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Protein

CoB--CoM heterodisulfide reductase iron-sulfur subunit A

Gene

hdrA

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
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 C (hdrC), CoB--CoM heterodisulfide reductase subunit B (hdrB), CoB--CoM heterodisulfide reductase iron-sulfur subunit A (hdrA)
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 bindingi255 – 2551Iron-sulfur 1 (4Fe-4S)Sequence analysis
Metal bindingi258 – 2581Iron-sulfur 1 (4Fe-4S)Sequence analysis
Metal bindingi261 – 2611Iron-sulfur 1 (4Fe-4S)Sequence analysis
Metal bindingi265 – 2651Iron-sulfur 2 (4Fe-4S)Sequence analysis
Metal bindingi302 – 3021Iron-sulfur 2 (4Fe-4S)Sequence analysis
Metal bindingi305 – 3051Iron-sulfur 2 (4Fe-4S)Sequence analysis
Metal bindingi308 – 3081Iron-sulfur 2 (4Fe-4S)Sequence analysis
Metal bindingi312 – 3121Iron-sulfur 1 (4Fe-4S)Sequence analysis
Metal bindingi592 – 5921Iron-sulfur 3 (4Fe-4S)Sequence analysis
Metal bindingi595 – 5951Iron-sulfur 3 (4Fe-4S)Sequence analysis
Metal bindingi598 – 5981Iron-sulfur 3 (4Fe-4S)Sequence analysis
Metal bindingi602 – 6021Iron-sulfur 4 (4Fe-4S)Sequence analysis
Metal bindingi621 – 6211Iron-sulfur 4 (4Fe-4S)Sequence analysis
Metal bindingi624 – 6241Iron-sulfur 4 (4Fe-4S)Sequence analysis
Metal bindingi627 – 6271Iron-sulfur 4 (4Fe-4S)Sequence analysis
Metal bindingi631 – 6311Iron-sulfur 3 (4Fe-4S)Sequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi159 – 18224FADSequence 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

BioCyciMTHE187420:GJNM-1383-MONOMER.
UniPathwayiUPA00647; UER00700.

Names & Taxonomyi

Protein namesi
Recommended name:
CoB--CoM heterodisulfide reductase iron-sulfur subunit A (EC:1.8.98.1)
Gene namesi
Name:hdrA
Ordered Locus Names:MTH_1381
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000005223 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 659659CoB--CoM heterodisulfide reductase iron-sulfur subunit APRO_0000150061Add
BLAST

Interactioni

Subunit structurei

The heterodisulfide reductase is composed of three subunits; HdrA, HdrB and HdrC. It forms a complex with the F420-non-reducing hydrogenase (Mvh), which provides the reducing equivalents to the heterodisulfide reductase (By similarity).By similarity

Protein-protein interaction databases

IntActiO27434. 2 interactions.
STRINGi187420.MTH1381.

Structurei

3D structure databases

ProteinModelPortaliO27434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini245 – 275314Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini293 – 322304Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini582 – 611304Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd
BLAST
Domaini612 – 641304Fe-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.
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]
PfamiPF00037. Fer4. 1 hit.
PF13237. Fer4_10. 1 hit.
PF07992. Pyr_redox_2. 2 hits.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 4 hits.
PS51379. 4FE4S_FER_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O27434-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEEKKEETM EEPRIGVYVC HCGVNIGGVV DIEAVRDYAA KLPNVVVSKD
60 70 80 90 100
YKYYCSDPGQ LEIQKDIKEL GLNRVVVAAC SPRLHEPTFR RCVEEAGLNQ
110 120 130 140 150
FLFEFANLRE QDSWVHMDDP EGATEKAKDL VRMAVAKARL LEPLEASKVS
160 170 180 190 200
VDDKALVIGG GVAGIQTALD LADMGFKTYM VEKRPSISGR MGQLDKTFPT
210 220 230 240 250
LDCSMCILAP KMVDVGKHDN IELITYAEVK EVDGYIGNFK VKIEKKPRYI
260 270 280 290 300
DEDLCTGCGS CVEVCPIEMP NYFDEGIGMT KAVYIPFPQA VPLCATIDKD
310 320 330 340 350
YCIECMLCDE ICERGAVKHD QEPEEIEIEV GTIIVATGYD AYDPTEKLEY
360 370 380 390 400
GYGRHTNVIT GLELERMINA SGPTDGKVIK PSDGEKPKRV AFIHCVGSRD
410 420 430 440 450
EQIGKPYCSR VCCMYIMKNA QLIKDKMPDT EVTLYYMDIR AFGKGFEEFY
460 470 480 490 500
KRSQEKYGIK FIRGRPAEIL ENPDLTLTVR SEDTLLGKVT EYDYDMVVLG
510 520 530 540 550
VGLVPPEGSE KLRQTIGLSK SADGFLMEAH PKLRPVDTLT DGVYLAGVAQ
560 570 580 590 600
GPKDIPDAVA QASGAAARAA IPMVKGEVEI EPIVAVTDSD VCGGCEVCIE
610 620 630 640 650
LCPFGAISIE EGHANVNVAL CKGCGTCVAA CPSGAMDQQH FRTEQIMAQI

EAALNEQAK
Length:659
Mass (Da):72,392
Last modified:January 16, 2004 - v2
Checksum:iED517077EC5B6CBD
GO

Sequence cautioni

The sequence AAB85858 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85858.1. Different initiation.
PIRiG69050.
RefSeqiWP_048061038.1. NC_000916.1.

Genome annotation databases

EnsemblBacteriaiAAB85858; AAB85858; MTH_1381.
GeneIDi24854496.
KEGGimth:MTH_1381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85858.1. Different initiation.
PIRiG69050.
RefSeqiWP_048061038.1. NC_000916.1.

3D structure databases

ProteinModelPortaliO27434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO27434. 2 interactions.
STRINGi187420.MTH1381.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB85858; AAB85858; MTH_1381.
GeneIDi24854496.
KEGGimth:MTH_1381.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00647; UER00700.
BioCyciMTHE187420:GJNM-1383-MONOMER.

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]
PfamiPF00037. Fer4. 1 hit.
PF13237. Fer4_10. 1 hit.
PF07992. Pyr_redox_2. 2 hits.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 4 hits.
PS51379. 4FE4S_FER_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHDRA_METTH
AccessioniPrimary (citable) accession number: O27434
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: July 6, 2016
This is version 104 of the entry and version 2 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.