ID A0A0A7KJ95_9DEIO Unreviewed; 591 AA.
AC A0A0A7KJ95;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:AIZ46165.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:AIZ46165.1};
GN ORFNames=QR90_15570 {ECO:0000313|EMBL:AIZ46165.1};
OS Deinococcus radiopugnans.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=57497 {ECO:0000313|EMBL:AIZ46165.1, ECO:0000313|Proteomes:UP000030634};
RN [1] {ECO:0000313|Proteomes:UP000030634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY59 {ECO:0000313|Proteomes:UP000030634};
RA Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT "Hymenobacter sp. DG25B genome submission.";
RL Submitted (NOV-2014) 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; CP010028; AIZ46165.1; -; Genomic_DNA.
DR RefSeq; WP_039685899.1; NZ_CP010028.1.
DR AlphaFoldDB; A0A0A7KJ95; -.
DR STRING; 1182571.QR90_15570; -.
DR KEGG; dsw:QR90_15570; -.
DR HOGENOM; CLU_013748_1_2_0; -.
DR Proteomes; UP000030634; 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:AIZ46165.1}; Lyase {ECO:0000313|EMBL:AIZ46165.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030634};
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 591 AA; 64340 MW; 080375867799353F CRC64;
MAKMRAIEAA VEVLKKEGVD IAFGVPGAAI NPLYAAMKKL GGIEHILARH VEGASHMADG
YTRAKSGNIG VCIGTSGPAG TDMITGLYAA IADSVPILCI TGQAPRARLY KEDFQAVDIE
SIAKPVTKWA VTVREPALVP RVFQQAFHVM RSGRPGPVHI DLPFDVQMAE IEFDVDTYEA
LPAYKPQASR AQIEKSLELL FASERPLLVA GGGIINADAS DDLVTFAELT GIPVIPTLMG
WGAIPDDHPL MAGMAGLQTS QMYGNATVLA SDFVYGIGNR WANRHTGSVE KYTEGRKFVH
IDIEPTQIGR VFGPDYGIVS DAGAALKLMV EVARELRQAG KLPDYGEWAE QCRERKRTML
RKTHYDNVPI KPQRVYEEML KSFGRDTVYV STIGLSQIAA AQFLHVYGPR QWINAGQAGP
LGWTLPAALG VVAADRSKTV VALSGDYDFQ FMIEELAVGA QFKLPYVHVL VNNSYLGLIR
QSQRGFEMDY QVQLAFDNIN NPDLNGYGVD HVAVAEGLGC RAIRVTEPGK IKAGLEEAKE
LAQKFQVPVV LEVILERVTN ISMGTELDNV VEFEELADAR EDAPTAIAML D
//
