HMEE_ARCFU
ID HMEE_ARCFU Reviewed; 142 AA.
AC O29747;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Hdr-like menaquinol oxidoreductase cytochrome c subunit;
DE Short=Hme subunit E;
GN Name=hmeE; OrderedLocusNames=AF_0503;
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.
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. HmeA, HmeB and HmeE
CC subunits may together catalyze electron transfer from menaquinol to
CC cytochrome c.
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; Single-pass membrane protein;
CC Extracellular side.
CC -!- PTM: Binds 3 heme groups per subunit. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB90740.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000782; AAB90740.1; ALT_INIT; Genomic_DNA.
DR PIR; G69312; G69312.
DR RefSeq; WP_048064247.1; NC_000917.1.
DR AlphaFoldDB; O29747; -.
DR STRING; 224325.AF_0503; -.
DR EnsemblBacteria; AAB90740; AAB90740; AF_0503.
DR GeneID; 1483720; -.
DR KEGG; afu:AF_0503; -.
DR eggNOG; arCOG10385; Archaea.
DR HOGENOM; CLU_130444_0_0_2; -.
DR OMA; PNCWNCH; -.
DR OrthoDB; 126257at2157; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..142
FT /note="Hdr-like menaquinol oxidoreductase cytochrome c
FT subunit"
FT /id="PRO_0000108451"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..142
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT BINDING 93
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 96
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 104
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 107
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 108
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 117
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 120
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255"
FT BINDING 121
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT CONFLICT 4
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 142 AA; 16373 MW; 8F25DB18F53F8898 CRC64;
MYNKKYVIPL ILVFLIGFFT PYWYNAMAGT LGHVPTLKEP AGNCVEDKDW MAANHMLLLQ
QWRTQAIRHG AEGGGIYHSF TTGEEYHAST NTCWSCHDSK EEFCDQCHDY VGIHPECWDC
HYTPSVEKPH YSGIEELSKY FS
