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Database: UniProt
Entry: D5WYM1_THIK1
LinkDB: D5WYM1_THIK1
Original site: D5WYM1_THIK1 
ID   D5WYM1_THIK1            Unreviewed;       582 AA.
AC   D5WYM1;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:ADG32198.1};
GN   OrderedLocusNames=Tint_2858 {ECO:0000313|EMBL:ADG32198.1};
OS   Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX   NCBI_TaxID=75379 {ECO:0000313|EMBL:ADG32198.1};
RN   [1] {ECO:0000313|EMBL:ADG32198.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 {ECO:0000313|EMBL:ADG32198.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA   Heinhorst S., Woyke T.;
RT   "Complete sequence of Thiomonas intermedia K12.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP002021; ADG32198.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5WYM1; -.
DR   STRING; 75379.Tint_2858; -.
DR   KEGG; tin:Tint_2858; -.
DR   eggNOG; COG3960; Bacteria.
DR   HOGENOM; CLU_013748_1_2_4; -.
DR   OMA; TLMGWGA; -.
DR   BioCyc; TINT75379:TINT_RS14300-MONOMER; -.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0009028; F:tartronate-semialdehyde synthase activity; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0009436; P:glyoxylate catabolic process; 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; IPR006397; Glyox_carbo_lig.
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   NCBIfam; TIGR01504; glyox_carbo_lig; 1.
DR   PANTHER; PTHR18968:SF14; GLYOXYLATE CARBOLIGASE; 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   Ligase {ECO:0000313|EMBL:ADG32198.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..121
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          193..327
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          393..553
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   582 AA;  63173 MW;  21F65FA8C33D5849 CRC64;
     MARMRAVDAA VLVLEKEGVH QAFGVPGAAI NPLYSALRKN GHIAHVLARH VEAASHMAEG
     YTRTAPGHIG VCIGTSGPAG TDMITGLYSA IADSIPILCI TGQAPRARLY KEDFQAVDIE
     SIAKPVCKWA VTVREPALVP QVFQQAFHVM RSGRPGPVLI DLPLDVQLAE IEFDADTYAP
     LAVYKPTATR AQIEKALDML EASERPLIVA GGGVINADAS DLLVQFAELT GVPVIPTLMG
     WGAIGDSHPL MAGMVGLQTS HRGGNANLLA SDLVLGIGNR WANRHTGSPE VYAKGRKILH
     VDIEPTQIGR VFMPDYGITS DAKAALELFI AVARERKAAG KLKNRSAWAN ACRERVQTLL
     RKWDYDQIPI KPHRVYKEMV EFFDANTRYV TTIGLSQIAA AQLLKVEKPR HWINAGQAGP
     LGWTMPAALG VRVADPTADV VAISGDYDFQ FLIEELAVGA QFKLPYIHIV VNNSYLGLIR
     QGQRQFDMDF CVQLSFDNVN SPEVSGYGID FVKVTEGLGC KAIRVFDPNQ IQPALAQARQ
     LMKEFAVPVV VEIILERVTN ISMGGEIDAI TEFDPVIDLV PA
//
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