ID A0A1V9UDY9_9PSED Unreviewed; 591 AA.
AC A0A1V9UDY9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:OQR28102.1};
GN ORFNames=BWR59_23710 {ECO:0000313|EMBL:OQR28102.1};
OS Pseudomonas sp. Bc-h.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1943632 {ECO:0000313|EMBL:OQR28102.1, ECO:0000313|Proteomes:UP000192462};
RN [1] {ECO:0000313|EMBL:OQR28102.1, ECO:0000313|Proteomes:UP000192462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bc-h {ECO:0000313|EMBL:OQR28102.1,
RC ECO:0000313|Proteomes:UP000192462};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:OQR28102.1}.
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DR EMBL; MUIN01000012; OQR28102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9UDY9; -.
DR STRING; 1943632.BWR59_23710; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000192462; 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; 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:OQR28102.1};
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 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; 64243 MW; DBA038B4104545BC CRC64;
MTIMRAIEAA VLVMRREGVD TAFGIPGAAI NPLYAAFKKL GGIDHVLARH VEGASHMAEG
YTRAIAGNIG VCIGTSGPAG TDMITGLYSA SADSIPILCI TGQAPRARMH KEDFQAVDIA
SIAAPVAKWA TTVMEPGQVP YVFQKAFQLM RSGRPGPVLI DLPFDVQMAE IEFDIDAYEP
LPVIKPQASR NQVEKALAML NASERPLIVA GGGIINADAS DALVEFAELT GIPVIPTLMG
WGTIPDDHPQ MAGMVGLQTS HRYGNATMLE SDMVLGIGNR WANRHTGTVS VYSEGRKFIH
VDIEPTQIGR VLTPDLGIVS DAGAALAMFL EVAREWHTAG KLKDRSTWLA SCQERKRTMQ
RKTHYENIPV KPQRVYEEMN QYFGKDTCYI STIGLSQIAG AQFLHVYKPR HWINCGQAGP
LGWTIPAALG VAKADPSRKV VALSGDYDFQ FMIEELAVGA QFKLPYIHVV VNNSYLGLIR
QAQRNFDIDY CVQLAFDNIN APELEGYGVD HIAVAEGLGC KAIRVTDPAH IQAAFAEATS
MMQQYSVPVV VEIILERVTN IAMGTEINAI NEFESLAEHR DDAPTAISLL D
//
