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Protein

CoB--CoM heterodisulfide reductase iron-sulfur subunit A

Gene

hdrA

Organism
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 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)DescriptionActionsGraphical viewLength
Metal bindingi254Iron-sulfur 1 (4Fe-4S)Sequence analysis1
Metal bindingi257Iron-sulfur 1 (4Fe-4S)Sequence analysis1
Metal bindingi260Iron-sulfur 1 (4Fe-4S)Sequence analysis1
Metal bindingi264Iron-sulfur 2 (4Fe-4S)Sequence analysis1
Metal bindingi301Iron-sulfur 2 (4Fe-4S)Sequence analysis1
Metal bindingi304Iron-sulfur 2 (4Fe-4S)Sequence analysis1
Metal bindingi307Iron-sulfur 2 (4Fe-4S)Sequence analysis1
Metal bindingi311Iron-sulfur 1 (4Fe-4S)Sequence analysis1
Metal bindingi591Iron-sulfur 3 (4Fe-4S)Sequence analysis1
Metal bindingi594Iron-sulfur 3 (4Fe-4S)Sequence analysis1
Metal bindingi597Iron-sulfur 3 (4Fe-4S)Sequence analysis1
Metal bindingi601Iron-sulfur 4 (4Fe-4S)Sequence analysis1
Metal bindingi620Iron-sulfur 4 (4Fe-4S)Sequence analysis1
Metal bindingi623Iron-sulfur 4 (4Fe-4S)Sequence analysis1
Metal bindingi626Iron-sulfur 4 (4Fe-4S)Sequence analysis1
Metal bindingi630Iron-sulfur 3 (4Fe-4S)Sequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi158 – 181FADSequence analysisAdd BLAST24

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

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 ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri79929 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000000345 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001500622 – 659CoB--CoM heterodisulfide reductase iron-sulfur subunit AAdd BLAST658

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)DescriptionActionsGraphical viewLength
Domaini244 – 2744Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST31
Domaini292 – 3214Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST30
Domaini581 – 6104Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd BLAST30
Domaini611 – 6404Fe-4S ferredoxin-type 4PROSITE-ProRule annotationAdd BLAST30

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.
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...

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 2, 2016
This is version 101 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.