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Protein

CoB--CoM heterodisulfide reductase iron-sulfur subunit A 2

Gene

hdrA2

Organism
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

Coenzyme B + coenzyme M + methanophenazine = N-(7-((2-sulfoethyl)dithio)heptanoyl)-O(3)-phospho-L-threonine + dihydromethanophenazine.

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterBy similarityNote: Binds 4 [4Fe-4S] clusters per subunit.By similarity
  • FADBy similarity

Pathwayi: coenzyme M-coenzyme B heterodisulfide reduction

This protein is involved in step 1 of the subpathway that synthesizes coenzyme B and coenzyme M from coenzyme M-coenzyme B heterodisulfide.
Proteins known to be involved in this subpathway in this organism are:
  1. CoB--CoM heterodisulfide reductase iron-sulfur subunit A 1 (hdrA1), CoB--CoM heterodisulfide reductase subunit B (hdrB), CoB--CoM heterodisulfide reductase iron-sulfur subunit C (hdrC), CoB--CoM heterodisulfide reductase iron-sulfur subunit A 2 (hdrA2)
This subpathway is part of the pathway coenzyme M-coenzyme B heterodisulfide reduction, which is itself part of Cofactor metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes coenzyme B and coenzyme M from coenzyme M-coenzyme B heterodisulfide, the pathway coenzyme M-coenzyme B heterodisulfide reduction and in Cofactor metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi248 – 2481Iron-sulfur 1 (4Fe-4S)Sequence analysis
Metal bindingi251 – 2511Iron-sulfur 1 (4Fe-4S)Sequence analysis
Metal bindingi254 – 2541Iron-sulfur 1 (4Fe-4S)Sequence analysis
Metal bindingi258 – 2581Iron-sulfur 2 (4Fe-4S)Sequence analysis
Metal bindingi295 – 2951Iron-sulfur 2 (4Fe-4S)Sequence analysis
Metal bindingi298 – 2981Iron-sulfur 2 (4Fe-4S)Sequence analysis
Metal bindingi301 – 3011Iron-sulfur 2 (4Fe-4S)Sequence analysis
Metal bindingi305 – 3051Iron-sulfur 1 (4Fe-4S)Sequence analysis
Metal bindingi586 – 5861Iron-sulfur 3 (4Fe-4S)Sequence analysis
Metal bindingi589 – 5891Iron-sulfur 3 (4Fe-4S)Sequence analysis
Metal bindingi592 – 5921Iron-sulfur 3 (4Fe-4S)Sequence analysis
Metal bindingi596 – 5961Iron-sulfur 4 (4Fe-4S)Sequence analysis
Metal bindingi619 – 6191Iron-sulfur 4 (4Fe-4S)Sequence analysis
Metal bindingi622 – 6221Iron-sulfur 4 (4Fe-4S)Sequence analysis
Metal bindingi625 – 6251Iron-sulfur 4 (4Fe-4S)Sequence analysis
Metal bindingi629 – 6291Iron-sulfur 3 (4Fe-4S)Sequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi152 – 17524FADSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Methanogenesis

Keywords - Ligandi

4Fe-4S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00647; UER00700.

Names & Taxonomyi

Protein namesi
Recommended name:
CoB--CoM heterodisulfide reductase iron-sulfur subunit A 2 (EC:1.8.98.1)
Gene namesi
Name:hdrA2
Synonyms:hdrA_2
Ordered Locus Names:MK0265
OrganismiMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Taxonomic identifieri190192 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus
Proteomesi
  • UP000001826 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 656656CoB--CoM heterodisulfide reductase iron-sulfur subunit A 2PRO_0000150059Add
BLAST

Interactioni

Subunit structurei

The heterodisulfide reductase is composed of three subunits; HdrA, HdrB and HdrC.By similarity

Protein-protein interaction databases

STRINGi190192.MK0265.

Structurei

3D structure databases

ProteinModelPortaliP96801.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini238 – 269324Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini286 – 315304Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini577 – 606304Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd
BLAST
Domaini610 – 639304Fe-4S ferredoxin-type 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the HdrA family.Curated
Contains 4 4Fe-4S ferredoxin-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiarCOG02235. Archaea.
COG1148. LUCA.
HOGENOMiHOG000230698.
KOiK03388.
OMAiGLNPYLC.

Family and domain databases

Gene3Di3.50.50.60. 5 hits.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF12831. FAD_oxidored. 1 hit.
PF12838. Fer4_7. 1 hit.
PF13187. Fer4_9. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 3 hits.
PS51379. 4FE4S_FER_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P96801-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEEEPRIGV YVCHCGVNIA GVVDVKEVAE FAKTLKNVVV ARDYKYVCSD
60 70 80 90 100
PGQEIIQRDI EKYDLNRVVV AACSPRLHEP TFRRCVEEAG LNPYCFEMAN
110 120 130 140 150
IREHCSWVHM DDPARATEKA KDLVRMAVAK ARLLESLETI KVDVTDRALV
160 170 180 190 200
IGGGVSGIQA ALDLADMGFE VILVEKEPSI GGRMAQLDKT FPTNDCSICI
210 220 230 240 250
LAPKMVDVSK HPNIKMYTYA EVVEVDGYVG NFTVKIEKKP RYVDEDACTG
260 270 280 290 300
CGACAEVCPI EVPNEFDEGL GMRKAIYKPF PQAVPSVFTI DEEHCIRCGL
310 320 330 340 350
CEEVCDADAI DFDQEPEIVE EEVGAIICAI GYDTCDPTER EEYGYGVYDN
360 370 380 390 400
VITSIELERL INASGPTGGK VVRPSDGKKP KRIAFIQCVG SRDPHRTNPY
410 420 430 440 450
CSNVCCMYAM KLAQLIREKY PETQIDIYYM DVRAFGKGYE EYYERSQKQY
460 470 480 490 500
GIRFIRGRPA EIVEDPETKN LIVRAEDTLL GDVVEREYDL VVLSVGMVPR
510 520 530 540 550
DSADVIQEVL SISRSPDGFF MEAHPKLRPV DTAIDGIFLA GACQGPKDIP
560 570 580 590 600
SSVAQGSAAA ARAATALAAG EVAVEPIVSE VDEEICGGCG TCVELCPYGA
610 620 630 640 650
IELVEKDGKL VAEVTAALCK GCGTCAAACP SGAMEQNHFK TEQLYKQIEG

AFRDPA
Length:656
Mass (Da):71,925
Last modified:May 1, 1997 - v1
Checksum:iC7CF218545ACEA7C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09871 Genomic DNA. Translation: CAA70999.1.
AE009439 Genomic DNA. Translation: AAM01482.1.

Genome annotation databases

EnsemblBacteriaiAAM01482; AAM01482; MK0265.
KEGGimka:MK0265.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09871 Genomic DNA. Translation: CAA70999.1.
AE009439 Genomic DNA. Translation: AAM01482.1.

3D structure databases

ProteinModelPortaliP96801.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190192.MK0265.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM01482; AAM01482; MK0265.
KEGGimka:MK0265.

Phylogenomic databases

eggNOGiarCOG02235. Archaea.
COG1148. LUCA.
HOGENOMiHOG000230698.
KOiK03388.
OMAiGLNPYLC.

Enzyme and pathway databases

UniPathwayiUPA00647; UER00700.

Family and domain databases

Gene3Di3.50.50.60. 5 hits.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF12831. FAD_oxidored. 1 hit.
PF12838. Fer4_7. 1 hit.
PF13187. Fer4_9. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 3 hits.
PS51379. 4FE4S_FER_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHDRA2_METKA
AccessioniPrimary (citable) accession number: P96801
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: May 1, 1997
Last modified: December 9, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.