HDRA1_METKA
ID HDRA1_METKA Reviewed; 669 AA.
AC Q8TYP4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit A 1 {ECO:0000305};
DE EC=1.8.98.- {ECO:0000305};
GN Name=hdrA1; Synonyms=hdrA_1; OrderedLocusNames=MK0249;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(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:Q6LWL2}.
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: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:Q6LWL2}.
CC -!- SUBUNIT: The ferredoxin:CoB-CoM heterodisulfide reductase is composed
CC of three subunits; HdrA, HdrB and HdrC. {ECO:0000250|UniProtKB:Q6LWL2}.
CC -!- SIMILARITY: Belongs to the HdrA family. {ECO:0000305}.
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DR EMBL; AE009439; AAM01466.1; -; Genomic_DNA.
DR STRING; 190192.MK0249; -.
DR KEGG; mka:MK0249; -.
DR PATRIC; fig|190192.8.peg.251; -.
DR HOGENOM; CLU_020302_0_0_2; -.
DR OMA; CPSGAMQ; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000001826; 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 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; PF12838; Fer4_7; 1.
DR Pfam; PF13187; Fer4_9; 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; Selenocysteine.
FT CHAIN 1..669
FT /note="CoB--CoM heterodisulfide reductase iron-sulfur
FT subunit A 1"
FT /id="PRO_0000150058"
FT DOMAIN 239..270
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 287..318
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 584..613
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 617..646
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 153..176
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 249
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 252
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
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 259
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 296
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 299
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 306
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 593
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 596
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 599
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 603
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 626
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 629
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 632
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 636
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT NON_STD 200
FT /note="Selenocysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 73742 MW; C2D8D120157026E5 CRC64;
MGDKDDVRIG VFVCHCGVNI KASVDVEEVV EYAKKLPGVV YATDYPFFCA DPGQEIIQEA
IKEHDLDRVV VAACTPKIHE NTFRNCVKEA GLSPYYMEMV NIREHCSFVH MQEPEKATEK
AKDLIRAAVE RAKRLEDVPT KEVEVENSVL IIGGGIAGIQ AALDLADQGF KVYLVEKEPT
IGGNMARLAK TFPTDDCAMU ILAPKMVQVG NHPNIEMITY AEVKDVDGYI GNFEVTIEKK
PRYVDEDACT GCGVCAEVCP IEVPNEFDLG IGTRKAIYVP FPQAMPLVYT IDMEHCIQCG
LCEEACPQDP PAIDFDQEPE EIRLKVGTII VATGYEEFDA SKLEEYGYGK YDNVITTLEL
ERMINPAGPT EGHVIRPSDG KEPHRIVFIH CVGSRCPGKE EKGEAYCSRI CCMFILKNAQ
LIKQHEPDAE VYCCYMDVRA FGKGYEEYYE RAQKQFGVRF IRGRPAEIVE DPETKNLIVR
VEDTLTGEPM EIEADLVVLG CGLVAPEETY SKLADILGID RSPDGFFKEL HPKLEPVSTK
VRGVQIAGVA QGPKDIPDTV AQAKGAASEA SIPMSQGKVE IELITATVDE DVCGGCGACA
QVCPFDAIEM VEKDGKRVAE VQDVACQGCG QCAAACPSGA MQLRYYRDEQ LMPQIEALLA
EALEEEEEE
