HDRA_METTH
ID HDRA_METTH Reviewed; 659 AA.
AC O27434;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit A {ECO:0000250|UniProtKB:Q50756};
DE EC=1.8.98.5 {ECO:0000250|UniProtKB:Q50756};
DE AltName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit A {ECO:0000250|UniProtKB:Q50756};
GN Name=hdrA; OrderedLocusNames=MTH_1381;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- FUNCTION: Part of a complex that catalyzes the reversible reduction of
CC CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB
CC (coenzyme B). {ECO:0000250|UniProtKB:Q50756}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coenzyme B + coenzyme M + 2 H(+) + 2 reduced [2Fe-2S]-
CC [ferredoxin] = coenzyme M-coenzyme B heterodisulfide + 2 H2 + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:55748, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18276, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:58319, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=1.8.98.5;
CC Evidence={ECO:0000250|UniProtKB:Q50756};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC Note=Binds 4 [4Fe-4S] clusters per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00711};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q50756};
CC -!- PATHWAY: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide
CC reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B
CC heterodisulfide: step 1/1. {ECO:0000250|UniProtKB:Q50756}.
CC -!- SUBUNIT: The heterodisulfide reductase is composed of three subunits;
CC HdrA, HdrB and HdrC. It forms a complex with the F420-non-reducing
CC hydrogenase (Mvh), which provides the reducing equivalents to the
CC heterodisulfide reductase. {ECO:0000250|UniProtKB:Q50756}.
CC -!- SIMILARITY: Belongs to the HdrA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85858.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000666; AAB85858.1; ALT_INIT; Genomic_DNA.
DR PIR; G69050; G69050.
DR RefSeq; WP_048061038.1; NC_000916.1.
DR AlphaFoldDB; O27434; -.
DR SMR; O27434; -.
DR IntAct; O27434; 2.
DR STRING; 187420.MTH_1381; -.
DR EnsemblBacteria; AAB85858; AAB85858; MTH_1381.
DR GeneID; 24854496; -.
DR KEGG; mth:MTH_1381; -.
DR PATRIC; fig|187420.15.peg.1346; -.
DR HOGENOM; CLU_020302_0_0_2; -.
DR OMA; TAKHAML; -.
DR BioCyc; MetaCyc:HDRAMAUTO-MON; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR039650; HdrA-like.
DR PANTHER; PTHR43498; PTHR43498; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF13237; Fer4_10; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 4.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
PE 3: Inferred from homology;
KW 4Fe-4S; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW Methanogenesis; Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..659
FT /note="H(2):CoB-CoM heterodisulfide,ferredoxin reductase
FT subunit A"
FT /id="PRO_0000150061"
FT DOMAIN 245..275
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 293..322
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 582..611
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 612..641
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 159..182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 255
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 258
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 261
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 265
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 302
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 305
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 308
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 312
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 592
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 595
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 598
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 602
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 621
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 624
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 627
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 631
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 659 AA; 72392 MW; ED517077EC5B6CBD CRC64;
MAEEKKEETM EEPRIGVYVC HCGVNIGGVV DIEAVRDYAA KLPNVVVSKD YKYYCSDPGQ
LEIQKDIKEL GLNRVVVAAC SPRLHEPTFR RCVEEAGLNQ FLFEFANLRE QDSWVHMDDP
EGATEKAKDL VRMAVAKARL LEPLEASKVS VDDKALVIGG GVAGIQTALD LADMGFKTYM
VEKRPSISGR MGQLDKTFPT LDCSMCILAP KMVDVGKHDN IELITYAEVK EVDGYIGNFK
VKIEKKPRYI DEDLCTGCGS CVEVCPIEMP NYFDEGIGMT KAVYIPFPQA VPLCATIDKD
YCIECMLCDE ICERGAVKHD QEPEEIEIEV GTIIVATGYD AYDPTEKLEY GYGRHTNVIT
GLELERMINA SGPTDGKVIK PSDGEKPKRV AFIHCVGSRD EQIGKPYCSR VCCMYIMKNA
QLIKDKMPDT EVTLYYMDIR AFGKGFEEFY KRSQEKYGIK FIRGRPAEIL ENPDLTLTVR
SEDTLLGKVT EYDYDMVVLG VGLVPPEGSE KLRQTIGLSK SADGFLMEAH PKLRPVDTLT
DGVYLAGVAQ GPKDIPDAVA QASGAAARAA IPMVKGEVEI EPIVAVTDSD VCGGCEVCIE
LCPFGAISIE EGHANVNVAL CKGCGTCVAA CPSGAMDQQH FRTEQIMAQI EAALNEQAK
