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Database: UniProt
Entry: Q3ADK7_CARHZ
LinkDB: Q3ADK7_CARHZ
Original site: Q3ADK7_CARHZ 
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
//
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