ID E3DLX8_HALPG Unreviewed; 317 AA.
AC E3DLX8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Thiamine pyrophosphate TPP-binding domain-containing protein {ECO:0000313|EMBL:ADO76237.1};
GN OrderedLocusNames=Hprae_0078 {ECO:0000313|EMBL:ADO76237.1};
OS Halanaerobium praevalens (strain ATCC 33744 / DSM 2228 / GSL).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=572479 {ECO:0000313|EMBL:ADO76237.1, ECO:0000313|Proteomes:UP000006866};
RN [1] {ECO:0000313|Proteomes:UP000006866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33744 / DSM 2228 / GSL
RC {ECO:0000313|Proteomes:UP000006866};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Chertkov O., Detter J.C., Han C., Larimer F., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Halanaerobium praevalens DSM 2228.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO76237.1, ECO:0000313|Proteomes:UP000006866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33744 / DSM 2228 / GSL
RC {ECO:0000313|Proteomes:UP000006866};
RX PubMed=21886858;
RA Ivanova N., Sikorski J., Chertkov O., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Huntemann M., Liolios K., Pagani I., Mavromatis K., Ovchinikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M.,
RA Kannan K.P., Rohde M., Tindall B.J., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Lapidus A.;
RT "Complete genome sequence of the extremely halophilic Halanaerobium
RT praevalens type strain (GSL).";
RL Stand. Genomic Sci. 4:312-321(2011).
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DR EMBL; CP002175; ADO76237.1; -; Genomic_DNA.
DR AlphaFoldDB; E3DLX8; -.
DR STRING; 572479.Hprae_0078; -.
DR KEGG; hpk:Hprae_0078; -.
DR PATRIC; fig|572479.3.peg.82; -.
DR eggNOG; COG1013; Bacteria.
DR HOGENOM; CLU_058423_0_0_9; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000006866; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd03376; TPP_PFOR_porB_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR42897; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR PANTHER; PTHR42897:SF2; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006866}.
FT DOMAIN 52..222
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 317 AA; 35890 MW; 18450B7CB18F5C4D CRC64;
MTEKYNFKQE MEKEERLTGG HRMCAGCGAP VAVRAVLRAL EEDDEAVIGC ATGCLEVSTF
MYPYTAWKDS FIHNAFENAG ATTSGAEAAY QSLKKQGKLA NDKDHKFIAF GGDGGTYDIG
FQSLSGAMER GHDMTYVCYD NGAYMNTGIQ RSSATPRFAD TTTTPVGTEK KGKSQYRKDL
TAIMADHNLP YVAQTTFIGN FKDLHQKAKK AIYTEGATFL NVMAPCPRGW RYPPEKMMEL
CKLAVETCYW PMFEIENGEW KLNYKPKEKM PIEKFLEAQG RFKHITKSEK KDMIEEMQAE
VDHRWEKLLI RCGEKEK
//
