ID A0A0N0SKC2_9ACTN Unreviewed; 594 AA.
AC A0A0N0SKC2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:KOU59379.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:KOU59379.1};
GN ORFNames=ADK57_33795 {ECO:0000313|EMBL:KOU59379.1};
OS Streptomyces sp. MMG1533.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU59379.1, ECO:0000313|Proteomes:UP000037741};
RN [1] {ECO:0000313|Proteomes:UP000037741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOU59379.1}.
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DR EMBL; LGDG01000245; KOU59379.1; -; Genomic_DNA.
DR RefSeq; WP_053753453.1; NZ_LGDG01000245.1.
DR AlphaFoldDB; A0A0N0SKC2; -.
DR STRING; 1415546.ADK57_33795; -.
DR PATRIC; fig|1415546.3.peg.7304; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000037741; Unassembled WGS sequence.
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:UniProtKB-EC.
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:KOU59379.1}; Lyase {ECO:0000313|EMBL:KOU59379.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037741};
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..552
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 594 AA; 63678 MW; 34541AFF46F41325 CRC64;
MARMTAARAA VEILRREGVT AAFGVPGAAI NPFYAALKAS GGIHHTLARH VEGASHMAEG
YTRTHPGNIG VCIGTSGPAG TDMITGLYSA IGDSIPILCI TGQAPTAVIH KEDFQAVDIA
SIATPVTKMA VTVLEAAQVP GVFQQAFHLM RSGRPGPVLI DLPIDVQLTE IEFDPDTYEP
LPVYKPAATR AQIEKAIGML NASERPLIVA GGGVINADAA ELLVEFAELT GVPVVPTLMG
WGVLPDDHEL NAGMVGLQTS HRYGNATFLE SDFVLGIGNR WANRHTGKLD VYTAGRTFVH
VDVEPTQIGR IFAPDYGIAS DAKAALELFV AVAREVKAAG KLPDRSAWAG AAQQKKATLQ
RRTHFDDIPI KPQRVYEEMN KAFGPETRYV STIGLSQIAG AQMLHVYRPR HWINCGQAGP
LGWTVPAALG VAKADPEAQV VALSGDYDFQ FMIEELAVGA QHKIPYVHVL VNNSYLGLIR
QAQRAFDIDF QVKLEFENIN SPELGVYGVD HVKVAEGLGC KAIRVTDPAE LGAAFEQAKK
LAAEFQVPVV VEAILERVTN ISMSTTNDIG NVVEFEEIAT EPGHAPTSIR TLKV
//
