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
//