ID A0A163CUA4_9NEIS Unreviewed; 581 AA.
AC A0A163CUA4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:KZE33187.1};
GN ORFNames=AVW16_09300 {ECO:0000313|EMBL:KZE33187.1};
OS Crenobacter luteus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Crenobacter.
OX NCBI_TaxID=1452487 {ECO:0000313|EMBL:KZE33187.1, ECO:0000313|Proteomes:UP000076625};
RN [1] {ECO:0000313|Proteomes:UP000076625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN10 {ECO:0000313|Proteomes:UP000076625};
RA Hong K.W.;
RT "Draft genome of Chromobacterium sp. F49.";
RL Submitted (JAN-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 -!- 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:KZE33187.1}.
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DR EMBL; LQQU01000016; KZE33187.1; -; Genomic_DNA.
DR RefSeq; WP_066611322.1; NZ_SLXG01000001.1.
DR AlphaFoldDB; A0A163CUA4; -.
DR STRING; 1452487.AVW16_09300; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000076625; 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: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:KZE33187.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076625};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..553
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 581 AA; 63217 MW; F48031961B8B37E7 CRC64;
MAKMTAVEAA VHVLLKEGVD TAFGVPGAAI NPFYSALRKV GGVSHVLARH VEGASHMAEG
YTRAKAGNVG LCIGTSGPAG TDMITGLYSA QADSIPILCI TGQAPRARLH KEDFQAVDIE
SIAKPVTKWA VTVREPAQVP RAFQQAFHLM RSGRPGPVLI DLPFDVQVAE IDFDPDTYEP
LPLHKPAATR AQVEKALSML VEADRPLIVS GGGVINADAA DLLQEFAEIV NVPVIPTLMG
WGTIPDDHPL MAGMVGLQTS HRYGNATMLA SDFVIGIGNR WANRHTGSVE TFTKGRKFVH
VDIEPTQIGR VFGPDYGIVS DAKAALQLFV EVAKEWKAAG KLKNTEGWVA ECQQRKATMH
RKSDFDNVPV KPQRVYQEMN AFFGKDVTYV TTIGLSQIAA AQFLHVYGPR HWINCGQAGP
LGWTIPAAIG VKTANPDADV VAISGDYDFQ FMIEELAVAA QFKKPYIHVL VNNAYLGLIR
QSQRMFEMDY CVQLSFENIN SPELGVYGVD HVKVAEGLGV KAIRVTNPDD IQPAFARARE
LMAEFQVPVV VEIILERVTN IAMGTEIDKV TEFEEILDLP A
//
