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Database: UniProt
Entry: P84621
LinkDB: P84621
Original site: P84621 
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   16-JAN-2019, entry version 55.
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 /
OS   Av18).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; 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.,
RA   Cheng J.F., Lucas S., Chen F., Nolan M., Goodwin L., Han C.,
RA   Pitluck S., Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Chertkov O., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Saunders E., Brettin T., Detter J.C.,
RA   Chain P., Eichinger K., Huber H., Spring S., Rohde M., Goker M.,
RA   Wirth R., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Archaeoglobus profundus type strain
RT   (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
CC       may together mediate electron transfer from hydrogen to an
CC       unidentified electron acceptor on the cytoplasmic side of the
CC       membrane. {ECO:0000269|PubMed:15009189}.
CC   -!- SUBUNIT: The heterodisulfide reductase is composed of three
CC       subunits; HdlA, HdlB and HdlC. It forms a complex with the F420-
CC       non-reducing hydrogenase (Mvh), which provides the reducing
CC       equivalents to the heterodisulfide reductase.
CC       {ECO:0000269|PubMed:15009189}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15009189}.
CC   -!- SIMILARITY: Belongs to the HdrC family. {ECO:0000305}.
DR   EMBL; CP001857; ADB58600.1; -; Genomic_DNA.
DR   RefSeq; WP_012940936.1; NC_013741.1.
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   eggNOG; COG1150; LUCA.
DR   HOGENOM; HOG000237015; -.
DR   KO; K03390; -.
DR   OMA; WLCTTCY; -.
DR   OrthoDB; 102216at2157; -.
DR   BioCyc; APRO572546:G1GH6-1557-MONOMER; -.
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   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   SUPFAM; SSF46548; SSF46548; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   4Fe-4S; Complete proteome; Cytoplasm; Direct protein sequencing; Iron;
KW   Iron-sulfur; Metal-binding; Oxidoreductase; Reference proteome;
KW   Repeat.
FT   CHAIN         1    188       Heterodisulfide reductase subunit C-like
FT                                protein.
FT                                /FTId=PRO_0000150085.
FT   DOMAIN       34     64       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       78    109       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        44     44       Iron-sulfur 1 (4Fe-4S). {ECO:0000255}.
FT   METAL        47     47       Iron-sulfur 1 (4Fe-4S). {ECO:0000255}.
FT   METAL        50     50       Iron-sulfur 1 (4Fe-4S). {ECO:0000255}.
FT   METAL        54     54       Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
FT   METAL        89     89       Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
FT   METAL        92     92       Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
FT   METAL        95     95       Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
FT   METAL        99     99       Iron-sulfur 1 (4Fe-4S). {ECO:0000255}.
FT   CONFLICT      4      4       M -> H (in Ref. 2; AA sequence).
FT                                {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
//
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