ID A0A1G1QB38_9BACT Unreviewed; 379 AA.
AC A0A1G1QB38;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Glyoxylate carboligase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2243_04285 {ECO:0000313|EMBL:OGX51372.1};
OS Omnitrophica WOR_2 bacterium RIFOXYA2_FULL_38_17.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801873 {ECO:0000313|EMBL:OGX51372.1, ECO:0000313|Proteomes:UP000179162};
RN [1] {ECO:0000313|EMBL:OGX51372.1, ECO:0000313|Proteomes:UP000179162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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:OGX51372.1}.
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DR EMBL; MHHG01000001; OGX51372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1QB38; -.
DR Proteomes; UP000179162; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd00568; TPP_enzymes; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 3: Inferred from homology;
FT DOMAIN 28..163
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 218..364
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 379 AA; 41867 MW; 08AE44A10036C4F2 CRC64;
MKVNNFREIK LNIKPILPQK KLIQEAAKAL ASSIKNNQQI MAIVGYGTIR SHAENELLAF
LEKFHIPFTA TMDAKGVIPE NHPLCLGVYG TSGDIGANKY FDASQTVLAI GNSFAQNATF
GFKPDLFKGK KLIYINIDDH ELNKFYKADY PILSDVKPAI VALMNEISKE VKSVPVKAVQ
KDKWHDSPLD YKGAKIHPGD LVKAISRNLP ENAIVMGDAG SHMLWLNCYL SLDKHQLYQN
PGSFGPMASH VNGSIGVKCA NPNRTVVCGC GDGAYQMAGF ELMTAIQYDI PVVWVIFNNG
EFNVIKKFLL NLFGDQAFMQ FTNPDFVKYS DACKAFGARV EKLEDFDEVF KKALTCGKAA
IIDVVVESEV YPPFGLGKV
//
