ID H0QTZ1_ARTGO Unreviewed; 592 AA.
AC H0QTZ1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:GAB16292.1};
GN Name=gcl {ECO:0000313|EMBL:GAB16292.1};
GN ORFNames=ARGLB_116_00340 {ECO:0000313|EMBL:GAB16292.1};
OS Arthrobacter globiformis NBRC 12137.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1077972 {ECO:0000313|EMBL:GAB16292.1, ECO:0000313|Proteomes:UP000003828};
RN [1] {ECO:0000313|EMBL:GAB16292.1, ECO:0000313|Proteomes:UP000003828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 12137 {ECO:0000313|EMBL:GAB16292.1,
RC ECO:0000313|Proteomes:UP000003828};
RA Miyazawa S., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Arthrobacter globiformis NBRC 12137.";
RL Submitted (DEC-2011) 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:GAB16292.1}.
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DR EMBL; BAEG01000116; GAB16292.1; -; Genomic_DNA.
DR RefSeq; WP_003806263.1; NZ_BAEG01000116.1.
DR AlphaFoldDB; H0QTZ1; -.
DR STRING; 1077972.ARGLB_116_00340; -.
DR eggNOG; COG3960; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000003828; 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: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:GAB16292.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003828};
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..553
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 592 AA; 63472 MW; BA6FFA5EED10CAF1 CRC64;
MTKMRTVDAA IAILEKEGAT EAFGLPGAAI NPFYSAMRAH GGIRHTLARH VEGASHMADG
YSRAADGNIG ICIGTSGPAG TDMITGLYAA WADSIPMLCI TGQAPVAKLH KEDFQAVDIE
SIAKPVTKMA MTILEPGQVP GAFQKAFQLM RSGRPGPVLL DLPIDVQMAE IEFDIDTYEP
LPAEKPKASR KQLEKALDML TAGERPLIVA GGGIINAGAS AQLVELAELL NVPVIPTLMG
WGAIPDDHGL MAGMVGLQTS HRYGNENFLR SDFVIGIGNR WANRHTGGLD TYTAGRKFVH
IDIEPTQIGR VFSPDFGIAS DAGAALDGLL EIARERRAAG TLPDYKAWVA ECAERKATLH
RKTHFDNVPI KPQRVYEEMN KAFGKDTTYV STIGLSQIAG AQMLHVFGAR KWINAGQAGP
LGWTAPAALG VVRGKPGETV VALSGDYDFQ FMIEELAVGA QFNLPYIHVV VNNSYLGLIR
QSQRGFNMDY HVSLGFDNIN SPETEGYGVD HIKVVEGLGC KAIRVTSPED MPAAFDKAKA
LMGEFQVPVV VEVILEKVTN ISMGLEINAV NEFEDLAASA ADAPTAILAL QD
//
