ID G5S7S7_SALET Unreviewed; 372 AA.
AC G5S7S7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:EHD05794.1};
GN ORFNames=LTSEWAN_0895 {ECO:0000313|EMBL:EHD05794.1};
OS Salmonella enterica subsp. enterica serovar Wandsworth str. A4-580.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913086 {ECO:0000313|EMBL:EHD05794.1, ECO:0000313|Proteomes:UP000003536};
RN [1] {ECO:0000313|EMBL:EHD05794.1, ECO:0000313|Proteomes:UP000003536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4-580 {ECO:0000313|EMBL:EHD05794.1,
RC ECO:0000313|Proteomes:UP000003536};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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:EHD05794.1}.
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DR EMBL; AFCX01000292; EHD05794.1; -; Genomic_DNA.
DR AlphaFoldDB; G5S7S7; -.
DR PATRIC; fig|913086.3.peg.714; -.
DR Proteomes; UP000003536; 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; cd02006; TPP_Gcl; 1.
DR Gene3D; 3.40.50.970; -; 1.
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; 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 SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:EHD05794.1}.
FT DOMAIN 2..106
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 172..332
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 372 AA; 41320 MW; 4D90C13F67625651 CRC64;
MLQQFAELTN VPVIPTLMGW GCIPDDHPLM AGMVGLQTAH RYGNATLLAS DMVFGIGNRF
ANRHTGSVEK YTQGRKIIHI DIEPTQIGRV LCPDLGIVSD AKAALTLLID VAQEMQKAGR
LPCRKTWVDE CQQRKRTLLR KTHFDNVPVK PQRVYEEMNK AFGRDVCYVT TIGLSQIAAA
QMLHVFKDRH WINCGQAGPL GWTIPAALGV CAADPQRNVV AISGDFDFQF LIEELAVGAQ
FNIPYIHVLV NNAYLGLIRQ SQRAFDMDYC VQLAFENINS SEVNGYGVDH VKVAEGLGCK
AIRVFKPEDI APAFEQAKAL MAQYRVPVVV EVILERVTNI SMGSELDNVT EFEEVADSAK
DAPTETCFMK YE
//
