ID A0A0G3CMW3_9GAMM Unreviewed; 593 AA.
AC A0A0G3CMW3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:AKJ41248.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:AKJ41248.1};
GN ORFNames=QQ39_03425 {ECO:0000313|EMBL:AKJ41248.1};
OS Pragia fontium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Pragia.
OX NCBI_TaxID=82985 {ECO:0000313|EMBL:AKJ41248.1, ECO:0000313|Proteomes:UP000068021};
RN [1] {ECO:0000313|EMBL:AKJ41248.1, ECO:0000313|Proteomes:UP000068021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24613 {ECO:0000313|EMBL:AKJ41248.1,
RC ECO:0000313|Proteomes:UP000068021};
RX PubMed=26159528;
RA Snopkova K., Sedlar K., Bosak J., Chaloupkova E., Provaznik I., Smajs D.;
RT "Complete Genome Sequence of Pragia fontium 24613, an Environmental
RT Bacterium from the Family Enterobacteriaceae.";
RL Genome Announc. 3:e00740-15(2015).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP010423; AKJ41248.1; -; Genomic_DNA.
DR RefSeq; WP_047779991.1; NZ_UGTK01000001.1.
DR STRING; 82985.QQ39_03425; -.
DR KEGG; pfq:QQ39_03425; -.
DR PATRIC; fig|82985.3.peg.716; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000068021; 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:AKJ41248.1}; Lyase {ECO:0000313|EMBL:AKJ41248.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000068021};
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 195..328
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; 64912 MW; 51783F3AC1AF4D29 CRC64;
MAKMSAVEAA MHVLEKEGIT VAFGVPGAAI NPFYSAMNKH GKIQHYLARH VEGASHMAEG
YTRANPGNIG MCLGTSGPAG TDMITGLYSA IADSIPILCI TGQAPRARLH KEDFQAVDIE
SIAKPVTKMA VTVLEPALVP RVLQQAFHTM RSGRPGPVLI DLPYDVQVAE IEFDPDSYEP
ISVYKPTASQ QQIVKAIDML MSAEKPLIVS GGGVINADAS ALLQEFAEIC QVPVIPTLMG
WGTIPDDHPL MAGMVGLQTS HRYGNATLLA SDLVFGIGNR WANRHTGSVD KYVANRKIIH
IDIEPTQIGR VLCPDLGIVS DAKAALELLV SVAKKMKAEN RIPDRSAWVE ECNQRKRTML
RKTHFDDVPV KPQRVYEEMN KAFGRDVCYV TTIGLSQIAA AQMLHVFKPR HWINCGQAGP
LGWTIPSALG VCVADPARKV VAISGDYDFQ FMIEELAVGA QFKLPYIHIL VNNAYLGLIR
QAQRAFDMDY CVQLSFDNIN SSEVNGYGVD HVKVVEGLGC KAIRVFNPDD IQPALVKAQA
LMKQFSVPVV VEIILERVTN ISMGGEIDNV NEFEPVTDRM EDAPTETCFM KYQ
//
