HDRA2_METAC
ID HDRA2_METAC Reviewed; 793 AA.
AC Q8TM02;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ferredoxin/F(420)H(2)-dependent CoB-CoM heterodisulfide reductase subunit A {ECO:0000305};
DE EC=1.8.7.3 {ECO:0000269|PubMed:28174314};
DE EC=1.8.98.4 {ECO:0000269|PubMed:28174314};
DE AltName: Full=Coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase subunit A {ECO:0000305};
DE AltName: Full=Ferredoxin:CoB-CoM heterodisulfide reductase subunit A {ECO:0000305};
GN Name=hdrA2 {ECO:0000303|PubMed:19968794}; OrderedLocusNames=MA_2868;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
RN [2]
RP INDUCTION.
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=19968794; DOI=10.1111/j.1365-2958.2009.06990.x;
RA Buan N.R., Metcalf W.W.;
RT "Methanogenesis by Methanosarcina acetivorans involves two structurally and
RT functionally distinct classes of heterodisulfide reductase.";
RL Mol. Microbiol. 75:843-853(2010).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=28174314; DOI=10.1128/mbio.02285-16;
RA Yan Z., Wang M., Ferry J.G.;
RT "A ferredoxin- and F420H2-dependent, electron-bifurcating, heterodisulfide
RT reductase with homologs in the domains Bacteria and Archaea.";
RL MBio 8:E02285-E02285(2017).
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). Catalyzes the transfer of electrons from ferredoxin to
CC CoM-S-S-CoB during methanogenesis from acetate. Electrons transfer from
CC ferredoxin to CoM-S-S-CoB via HdrA2, HdrC2 and HdrB2. In addition, the
CC complex can use electron bifurcation to direct electron pairs from
CC reduced coenzyme F420 towards the reduction of both ferredoxin and CoB-
CC CoM heterodisulfide. This activity may take place during Fe(III)-
CC dependent anaerobic methane oxidation. {ECO:0000269|PubMed:28174314}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coenzyme B + coenzyme M + 2 oxidized [2Fe-2S]-[ferredoxin] =
CC coenzyme M-coenzyme B heterodisulfide + 2 H(+) + 2 reduced [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:55160, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:58319, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=1.8.7.3;
CC Evidence={ECO:0000269|PubMed:28174314};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coenzyme B + coenzyme M + 4 H(+) + 2 oxidized coenzyme F420-
CC (gamma-L-Glu)(n) + 2 reduced [2Fe-2S]-[ferredoxin] = coenzyme M-
CC coenzyme B heterodisulfide + 2 oxidized [2Fe-2S]-[ferredoxin] + 2
CC reduced coenzyme F420-(gamma-L-Glu)(n); Xref=Rhea:RHEA:55744,
CC Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:12939,
CC Rhea:RHEA-COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:58319, ChEBI:CHEBI:58411,
CC ChEBI:CHEBI:58596, ChEBI:CHEBI:133980, ChEBI:CHEBI:139511;
CC EC=1.8.98.4; Evidence={ECO:0000269|PubMed:28174314};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711,
CC ECO:0000269|PubMed:28174314};
CC Note=Binds 4 [4Fe-4S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00711,
CC ECO:0000269|PubMed:28174314};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:28174314};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:28174314};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:28174314};
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:0000305}.
CC -!- SUBUNIT: The ferredoxin/F(420)H(2)-dependent CoB-CoM heterodisulfide
CC reductase is composed of three subunits; HdrA2, HdrB2 and HdrC2.
CC {ECO:0000269|PubMed:28174314}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28174314}.
CC -!- INDUCTION: Induced by growth on methanol or acetate.
CC {ECO:0000269|PubMed:19968794}.
CC -!- SIMILARITY: Belongs to the HdrA family. {ECO:0000305}.
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DR EMBL; AE010299; AAM06247.1; -; Genomic_DNA.
DR RefSeq; WP_011022820.1; NC_003552.1.
DR AlphaFoldDB; Q8TM02; -.
DR SMR; Q8TM02; -.
DR STRING; 188937.MA_2868; -.
DR EnsemblBacteria; AAM06247; AAM06247; MA_2868.
DR GeneID; 1474765; -.
DR KEGG; mac:MA_2868; -.
DR HOGENOM; CLU_020302_0_0_2; -.
DR InParanoid; Q8TM02; -.
DR OMA; TAKHAML; -.
DR OrthoDB; 1148at2157; -.
DR PhylomeDB; Q8TM02; -.
DR BioCyc; MetaCyc:MON-20159; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
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 InterPro; IPR003813; MvhD/FlpD.
DR PANTHER; PTHR43498; PTHR43498; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF02662; FlpD; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
PE 1: Evidence at protein level;
KW 2Fe-2S; 4Fe-4S; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur;
KW Metal-binding; Methanogenesis; Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..793
FT /note="Ferredoxin/F(420)H(2)-dependent CoB-CoM
FT heterodisulfide reductase subunit A"
FT /id="PRO_0000150056"
FT DOMAIN 233..264
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 282..311
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 571..600
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 601..629
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 147..170
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 243
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 246
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 250
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 254
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 291
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 294
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 297
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 301
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 580
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 583
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 586
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 590
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 609
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 612
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 615
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 619
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 793 AA; 86918 MW; 80204B5433039032 CRC64;
MRIGVYICHC GLNIAGVIDV SALEAMANEL EDVVLAREVQ FLCSDSGQEG IIKDIKDNKL
DRVVVAACSP RLHEKTFRHV MEKAGLNPYL MEMVNIREQC SWVHADDPQM ATQKAFDLIR
MGVAKARFLR ELSATNSKAS RNVLIIGGGV AGIEAALNLA EAGFPVTMVE KESTIGGKMA
LMNEVFPTND CSICVLAPKM TEVQNHPNIT LYTYSEVTDI SGSVGKFHVR VKRKPRFVLE
DKCKGCVDLC SGVCPVEIEN PMNYGIGKTR AIYMPIPQSV PQVVLIDPDH CVGCGLCQLA
CPAEAVDYEQ KPEEIEFEAG AIIVSTGYQL FDASRKKEYG FGKYPDVITN MQLERMLNSA
GPTGGRVLVP STGEPPKSVA FIQCVGSRDK TVGNEYCSRV CCMAALKNSQ MVKERYPDTD
VTIHYIDIRA AGEMYEEYYT RTQEMGVDFI RGKVAEVYSG EDGRPVVRFE NTLESSVEEE
AHDLVVLSTG YEPTKAAEGI GRMLNLARRP DRFFASAHPK MRPVDAPVSG VFLAGCASGP
KEIQVSIAQG SACASKVMQL LGTGELEADP MGAHVDPDKC IGCRTCVEVC KFGKISIENK
KAVVDEVSCY GCGDCSAACP VGAIQMRNFE NEQILAQVRE ATAHKSQCPF IVAFLCNWCS
YACADLTGMS RIRYPTNIRV IRTMCSARVN PEFVLEALKG GADGVLVAGC RMDECHYIHG
NFDAKKRMDI LKEVIKEIGL DPKRLRTLWI SAAEGERFSN TINEFVKELE EIGPIGSEFK
QECAVPGVEE VTQ
