ID A0A2U9LKA0_ECOLX Unreviewed; 593 AA. AC A0A2U9LKA0; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 24-JAN-2024, entry version 20. DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:AWS64858.1}; DE EC=4.1.1.47 {ECO:0000313|EMBL:EFB6351721.1}; GN Name=gcl {ECO:0000313|EMBL:AWS64858.1}; GN ORFNames=AM464_19580 {ECO:0000313|EMBL:AWS64858.1}, CX938_003433 GN {ECO:0000313|EMBL:EFB6351721.1}; OS Escherichia coli. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562 {ECO:0000313|EMBL:AWS64858.1, ECO:0000313|Proteomes:UP000247477}; RN [1] {ECO:0000313|EMBL:AWS64858.1, ECO:0000313|Proteomes:UP000247477} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AR_0085 {ECO:0000313|EMBL:AWS64858.1, RC ECO:0000313|Proteomes:UP000247477}; RA Conlan S., Thomas P.J., Mullikin J., Frank K.M., Segre J.A.; RT "Whole genome sequencing of Escherichia coli AR_0085."; RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EFB6351721.1, ECO:0000313|Proteomes:UP000539866} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSIS11706019 {ECO:0000313|EMBL:EFB6351721.1, RC ECO:0000313|Proteomes:UP000539866}; RG NARMS: The National Antimicrobial Resistance Monitoring System; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the TPP enzyme family. CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP029741; AWS64858.1; -; Genomic_DNA. DR EMBL; AASGIQ010000034; EFB6351721.1; -; Genomic_DNA. DR RefSeq; WP_001355653.1; NZ_VNXK01000004.1. DR AlphaFoldDB; A0A2U9LKA0; -. DR Proteomes; UP000247477; Chromosome. DR Proteomes; UP000539866; 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; cd02006; TPP_Gcl; 1. 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; IPR047034; Gcl_TPP-bd. 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:AWS64858.1}; KW Lyase {ECO:0000313|EMBL:EFB6351721.1}; 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 593 AA; 64702 MW; EF35F172E00C62E7 CRC64; MAKMRAVDAA MYVLEKEGIT TAFGVPGAAI NPFYSAMRKH GGIRHILARH VEGASHMAEG YTRATAGNIG VCLGTSGPAG TDMITALYSA SADSIPILCI TGQAPRARLH KEDFQAVDIE AIAKPVSKMA VTVREAALVP RVLQQAFHLM RSGRPGPVLV DLPFDVQVAE IEFDPDMYEP LPVYKPAASR MQIEKAVEML IQAERPVIVA GGGVINADAA ALLQQFAELT SVPVIPTLMG WGCIPDDHEL MAGMVGLQTA HRYGNATLLA SDMVFGIGNR FANRHTGSVE KYTEGRKIVH IDIEPTQIGR VLCPDLGIVS DAKAALTLLV EVAQEMQKAG RLPCRKEWVA DCQQRKRTLL RKTHFDNVPV KPQRVYEEMN KAFGRDVCYV TTIGLSQIAA AQMLHVFKDR HWINCGQAGP LGWTIPAALG VCAADPKRNV VAISGDFDFQ FLIEELAVGA QFNIPYIHVL VNNAYLGLIR QSQRAFDMDY CVQLAFENIN SSEVNGYGVD HVKVAEGLGC KAIRVFKPED IAPAFEQAKA LMAQYRVPVV VEVILERVAN ISMGSELDNV MEFEDIADNA ADAPTETCFM HYE //