ID A0A101R241_9ACTN Unreviewed; 594 AA.
AC A0A101R241;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:KUN40290.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:KUN40290.1};
GN ORFNames=AQJ30_06335 {ECO:0000313|EMBL:KUN40290.1};
OS Streptomyces longwoodensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68231 {ECO:0000313|EMBL:KUN40290.1, ECO:0000313|Proteomes:UP000053271};
RN [1] {ECO:0000313|EMBL:KUN40290.1, ECO:0000313|Proteomes:UP000053271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41677 {ECO:0000313|EMBL:KUN40290.1,
RC ECO:0000313|Proteomes:UP000053271};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces longwoodensis DSM 41677, type strain
RT for the species Streptomyces longwoodensis.";
RL Submitted (OCT-2015) 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:KUN40290.1}.
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DR EMBL; LMWS01000008; KUN40290.1; -; Genomic_DNA.
DR RefSeq; WP_067229701.1; NZ_KQ948550.1.
DR AlphaFoldDB; A0A101R241; -.
DR STRING; 68231.AQJ30_06335; -.
DR Proteomes; UP000053271; 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:KUN40290.1}; Lyase {ECO:0000313|EMBL:KUN40290.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053271};
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..552
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 594 AA; 63907 MW; 8E239C64B411E646 CRC64;
MARMTAARAA VEILRREGVT AAFGVPGAAI NPFYAALKAS GGITHTLARH VEGASHMAEG
YTRTRPGNIG VCIGTSGPAG TDMITGLYSA IGDSIPILCI TGQAPTAVIH KEDFQAVDIA
SIARPVTKMA VTVLEAAQVP GVFQKAFHLM RSGRPGPVLI DLPVDVQQTE IEFDPDTYEP
LPVYKPAATR AQIDKALAML NAAERPLIVA GGGVVTADAC DLLVQFAELT GVPVVPTLMG
WGALPDDHEL NAGMVGLQTS HRYGNATFLE SDFVLGIGNR WANRHTGRLD VYTAGRTFVH
VDVEPTQIGR IFAPDYGIAS DAAAALELFV EAAREAQRAG RLPDRSEWSA TAQERRATLQ
RRTHFDDVPI KPQRVYEEMN KAFGPETRYV STIGLSQIAG AQMLHVYRPR HWINCGQAGP
LGWTIPAALG VATADPDAQV VALSGDYDFQ FMIEELAVGA QHRIPYVHVL VNNSYLGLIR
QAQRAFDIDF QVKLEFENIN SPELGVYGVD HVKVAEGLGC KAIRVTDPAD LGAAFEQAKK
LAAEFRVPVV VEAILERVTN IAMSTTNDIG NVVEFEELAT EPSHAPTSIR PLKA
//