ID   A0A0S9C0W5_9MICC        Unreviewed;       596 AA.
AC   A0A0S9C0W5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:KQN87260.1};
DE            EC=4.1.1.47 {ECO:0000313|EMBL:KQN87260.1};
GN   ORFNames=ASE96_11275 {ECO:0000313|EMBL:KQN87260.1};
OS   Arthrobacter sp. Leaf69.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN87260.1, ECO:0000313|Proteomes:UP000051467};
RN   [1] {ECO:0000313|EMBL:KQN87260.1, ECO:0000313|Proteomes:UP000051467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf69 {ECO:0000313|EMBL:KQN87260.1,
RC   ECO:0000313|Proteomes:UP000051467};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN87260.1, ECO:0000313|Proteomes:UP000051467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf69 {ECO:0000313|EMBL:KQN87260.1,
RC   ECO:0000313|Proteomes:UP000051467};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQN87260.1}.
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DR   EMBL; LMLR01000012; KQN87260.1; -; Genomic_DNA.
DR   RefSeq; WP_056430560.1; NZ_LMLR01000012.1.
DR   AlphaFoldDB; A0A0S9C0W5; -.
DR   STRING; 1736232.ASE96_11275; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000051467; 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:KQN87260.1}; Lyase {ECO:0000313|EMBL:KQN87260.1};
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..328
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          393..557
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   596 AA;  63489 MW;  C6E1D7489821EDDC CRC64;
     MTKMRTVDAA VAILEKEGAT EAFGLPGAAI NPFYSAMRNH GGIRHTLARH VEGASHMADG
     YSRSQDGNIG ICIGTSGPAG TDMITGLYAA WADSIPMLCI TGQAPVAKLH KEDFQAVDIE
     SIAKPVTKMA MTVLEPGQVP GAFQKAFQLM RSGRPGPVLL DLPIDVQLAE IEFDIDAYEP
     LAVEKPRASR KQLEKALDML TAARHPLIVA GGGVINAGAS AELVELAELL GVPVIPTLMG
     WGAIPDDHPL MAGMVGLQTS HRYGNETMLA SDFVIGIGNR WANRHTGGLD TYTAGRTFVH
     IDIEPTQIGR VFSPDLGIAS DAGAALAGLV DLARERQAAG TLPDYSGWAA ECAGRKATMH
     RKTHFENIPI KPQRVYEEMN KAFGKDTTYV STIGLSQIAG AQMLHVFGPR QWINAGQAGP
     LGWTAPAALG VVRGKPDQTV VALSGDYDFQ FMIEELAVGA QFNLPYIHVV VNNSYLGLIR
     QSQRGFNMEQ NVSLAFENIN STGLSATASG YGVDHIKVAE GLGCKAIRVE DPNDLASAFG
     KAKAIMGEFQ VPVVVEVILE KVTNISMGVE INAVNEFEAL AETREDAPTA ILALQA
//