ID A0A127K1T0_9BURK Unreviewed; 596 AA.
AC A0A127K1T0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:AMO25372.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:AMO25372.1};
GN ORFNames=UC35_10285 {ECO:0000313|EMBL:AMO25372.1};
OS Ramlibacter tataouinensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=94132 {ECO:0000313|EMBL:AMO25372.1, ECO:0000313|Proteomes:UP000070433};
RN [1] {ECO:0000313|EMBL:AMO25372.1, ECO:0000313|Proteomes:UP000070433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-10 {ECO:0000313|EMBL:AMO25372.1,
RC ECO:0000313|Proteomes:UP000070433};
RX PubMed=24425747; DOI=10.1099/ijs.0.058396-0;
RA Lee H.J., Lee S.H., Lee S.S., Lee J.S., Kim Y., Kim S.C., Jeon C.O.;
RT "Ramlibacter solisilvae sp. nov., isolated from forest soil, and emended
RT description of the genus Ramlibacter.";
RL Int. J. Syst. Evol. Microbiol. 64:1317-1322(2014).
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; CP010951; AMO25372.1; -; Genomic_DNA.
DR RefSeq; WP_061503781.1; NZ_CP010951.1.
DR AlphaFoldDB; A0A127K1T0; -.
DR PATRIC; fig|94132.3.peg.2094; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000070433; Chromosome.
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:AMO25372.1}; Lyase {ECO:0000313|EMBL:AMO25372.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070433};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..555
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 596 AA; 65332 MW; C1A23AEF152CE080 CRC64;
MAMMKAVMAA VLVMEKEGVT QAFGVPGAAI NPLYSALRER QSIAHVLARH VEGASHMAEG
YTRARAGNIG VCIGTSGPAG TDMITGLYSA SADSIPILCI TGQAPRARLY KEDFQAVDIE
SIAKPVTKWA VTVREPALVP RVFQQAFHLM RSGRPGPVLI DLPFDVQMAE IEFDIDTYEP
LPVYKPAATR AQAEKAIDML CAAHKPLIVA GGGIINADAS ALLVELAETL NVPVVPTLMG
WGTIPDDHPL MAGMCGLQTS HRYGNATMLA SDFVLGIGNR WANRHTGGID TYTKGRKFVH
VDIEPTQIGR VFNPDFGIVS DAKAALELFV QVARERKAQG RLPDYTDWGQ RCLERKRLMH
RRTNYDTVPI KPQRVYQEMN EAFPRDTVYV STIGLSQIAG AQFLHVYGPR QWINCGQAGP
LGWTIPAALG VVAADPMRTV VGLSGDYDFQ FLVEELAVGA QFRLPYVQVL VNNSYLGLIR
QAQRNFDMDY CVQLGFENQN VSDPALQNYG VDHLKVVEGL GCKGLRVSHP DDLYDSLRKA
QALAREHRVP VVVEVMLEKV TNIAMGTEID KITEFEDIDC RHPEGLKGLE LAGLLD
//
