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Database: UniProt
Entry: I3VVL5_THESW
LinkDB: I3VVL5_THESW
Original site: I3VVL5_THESW 
ID   I3VVL5_THESW            Unreviewed;       504 AA.
AC   I3VVL5;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Hydrogenase large subunit domain protein {ECO:0000313|EMBL:AFK86560.1};
GN   OrderedLocusNames=Tsac_1553 {ECO:0000313|EMBL:AFK86560.1};
OS   Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacterium.
OX   NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK86560.1, 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:AFK86560.1, 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).
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DR   EMBL; CP003184; AFK86560.1; -; Genomic_DNA.
DR   RefSeq; WP_014758430.1; NC_017992.1.
DR   AlphaFoldDB; I3VVL5; -.
DR   STRING; 1094508.Tsac_1553; -.
DR   KEGG; tsh:Tsac_1553; -.
DR   PATRIC; fig|1094508.3.peg.1574; -.
DR   eggNOG; COG2768; Bacteria.
DR   eggNOG; COG4624; Bacteria.
DR   BioCyc; TSAC1094508:GLMA-1576-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   CDD; cd10549; MtMvhB_like; 1.
DR   Gene3D; 3.30.70.20; -; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR009016; Fe_hydrogenase.
DR   InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR   InterPro; IPR027631; Mono_FeFe_hydrog.
DR   NCBIfam; TIGR04105; FeFe_hydrog_B1; 1.
DR   PANTHER; PTHR11615:SF368; HYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR11615; NITRATE, FORMATE, IRON DEHYDROGENASE; 1.
DR   Pfam; PF02906; Fe_hyd_lg_C; 1.
DR   Pfam; PF00037; Fer4; 2.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF53920; Fe-only hydrogenase; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
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          98..127
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          128..157
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          174..203
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   504 AA;  55601 MW;  C46E92AFAE949035 CRC64;
     MFKFNTDVQM LKYEVLYNVA KLTLEDRLED EYDEIPYEII PGTKPRFRCC VYKERAIIEQ
     RTKVAMGKNL KRTMKHAVDG EEPIIQVLDI ACEECPIKRY RVTEACRGCI THRCTEVCPK
     GAITIINKKA NIDYDKCIEC GRCKDACPYN AISDNLRPCI RSCSAKAITM DEELKAAINY
     EKCTSCGACT LACPFGAITD KSYIVDIIRA IKSGKKVYAL VAPAIASQFK DVTVGQIKSA
     LKEFGFVDVI EVALGADFVA MEEAKEFSHK IKDIKVMTSS CCPAFVAHIK KSYPELSQNI
     STTVSPMTAI SKYIKKHDPM AVTVFIGPCT AKKSEVMRDD VKGITDFAMT FEEMVAVLDA
     AKIDMKEQQD VEVDDATLFG RKFARSGGVL EAVVEAVKEI GADVEVNPVV CNGLDECNKT
     LKIMKAGKLP NNFIEGMACI GGCIGGAGVI NNNVNQAKLA VNKFGDSSYH KSIKDRISQF
     DTDDVDFHVD SGEDESSETS FKEA
//
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