ID V6L0K1_STRRC Unreviewed; 592 AA.
AC V6L0K1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:EST34739.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:EST34739.1};
GN ORFNames=M878_09035 {ECO:0000313|EMBL:EST34739.1};
OS Streptomyces roseochromogenus subsp. oscitans DS 12.976.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST34739.1, ECO:0000313|Proteomes:UP000017984};
RN [1] {ECO:0000313|EMBL:EST34739.1, ECO:0000313|Proteomes:UP000017984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS 12.976 {ECO:0000313|EMBL:EST34739.1,
RC ECO:0000313|Proteomes:UP000017984};
RX PubMed=24407645;
RA Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces roseochromogenes subsp. oscitans DS
RT 12.976, Producer of the Aminocoumarin Antibiotic Clorobiocin.";
RL Genome Announc. 2:e01147-e01113(2014).
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:EST34739.1}.
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DR EMBL; AWQX01000071; EST34739.1; -; Genomic_DNA.
DR AlphaFoldDB; V6L0K1; -.
DR STRING; 1352936.M878_09035; -.
DR PATRIC; fig|1352936.5.peg.1933; -.
DR HOGENOM; CLU_013748_1_3_11; -.
DR Proteomes; UP000017984; 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: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:EST34739.1}; Lyase {ECO:0000313|EMBL:EST34739.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017984};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..325
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..550
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 592 AA; 63948 MW; 477BCF2A8EF2E91B CRC64;
MTAARAAVEI LKREGVTDAF GVPGAAINPF YKALKEGGGI NHTLARHVEG ASHMAEGYTR
TKPGNIGVCI GTSGPAGTDM ITGLYSAIGD SIPILCITGQ APTSVIHKED FQAVDIASIA
KPVTKMAVTV LEAAQVPGVF QQAFHLMRSG RPGPVLIDLP IDVQLTEIEF DPETYEPLPV
YKPAATRAQI EKAISFLLAA ERPVIVAGGG IIGADAADLL VEFAELTQTP VVPTLMGWGA
LSDDHELNAG MVGVQTSHRY GNANFLESDF VLGIGNRWAN RHTGYKLDVY RQGRKFVHVD
IEPTQIGKIF PPDYGVVSDA KAALELFVEV AKELKAAGKL PDRTAWVAST QERKATLLRR
THFDNVPMKP QRVYEEMNKA FGPDTRYVTT IGLSQIAGAQ MLHVYKPRHW INCGQAGPLG
WTIPAAIGVA KADPESPVVA LSGDYDFQFL IEELAVAAQH KIPYVHVLVN NAYLGLIRQA
QIGLDINFQV NLEFENINTP EIGVYGVDHV KVAEGLGCKA IRVTEPDQLG AAFEQAKKLA
AEYQVPVVVE AILERITNIS MSRTMDISDI SEFEELATEP GHAPTSIKPL KV
//