ID A0A101TCC2_9ACTN Unreviewed; 592 AA.
AC A0A101TCC2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:KUN89808.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:KUN89808.1};
GN ORFNames=AQJ66_01665 {ECO:0000313|EMBL:KUN89808.1};
OS Streptomyces bungoensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN89808.1, ECO:0000313|Proteomes:UP000053024};
RN [1] {ECO:0000313|EMBL:KUN89808.1, ECO:0000313|Proteomes:UP000053024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN89808.1,
RC ECO:0000313|Proteomes:UP000053024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces bungoensis DSM 41781, type strain
RT for the species Streptomyces bungoensis.";
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:KUN89808.1}.
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DR EMBL; LMWX01000003; KUN89808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101TCC2; -.
DR STRING; 285568.AQJ66_01665; -.
DR Proteomes; UP000053024; 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:KUN89808.1}; Lyase {ECO:0000313|EMBL:KUN89808.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053024};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..325
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..550
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 592 AA; 64233 MW; 97DB99B3F55383FC CRC64;
MTAARAAVEI LKREGVRDAF GVPGAAINPF YKALKEGGGI HHTLARHVEG ASHMAEGYTR
ARPGNIGVCV GTSGPAGTDM ITGLYSATGD SIPILCITGQ APTSVIHKED FQAVDIASIA
GPVTKMAVTV LEAAQVPGVF QQAFHLMRSG RPGPVLIDLP IDVQQTEIEF DPDTYEPLPV
YRPAATRAQI EKALSFLLAA ERPVVVAGGG VIGADACDLL TEFAELTRTP VVPTLMGWGA
LPDDHELNAG MVGVQTSHRY GNATFLESDF VLGIGNRWAN RHTGYKLDVY RRGRTFVHVD
IEPTQIGRIF PPDYGVVSDA RAALELFVEV AKELKAEGRL PDRTAWVASA QERKATLLRR
THFDDVPMKP QRVYEEMNRA FGPDTRYVTT IGLSQIAGAQ MLHVYRPRHW INCGQAGPLG
WTIPAAIGVA KADPDTPVVA LSGDYDFQFM IEELAVAAQH RVPYVHVLVN NAYLGLIRQA
QLGLDIDFQV NLEFENINTP EIGVYGVDHV KVAEGLGCRA IRVTEPDQLG AAFEEAKKLA
AEYRVPVVVE AILERVTNIS MSRTMDISDI SEFEELATEP GHAPTSLKPL KV
//
