HMED_ARCPA
ID HMED_ARCPA Reviewed; 557 AA.
AC P84622; D2RF81;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Hdr-like menaquinol oxidoreductase iron-sulfur subunit;
DE Short=Hme subunit D;
GN Name=hmeD; OrderedLocusNames=Arcpr_1730;
OS Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=572546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5631 / JCM 9629 / NBRC 100127 / Av18;
RX PubMed=21304717; DOI=10.4056/sigs.942153;
RA von Jan M., Lapidus A., Del Rio T.G., Copeland A., Tice H., Cheng J.F.,
RA Lucas S., Chen F., Nolan M., Goodwin L., Han C., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Chertkov O., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Saunders E.,
RA Brettin T., Detter J.C., Chain P., Eichinger K., Huber H., Spring S.,
RA Rohde M., Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Archaeoglobus profundus type strain (AV18).";
RL Stand. Genomic Sci. 2:327-346(2010).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 3-21, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=15009189; DOI=10.1111/j.1432-1033.2004.04013.x;
RA Mander G.J., Pierik A.J., Huber H., Hedderich R.;
RT "Two distinct heterodisulfide reductase-like enzymes in the sulfate-
RT reducing archaeon Archaeoglobus profundus.";
RL Eur. J. Biochem. 271:1106-1116(2004).
CC -!- FUNCTION: Has menaquinol-oxidizing activity. The HmeC and HmeD subunits
CC may together mediate electron transfer from menaquinol to an
CC unidentified electron acceptor on the cytoplasmic side of the membrane.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:15009189};
CC Note=Binds 2 [4Fe-4S] clusters per subunit.
CC {ECO:0000269|PubMed:15009189};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15009189};
CC Peripheral membrane protein {ECO:0000269|PubMed:15009189}.
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DR EMBL; CP001857; ADB58775.1; -; Genomic_DNA.
DR RefSeq; WP_012941110.1; NC_013741.1.
DR AlphaFoldDB; P84622; -.
DR STRING; 572546.Arcpr_1730; -.
DR EnsemblBacteria; ADB58775; ADB58775; Arcpr_1730.
DR GeneID; 8740424; -.
DR KEGG; apo:Arcpr_1730; -.
DR eggNOG; arCOG00333; Archaea.
DR HOGENOM; CLU_023081_6_0_2; -.
DR OMA; HDSCNVA; -.
DR OrthoDB; 21885at2157; -.
DR Proteomes; UP000001901; Chromosome.
DR GO; GO:0016020; C: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 Pfam; PF13183; Fer4_8; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..557
FT /note="Hdr-like menaquinol oxidoreductase iron-sulfur
FT subunit"
FT /id="PRO_0000150087"
FT DOMAIN 86..115
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 155..184
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 95
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 98
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="1"
FT /evidence="ECO:0000255"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 164
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 167
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="2"
FT /evidence="ECO:0000255"
FT BINDING 174
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT CONFLICT 9
FT /note="K -> KL (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="D -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 64255 MW; B53B3453ED6F50EC CRC64;
MSEVPEELKI KQKFPNWYDW LKPITQKDIK HGFASYIALP KQVNSEFFKM PFGDVERDVF
SEDWKLPENW KEIILDSFKE TLEKNRAFKV FMDICVRCGA CADKCHYYIG TGDPKNMPVM
RAETVRSVYR YYFTIGGKLF GKWAGARPLD ENVIKEWYYY LLQCSLCRRC SLFCPYGIDT
AEVVWWARRM LSRVGLNQRF MCISIEASAR TGNHLGLYAG GMAGSIEQGL SELKDITGFD
LHTYINKPGA DVLFVAPSAD YFATPHWYAM LGYLLLFNEL EERYGLTVTW STYASEGGNF
GTFHSYEAAQ LLNSKIYKEA ERLGVKFIIG GECGHMWRDK HQFINTMNNP PKHAEWKKFW
DDPDLGQISE KLKGINLGEF ISGEHGWIHV LEFVAALIKH KKIDIDPSRN DHWRATYHDP
CNVARGMGML EEPRYVLRNV MNNFYDMPEH TIREKTYCCA AGGGMLAEEL MELRMRGVMP
RMMALRYVVK KYGVNIMLTP CAIDKAQFPI AVDYWKIPVE IGGPMEMVGN ALVLTAFGEK
PEDRKYDLRG TPIREEE
