HMED_ARCFU
ID HMED_ARCFU Reviewed; 555 AA.
AC O29748;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Hdr-like menaquinol oxidoreductase iron-sulfur subunit 2;
DE Short=Hme subunit D;
GN Name=hmeD; OrderedLocusNames=AF_0502;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP PROTEIN SEQUENCE OF 1-15, EPR SPECTROSCOPY, AND REDOX POTENTIOMETRY OF
RP HEMES.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=11952791; DOI=10.1046/j.1432-1033.2002.02839.x;
RA Mander G.J., Duin E.C., Linder D., Stetter K.O., Hedderich R.;
RT "Purification and characterization of a membrane-bound enzyme complex from
RT the sulfate-reducing archaeon Archaeoglobus fulgidus related to
RT heterodisulfide reductase from methanogenic archaea.";
RL Eur. J. Biochem. 269:1895-1904(2002).
CC -!- FUNCTION: Has menaquinol-oxidizing activity. HmeC and HmeD subunits may
CC together mediate electron transfer from menaquinol to an unidentified
CC electron acceptor on the cytoplasmic side of the membrane.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000305};
CC -!- SUBUNIT: Consists of five subunits: an integral membrane subunit, a
CC cytochrome b-like subunit, a cytochrome c subunit and two iron-sulfur
CC subunits.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
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DR EMBL; AE000782; AAB90735.1; -; Genomic_DNA.
DR PIR; F69312; F69312.
DR RefSeq; WP_010878009.1; NC_000917.1.
DR AlphaFoldDB; O29748; -.
DR STRING; 224325.AF_0502; -.
DR PRIDE; O29748; -.
DR EnsemblBacteria; AAB90735; AAB90735; AF_0502.
DR GeneID; 24794042; -.
DR KEGG; afu:AF_0502; -.
DR eggNOG; arCOG00333; Archaea.
DR HOGENOM; CLU_023081_6_0_2; -.
DR OMA; HDSCNVA; -.
DR OrthoDB; 21885at2157; -.
DR PhylomeDB; O29748; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005886; C:plasma membrane; 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 Gene3D; 1.10.1060.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004017; Cys_rich_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR Pfam; PF02754; CCG; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..555
FT /note="Hdr-like menaquinol oxidoreductase iron-sulfur
FT subunit 2"
FT /id="PRO_0000159262"
FT DOMAIN 82..111
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 151..180
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 91
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 94
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 101
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 160
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 163
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 166
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 170
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT CONFLICT 3
FT /note="E -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 5
FT /note="P -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="R -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="Q -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 555 AA; 64368 MW; D08291A749B8BE88 CRC64;
MEEMPERIEI KQKFPSWREM LKPVKEFEEG RLSYLSLPKQ VDSEWFKMPF GDVERDFHDL
KLPENWKEIF LEAMKDTLEK NRSFKLFMDI CVRCGACADK CHYYIGTGDP KNMPVARAEL
IRSVYRRYFT PAGKFFGEWA GARELNEDVL KELYYYAYQC SLCRRCSLFC PYGIDTAEIV
WWLRRMLSRV GLNQRFMTIS IEASSRTGNH LGLLPGGMYG AIQQGLEELK DYTGFDLHTY
INKKGADILF VAPSADYFAT PHWYVMLGYL LLFNELEEKY GLTITWSTYA SEGGNFGTFH
SYEAAQLLNS KIYKEAERLG VSFIIGGECG HMWRDKHQFI NTMNLPPKHE EWRRFWEDPD
LGNLAEGLRG VRFDSYASGE HGWIHILEFV AALIEHKKIV VDKSRNDKWI ATYHDPCNVA
RGMGLIEEPR YVLRNVMNNF YDMPEHTIKD KTYCCGAGGG MLADELMDLR MRGVMPRMMA
VRHVYRKYGV NILLTPCAID KAQFPHALEY WKIPIEVGGP MEMVGNALVM TAFGEKPEDR
QFDLRGEPLK PEEGE
