ID A0A1M7AKH0_PSETH Unreviewed; 592 AA.
AC A0A1M7AKH0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Tartronate-semialdehyde synthase {ECO:0000313|EMBL:SHL43260.1};
GN ORFNames=SAMN05443637_12863 {ECO:0000313|EMBL:SHL43260.1};
OS Pseudonocardia thermophila.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1848 {ECO:0000313|EMBL:SHL43260.1, ECO:0000313|Proteomes:UP000184363};
RN [1] {ECO:0000313|EMBL:SHL43260.1, ECO:0000313|Proteomes:UP000184363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43832 {ECO:0000313|EMBL:SHL43260.1,
RC ECO:0000313|Proteomes:UP000184363};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FRAP01000028; SHL43260.1; -; Genomic_DNA.
DR RefSeq; WP_073460297.1; NZ_FRAP01000028.1.
DR AlphaFoldDB; A0A1M7AKH0; -.
DR STRING; 1848.SAMN05443637_12863; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000184363; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000184363};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..126
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..333
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 394..554
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 592 AA; 63597 MW; E79A64078C8094AA CRC64;
MTRMRAVDAA VAILVKEGVR HAFGLPGAAI NPFYSALRAN QAASGVSIRH ILARHVEAAS
HMAEGYTRAT PGAIGVCVGT SGPAGTDMIT GLYSASADSI PILAITGQAP VSRLHKEDFQ
AVDIAAIAAP VTKWATTVRE PGQVPGAFAK AFHVMRSGRP GPVLIDLPID VQQAEIDFDV
DTYEPLPVHR PAATRAQVEK VLDMLAVAER PLIVAGGGVI GADACAELVE LAELLDVPVI
PTLMGWGAIP DDHPLMAGMA GLQTAHRYGN ATLLASDFVL GIGNRWANRH TGGLDVYRAG
RTFVHVDIEP TQIGRVFAPD YGVVSDAGAF LREMLAAARE RELPRRTAWV RECAERKGSM
QRRTHFDDVP VKPQRVYEEM NKAFGPDVRY VTTIGLSQIA AAQLLHVYRP RHWINAGQAG
PLGWTGPAAI GVCVADPDAT VVALSGDYDF QFMIEELAVG AQFNLPYLHI VVNNSYLGLI
RQAQRAFDMD YCVQLGFDNI NSPEVDKYGV DHVKVAEGLG CKAIRVTDPR ELGAAFDRAR
QLMAVHRVPV VVEVVLERVT NIAMGTELDA VVEFEDLART AADAPTATIP LS
//
