ID A0A411WX40_9BURK Unreviewed; 593 AA.
AC A0A411WX40;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:QBI01354.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:QBI01354.1};
GN Name=gcl {ECO:0000313|EMBL:QBI01354.1};
GN ORFNames=EYF70_11220 {ECO:0000313|EMBL:QBI01354.1}, GCM10007387_18300
GN {ECO:0000313|EMBL:GGY36319.1};
OS Pseudoduganella albidiflava.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Pseudoduganella.
OX NCBI_TaxID=321983 {ECO:0000313|EMBL:QBI01354.1, ECO:0000313|Proteomes:UP000292307};
RN [1] {ECO:0000313|EMBL:GGY36319.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KCTC 12343 {ECO:0000313|EMBL:GGY36319.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [2] {ECO:0000313|EMBL:QBI01354.1, ECO:0000313|Proteomes:UP000292307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17472 {ECO:0000313|EMBL:QBI01354.1,
RC ECO:0000313|Proteomes:UP000292307};
RA Miess H., Frediansyhah A., Gross H.;
RT "Draft Genome Sequences of Six Type Strains of the Genus Massilia.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GGY36319.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KCTC 12343 {ECO:0000313|EMBL:GGY36319.1};
RA Sun Q., Kim S.;
RL Submitted (DEC-2022) 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; BMWV01000003; GGY36319.1; -; Genomic_DNA.
DR EMBL; CP036401; QBI01354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411WX40; -.
DR KEGG; mali:EYF70_11220; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000292307; Chromosome.
DR Proteomes; UP000628442; 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:QBI01354.1}; Lyase {ECO:0000313|EMBL:QBI01354.1};
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 194..329
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; 64409 MW; 563C685B2F09BC64 CRC64;
MARMRAIDAA AAVLRKEGIS TVFGVPGAAI NPLYSAMKKD GGFRHVLARH VEGASHMAEG
FTRAKAGNIG VCIGTSGPAG TDMITGLYSA IADSIPILCI TGQAPRARLY KEDFQAVDIE
SIAKPVTKWA VTVREPALVP RVFQQAFHIM RSGRPGPVLI DLPFDVQMAE IEFDIDTYES
LSLYKPAATR AQAEKALEML NAAERPVIVC GGGVINADAA AKLREFAEIL NVPVIPTLMG
WGALPDDHPL MAGMAGLQTS HRYGNATILA SDFVIGIGNR WANRHTGSVE VYTEGRKFVH
IDIEPTQIGR VFGPDYGIVS DAGAALDQLI NVACGLDALG ALKDRSAWVA ECQERKRTML
RKTHFDNEPI KPQRVYEEMN KAFGQDTCYV STIGLSQIAA AQFLHVYKPR NWINCGQAGP
LGWTISAALG VCAADPERQV VAISGDYDFQ FMIEELAVGA QFNLPYLHVV VNNAYLGLIR
QAQRNFDIDY CVQLAFENIN APELGVYGVD HVAVVEGLGC KAIRVREIAD IQPAFAKARE
LMKEFRVPVV VEIMLERVTN IAMGTEINAI NEFEALATEE GDAPTAVAKR NLK
//
