ID A0A1B2HYZ3_9PSEU Unreviewed; 559 AA.
AC A0A1B2HYZ3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:ANZ42926.1};
GN ORFNames=BBK82_21915 {ECO:0000313|EMBL:ANZ42926.1};
OS Lentzea guizhouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=1586287 {ECO:0000313|EMBL:ANZ42926.1, ECO:0000313|Proteomes:UP000093053};
RN [1] {ECO:0000313|EMBL:ANZ42926.1, ECO:0000313|Proteomes:UP000093053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHS C013 {ECO:0000313|EMBL:ANZ42926.1,
RC ECO:0000313|Proteomes:UP000093053};
RA Cao C.;
RT "Complete genome sequence of the Lentzea guizhouensis DHS C013.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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; CP016793; ANZ42926.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B2HYZ3; -.
DR STRING; 1586287.BBK82_21915; -.
DR KEGG; led:BBK82_21915; -.
DR Proteomes; UP000093053; 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: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:ANZ42926.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000093053};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 2..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 186..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 381..535
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 559 AA; 61048 MW; A6E2471996243B8D CRC64;
MQAVVEVLKS EGIDTVFGCP GAAILPLYKA MEQDGSIEHL IVRHEEGATH MADGWSRTTG
NVGVAIGTSG PAGTNMITGL YTAQADSVPI LCITGQAAVS KLHQEAFQAV DIVSIAAPVT
KWAVQVREAA QMPWIFREAF RIARSGRPGP VLIDLPIDVQ KQEIEWDPTI DEPLPVAKSA
PSDARVERAL EMLLAAERPL LLAGGGVILG EAAAELLDLA ELLQIPVQAT LMGKGAVDED
HPLYAGMTGI QTSQRYGNAS FLESDLVLAL GARFGDRHTG DLATYRGDRK FIHVDVEPTQ
IGKVFGPDLG IVADTKLFLR ALLEKARAHA RPAGAWVERC QELKRTLLRR EDFDTVPVKA
PRVFKEINEF YGPDTYFVTA IGLYQIWSGQ HQKAHKPRHY QVCGQAGPLG WEIPAAIGVK
KARPDAEVVG IVGDYSFQFL VEELAVGAQY DVPFVLIMLN NEYLGLIRMA EDHGGYDMKY
EVDIHYDTTG SDNVKIMEAY GCSGIRVADP GEIRSSLEWA RKEADRTQRP VLVEVMIERE
GNTANGTSIA AMKEYEPIP
//
