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}.
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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
//