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Database: UniProt
Entry: C2KUD1_9FIRM
LinkDB: C2KUD1_9FIRM
Original site: C2KUD1_9FIRM 
ID   C2KUD1_9FIRM            Unreviewed;       727 AA.
AC   C2KUD1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Thiamine pyrophosphate enzyme, central domain protein {ECO:0000313|EMBL:EEJ52619.1};
GN   ORFNames=HMPREF6123_0100 {ECO:0000313|EMBL:EEJ52619.1};
OS   Oribacterium sinus F0268.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Oribacterium.
OX   NCBI_TaxID=585501 {ECO:0000313|EMBL:EEJ52619.1, ECO:0000313|Proteomes:UP000004121};
RN   [1] {ECO:0000313|EMBL:EEJ52619.1, ECO:0000313|Proteomes:UP000004121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0268 {ECO:0000313|EMBL:EEJ52619.1,
RC   ECO:0000313|Proteomes:UP000004121};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:EEJ52619.1}.
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DR   EMBL; ACKX01000013; EEJ52619.1; -; Genomic_DNA.
DR   RefSeq; WP_007157635.1; NZ_GG668535.1.
DR   AlphaFoldDB; C2KUD1; -.
DR   STRING; 585501.HMPREF6123_0100; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_1_3_9; -.
DR   InParanoid; C2KUD1; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000004121; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd00568; TPP_enzymes; 1.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF142; ACETOLACTATE SYNTHASE; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000004121};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..116
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          263..399
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          497..678
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   727 AA;  80061 MW;  B1F0567A5C059ECD CRC64;
     MKIRVADYIA QKCYSMGLSR NFSVVGGGAM HLNDALGHHK GIKTLYQHHE QACAMAAESY
     ARIHNVPGIV CVTSGPGGTN AITGVVGAYL DSIPMLVLSG QVRHDNTARW SGRALRAMGD
     QEFDILQSVS CMCKYSEMLI DPYRVRYAIE KAIYLCQTGR PGPCWLDVPV DVQGFMVEEE
     DLLGFSPESY AAGGDGWADG TVKNSHPETA TALRRYFASD AEKEALLKAL SSEKNPHILE
     EDKTEKKEKT GIQNWQDFLP LAKEVLEKIR SSEHPIFYTG NGVRIAGAEG LFLECAEKLG
     IPVVLGWNAP DIFPTTHPLN AGRPGGRGDR PGNLAVQNAD VILSIGSRLN IRQVGYSFWE
     WAPKACVMQN DIDLEEIAKP SVHCDLPLHG DAKALLEALL HLLKQEEKLP LFAGGKGISR
     EKAKGFVRED AAGKILAEKQ DANLTWLDTI RFYQANYPTV LPEYLEERKG ELTNVYALVE
     KLSERASEDQ ITVVGNGSPC VAGGQSYIIK KGTRFISQDG VASMGYGLPA AIGAYYGVVD
     FTEEEKKRLS EDPYWKGKGE IYPPYQGKDI LLMTGDGSIQ MNLQELQTII HHQMPIKIFV
     VNNGGYHSIR QTQNSFFGKP LVGIGVDSGV EGCDLSFPNL EKLAHAYGYP YVSIKENAEL
     EQGIEKTLGQ SGPVICEVFV SMEQQFLPKS SAKKDAEGNL FSPPLEDMAP FLPEEEMEML
     MLYPRKK
//
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