HDRA1_METAC
ID HDRA1_METAC Reviewed; 801 AA.
AC Q8TLB0;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Ferredoxin:CoB-CoM heterodisulfide reductase subunit A {ECO:0000305};
DE EC=1.8.7.3 {ECO:0000305|PubMed:19968794};
GN Name=hdrA1 {ECO:0000303|PubMed:19968794};
GN OrderedLocusNames=MA_3128 {ECO:0000312|EMBL:AAM06501.1};
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 FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
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).
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). Probably involved in methylotrophic methanogenesis but
CC not in aceticlastic methanogenesis. {ECO:0000269|PubMed:19968794}.
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:0000305|PubMed:19968794};
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:0000305}.
CC -!- SUBUNIT: The ferredoxin:CoB-CoM heterodisulfide reductase is composed
CC of three subunits; HdrA1, HdrB1 and HdrC1.
CC {ECO:0000269|PubMed:19968794}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced on trimethylamine or methanol, but not on acetate as
CC the sole energy source. {ECO:0000269|PubMed:19968794}.
CC -!- DISRUPTION PHENOTYPE: Triple hdrA1C1B1 deletion decreases methane
CC production from methanol, but does not affect methanogenesis from
CC acetate. Deletion results in up-regulation of CoB-SH and CoM-SH
CC synthesis and transport, and methylsulfide methyltransferases.
CC {ECO:0000269|PubMed:19968794}.
CC -!- SIMILARITY: Belongs to the HdrA family. {ECO:0000305}.
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DR EMBL; AE010299; AAM06501.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TLB0; -.
DR SMR; Q8TLB0; -.
DR STRING; 188937.MA_3128; -.
DR EnsemblBacteria; AAM06501; AAM06501; MA_3128.
DR KEGG; mac:MA_3128; -.
DR HOGENOM; CLU_020302_0_0_2; -.
DR OMA; YCCMAAL; -.
DR PhylomeDB; Q8TLB0; -.
DR BioCyc; MetaCyc:MON-20156; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000002487; 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 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; IPR039650; HdrA-like.
DR InterPro; IPR003813; MvhD/FlpD.
DR PANTHER; PTHR43498; PTHR43498; 1.
DR Pfam; PF02662; FlpD; 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 4Fe-4S; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW Methanogenesis; Oxidoreductase; Reference proteome.
FT CHAIN 1..801
FT /note="Ferredoxin:CoB-CoM heterodisulfide reductase subunit
FT A"
FT /id="PRO_0000443934"
FT DOMAIN 239..269
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 285..320
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 606..634
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 635..664
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT REGION 382..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149..172
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 248
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 251
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="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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 295
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 303
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 306
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 310
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 615
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 618
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 621
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
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 644
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 647
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 650
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 654
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 801 AA; 86966 MW; DAD42CD2913BFEBC CRC64;
MTDGLNKAAV FICHCSGNIS EHVDIDAVKK TLKAEGISVF DYEYMCSSQG QALIKKKIVE
GSLDRVVIGS CTPSKHGTLF KKCIQETGLN RAGLEIANLR EQCAWVHPDR TGATEKALSL
LRAKLKRLEN VEPLDEIKVD IAQQALVIGG GIAGITAALN LADNGVSTVL VENNSSIGGQ
MAKIGKIFSP DKLAEECAMC SLSPLMNEVA AHPKITLLTR TEVESLSGSA GNFTIRLRKK
PRYVKDSCTA CGRCSRVCPV QVEDEFNCGH MDKKAISLRF SQSVPKIYCI DPDYCLQLNG
EACGKCADAC KNEAIDFSQK EEIVELNVGA VVVATGFEEY DVSQKPQYGY GIFENVLTQM
ELARVLGING PTKGELLRVS DFSKASSDPT PATCDSRCED SSDESQGTDT PKRIVMIQCV
GSRDEKEGGN RYCSRYCCMA ALKHASLIKK KHPETEITIC YIDVRAFGFY ENYYRAVQET
GVNFVRGRPA EVIEKPDKSL VVRVEDTLDQ KMRELPADLV VLSAAMVPSP GTRKIASVLN
LSQDESGFIK ERHSKLKPVD SSLDGIFVCG TAQSPKDVTD TIAQAGLAAV RARAFITDSP
KVLDNEIATI NQLLCTRCGE CLKCPFDALS VNESGRVVLD PLICTGCGYC TKLCGEGAVQ
IAGFTKLQLK AEMEGVLEEG DVLGFVNSGI ASLTCDNIGN SVLTYPSNVK LIKVPTGLVV
DRDLVLHAFR HGASSVLFVE DPPDNPRAEV IYPLTVSHFE ELKEELGDSG NRIYFKKAYV
PNTKGLAGTF TSLAREGEMI R
