ID A0A0R0MAG7_9BURK Unreviewed; 588 AA.
AC A0A0R0MAG7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:KRH98652.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:KRH98652.1};
GN ORFNames=AO057_07225 {ECO:0000313|EMBL:KRH98652.1};
OS Curvibacter sp. PAE-UM.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Curvibacter.
OX NCBI_TaxID=1714344 {ECO:0000313|EMBL:KRH98652.1, ECO:0000313|Proteomes:UP000051912};
RN [1] {ECO:0000313|EMBL:KRH98652.1, ECO:0000313|Proteomes:UP000051912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAE-UM {ECO:0000313|EMBL:KRH98652.1,
RC ECO:0000313|Proteomes:UP000051912};
RA Ma D.;
RT "The whole genome sequence of a typical ultramicrobacteria PAE-UM from
RT river sediment.";
RL Submitted (SEP-2015) 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:KRH98652.1}.
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DR EMBL; LKCX01000032; KRH98652.1; -; Genomic_DNA.
DR RefSeq; WP_057674989.1; NZ_KQ483358.1.
DR AlphaFoldDB; A0A0R0MAG7; -.
DR STRING; 1714344.AO057_07225; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000051912; 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:KRH98652.1}; Lyase {ECO:0000313|EMBL:KRH98652.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051912};
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..556
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 588 AA; 63835 MW; AF43A3DE923951DB CRC64;
MAKMKAIEAA VWVMEKEGVT QAFGVPGAAI NPLYAAMRKQ GTISHILARH VEGASHMAEG
YTRANAGNIG VCIGTSGPAG TDMITGLYSA QADSIPILCI TGQAPRARLY KEDFQAVDIE
SISKPVTKWS VTVREPAQVP RAFQQAFHLM RSGRPGPVLI DLPFDVQMAE IEFDPETYSS
LPAYKPAATR AQVEKALTML NESAKPLLVS GGGIINADAS DLLVEFAELT GVPVIPTLMG
WGTIPDDHPL MAGMCGLQTS HRYGNATMLA SDFVLGIGNR WANRHTGSVE VYTKGRKFVH
VDIEPTQIGR VFSPDYGIVS DAKAALELFV QVAKEWKAAG KLADRKSWAA ECLERKATLH
RKTDFDNVPM KPQRVYQGMV EAFGKDVCYV STIGLSQIAG AQMLHVYKPR HWINCGQAGP
LGWTVPAALG VRAADPSRKI VALSGDYDFQ FMIEELAVGA QFKLPYIHVV VNNSYLGLIR
QAQRGFEMDY CVQLAFENIN TQGDPVAQGY GVDHVKVVEG LGCKAIRVHS PAELAPAIAQ
AEALMEQFSV PVVIEVILER VTNIAMGTEI DNIIEFEETE NRRVGAPA
//