CoB--CoM heterodisulfide reductase iron-sulfur subunit A 1 - Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)

Preferred order of sections

Names and origin

Protein names

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

Gene names

Name:	hdrA1
Synonyms:	hdrA_1
Ordered Locus Names:	MK0249

Organism

Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) [Reference proteome] [HAMAP]

Taxonomic identifier

190192 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus ›

Protein attributes

Sequence length	669 AA.
Sequence status	Complete.
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 M-coenzyme B heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B 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
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	methanogenesis 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 metal 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 – 669

669

CoB--CoM heterodisulfide reductase iron-sulfur subunit A 1

PRO_0000150058

Regions

Domain

239 – 270

32

4Fe-4S ferredoxin-type 1

Domain

287 – 318

32

4Fe-4S ferredoxin-type 2

Domain

584 – 613

30

4Fe-4S ferredoxin-type 3

Domain

617 – 646

30

4Fe-4S ferredoxin-type 4

Nucleotide binding

153 – 176

24

FAD Potential

Sites

Metal binding

249

1

Iron-sulfur 1 (4Fe-4S) Potential

Metal binding

252

1

Iron-sulfur 1 (4Fe-4S) Potential

Metal binding

255

1

Iron-sulfur 1 (4Fe-4S) Potential

Metal binding

259

1

Iron-sulfur 2 (4Fe-4S) Potential

Metal binding

296

1

Iron-sulfur 2 (4Fe-4S) Potential

Metal binding

299

1

Iron-sulfur 2 (4Fe-4S) Potential

Metal binding

302

1

Iron-sulfur 2 (4Fe-4S) Potential

Metal binding

306

1

Iron-sulfur 1 (4Fe-4S) Potential

Metal binding

593

1

Iron-sulfur 3 (4Fe-4S) Potential

Metal binding

596

1

Iron-sulfur 3 (4Fe-4S) Potential

Metal binding

599

1

Iron-sulfur 3 (4Fe-4S) Potential

Metal binding

603

1

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

626

1

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

629

1

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

632

1

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

636

1

Iron-sulfur 3 (4Fe-4S) Potential

Amino acid modifications

Non-standard residue

200

1

Selenocysteine Probable

Sequences

Sequence

Length

Mass (Da)

Tools

Q8TYP4 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: C2D8D120157026E5
Show »

FASTA

669

73,742

        10         20         30         40         50         60 
MGDKDDVRIG VFVCHCGVNI KASVDVEEVV EYAKKLPGVV YATDYPFFCA DPGQEIIQEA 

        70         80         90        100        110        120 
IKEHDLDRVV VAACTPKIHE NTFRNCVKEA GLSPYYMEMV NIREHCSFVH MQEPEKATEK 

       130        140        150        160        170        180 
AKDLIRAAVE RAKRLEDVPT KEVEVENSVL IIGGGIAGIQ AALDLADQGF KVYLVEKEPT 

       190        200        210        220        230        240 
IGGNMARLAK TFPTDDCAMU ILAPKMVQVG NHPNIEMITY AEVKDVDGYI GNFEVTIEKK 

       250        260        270        280        290        300 
PRYVDEDACT GCGVCAEVCP IEVPNEFDLG IGTRKAIYVP FPQAMPLVYT IDMEHCIQCG 

       310        320        330        340        350        360 
LCEEACPQDP PAIDFDQEPE EIRLKVGTII VATGYEEFDA SKLEEYGYGK YDNVITTLEL 

       370        380        390        400        410        420 
ERMINPAGPT EGHVIRPSDG KEPHRIVFIH CVGSRCPGKE EKGEAYCSRI CCMFILKNAQ 

       430        440        450        460        470        480 
LIKQHEPDAE VYCCYMDVRA FGKGYEEYYE RAQKQFGVRF IRGRPAEIVE DPETKNLIVR 

       490        500        510        520        530        540 
VEDTLTGEPM EIEADLVVLG CGLVAPEETY SKLADILGID RSPDGFFKEL HPKLEPVSTK 

       550        560        570        580        590        600 
VRGVQIAGVA QGPKDIPDTV AQAKGAASEA SIPMSQGKVE IELITATVDE DVCGGCGACA 

       610        620        630        640        650        660 
QVCPFDAIEM VEKDGKRVAE VQDVACQGCG QCAAACPSGA MQLRYYRDEQ LMPQIEALLA 


EALEEEEEE

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References

[1]

"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009439 Genomic DNA. Translation: AAM01466.1.
RefSeq	NP_613536.1. NC_003551.1.
3D structure databases
ProteinModelPortal	Q8TYP4.
ModBase	Search...
Protein-protein interaction databases
STRING	190192.MK0249.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM01466; AAM01466; MK0249.
GeneID	1477552.
KEGG	mka:MK0249.
Phylogenomic databases
eggNOG	COG1148.
HOGENOM	HOG000230698.
KO	K03388.
OMA	CTPKIHE.
ProtClustDB	CLSK876667.
Enzyme and pathway databases
UniPathway	UPA00647; UER00700.
Family and domain databases
InterPro	IPR001450. 4Fe4S-bd_dom. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. [Graphical view]
Pfam	PF00037. Fer4. 2 hits. PF12838. Fer4_7. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PROSITE	PS00198. 4FE4S_FER_1. 4 hits. PS51379. 4FE4S_FER_2. 4 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HDRA1_METKA

Accession

Primary (citable) accession number: Q8TYP4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	February 26, 2008
Last modified:	May 1, 2013
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents