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Protein

H(2):CoB-CoM heterodisulfide,ferredoxin reductase 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: -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).3 Publications

Catalytic activityi

2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB.1 Publication1 Publication

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterPROSITE-ProRule annotation1 PublicationNote: Binds 4 [4Fe-4S] clusters per subunit.PROSITE-ProRule annotation1 Publication
  • FAD1 Publication

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.Curated
Proteins known to be involved in this subpathway in this organism are:
  1. H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit C (hdrC), H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit B (hdrB), H(2):CoB-CoM heterodisulfide,ferredoxin reductase 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)PROSITE-ProRule annotation1
Metal bindingi257Iron-sulfur 1 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi260Iron-sulfur 1 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi264Iron-sulfur 2 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi301Iron-sulfur 2 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi304Iron-sulfur 2 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi307Iron-sulfur 2 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi311Iron-sulfur 1 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi591Iron-sulfur 3 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi594Iron-sulfur 3 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi597Iron-sulfur 3 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi601Iron-sulfur 4 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi620Iron-sulfur 4 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi623Iron-sulfur 4 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi626Iron-sulfur 4 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi630Iron-sulfur 3 (4Fe-4S)PROSITE-ProRule annotation1

Regions

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

GO - Molecular functioni

GO - Biological processi

  • methanogenesis Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase
Biological processMethanogenesis
Ligand4Fe-4S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciMMAR79929:G1GML-1739-MONOMER
BRENDAi1.8.98.1 7427
UniPathwayiUPA00647; UER00700

Names & Taxonomyi

Protein namesi
Recommended name:
H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit ACurated (EC:1.8.98.51 Publication1 Publication)
Alternative name(s):
CoB--CoM heterodisulfide reductase iron-sulfur subunit ACurated
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 – 659H(2):CoB-CoM heterodisulfide,ferredoxin reductase 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.4 Publications

Protein-protein interaction databases

DIPiDIP-59606N
IntActiQ50756, 5 interactors
STRINGi79929.MTBMA_c17680

Structurei

3D structure databases

ProteinModelPortaliQ50756
SMRiQ50756
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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiarCOG02235 Archaea
COG1148 LUCA
HOGENOMiHOG000230698
KOiK03388
OMAiTAKHAML
OrthoDBiPOG093Z04QZ

Family and domain databases

Gene3Di3.50.50.60, 1 hit
InterProiView protein in InterPro
IPR017896 4Fe4S_Fe-S-bd
IPR017900 4Fe4S_Fe_S_CS
IPR036188 FAD/NAD-bd_sf
IPR023753 FAD/NAD-binding_dom
PfamiView protein in Pfam
PF00037 Fer4, 1 hit
PF13237 Fer4_10, 1 hit
PF07992 Pyr_redox_2, 1 hit
SUPFAMiSSF51905 SSF51905, 1 hit
PROSITEiView protein in PROSITE
PS00198 4FE4S_FER_1, 4 hits
PS51379 4FE4S_FER_2, 4 hits

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
PATRICifig|79929.8.peg.1705

Similar proteinsi

Entry informationi

Entry nameiHDRA_METTM
AccessioniPrimary (citable) accession number: Q50756
Secondary accession number(s): D9PYN8, Q50752
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 109 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing
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Main funding by: National Institutes of Health