ID A0A0Q8NM26_9ACTN Unreviewed; 590 AA.
AC A0A0Q8NM26;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:KRB62450.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:KRB62450.1};
GN ORFNames=ASE03_07625 {ECO:0000313|EMBL:KRB62450.1};
OS Kitasatospora sp. Root187.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1736486 {ECO:0000313|EMBL:KRB62450.1, ECO:0000313|Proteomes:UP000051829};
RN [1] {ECO:0000313|EMBL:KRB62450.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB62450.1,
RC ECO:0000313|Proteomes:UP000051829};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB62450.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB62450.1,
RC ECO:0000313|Proteomes:UP000051829};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRB62450.1}.
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DR EMBL; LMHX01000045; KRB62450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8NM26; -.
DR STRING; 1736486.ASE03_07625; -.
DR Proteomes; UP000051829; 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:KRB62450.1}; Lyase {ECO:0000313|EMBL:KRB62450.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051829};
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..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..549
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 590 AA; 63570 MW; 782CBB57C1E8AAD4 CRC64;
MTAARAAVEI LKREGVDVAF GVPGAAINPF YKALKEGGGI SHTLARHVEG ASHMAEGYTR
AKAGNIGVCI GTSGPAGTDM ITGLYSAIAD SIPILCITGQ APVAKLHKED FQAVDIASIA
KPVTKAATTV LEAAQVPGVF QQAFHLMRSG RPGPVLIDLP IDVQLTEIEF DPETYAPLPV
YKPAATRAQI EKAIGFLLES ERPLIVAGGG IINADATELL VEFAELTGTP VIPTLMGWGI
IADDHELNAG MVGLQTSHRY GNANFLESDF VLGIGNRWAN RHTGDLAVYT KDRKFVHVDI
EPTQLGRIFA PDFGIASDAK AALELFVEVA KELKAAGKLP DRSEWAASTQ ERKATLLRRT
HFDNVPLKPQ RVYEEMNKAF GPETRYVTTI GLSQIAGAQM LHVYKPRHWI NCGQAGPLGW
TIPAALGVAT ADPETPVVAL SGDYDFQFML EELAVGAQHR IPYVHVLVNN AYLGLIRQAQ
RNLDINFQVN LEFENINSPE LGVYGVDHVK VVEGLGCKAI RVTEPDQLLP AFEQAKKLAA
EFRVPVVVEA ILERVTNISM GGAGIDAINE WEDLATEPGH APTAIKTLKV
//
