290 300 DKCKGCVDLC SEVCPVEIEN PMNYGIGKSR AIYMPIPQSV PQVVLIDPDH CVGCGLCQLA 310 320 330 340 350 360 CPAEAVDYEQ KPEEIEFEAG AVIVSTGYQL FDASRKKEYG FGKYPDVITN MQLERMLNSA 370 380 390 400 410 420 GPTGGRVLVP STGQPPESVA FIQCVGSRDK TVGNEHCSRV CCMAALKNSQ MVKERYPGTD 430 440 450 460 470 480 ITIHYIDIRA AGEMYEEYYA RTQGMGVDFI RGKVAEVYAG EDGRPVVRYE NTLESRVEEE 490 500 510 520 530 540 AHDLVVLSTG YEPSKAAEGI GRMLNLARRP DRFFASAHPK MRPVDAPVSG VFLAGCASGP 550 560 570 580 590 600 KEIQVSIAQG SACASKVMQL LGTGELEADP MGAHVDPDKC IGCRTCVEVC KFGKISIVDK 610 620 630 640 650 660 KAVVDEVSCY GCGDCSAACP VGAIQMRNFE NEQILAQVRA ATAHKSQCPF VVAFLCNWCS 670 680 690 700 710 720 YACADLTGMS RIHYPTNIRV IRTMCSARIN PEFVLEALKG GADGVLVAGC RMDECHYIHG 730 740 750 760 770 780 NFDAKKRMDV LKEIIKEIGL DPKRLRTLWI SAAEGERFSN TITEFVKELE EIGPIGSELK 790 REYTATGLEE VAK

References

[1]

"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea." Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G. J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE008384 Genomic DNA. Translation: AAM29752.1.
RefSeq	NP_632080.1.
3D structure databases
HSSP	HSSP built from PDB template 2FDN based on UniProtKB P00198.
ModBase	Search...
Genome annotation databases
GeneID	1478398.
GenomeReviews	Gene locus MM_0056 in contig AE008384_GR.
KEGG	mma:MM_0056.
NMPDR	fig|192952.1.peg.56.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8Q0T0.
OMA	Q8Q0T0. ACSPRMH.
Enzyme and pathway databases
BioCyc	MMAZ192952:MM0056-MON.
BRENDA	1.8.98.1. 261165.
Family and domain databases
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR001450. 4Fe4S_Fe_S_bd_subgr. IPR017900. 4Fe4S_Fe_S_CS. IPR003813. FlpD. IPR002218. GIDA-rel. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00037. Fer4. 3 hits. PF02662. FlpD. 1 hit. PF01134. GIDA. 1 hit. [Graphical view]
PROSITE	PS00198. 4FE4S_FER_1. 2 hits. PS51379. 4FE4S_FER_2. 4 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HDRA_METMA

Accession

Primary (citable) accession number: Q8Q0T0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)