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Database: UniProt
Entry: N6XIT2_9RHOO
LinkDB: N6XIT2_9RHOO
Original site: N6XIT2_9RHOO 
ID   N6XIT2_9RHOO            Unreviewed;       591 AA.
AC   N6XIT2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:ENO81611.1};
DE            EC=4.1.1.47 {ECO:0000313|EMBL:ENO81611.1};
GN   ORFNames=B447_06977 {ECO:0000313|EMBL:ENO81611.1};
OS   Thauera sp. 27.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=305700 {ECO:0000313|EMBL:ENO81611.1, ECO:0000313|Proteomes:UP000013140};
RN   [1] {ECO:0000313|EMBL:ENO81611.1, ECO:0000313|Proteomes:UP000013140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=27 {ECO:0000313|EMBL:ENO81611.1,
RC   ECO:0000313|Proteomes:UP000013140};
RA   Liu B., Shapleigh J.P., Frostegard A.H.;
RT   "Draft Genome Sequences of 6 Strains from Genus Thauera.";
RL   Submitted (SEP-2012) 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:ENO81611.1}.
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DR   EMBL; AMXB01000010; ENO81611.1; -; Genomic_DNA.
DR   RefSeq; WP_002924363.1; NZ_AMXB01000010.1.
DR   AlphaFoldDB; N6XIT2; -.
DR   eggNOG; COG3960; Bacteria.
DR   Proteomes; UP000013140; 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:ENO81611.1}; Lyase {ECO:0000313|EMBL:ENO81611.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013140};
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          194..329
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   591 AA;  64301 MW;  CA6BC57CDD9180C3 CRC64;
     MARMRAVDAA AAVMRKEGVS TVFGVPGAAI NPLYSAMKKN GGFQHILGRH VEGASHMAEG
     YTRANPGNIG VCIGTSGPAG TDMITGLYSA SADSIPILCI TGQAPRARLY KEDFQAVDIE
     SIAKPVTKWA VTVREPALVP RVFQQAFHIM RSGRPGPVLI DLPFDVQMAE IEFDIDTYEP
     LPAYKPAATR AQAEKAMAML NAAARPLIVA GGGVINANAA DKLQAFAELT GVPVIPTLMG
     WGTIPDDHPL MAGMVGLQTA HRYGNATMLA SDFVFGIGNR WANRHTGSVE VYTEGRKFVH
     VDIEPTQIGR VFGPDYGIVS DAGAALDRLI EVAREMKAAG QLPDRSAWTA ECQQRKRTMQ
     RKTHFDNTPM KPQRVYEEMN RVFGQDTCYV STIGLSQIAA AQFLHVYKPR NWINCGQAGP
     LGWTIPAALG VCAADPQRKV VAISGDYDFQ FMIEELAVGA QFKLPYIHVL VNNAYLGLIR
     QSQRGFDMDY CVQLAFENIN APETEGYGVD HVGVVEGLGC KAIRVRTPEE IQPAFAKAQQ
     WMETYRVPVV VEIILERVTN ISMGTEINAI NEFEELAEKG ADAPTAISML D
//
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