ID A0A0G1JHS7_9BACT Unreviewed; 550 AA.
AC A0A0G1JHS7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding protein {ECO:0000313|EMBL:KKT34934.1};
GN ORFNames=UW24_C0018G0007 {ECO:0000313|EMBL:KKT34934.1};
OS Parcubacteria group bacterium GW2011_GWA2_44_12.
OC Bacteria.
OX NCBI_TaxID=1618829 {ECO:0000313|EMBL:KKT34934.1, ECO:0000313|Proteomes:UP000034439};
RN [1] {ECO:0000313|EMBL:KKT34934.1, ECO:0000313|Proteomes:UP000034439}
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:KKT34934.1}.
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DR EMBL; LCHO01000018; KKT34934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1JHS7; -.
DR PATRIC; fig|1618829.3.peg.602; -.
DR Proteomes; UP000034439; 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; cd02010; TPP_ALS; 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:SF129; 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..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 186..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 379..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 550 AA; 61109 MW; 61B2DDFEC14523E4 CRC64;
MDASHLFVKA LENEGVEYIF GIPGEENLPL LEAIRTSSIR FILTRHEQVA GFMAATYGRL
TGRAGVCLST LGPGATNLVT SAAYGLLGGM PMVIITGQKP IKENKQGHFQ VVNVVELMRP
ITKYATQIVS GNKVPDMVRE AFRVAQEERP GPVHLEFPED ISMEQADASL LAVTRPRRPI
AGEQAIAQAV EMIAKSQKPL ILVGAAANRQ HISTTLDAFI NATGIPFFNT QMGKGVVDER
HPLFLGTAAL SSGDYLHQII DDADLIINIG HDVVEKPPFL MRNADKRRVI HINFLSAQVD
SIYFPQLEVI GDIRNILLCL QRAVKRQDSW NFENFNRNKD ELERHIQEKQ DDKGFPLLPQ
RIVSDVRKAM PADGIVVLDN GMYKIWFARN YKAYKENTLL LDNALGTMGA GLSSAMAAKL
LHLEKKVLAV VGDGGFMMNS QELETAVRLG LSLVVLVIND GAYGMIKWKQ RAMNLKSFGL
DYGNPDFVKY AESYGAHGYR IESAEELLPL LTDCLQKEGI YLIDVPVDYS ENYTVLVKEL
KEKVNLENER
//