ID   R4KQA8_9FIRM            Unreviewed;       597 AA.
AC   R4KQA8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Thiamine pyrophosphate-dependent enzyme, possible carboligase or decarboxylase {ECO:0000313|EMBL:AGL02765.1};
GN   ORFNames=Desgi_3422 {ECO:0000313|EMBL:AGL02765.1};
OS   Desulfoscipio gibsoniae DSM 7213.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC   Desulfoscipio.
OX   NCBI_TaxID=767817 {ECO:0000313|EMBL:AGL02765.1, ECO:0000313|Proteomes:UP000013520};
RN   [1] {ECO:0000313|EMBL:AGL02765.1, ECO:0000313|Proteomes:UP000013520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7213 {ECO:0000313|EMBL:AGL02765.1,
RC   ECO:0000313|Proteomes:UP000013520};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Parshina S.,
RA   Plugge C., Muyzer G., Kuever J., Ivanova A., Nazina T., Klenk H.-P.,
RA   Brambilla E., Spring S., Stams A.F., Woyke T.;
RT   "Complete sequence of Desulfotomaculum gibsoniae DSM 7213.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP003273; AGL02765.1; -; Genomic_DNA.
DR   RefSeq; WP_006524574.1; NC_021184.1.
DR   AlphaFoldDB; R4KQA8; -.
DR   STRING; 767817.Desgi_3422; -.
DR   KEGG; dgi:Desgi_3422; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_1_3_9; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000013520; 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   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:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:AGL02765.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013520};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          1..122
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          206..340
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          402..551
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   597 AA;  65757 MW;  FA861E9E3CFA0A17 CRC64;
     MKLSDYIIDF LVQEGVSHVF ELIGGAITHL LDSVYTRDDI QCISLHHEQS AAFAAEAYAR
     INGNLGVAIA TSGPGALNLV TGIGSCYFDS VPCLFITGQV NTYEYKFGRS VRQLGFQETD
     IVSVVKPITK YAQLVTNAEQ IRYYLEKAIY IARSGRPGPV LLDIPMNIQR AQIEPDKLAS
     FWDSAEYKKL YAEEIGHIFK QGANIIDEVI KLIKEAKRPV ILAGGGVRTA RAITEFGLLV
     EKTGIPVVTS LMGLDALPHD NRAFFGMIGS YGNRYSNLTL ANSDFLLILG SRLDTRQTGT
     RPETFARAAK KVHVDIDPVE LNAKVQVDTA INCNVREFLS LINAKLEGYV KPDFSPWYQT
     INGFKEKYST LAQPGKAENI DPNHFMEILS SYCAAGDIIC IDVGQNQMWA AQSFRLKKKQ
     RMLISGGMGA MGFALPAALG AAMSAPERKV IIIAGDGGIQ VNIQELDAFV NHNLPVKIFV
     MNNQCLGMVR QFQDLYFGGR QQSTVKGYSC PNLGKVAAAY GIPSYNIASW SSARDIIETA
     LKTEGPAFVE VKLEQTTCVD PKLVVNRPIE DMSPHLDRSE LQEIMLIDLM EEMDVPV
//