HMEA_ARCFU
ID HMEA_ARCFU Reviewed; 269 AA.
AC O29751;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Hdr-like menaquinol oxidoreductase iron-sulfur subunit 1;
DE Short=Hme subunit A;
DE Flags: Precursor;
GN Name=hmeA; OrderedLocusNames=AF_0499;
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 27-40, 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. HmeA, HmeB and HmeE
CC subunits may together catalyze electron transfer from menaquinol to
CC cytochrome c.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250};
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;
CC Extracellular side.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
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DR EMBL; AE000782; AAB90738.1; -; Genomic_DNA.
DR PIR; C69312; C69312.
DR RefSeq; WP_010878006.1; NC_000917.1.
DR AlphaFoldDB; O29751; -.
DR SMR; O29751; -.
DR STRING; 224325.AF_0499; -.
DR EnsemblBacteria; AAB90738; AAB90738; AF_0499.
DR GeneID; 24794039; -.
DR KEGG; afu:AF_0499; -.
DR eggNOG; arCOG01500; Archaea.
DR HOGENOM; CLU_043374_1_0_2; -.
DR OMA; RYCMAGC; -.
DR OrthoDB; 105930at2157; -.
DR PhylomeDB; O29751; -.
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 InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF13247; Fer4_11; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51318; TAT; 1.
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 Signal; Transport.
FT SIGNAL 1..26
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:11952791"
FT CHAIN 27..269
FT /note="Hdr-like menaquinol oxidoreductase iron-sulfur
FT subunit 1"
FT /id="PRO_0000008844"
FT DOMAIN 141..170
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 38
FT /note="R -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 30459 MW; C1889F20EB0DEDFE CRC64;
MMSRRKFLLL TGAAAAGAIL TPQISAKTQF IESPEEVREK RRWAMAVDVE RCTQCMEELI
AKTGDEKIKP PCVVACDKEN NVPEFEEERF DPQWMRIAKL KLDKPEVNPK EYYIPLLCNH
CEHPPCVQVC LTKASFKRPD GIVEIDMHRC IGCRYCMIAC PYGARCFNFI DPREGLKEVN
PNVQMRTEGV VEKCTFCVHR IDEAVKKGEE PIPACVEACH KYGKGALVFG NIKDPNSEIS
KILRENIVVQ LRANLGTDPH VFYAKLGGE
