HDRA_METMA
ID HDRA_METMA Reviewed; 793 AA.
AC Q8Q0T0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ferredoxin:CoB-CoM heterodisulfide reductase subunit A {ECO:0000250|UniProtKB:Q8TLB0};
DE EC=1.8.7.3 {ECO:0000250|UniProtKB:Q8TLB0};
GN Name=hdrA; OrderedLocusNames=MM_0056;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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:Q8TLB0}.
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:0000250|UniProtKB:Q8TLB0};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC Note=Binds 4 [4Fe-4S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00711};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q8TM02};
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:Q8TLB0}.
CC -!- SUBUNIT: The ferredoxin:CoB-CoM heterodisulfide reductase is composed
CC of three subunits; HdrA, HdrB and HdrC. {ECO:0000250|UniProtKB:Q8TLB0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TLB0}.
CC -!- SIMILARITY: Belongs to the HdrA family. {ECO:0000305}.
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DR EMBL; AE008384; AAM29752.1; -; Genomic_DNA.
DR RefSeq; WP_011032010.1; NC_003901.1.
DR AlphaFoldDB; Q8Q0T0; -.
DR SMR; Q8Q0T0; -.
DR STRING; 192952.MM_0056; -.
DR EnsemblBacteria; AAM29752; AAM29752; MM_0056.
DR GeneID; 24877469; -.
DR KEGG; mma:MM_0056; -.
DR PATRIC; fig|192952.21.peg.69; -.
DR eggNOG; arCOG02235; Archaea.
DR eggNOG; arCOG02476; Archaea.
DR HOGENOM; CLU_020302_0_0_2; -.
DR OMA; TAKHAML; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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; PF13187; Fer4_9; 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 3: Inferred from homology;
KW 4Fe-4S; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW Methanogenesis; Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..793
FT /note="Ferredoxin:CoB-CoM heterodisulfide reductase subunit
FT A"
FT /id="PRO_0000150060"
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; 86803 MW; F34517E61FD4B362 CRC64;
MRIGVYVCHC GLNIAGVIDV SALEEMAGEL EDVVLAREVQ FLCSDSGQEG IIKDIKDNKI
DRVVIAACSP RLHEKTFRHV MEKADLNPYL MEMVNIREQC SWVHADDPQM ATQKAFDLIR
MGVAKARFLR ELSATSSKAS RNVLIIGGGV AGIEAALNLA EAGFPVTMVE RESTIGGKMA
LMNEVFPTND CSICVLAPKM TEVQNHPNIT LYTYSEVTDI SGSVGKFHVR VTRKPRFVLE
DKCKGCVDLC SEVCPVEIEN PMNYGIGKSR AIYMPIPQSV PQVVLIDPDH CVGCGLCQLA
CPAEAVDYEQ KPEEIEFEAG AVIVSTGYQL FDASRKKEYG FGKYPDVITN MQLERMLNSA
GPTGGRVLVP STGQPPESVA FIQCVGSRDK TVGNEHCSRV CCMAALKNSQ MVKERYPGTD
ITIHYIDIRA AGEMYEEYYA RTQGMGVDFI RGKVAEVYAG EDGRPVVRYE NTLESRVEEE
AHDLVVLSTG YEPSKAAEGI GRMLNLARRP DRFFASAHPK MRPVDAPVSG VFLAGCASGP
KEIQVSIAQG SACASKVMQL LGTGELEADP MGAHVDPDKC IGCRTCVEVC KFGKISIVDK
KAVVDEVSCY GCGDCSAACP VGAIQMRNFE NEQILAQVRA ATAHKSQCPF VVAFLCNWCS
YACADLTGMS RIHYPTNIRV IRTMCSARIN PEFVLEALKG GADGVLVAGC RMDECHYIHG
NFDAKKRMDV LKEIIKEIGL DPKRLRTLWI SAAEGERFSN TITEFVKELE EIGPIGSELK
REYTATGLEE VAK
