Reviewed, UniProtKB/Swiss-Prot P60200 (HDRA_METJA)

Names and origin

Protein names

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

Gene names

Name:	hdrA
Ordered Locus Names:	MJ1190

Organism

Methanocaldococcus jannaschii (Methanococcus jannaschii) [Complete proteome] [HAMAP]

Taxonomic identifier

2190 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length	657 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 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
Coding sequence diversity	Selenocysteine
Domain	Repeat
Ligand	4Fe-4S FAD Flavoprotein Iron Iron-sulfur Metal-binding Selenium
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
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 electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW selenium 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 – 657	657	CoB--CoM heterodisulfide reductase iron-sulfur subunit A		PRO_0000150057
Regions
	Domain	235 – 266	32	4Fe-4S ferredoxin-type 1
	Domain	283 – 312	30	4Fe-4S ferredoxin-type 2
	Domain	574 – 603	30	4Fe-4S ferredoxin-type 3
	Domain	607 – 636	30	4Fe-4S ferredoxin-type 4
	Nucleotide binding	149 – 172	24	FAD Potential
Sites
	Metal binding	245	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	248	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	251	1	Iron-sulfur 1 (4Fe-4S) Potential
	Metal binding	255	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	292	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	295	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	298	1	Iron-sulfur 2 (4Fe-4S) Potential
	Metal binding	302	1	Iron-sulfur 1 (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	589	1	Iron-sulfur 3 (4Fe-4S) Potential
	Metal binding	593	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	616	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	619	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	622	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	626	1	Iron-sulfur 3 (4Fe-4S) Potential
Amino acid modifications
	Non-standard residue	196	1	Selenocysteine Probable

Sequences

	Sequence		Length	Mass (Da)
	P60200-1 [UniParc]. Last modified February 26, 2008. Version 2. Checksum: D3607042434DBC32	FASTA	657	71,922
	10 20 30 40 50 60 MSPRVGVFVC YCGANINGVV DCEAVRDFAE KLDGVVVAKT YPFMCADPGQ NLIKEAIKEY 70 80 90 100 110 120 NLDRVVVAAC TPKIHEPTFR NCIKEAGLSP YYLEFVNIRE HCSFVHMNDR EKATKKAMEL 130 140 150 160 170 180 VAGAVERAKR LEDVPQKIVE VDKSCLIIGG GIAGIQAALD LGDQGYKVYL VEKEPSIGGR 190 200 210 220 230 240 MAQLAKTFPT DDCALUILAP KMVSVANHPN VELITYAEVK NVEGFIGNFE VTIEKKPRYV 250 260 270 280 290 300 DENICTGCGA CAAVCPIEVP NEFDLGLGTR KAIYVPFAQA VPLVYTIDMD HCIRCGLCEK 310 320 330 340 350 360 ACGPGAIRYD QKPEEIKLKV GTIICAVGYD EFDATLKEEY GYGVYDNVIT TLELERMINP 370 380 390 400 410 420 AGPTGGHEIR PSDGKHPHRV VFIQCVGSRD AKVGKHYCSR ICCMFALKNA QLIKQHDPST 430 440 450 460 470 480 EVYICYMDIR SFGKGYEEYY RRAQEQFGVK FIRGRPACIM EDPETKNLIV RVEDTLLGEI 490 500 510 520 530 540 VEIEADLVVL SAGLSPRPDN PKLAKMLGLE LSPDGFFKEL HPKLAPVNTK VDGIAIAGVA 550 560 570 580 590 600 QGPKDIPDTV AQAKGAASAV SIPMAQGQFR IEMIRAVVDE DVCGGCQVCA KMCPYNAITY 610 620 630 640 650 VEKDGHLVAQ VNDVACKGCG SCAGACPSGA MQLRYYRDEQ IISFIDGVLE AHQKLES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"Selenoprotein synthesis in archaea: identification of an mRNA element of Methanococcus jannaschii probably directing selenocysteine insertion." Wilting R., Schorling S., Persson B.C., Boeck A. J. Mol. Biol. 266:637-641(1997) [PubMed: 9102456] [Abstract] Cited for: PROBABLE SELENOCYSTEINE AT SEC-196.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L77117 Genomic DNA. No translation available.
3D structure databases
ModBase	Search...
Genome annotation databases
GenomeReviews	Gene locus MJ1190 in contig L77117_GR.
TIGR	MJ1190.
Phylogenomic databases
HOGENOM	P60200.
Enzyme and pathway databases
BRENDA	1.8.98.1. 256362.
Family and domain databases
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR001450. 4Fe4S_Fe_S_bd_subgr. IPR017900. 4Fe4S_Fe_S_CS. IPR003953. FAD_bind2_N. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00890. FAD_binding_2. 1 hit. PF00037. Fer4. 4 hits. [Graphical view]
PROSITE	PS00198. 4FE4S_FER_1. 4 hits. PS51379. 4FE4S_FER_2. 4 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HDRA_METJA

Accession

Primary (citable) accession number: P60200

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	February 26, 2008
Last modified:	June 16, 2009
This is version 43 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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