ID L0M282_ENTBF Unreviewed; 546 AA.
AC L0M282;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Thiamine pyrophosphate-dependent enzyme, possible carboligase or decarboxylase {ECO:0000313|EMBL:AGB76826.1};
GN OrderedLocusNames=D782_0777 {ECO:0000313|EMBL:AGB76826.1};
OS Enterobacteriaceae bacterium (strain FGI 57).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=693444 {ECO:0000313|EMBL:AGB76826.1, ECO:0000313|Proteomes:UP000011002};
RN [1] {ECO:0000313|EMBL:AGB76826.1, ECO:0000313|Proteomes:UP000011002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI 57 {ECO:0000313|EMBL:AGB76826.1,
RC ECO:0000313|Proteomes:UP000011002};
RX PubMed=23469353; DOI=10.1128/genomeA.00238-12;
RA Aylward F.O., Tremmel D.M., Bruce D.C., Chain P., Chen A.,
RA Walston Davenport K., Detter C., Han C.S., Han J., Huntemann M.,
RA Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M.,
RA Pagani I., Pati A., Pitluck S., Deshpande S., Goodwin L., Woyke T.,
RA Currie C.R.;
RT "Complete genome of Enterobacteriaceae bacterium strain FGI 57, a strain
RT associated with leaf-cutter ant fungus gardens.";
RL Genome Announc. 1:E00238-12(2013).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP003938; AGB76826.1; -; Genomic_DNA.
DR AlphaFoldDB; L0M282; -.
DR STRING; 693444.D782_0777; -.
DR KEGG; ebf:D782_0777; -.
DR PATRIC; fig|693444.3.peg.747; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_6; -.
DR OrthoDB; 8664451at2; -.
DR Proteomes; UP000011002; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:AGB76826.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011002};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 546 AA; 57638 MW; 684B042012198C11 CRC64;
MSEMITVGEA IARTLEQYQV DAIYGVISIH NLPIADAVGQ RGNIRFVPAR GEAGSVTMAD
AHGRFSGLGV ALTSTGAGAG NAVGALVEAM NACTPLLHLT GQVEKAWLDA DTGFIHETRD
QLTFLKASSK RAYRISNANQ AIAILHKAIQ DAQTPPCGPV SVEIPIDIQG AKIPASLVTA
AVRPATPVAV DTAIVDALWA QLKQAKQPLL WLGGGALSSA AAVKKLADAG MTVISSTHAR
GVLPDNHRAS LRAFHNSPSV EAMMETCDFT LVAGSRLRSN ETRSWTLTLP EPRVQIDIDP
AAASRNYLMD QTIITDCGAL LTALAAKAQG REWGNSAWDE QVQQAVVAAE QGLREQCGAY
AGLNDAIEHA LPDDGILVRD ITVSGSLWGS RLFRAHQPLK NIHSLAGAIG MGLPMAIGTA
IANPQHKVVG LVGDGGLSLN LGELATLAQE KANVTLLIMN DGGYGVMRGI QDKYFGGRQY
YNELHTPDFT ALAQAIGLQA WTVNRAEDFQ AAMTEALAMP GPSVVEVRMG EIGALRFAGP
PQKSLY
//
