HDLA_ARCPA
ID HDLA_ARCPA Reviewed; 701 AA.
AC P84626; D2REQ7;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Heterodisulfide reductase subunit A-like protein;
DE EC=1.8.-.-;
GN Name=hdlA; OrderedLocusNames=Arcpr_1555;
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 2-14, FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR
RP 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:15009189};
CC Note=Binds 4 [4Fe-4S] clusters per subunit.
CC {ECO:0000269|PubMed:15009189};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={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 HdrA family. {ECO:0000305}.
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DR EMBL; CP001857; ADB58601.1; -; Genomic_DNA.
DR RefSeq; WP_012940937.1; NC_013741.1.
DR AlphaFoldDB; P84626; -.
DR SMR; P84626; -.
DR STRING; 572546.Arcpr_1555; -.
DR PRIDE; P84626; -.
DR EnsemblBacteria; ADB58601; ADB58601; Arcpr_1555.
DR GeneID; 8740245; -.
DR KEGG; apo:Arcpr_1555; -.
DR eggNOG; arCOG02235; Archaea.
DR HOGENOM; CLU_020302_0_0_2; -.
DR OMA; YEEFYHR; -.
DR OrthoDB; 1148at2157; -.
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; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR039650; HdrA-like.
DR PANTHER; PTHR43498; PTHR43498; 1.
DR Pfam; PF12838; Fer4_7; 2.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 3.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Metal-binding; Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..701
FT /note="Heterodisulfide reductase subunit A-like protein"
FT /id="PRO_0000150063"
FT DOMAIN 239..268
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 618..647
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 651..680
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 152..175
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 248
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 251
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 254
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 326
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 627
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 630
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 633
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 637
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 660
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 663
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 666
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 670
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT CONFLICT 2
FT /note="A -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 77281 MW; C4AB9F1A860BA328 CRC64;
MAEEEPKIGV YICHCGENIA GAVNIEEVKK FAETLPNVVV VRDYLFMCSD PGQELIKQDI
KEGRVNRVVV AACTPRTHEP IFRKACEDAG LNKYYFEMAN IRDQCSWAHW HEKEKATEKA
KQIIAAAVAK ARLLEPLEDR YVDITQKVLV IGGGIAGIFA ALDIANAGYK VYLVERNPSI
GGNMAKLDKT FPTNDCSACI LTPLMVEVAN HPNIELLTYS EVEAVEGTVG NFKVKVRKKQ
TWVDWDLCTG CGACTDVCPP KARVPDEFNE GLSKRGAIYI QFPQAVPKKA VIDIDACIEC
GGRKFGTEPR KTKDGKPILA PCEKVCPTGA ADRTKPRNPE GELIELDVGA IIVATGYKVM
DKTHFKEFAP DSPNVITALQ MERLISATGP TEGKLIVPSD IPKYEEWKKK VAKGEEVELE
ARKPHRIVYV SCVGSRDERF HTYCSKVCCM YMLKQAMLLK EKYPDLDIYI FFIDVRTPGK
DFDEYYMRCR QLGIKVIKGK VGGIRRMPDE RLWVRGYDAE IGKPVEVIAD LVVLATAIEP
SDGTIELARK LGINIGAEGF FRERHTKLYP VDTMTEGIFI CGCAQGPKDI PDSVAQAKAA
ASSAMSLIAP GKMKLEPLVS EVDKEKCSGC GICVPLCPYG AITMTKYNES MRAEINPALC
KGCGVCAAAC PSKAIKLHGF TFEQVLAQVR TLAKRGIVEV L
