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Protein

CoB--CoM heterodisulfide reductase iron-sulfur subunit A

Gene

hdrA

Organism
Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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.1 Publication

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:

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 bindingi254 – 2541Iron-sulfur 1 (4Fe-4S)Sequence analysis
Metal bindingi257 – 2571Iron-sulfur 1 (4Fe-4S)Sequence analysis
Metal bindingi260 – 2601Iron-sulfur 1 (4Fe-4S)Sequence analysis
Metal bindingi264 – 2641Iron-sulfur 2 (4Fe-4S)Sequence analysis
Metal bindingi301 – 3011Iron-sulfur 2 (4Fe-4S)Sequence analysis
Metal bindingi304 – 3041Iron-sulfur 2 (4Fe-4S)Sequence analysis
Metal bindingi307 – 3071Iron-sulfur 2 (4Fe-4S)Sequence analysis
Metal bindingi311 – 3111Iron-sulfur 1 (4Fe-4S)Sequence analysis
Metal bindingi591 – 5911Iron-sulfur 3 (4Fe-4S)Sequence analysis
Metal bindingi594 – 5941Iron-sulfur 3 (4Fe-4S)Sequence analysis
Metal bindingi597 – 5971Iron-sulfur 3 (4Fe-4S)Sequence analysis
Metal bindingi601 – 6011Iron-sulfur 4 (4Fe-4S)Sequence analysis
Metal bindingi620 – 6201Iron-sulfur 4 (4Fe-4S)Sequence analysis
Metal bindingi623 – 6231Iron-sulfur 4 (4Fe-4S)Sequence analysis
Metal bindingi626 – 6261Iron-sulfur 4 (4Fe-4S)Sequence analysis
Metal bindingi630 – 6301Iron-sulfur 3 (4Fe-4S)Sequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi158 – 18124FADSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • methanogenesis Source: UniProtKB
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

BioCyciMMAR79929:GH5J-1774-MONOMER.
BRENDAi1.8.98.1. 7427.
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:MTBMA_c17680
OrganismiMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri79929 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000000345 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 659658CoB--CoM heterodisulfide reductase iron-sulfur subunit APRO_0000150062Add
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.1 Publication

Protein-protein interaction databases

DIPiDIP-59606N.
STRINGi79929.MTBMA_c17680.

Structurei

3D structure databases

ProteinModelPortaliQ50756.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini244 – 274314Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini292 – 321304Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini581 – 610304Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd
BLAST
Domaini611 – 640304Fe-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]
PfamiPF00037. Fer4. 1 hit.
PF13237. Fer4_10. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 4 hits.
PS51379. 4FE4S_FER_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q50756-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEEKKETME EPKIGVYVCH CGVNIGGVVD VEAVRDYAAK LPNVVIAKDY
60 70 80 90 100
KYYCSDPGQL EIQKDIKELG INRVVVAACS PRLHEPTFRR CVEEAGLNQF
110 120 130 140 150
LFEFANIREH DSWVHMDNPE GATEKAKDLV RMAVAKARLL EPLEASKVSV
160 170 180 190 200
DDKALVIGGG VAGIQAALDL ADMGFKTYMV EKRPSISGRM GQLDKTFPTL
210 220 230 240 250
DCSMCILAPK MVDVGKHDNI ELITYAEVKE VDGYIGNFKV KIEKKPRYID
260 270 280 290 300
EELCTGCGSC VEVCPIEMPN YFDEGIGMTK AVYIPFPQAV PLCATIDKDY
310 320 330 340 350
CIECMLCDEV CERGAVKHDQ EPEEIEIEVG TIIVATGYDA YDPTEKLEYG
360 370 380 390 400
YGRHTNVITG LELERMINAS GPTDGKVLKP SDGEKPKRVA FIHCVGSRDE
410 420 430 440 450
QIGKPYCSRV CCMYIMKNAQ LIKDKMPDTE VTLYYMDIRA FGKGFEEFYK
460 470 480 490 500
RSQEKYGIKF IRGRPAEVIE NPDLTLTVRS EDTLLGKVTE YDYDMVVLGV
510 520 530 540 550
GLVPPEGAET LRQTIGLSKS ADGFLMEAHP KLRPVDTLTD GVYLAGVAQG
560 570 580 590 600
PKDIPDAVAQ ASGAAARAAI PMVKGEVEIE PIIAVTDSDV CGGCEVCIEL
610 620 630 640 650
CPFGAISIEE GHANVNVALC KGCGTCVAAC PSGAMDQQHF KTEQIMAQIE

AALNEPASK
Length:659
Mass (Da):72,182
Last modified:January 23, 2007 - v3
Checksum:iFC01196FEE3A5F9E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81134 Genomic DNA. Translation: CAA57039.1.
CP001710 Genomic DNA. Translation: ADL59336.1.
X92083 Genomic DNA. Translation: CAA63065.1.
PIRiS48720.
RefSeqiWP_013296546.1. NC_014408.1.

Genome annotation databases

EnsemblBacteriaiADL59336; ADL59336; MTBMA_c17680.
GeneIDi9705479.
KEGGimmg:MTBMA_c17680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81134 Genomic DNA. Translation: CAA57039.1.
CP001710 Genomic DNA. Translation: ADL59336.1.
X92083 Genomic DNA. Translation: CAA63065.1.
PIRiS48720.
RefSeqiWP_013296546.1. NC_014408.1.

3D structure databases

ProteinModelPortaliQ50756.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59606N.
STRINGi79929.MTBMA_c17680.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADL59336; ADL59336; MTBMA_c17680.
GeneIDi9705479.
KEGGimmg:MTBMA_c17680.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00647; UER00700.
BioCyciMMAR79929:GH5J-1774-MONOMER.
BRENDAi1.8.98.1. 7427.

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. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 4 hits.
PS51379. 4FE4S_FER_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The heterodisulfide reductase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic of pyridine-nucleotide-dependent thioredoxin reductases."
    Hedderich R., Koch J., Linder D., Thauer R.K.
    Eur. J. Biochem. 225:253-261(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18; 210-226; 425-435; 455-459 AND 641-650.
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
  2. "Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism."
    Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K.
    J. Bacteriol. 192:5850-5851(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
  3. "Primary structure of cyclohydrolase (Mch) from Methanobacterium thermoautotrophicum (strain Marburg) and functional expression of the mch gene in Escherichia coli."
    Vaupel M., Dietz H., Linder D., Thauer R.K.
    Eur. J. Biochem. 236:294-300(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 651-659.
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
  4. "Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg)."
    Hedderich R., Berkessel A., Thauer R.K.
    Eur. J. Biochem. 193:255-261(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, SUBUNIT.
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
  5. "H2: heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum. Composition and properties."
    Setzke E., Hedderich R., Heiden S., Thauer R.K.
    Eur. J. Biochem. 220:139-148(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH F420-NON-REDUCING HYDROGENASE, PROTEIN SEQUENCE OF 2-18.
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
  6. "Physiological role of the F420-non-reducing hydrogenase (Mvh) from Methanothermobacter marburgensis."
    Stojanowic A., Mander G.J., Duin E.C., Hedderich R.
    Arch. Microbiol. 180:194-203(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH F420-NON-REDUCING HYDROGENASE.
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

Entry informationi

Entry nameiHDRA_METTM
AccessioniPrimary (citable) accession number: Q50756
Secondary accession number(s): D9PYN8, Q50752
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 23, 2007
Last modified: November 11, 2015
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing

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.