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
//