ID A0A099JAF1_9MICO Unreviewed; 596 AA.
AC A0A099JAF1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:KGJ75394.1};
DE SubName: Full=Tartronate-semialdehyde synthase {ECO:0000313|EMBL:MBB5639955.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:KGJ75394.1, ECO:0000313|EMBL:MBB5639955.1};
GN ORFNames=BJ997_000503 {ECO:0000313|EMBL:MBB5639955.1}, GY21_09700
GN {ECO:0000313|EMBL:KGJ75394.1};
OS Cryobacterium roopkundense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=1001240 {ECO:0000313|EMBL:KGJ75394.1, ECO:0000313|Proteomes:UP000029864};
RN [1] {ECO:0000313|EMBL:KGJ75394.1, ECO:0000313|Proteomes:UP000029864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuG17 {ECO:0000313|EMBL:KGJ75394.1,
RC ECO:0000313|Proteomes:UP000029864};
RA Sisinthy S.;
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB5639955.1, ECO:0000313|Proteomes:UP000561726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21065 {ECO:0000313|EMBL:MBB5639955.1,
RC ECO:0000313|Proteomes:UP000561726};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) 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:KGJ75394.1}.
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DR EMBL; JPXF01000035; KGJ75394.1; -; Genomic_DNA.
DR EMBL; JACHBQ010000001; MBB5639955.1; -; Genomic_DNA.
DR RefSeq; WP_035836534.1; NZ_JPXF01000035.1.
DR AlphaFoldDB; A0A099JAF1; -.
DR STRING; 1001240.GY21_09700; -.
DR eggNOG; COG3960; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000029864; Unassembled WGS sequence.
DR Proteomes; UP000561726; 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: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:KGJ75394.1}; Lyase {ECO:0000313|EMBL:KGJ75394.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029864};
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..329
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 596 AA; 64241 MW; 43FD63454B6814AE CRC64;
MPKMRAVDVA VAILEKEGAT QTFGVPGAAI NPFYSAMRAH GGIDHILARH VEGASHMAEG
YTRTKAGNIG VCIGTSGPAG TDMLTGLYSA WADSTPILCI TGQAPVAKLH KEDFQGVDIA
SIAAPVTKMA VTVLEAGQVP GVFQKAFSLM RTGRPGPVLI DLPIDVQLTE IEFDIETYEP
LAVARPAASV AQLEKALDML VRAERPVIIA GGGVINADAA AQLVELAEVL NVPVIPTLMG
WGAIPDDHRL AAGMVGLMTS HRYGNATMLE SDFVLGIGNR WANRHTGGLD TYTRGRTFIH
IDIEPTQIGR IFAPDFGIVS DAGEALRGLV ELARERRAAS ALPDWENWVQ SCAHRKATLQ
RKTHFENVPI KPQRVYEEMN RAFGADTRYV TTIGLSQIAG AQFLNVFRPR HWINCGQAGP
LGWTLPAALG VAVADPTTTV VGLSGDYDFQ FMLEELAVGA QFHIPYIHVV VNNSYLGLIR
QAQRRFDMDY QVSLAFENVN SPELEGYGVD HLKVAEGLGC KAIRVREADD LQAAFTEARA
LMTEFRVPVV VEVMLERVTN IAMAATDIDA VIEFDDVAKT AADAPTSLAR LVSPTA
//