ID A0A0N0T0W0_9ACTN Unreviewed; 592 AA.
AC A0A0N0T0W0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:KOV66912.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:KOV66912.1};
GN ORFNames=ADK64_10640 {ECO:0000313|EMBL:KOV66912.1};
OS Streptomyces sp. MMG1121.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415544 {ECO:0000313|EMBL:KOV66912.1, ECO:0000313|Proteomes:UP000037687};
RN [1] {ECO:0000313|Proteomes:UP000037687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1121 {ECO:0000313|Proteomes:UP000037687};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-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:KOV66912.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGDV01000107; KOV66912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0T0W0; -.
DR STRING; 1415544.ADK64_10640; -.
DR PATRIC; fig|1415544.3.peg.2257; -.
DR Proteomes; UP000037687; 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:KOV66912.1}; Lyase {ECO:0000313|EMBL:KOV66912.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037687};
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; 64044 MW; 5E7B99B1112F5CD4 CRC64;
MTAARAAVEI LKLEGVTDAF GVPGAAINPF YKALKEGGGI SHTLARHVEG ASHMAEGYTR
TKPGNIGVCI GTSGPAGTDM ITGLYSAIGD SIPILCITGQ APTHVIHKED FQAVDIASIA
KPVTKMAVTV LEAAQVPGVF QQAFHLMRSG RPGPVLIDLP IDVQLTEIEF DPETYEPLPV
YKPAATRAQI EKAISFLLRS ERPVIVAGGG IIGADASELL VEFAELTQTP VIPTLMGWGT
LADDHELNAG MVGVQTSHRY GNANFLESDF VLGIGNRWAN RHTGYKLDVY REGRKFVHVD
IEPTQIGKIF PPDYGVVSDA KAALELFVEV AKELKAAGKL PDRADWVAST QERKATLLRR
THFDNVPMKP QRVYEEMNKA FGPDTRYVTT IGLSQIAGAQ MLHVYKPRHW INCGQAGPLG
WTIPAAIGVA KADPESPVVA LSGDYDFQFL IEELAVAAQH KIPYVHVLVN NAYLGLIRQA
QIGLDINFQV NLEFENVNAP ELGVYGVDHV KVAEGLGCKA IRVTEPDQLG AAFEQAKKLA
AEYQVPVVVE AILERITNIS MSRTMDISDI SEFEDLATEP GHAPTSIKPL KV
//
