ID A0A0X3WZ22_9ACTN Unreviewed; 592 AA.
AC A0A0X3WZ22;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:KUL62143.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:KUL62143.1};
GN ORFNames=ADL30_06030 {ECO:0000313|EMBL:KUL62143.1};
OS Streptomyces sp. NRRL S-1521.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609100 {ECO:0000313|EMBL:KUL62143.1, ECO:0000313|Proteomes:UP000053420};
RN [1] {ECO:0000313|EMBL:KUL62143.1, ECO:0000313|Proteomes:UP000053420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-1521 {ECO:0000313|EMBL:KUL62143.1,
RC ECO:0000313|Proteomes:UP000053420};
RA Gilbert D.G.;
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:KUL62143.1}.
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DR EMBL; LLZK01000041; KUL62143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X3WZ22; -.
DR Proteomes; UP000053420; 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:KUL62143.1}; Lyase {ECO:0000313|EMBL:KUL62143.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053420};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..117
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; 64034 MW; 17A95636D34ECE19 CRC64;
MTAVRAAVEI LKREGVVNAF GVPGAAINPF YKALKEGGGI DHTLARHVEG ASHMAEGYTR
ANPGNIGVCI GTSGPAGTDM ITGLYSAIGD SIPILCITGQ APTHLLHKED FQAVDIATIA
KPVTKMAVTV LEAAQVPGIF QQAFHLMRSG RPGPVLIDLP IDVQQTEIEF DPETYEPLPV
YKPAATRAQI EKAIGFLLES ERPLIVAGGG IINADASDLL VEFAELTDTP VVPTLMGWGA
IPDDHDLNAG MVGQQTGHRY GNATFLESDF VLGVGNRWAN RHTGYKLDVY TQGRKFVHVD
IEPTQIGKIF APDYGIASDA KAALELFVEV AKELKAAGKL PDRSAWVASH LRRKETLQRR
THFDDVPMKP QRVYEEMNKA FGPETRYVTT IGLSQIAGAQ MLHVYKPRHW INCGQAGPLG
WTIPAALGVA KADPETPVVA LSGDYDFQFM IEELAVGAQH RIPYVHVLVN NAYLGLIRQA
QIGLDINFQV NLEFENQNSP ELGVYGVDHV KVAEGLGCKA IRVTEPGELG AAFEQAKKLA
VEHRVPVVVE AILERITNIS MSPTADISAV KEFEEIATEA AHAPTAIRPL KV
//
