HDLC_ARCPA
ID HDLC_ARCPA Reviewed; 188 AA.
AC P84621; D2REQ6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Heterodisulfide reductase subunit C-like protein;
DE EC=1.8.-.-;
GN Name=hdlC; OrderedLocusNames=Arcpr_1554;
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 1-20, FUNCTION, SUBUNIT, 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 oxidoreductase activity. The Hdl and Mvh subunits may
CC together mediate electron transfer from hydrogen to an unidentified
CC electron acceptor on the cytoplasmic side of the membrane.
CC {ECO:0000269|PubMed:15009189}.
CC -!- SUBUNIT: The heterodisulfide reductase is composed of three subunits;
CC HdlA, HdlB and HdlC. It forms a complex with the F420-non-reducing
CC hydrogenase (Mvh), which provides the reducing equivalents to the
CC heterodisulfide reductase. {ECO:0000269|PubMed:15009189}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15009189}.
CC -!- SIMILARITY: Belongs to the HdrC family. {ECO:0000305}.
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DR EMBL; CP001857; ADB58600.1; -; Genomic_DNA.
DR RefSeq; WP_012940936.1; NC_013741.1.
DR AlphaFoldDB; P84621; -.
DR SMR; P84621; -.
DR STRING; 572546.Arcpr_1554; -.
DR EnsemblBacteria; ADB58600; ADB58600; Arcpr_1554.
DR GeneID; 8740244; -.
DR KEGG; apo:Arcpr_1554; -.
DR eggNOG; arCOG00964; Archaea.
DR HOGENOM; CLU_121273_0_0_2; -.
DR OMA; DPDLWLC; -.
DR OrthoDB; 102216at2157; -.
DR Proteomes; UP000001901; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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; IPR009051; Helical_ferredxn.
DR Pfam; PF13183; Fer4_8; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..188
FT /note="Heterodisulfide reductase subunit C-like protein"
FT /id="PRO_0000150085"
FT DOMAIN 34..64
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 78..109
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 44
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 47
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 95
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT CONFLICT 4
FT /note="M -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 21306 MW; 358DADAC57DF5891 CRC64;
MEMMEEGVPD VINLSYLAER EETELEKRVA EIIKELGAER LMYCMQCGAC ASICPLARVG
FEWYNKKLIK ALILGLRDEL LDDPTPWACV ACNRCTEICP RRVSPFEVMF AMRRLMAEEY
AIGSLAIEGL RSLYEYGHAV YMAGREARKK VGLPEKPPST ESDPKALEDL RKILKQTKLA
ELGLVPME
