ID A0A0W7X0U9_9ACTN Unreviewed; 592 AA.
AC A0A0W7X0U9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:KUF16450.1};
GN ORFNames=AT728_11640 {ECO:0000313|EMBL:KUF16450.1};
OS Streptomyces silvensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1765722 {ECO:0000313|EMBL:KUF16450.1, ECO:0000313|Proteomes:UP000054804};
RN [1] {ECO:0000313|EMBL:KUF16450.1, ECO:0000313|Proteomes:UP000054804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53525 {ECO:0000313|EMBL:KUF16450.1,
RC ECO:0000313|Proteomes:UP000054804};
RA Johnston C.W., Li Y., Magarvey N.A.;
RT "Draft genome sequence of Streptomyces silvensis ATCC 53525, a producer of
RT novel hormone antagonists.";
RL Submitted (DEC-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:KUF16450.1}.
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DR EMBL; LOCL01000038; KUF16450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W7X0U9; -.
DR STRING; 1765722.AT728_11640; -.
DR Proteomes; UP000054804; 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:KUF16450.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054804};
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; 64132 MW; EFE18127C925BBF6 CRC64;
MTAARAAVEI LKREGVTDAF GVPGAAINPF YKALKEGGSI AHTLARHVEG ASHMAEGYTR
TEAGNIGVCI GTSGPAGTDM ITGLYSAIGD SIPILCITGQ APTHVIHKED FQAVDIAAIA
KPVTKMAVTV LEAAQVPGVF QQAFHLMRSG RPGPVLIDLP IDVQLTEIEF DPETYQPLPV
YKPAASRAQV EKAVGMLIES ERPLIVAGGG IINADACELL VEFAELTGTP VVPTLMGWGI
LPDDHELNAG MVGLQTSHRY GNATFLESDF VLGIGNRWAN RHTGYKLDVY REGRTFVHVD
VEPTQIGKIF APDYGIASDA KAALELFVEV ARELKAAGRL PDRGAWIARG QEHRSTLLRR
THFDDIPIKP QRVYEEMNKA FGPETRYVST IGLSQIAGAQ MLHVYKPRHW INCGQAGPLG
WTVPAALGVA TADPDAQVVA LSGDYDFQFM IEELAVGAQH RIPYVHVLVN NSYLGLIRQA
QLGLDIDFQV NLEFENINSP ELGVYGVDHV KVAEGLGCKA IRVTDPNELG AAFEQAKKLA
QEYRVPVVVE AILERVTNIS MSRTADISDV TEFEEIATEP WHAPSSIKTL KV
//
