ID Q3ADK7_CARHZ Unreviewed; 660 AA.
AC Q3ADK7;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Heterodisulfide reductase, subunit A, selenocysteine-containing {ECO:0000313|EMBL:ABB15769.1};
GN OrderedLocusNames=CHY_0930 {ECO:0000313|EMBL:ABB15769.1};
OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS Z-2901).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Carboxydothermus.
OX NCBI_TaxID=246194 {ECO:0000313|EMBL:ABB15769.1, ECO:0000313|Proteomes:UP000002706};
RN [1] {ECO:0000313|EMBL:ABB15769.1, ECO:0000313|Proteomes:UP000002706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901
RC {ECO:0000313|Proteomes:UP000002706};
RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA Madupu R., Sullivan S.A., Kolonay J.F., Haft D.H., Nelson W.C.,
RA Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B.,
RA Robb F.T., Eisen J.A.;
RT "Life in hot carbon monoxide: the complete genome sequence of
RT Carboxydothermus hydrogenoformans Z-2901.";
RL PLoS Genet. 1:563-574(2005).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the HdrA family.
CC {ECO:0000256|ARBA:ARBA00006561}.
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DR EMBL; CP000141; ABB15769.1; -; Genomic_DNA.
DR STRING; 246194.CHY_0930; -.
DR KEGG; chy:CHY_0930; -.
DR eggNOG; COG1148; Bacteria.
DR HOGENOM; CLU_020302_0_0_9; -.
DR InParanoid; Q3ADK7; -.
DR OrthoDB; 9758544at2; -.
DR Proteomes; UP000002706; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.30.70.3270; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR039650; HdrA-like.
DR PANTHER; PTHR43498:SF1; COB--COM HETERODISULFIDE REDUCTASE IRON-SULFUR SUBUNIT A; 1.
DR PANTHER; PTHR43498; FERREDOXIN:COB-COM HETERODISULFIDE REDUCTASE SUBUNIT A; 1.
DR Pfam; PF12831; FAD_oxidored; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002706};
KW Selenium {ECO:0000313|EMBL:ABB15769.1};
KW Selenocysteine {ECO:0000313|EMBL:ABB15769.1}.
FT DOMAIN 235..265
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 282..316
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 576..605
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 617..646
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT NON_STD 195
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:ABB15769.1"
SQ SEQUENCE 660 AA; 71644 MW; 888A5D85271BF8CA CRC64;
MKRIGVFVCW CGSNIGGVVD VPRVAEAAKE MPNVVFATDY KYMCSEPGQE LIIKAAKEHN
LDRVVVASCS PRLHEQTFRK AAERAGLNPY MFEMANIREH VSWVHAQEKE KATEKAIELV
RRAVFKAARL EPLYKSAIGI TKKALVIGGG IAGIQAALDI ADAGYQVILV EKEPTIGGKM
AQLDKTFPTL DCSSUISTPK MAAAAQHPNI KLYTYAEVTE VSGYIGNFEV TIKQKAKSVD
HNKCTGCGTC WEKCPTKVDS EFDLGLGKRK AIYIPFAQAV PNKPVIDRTT CRQFTKGKCG
VCQKVCPTGA VDYDQQDEYI KEKVGAIIMA TGYDLFEWEK VYGEYGYGQY PDVITGLHFE
RMASASGPTG GKIIRPSDGK EPKTVVFIKC VGSRDDQKGK SYCSRACCMY TAKHAHQVLE
KIPGAQVYIF YMDVRTAGKM YEEFYAKTLE DGAQYIRGRV SKIYPLGDKL IVRGADTLAG
VPVEIEADLV VLATAMVPAK GSEEIAKIVG FSLDKDGFFQ EAHPKLGPVE TTTGGVFLAG
ACQGPKDIPD TVAQASAAAA KVIGLLSKDQ LAAEPIVSQV NEALCSGCEL CKPICPYKAI
DMKKITERVH GKVIERTVAT VNTSLCQGCG ACTVACRVGA LNLKGFTNEQ LLAEVEAICL
//