GenomeNet

Database: UniProt
Entry: E8TLG6_MESCW
LinkDB: E8TLG6_MESCW
Original site: E8TLG6_MESCW 
ID   E8TLG6_MESCW            Unreviewed;       593 AA.
AC   E8TLG6;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:ADV12717.1};
GN   OrderedLocusNames=Mesci_3597 {ECO:0000313|EMBL:ADV12717.1};
OS   Mesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838 /
OS   WSM1271).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV12717.1, ECO:0000313|Proteomes:UP000007471};
RN   [1] {ECO:0000313|Proteomes:UP000007471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 2942 / LMG 23838 / WSM1271
RC   {ECO:0000313|Proteomes:UP000007471};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Nandasena K., Reeve W.G., Howieson J.G., O'Hara G.,
RA   Tiwari R.P., Woyke T.;
RT   "Complete sequence of chromosome of Mesorhizobium ciceri bv. biserrulae
RT   WSM1271.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002447; ADV12717.1; -; Genomic_DNA.
DR   RefSeq; WP_013531397.1; NC_014923.1.
DR   RefSeq; YP_004142767.1; NC_014923.1.
DR   AlphaFoldDB; E8TLG6; -.
DR   STRING; 765698.Mesci_3597; -.
DR   KEGG; mci:Mesci_3597; -.
DR   PATRIC; fig|765698.3.peg.4102; -.
DR   eggNOG; COG3960; Bacteria.
DR   HOGENOM; CLU_013748_1_2_5; -.
DR   OMA; TLMGWGA; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000007471; Chromosome.
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:ADV12717.1};
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..554
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   593 AA;  64580 MW;  CC5829CAA6DF9073 CRC64;
     MARMRAVDAA VLVLEKEGIS CAFGVPGAAI NPFYSALKAR GTIRHVLARH VEGASHMAEG
     FTRAKAGNIG LCIGTSGPAG TDMITGLYSA AADSIPILCI TGQAPRARLN KEDFQAVDIS
     AIAAPVAKWA VTVMEPYLVP MALQKAFHLM RSSRPGPVLI DLPVDVQLAE IEFDIDAYEP
     LTPFKPAMTR AQAEKALTML NAAEKPLIVA GGGIINADAS DLLIEFAEIS GVPVVPTLMG
     WGAIPDDHRL MAGMCGLQTS HRYGNATMLE ADFVFGIGNR WANRHTGSVD VYTKGKKFIH
     VDIEPTQIGR VFAPDLGVVS DAGAALKMLL DVATEWKTAG RLRDWSGWAR ECQARKKTMK
     RKTHFDQVPL KPQRVYEEMN KAFGRDVTYV TTIGLSQIAG AQFLHVYKPR NWINCGQAGP
     LGWTLPAALG VRAADPDRTI VALSGDYDFQ FMIEELAVGA QHKLPYLHVV VNNAYLGLIR
     QAQRGFSMDF EVDLAFENIN RAGDPEAGYG VDHVAVAEAM GCKAVRVRKP EEFAGAFKEA
     QRLMKEHRIP VVLEFILERV TNISMGTEID KITEFEELAE SHEDAPTSIV MLD
//
DBGET integrated database retrieval system