ID A0A0G0N4W4_9BACT Unreviewed; 554 AA.
AC A0A0G0N4W4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Thiamine pyrophosphate central domain-containing protein {ECO:0000313|EMBL:KKR11229.1};
GN ORFNames=UT38_C0002G0043 {ECO:0000313|EMBL:KKR11229.1};
OS Microgenomates group bacterium GW2011_GWA2_39_19.
OC Bacteria.
OX NCBI_TaxID=1618498 {ECO:0000313|EMBL:KKR11229.1, ECO:0000313|Proteomes:UP000034208};
RN [1] {ECO:0000313|EMBL:KKR11229.1, ECO:0000313|Proteomes:UP000034208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKR11229.1}.
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DR EMBL; LBWO01000002; KKR11229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0N4W4; -.
DR PATRIC; fig|1618498.3.peg.99; -.
DR Proteomes; UP000034208; 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 1..104
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..335
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..535
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 554 AA; 61543 MW; 9B820F4B3C553F6D CRC64;
MKLSDFVFKH LENFTDTVFL LSGGGIMHLV DSLGKSKLDA ICCHHEQAAA IAAEGYARIK
NDIGVVLVTT GPGGTNAITG VAGAWLDSIP MLVISGQVKM DNIAPRKNGV PQVRAIGFQE
LNVIDIVKPI TKYTVTVENP DDIKYEIEKA IYLAKSGRPG PVWIEIPLDI QAANVDTKKL
KKFTPAPQSE FDTPRIPIKL VVEKLKQSKR PLMLVGNGIR LAGGEKALWK LIEKLKINVA
TTIFTSDDLV TYEYPHYLGR QGMPGNETAN WAVDNCDLLL VVGDRLQLTQ TSYDYKNFAT
QALKIMVDID ESELHKKTLN IDIPIQADAK EFLELLVKQD FKINQWRVTP KKINADNYKP
GKNFVNVYKF LEALGKYSKK GLHVATSDGM ASVAPHQTLN IVRGQRFITN AGLGHMGSGL
PMAIGACIAT NKKQVLCMEG DGSIMLNIQE LQTMIYHRLP IKLFIYNNNG YFSIRNTHKS
YFNKIFAADP ESGVSFPNFE SVIKGWGLEY VKISTDEEIE KLNKIMKSSS PVVCELMIDP
NQPMLPKWTA GQFI
//
