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Database: UniProt
Entry: G2PTM7_9FIRM
LinkDB: G2PTM7_9FIRM
Original site: G2PTM7_9FIRM 
ID   G2PTM7_9FIRM            Unreviewed;       312 AA.
AC   G2PTM7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Thiamine pyrophosphate TPP-binding domain-containing protein {ECO:0000313|EMBL:AEM74308.1};
GN   ORFNames=Calla_1719 {ECO:0000313|EMBL:AEM74308.1};
OS   Caldicellulosiruptor acetigenus 6A.
OC   Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC   Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX   NCBI_TaxID=632516 {ECO:0000313|EMBL:AEM74308.1, ECO:0000313|Proteomes:UP000009257};
RN   [1] {ECO:0000313|EMBL:AEM74308.1, ECO:0000313|Proteomes:UP000009257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6A {ECO:0000313|EMBL:AEM74308.1,
RC   ECO:0000313|Proteomes:UP000009257};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Blumer-Schuette S.E.,
RA   Kelly R.M., Woyke T.;
RT   "Complete sequence of Caldicellulosiruptor lactoaceticus 6A.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003001; AEM74308.1; -; Genomic_DNA.
DR   RefSeq; WP_014042899.1; NC_015949.1.
DR   AlphaFoldDB; G2PTM7; -.
DR   KEGG; clc:Calla_1719; -.
DR   HOGENOM; CLU_058423_0_0_9; -.
DR   Proteomes; UP000009257; 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; -; 1.
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}.
FT   DOMAIN          50..219
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   312 AA;  34732 MW;  C126A82BB311C30B CRC64;
     MAYNIKELAA RPERFTGGHR MCAGCGAPVA VRAVLRALKP EDRAVVGVAT GCLEVSSCIY
     PYTAWKDSFI HSAFENAAAT VAGAEAAYKV LKKKGKVQGE FKFIAFGGDG GTYDIGLQSL
     SGAMERGHNM VYVCYDNGAY MNTGIQRSSA TPLYADTTTS PQGKVIPGKM QWRKDLTEVM
     VAHGIPYVAQ TAFITPNLKD LIEKAEKALY TDGPAFLNVL APCPRGWRYE TSKLIEISKL
     AVDTCFWPLY EVVNGQYRLS YKPKEKLPVV EFLKTQGRFR HLFKKGNEHL IEQIQQEVDR
     RWERLLELCG EK
//
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