ID A0A176L6K6_9ACTN Unreviewed; 592 AA.
AC A0A176L6K6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:OAB00146.1};
GN ORFNames=A6P39_13945 {ECO:0000313|EMBL:OAB00146.1};
OS Streptomyces sp. FXJ1.172.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAB00146.1};
RN [1] {ECO:0000313|EMBL:OAB00146.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAB00146.1};
RA Liu M., Liu N., Shang F., Huang Y.;
RT "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT from red soil-derived Streptomyces sp. FXJ1.172.";
RL Submitted (APR-2016) 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:OAB00146.1}.
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DR EMBL; LWRP01000070; OAB00146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176L6K6; -.
DR STRING; 710705.A6P39_13945; -.
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:OAB00146.1};
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; 63967 MW; BED479491C464BB1 CRC64;
MTAARAAVEI LKREGVTDAF GVPGAAINPF YKALKEGGGI NHTLARHVEG ASHMAEGYTR
TKPGNIGVCI GTSGPAGTDM ITGLYSAIGD SVPILCITGQ APTHVIHKED FQAVDIASIA
KPVTKMAVTV LEAAQVPGVF QQAFHLMRSG RPGPVLIDLP IDVQLTEIEF DPETYEPLPV
YKPAATRAQI EKAISFLLDS ERPVIVAGGG IIGADAAGLL VEFAELTQTP VIPTLMGWGA
LPDDHELNAG MVGVQTSHRY GNANFLESDF VLGIGNRWAN RHTGYKLDVY RGERKFVHVD
IEPTQIGKIF PPDYGVVSDA KAALELFIEV AKELKAAGKL PDRAGWVAST QERKATLLRR
THFDNVPMKP QRVYEEMNKA FGPDTRYVTT IGLSQIAGAQ MLHVYKPRHW INCGQAGPLG
WTIPAAIGVA KADPDAPVVA LSGDYDFQFL IEELAVAAQH RIPYVHVLVN NAYLGLIRQA
QIGLDINFQV NLEFENINTP EIGVYGVDHV KVAEGLGCKA IRVTEPEQLG AAFEQAKKLA
AEHRVPVVVE AILERITNIS MSRTMDISDI SEFEDLATEP GHAPTSVKPL KV
//
