ID C0FUY0_9FIRM Unreviewed; 606 AA.
AC C0FUY0;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Thiamine pyrophosphate enzyme, central domain protein {ECO:0000313|EMBL:EEG93584.1};
GN ORFNames=ROSEINA2194_02551 {ECO:0000313|EMBL:EEG93584.1};
OS Roseburia inulinivorans DSM 16841.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=622312 {ECO:0000313|EMBL:EEG93584.1, ECO:0000313|Proteomes:UP000003561};
RN [1] {ECO:0000313|EMBL:EEG93584.1, ECO:0000313|Proteomes:UP000003561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16841 {ECO:0000313|EMBL:EEG93584.1,
RC ECO:0000313|Proteomes:UP000003561};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG93584.1, ECO:0000313|Proteomes:UP000003561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16841 {ECO:0000313|EMBL:EEG93584.1,
RC ECO:0000313|Proteomes:UP000003561};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Roseburia inulinivorans (DSM 16841).";
RL Submitted (MAR-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:EEG93584.1}.
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DR EMBL; ACFY01000096; EEG93584.1; -; Genomic_DNA.
DR RefSeq; WP_007886863.1; NZ_JAJFOJ010000001.1.
DR AlphaFoldDB; C0FUY0; -.
DR GeneID; 75161070; -.
DR eggNOG; COG0028; Bacteria.
DR Proteomes; UP000003561; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..108
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 204..340
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 405..553
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 606 AA; 66768 MW; A9748C1566A07DF7 CRC64;
MKIKVAKFIS QFLVDNGITD CFMVTGGGAM HLDDAIGHQE GMHCVFNHHE QACSIAAEGY
TRMTGKLAAV CVTSGPGGTN AITGVMGGWL DSIPMFVISG QVKRETTTWS CQELGLRQLG
DQEFDIINSV SNMTKYAVML TNPKEVAYHM EKALYLALNG RGGPVWIDVP LDVQGAMIET
EELIHFNPAE EKPWQVPEVK LEVVDTILEK IKKAKAPLIL VGTGIRLGGA EELLLKLLDK
LQIPVVTAWN ANDVLAADSP YFAGMPGTVG TRPGNFAIQN CDLLLSLGCR LNIRMIGYNH
YDFAKNAYKI IVDIDPRELV KPTIRPDMPV NADVKDLISK MLDSDYNAET KHKKWLVWCQ
NLMKEYPAAC KEYHRNDGGV INPYIFMDKL FDHLNNNDRI ICGNGSACVI TFQAGKIKQG
QRMFTNSGCA AMGYGLPAAL GVAVSDNSRR TICIDGDGSI MMNVQELATI VQNNLDIKII
LLNNNGYHSI RQTQTNLFQP PFIGIDEKSG VGFPDFKVLA QAFGMKYYVL DNEENCSQVL
EEALNCEGAC ICEAIVDPSQ NFAPKSSSKV LPDGRITSPS LDDMAPFLDR EEFEKIKSEA
TMIKEE
//