ID A0A101ICQ3_9BACT Unreviewed; 509 AA.
AC A0A101ICQ3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:KUK92900.1};
DE Flags: Fragment;
GN ORFNames=XE05_1247 {ECO:0000313|EMBL:KUK92900.1};
OS Thermotogales bacterium 46_20.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales.
OX NCBI_TaxID=1635293 {ECO:0000313|EMBL:KUK92900.1, ECO:0000313|Proteomes:UP000054930};
RN [1] {ECO:0000313|Proteomes:UP000054930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUK92900.1}.
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DR EMBL; LGGZ01000081; KUK92900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101ICQ3; -.
DR Proteomes; UP000054930; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-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 CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR041117; SoxA_A3.
DR PANTHER; PTHR42949; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR PANTHER; PTHR42949:SF2; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF17806; SO_alpha_A3; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
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 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 283..312
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 315..344
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KUK92900.1"
SQ SEQUENCE 509 AA; 55027 MW; 7C20CEE66C70B361 CRC64;
LHLPSDTTRL FRPKRVVVAT GASEKFLQFE NNDLPGVYGA GAVQTLMNQF GIMPGKNVLM
IGSGNIGLIV SYQLVQAGVN VKAIVEIADR IGGYEVHADK VKRLGIPVLL KHTVTRALGV
ESVEGAEICE VDEKFSPIPS TARELVVDTV CIAVGLNPSV ELIAQAGGQI RYVAELGGYV
PVRDEDMRAT AEGFFVAGDV SGIEEATTAM IEGRIAGLSV VRDLKGSTDE NKVSRLKKEL
VGFRNGPISA RVREGLQKLG FDVSSGESRT GNLNNPQKYR GKLRPIIECF EAIPCNPCET
SCPTGAIVVG GNINDVPVID YDKCNGCGIC MTKCPGLAIF MLQELPDEDS ALIGIPYEFI
PLPSKGDQVH LLGRQGEMLA EGTVQRVFRS PHKTNSVYVK TPLELADKVR SIRPVLQEDN
AFVCRCEELT VSDIEAAIDE GYTDFEELRR KLRISMGPCG GRTCRLNALR ILSRKTGKSI
EELSFGVLRP PSIPSTLGSI ARQKGAEDD
//
