ID K6X9X8_9MICO Unreviewed; 592 AA.
AC K6X9X8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:GAB95639.1};
GN Name=gcl {ECO:0000313|EMBL:GAB95639.1};
GN ORFNames=KILIM_024_00490 {ECO:0000313|EMBL:GAB95639.1};
OS Kineosphaera limosa NBRC 100340.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Kineosphaera.
OX NCBI_TaxID=1184609 {ECO:0000313|EMBL:GAB95639.1, ECO:0000313|Proteomes:UP000008366};
RN [1] {ECO:0000313|EMBL:GAB95639.1, ECO:0000313|Proteomes:UP000008366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100340 {ECO:0000313|EMBL:GAB95639.1,
RC ECO:0000313|Proteomes:UP000008366};
RA Yoshida I., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y.,
RA Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Kineosphaera limosa NBRC 100340.";
RL Submitted (AUG-2012) 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:GAB95639.1}.
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DR EMBL; BAHD01000024; GAB95639.1; -; Genomic_DNA.
DR RefSeq; WP_006592171.1; NZ_BAHD01000024.1.
DR AlphaFoldDB; K6X9X8; -.
DR STRING; 1184609.KILIM_024_00490; -.
DR eggNOG; COG3960; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000008366; 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: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:GAB95639.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008366};
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..553
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 592 AA; 63602 MW; 4995DF6E697DCF5C CRC64;
MPKMRAVDAA VLIMEKEGAT QVFGLPGAAI NPLYSAMRSH GGIKHVLARH VEAASHMAEG
YTRAAPGNIG VCTGTSGPAG TDMITGLYSA SADSIPILCI TGQAPIAKLD KEDFQAVDIA
AIAGPVSKWA VTVKEGAQVP GTFQRAFWLM REGRRGPVLI DLPLDVQLTE IDFDIDTYEP
LPVAKPAMTP AQANKVLDLL TASQRPVLVA GGGIINADAA DKLVELAELL QIPVIPTLMG
WGIIPDNHPL HAGMVGLQTS HRYGNATMLE ADFVLGIGNR WANRHTGALD VYTKGRTFVH
VDIEPTQIGR VFAPDYGVVS DAGLALDALL AQARERAQRQ EVPDYGVWVK DVAQRKATLQ
RKTHFDDIPI KPQRVYEEMN RAFDADTVYV STIGLSQIAG AQLLHVFRPR HWINCGQAGP
LGWTMPAALG VATARPDAQV VALSGDYDFQ FLIEELAVGA QFNIPYVHVL VNNSYLGLIR
QSQRGFEMDY HVQLGFDNIN SPETAGYGVD HVKVVEGLGC RAIRVTDPAD LGAALEEAKV
LAAQHRVPVV VEIILEKVTN ISMGGVGIDT VMEFEALAES GLDAPTAISV ME
//
