ID H5Y809_9BRAD Unreviewed; 596 AA.
AC H5Y809;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:EHR02333.1};
GN ORFNames=Bra471DRAFT_03086 {ECO:0000313|EMBL:EHR02333.1};
OS Bradyrhizobium sp. WSM471.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR02333.1};
RN [1] {ECO:0000313|EMBL:EHR02333.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM471 {ECO:0000313|EMBL:EHR02333.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA Howieson J., Reeve W., Woyke T.;
RT "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL Submitted (NOV-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; CM001442; EHR02333.1; -; Genomic_DNA.
DR RefSeq; WP_007608373.1; NZ_CM001442.1.
DR AlphaFoldDB; H5Y809; -.
DR HOGENOM; CLU_013748_1_2_5; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000005774; 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:EHR02333.1};
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 193..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..552
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 596 AA; 65231 MW; 0400BA7F5BE8C01B CRC64;
MAKMRAIDAA VRILEKEGIS TAFGVPGAAI NPLYSALKKR GSIRHILARH VEGASHMAEG
YTRAKAGNIG VCIGTSGPAG TDMITGLYSA IADSIPILCI TGQAPRARLY KEDFQAVDIE
SIAKPVTKWA VTVREPALVP RVFSQAFHVM RSGRPGPVLI DMPLDVQLAE IEFDDETYEP
LPVYRPTASR KQVEKALEML NAAERPLIVA GGGVINADAS DLLVEFAEIA NVPVVPTLMG
WGAIPDDHVL MAGMVGLQTS HRYGNATMLE SDFVLGIGNR WANRHTGSVE TYTKGRTFVH
VDIEPTQIGR VFNPDLGIVS DAKAALELFV TVAREWRRSG RLRERQAWPA SCRDRKRTML
RKSHFDNVPI KPQRVYEEMT KAFGRDTCYV SVIGLSQIAG AQFLGVYKPR NWINAGQAGP
LGWTLPAALG VRAACPDRDI VALSGDYDFQ FLIEELAVGA QFNLPYIHVV VNNSYLGLIR
QAQRGFDMDY HVQLSFENIN APELGGYGVD HVAVAEGLGC KAIRVTDPKD SQAAFATARE
WMAKYRVPVV VEFILERVTN IAMGTEIDNI VEFEEVLDLP LDEVATARPG VLQPAE
//
