ID A0A0G3UQ07_9ACTN Unreviewed; 592 AA.
AC A0A0G3UQ07;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:AKL68492.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:AKL68492.1};
GN ORFNames=M444_27115 {ECO:0000313|EMBL:AKL68492.1};
OS Streptomyces sp. Mg1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL68492.1, ECO:0000313|Proteomes:UP000035653};
RN [1] {ECO:0000313|EMBL:AKL68492.1, ECO:0000313|Proteomes:UP000035653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL68492.1,
RC ECO:0000313|Proteomes:UP000035653};
RX PubMed=23908282;
RA Hoefler B.C., Konganti K., Straight P.D.;
RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT Single-Molecule Sequencing.";
RL Genome Announc. 1:e00535-13(2013).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP011664; AKL68492.1; -; Genomic_DNA.
DR RefSeq; WP_037795085.1; NZ_DS570455.1.
DR AlphaFoldDB; A0A0G3UQ07; -.
DR KEGG; strm:M444_27115; -.
DR PATRIC; fig|465541.12.peg.5728; -.
DR Proteomes; UP000035653; Chromosome.
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:AKL68492.1}; Lyase {ECO:0000313|EMBL:AKL68492.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035653};
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 191..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; 63550 MW; 68C9A353BD8E5BBC CRC64;
MTAAAAAVEI LKIEGVSQAF GVPGAAINPF YRELKNVGGI GHTLARHVEG ASHMAEGYTR
AKAGNIGVCI GTSGPAGTDM ITGLYSAIAD SIPILCITGQ APVSKLHKED FQAVDIASIA
GPVTKKATTV LEAAQVPGVF QEAFHLMRSG RPGPVLIDLP IDVQLTEIEF DPETYAPLPV
YKPRATRAQA AKALGFLLES QRPLIVAGGG IINADASDLL VEFAELVGVP VISTLMGWGT
IPDDHELAAG MVGVQTAHRY GNATFLESDF VFGIGNRWAN RHTGYNLDAY TKGRTFVHVD
IEPTQLGKIF APDFGIASDA KAALELFIEI AKELKAEGKL PDFSAWAASA QERKGSLQRR
THFDDIPLKP QRVYEEMNKA FGPETRYVTT IGLSQIAAAQ FLHVYRPRNW INCGQAGPLG
WTIPAAIGAA TAEPETPIVA LSGDYDFQFM IEELAVAAQH RVPYVHVLVN NAYLGLIRQA
QGGLGINFEV NLEFENINTP ELGVYGVDHV KVAEGLGVKA IRVTDPDKLG EAFEEAKKLA
QEFQVPVVVE AILERITNIA MSKTVDMSDV TEFEELATEP GHAPTAIRPL TV
//
