ID Q3SIC8_THIDA Unreviewed; 752 AA.
AC Q3SIC8;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Heterodisulfide reductase, subunit A {ECO:0000313|EMBL:AAZ97600.1};
DE EC=1.8.98.1 {ECO:0000313|EMBL:AAZ97600.1};
GN OrderedLocusNames=Tbd_1647 {ECO:0000313|EMBL:AAZ97600.1};
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415 {ECO:0000313|EMBL:AAZ97600.1, ECO:0000313|Proteomes:UP000008291};
RN [1] {ECO:0000313|EMBL:AAZ97600.1, ECO:0000313|Proteomes:UP000008291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259 {ECO:0000313|EMBL:AAZ97600.1,
RC ECO:0000313|Proteomes:UP000008291};
RX PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ97600.1; -; Genomic_DNA.
DR RefSeq; WP_011312159.1; NC_007404.1.
DR AlphaFoldDB; Q3SIC8; -.
DR STRING; 292415.Tbd_1647; -.
DR KEGG; tbd:Tbd_1647; -.
DR eggNOG; COG1148; Bacteria.
DR eggNOG; COG1908; Bacteria.
DR HOGENOM; CLU_020302_0_0_4; -.
DR OrthoDB; 9808559at2; -.
DR Proteomes; UP000008291; Chromosome.
DR GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IEA:UniProtKB-EC.
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; 3.50.50.60; FAD/NAD(P)-binding 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; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR039650; HdrA-like.
DR InterPro; IPR003813; MvhD/FlpD.
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; PF13187; Fer4_9; 1.
DR Pfam; PF02662; FlpD; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
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 Oxidoreductase {ECO:0000313|EMBL:AAZ97600.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008291}.
FT DOMAIN 537..566
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 567..596
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 752 AA; 80812 MW; 4FA1FD62CD5B1526 CRC64;
MADIKVAAYI CKGCGLGERL DTDALVKIAQ KDGKVPLAKS HDFLCNADGV AMIKNDIANE
GVTHIMIGAC SRRAKTEAFY FPENAVARAN LREGVIWIRP DTDEARETTQ EMAEDYVRMG
CAEVKAMAAP AGNPNTGSSK TLLVVGGGVT GMTTAIEASK TGYPVVLVEK SGALGGWGGK
LYKRVPVHEP YKTPMDTGVA DLVSQVLGDS NIKLYLNASI AKTDGAPGRF VVEIATESGA
THTEDIGAIV QATGFTLYDM NKLPELGAGK SPNVVDQAGL EALANAAAAG DGVIRRPSDG
QPVKSVVFVQ CAGQRDPTGQ HLSYCSGFCC NASIKQAMYF KDANPAVDTT IIYTDLRTPG
NGEDFYRSAQ EKGVIFTKGK VSEVVPGGDS LTVTFHDLIL DDSKATMGDV DLVVLATGQV
ANSGVNIDAL TKPQVEGQEG GQQSGATVEV KPISILNLTY RQGPDVPQLK QGFTDSHFIC
FPYETRRTGI YTAGPVRRPM DMTQAREDAT GAALKAIQAL ENAELGRAAH PRSGDLSFPK
VRLEGCTQCK RCTVECPFGA IDEDEKRFPV FNESRCRRCG TCMGACPVRV ISFENYSVNT
VGAQIKAVDI PDEFSEKPRI LILACENDAY PALDMAGMNR NEYSAFVRII PIRCLGSVNT
IWVTDALNAG YDGVMMMGCK SGDEYQCHFV KGSELGRVRM SKIDDTLKTL NLESERVRDL
EVAITDIERV PEMINKYAEE LVAVGPSPFK GF
//
