ID I3VTG1_THESW Unreviewed; 379 AA.
AC I3VTG1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Aldo/keto reductase {ECO:0000313|EMBL:AFK85806.1};
GN OrderedLocusNames=Tsac_0784 {ECO:0000313|EMBL:AFK85806.1};
OS Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacterium.
OX NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK85806.1, ECO:0000313|Proteomes:UP000006178};
RN [1] {ECO:0000313|Proteomes:UP000006178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RA Brown S.D., Land M.L., Herring C.D.;
RT "Thermoanaerobacterium saccharolyticum JW/SL-YS485.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFK85806.1, ECO:0000313|Proteomes:UP000006178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RX PubMed=24907337; DOI=10.1128/AEM.00998-14;
RA Currie D.H., Guss A.M., Herring C.D., Giannone R.J., Johnson C.M.,
RA Lankford P.K., Brown S.D., Hettich R.L., Lynd L.R.;
RT "Profile of Secreted Hydrolases, Associated Proteins, and SlpA in
RT Thermoanaerobacterium saccharolyticum during the Degradation of
RT Hemicellulose.";
RL Appl. Environ. Microbiol. 80:5001-5011(2014).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003184; AFK85806.1; -; Genomic_DNA.
DR RefSeq; WP_014757711.1; NC_017992.1.
DR AlphaFoldDB; I3VTG1; -.
DR STRING; 1094508.Tsac_0784; -.
DR KEGG; tsh:Tsac_0784; -.
DR PATRIC; fig|1094508.3.peg.791; -.
DR eggNOG; COG1453; Bacteria.
DR BioCyc; TSAC1094508:GLMA-794-MONOMER; -.
DR Proteomes; UP000006178; 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 GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd19096; AKR_Fe-S_oxidoreductase; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43312; D-THREO-ALDOSE 1-DEHYDROGENASE; 1.
DR PANTHER; PTHR43312:SF2; OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 336..370
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 379 AA; 43577 MW; AA55B2E691301AD5 CRC64;
MQYRKFGNTG VKVSALGFGA MRLPTIGGDN SKIDEEEAIK MIRYAIDNGV NYVDTAYPYH
SGQSEIVVGK ALKDGYREKT YLATKLPSWL INEKEDMDKY LNEQLKKLDV DYIDFYLLHA
LDKDRWEKYK RLDVFNWMEK VKREGKVKFI GFSFHDEYDV FKNIIDDYDK WDFCQIQYNY
MDIENQAGLK GLKYAASKGL AVIVMEPIRG GKLAGDPPQA IKELWNSASV KRTPAEWALQ
WVWNHPEVSL VLSGMSTMEQ VKQNIESASR SKANGLTDDE VKLVDKVRET YNKLSPVGCT
ACNYCMPCPN GVNIPKNFAI YNEAHMYNNY NEALRNYNSL NEGKASSCIE CGECETKCPQ
HLTIIEYLKD VRRYFKEAV
//
