ID A0A0M2HSE3_9MICO Unreviewed; 595 AA.
AC A0A0M2HSE3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:KJL47835.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:KJL47835.1};
GN Name=gcl {ECO:0000313|EMBL:KJL47835.1};
GN ORFNames=RS84_01463 {ECO:0000313|EMBL:KJL47835.1};
OS Microbacterium hydrocarbonoxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=273678 {ECO:0000313|EMBL:KJL47835.1, ECO:0000313|Proteomes:UP000033900};
RN [1] {ECO:0000313|EMBL:KJL47835.1, ECO:0000313|Proteomes:UP000033900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA35 {ECO:0000313|EMBL:KJL47835.1,
RC ECO:0000313|Proteomes:UP000033900};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL47835.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYJB01000008; KJL47835.1; -; Genomic_DNA.
DR RefSeq; WP_045257118.1; NZ_JYJB01000008.1.
DR AlphaFoldDB; A0A0M2HSE3; -.
DR STRING; 273678.RS84_01463; -.
DR PATRIC; fig|273678.4.peg.1461; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000033900; 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:KJL47835.1}; Lyase {ECO:0000313|EMBL:KJL47835.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033900};
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 391..556
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 595 AA; 64070 MW; F44747D70AD068E6 CRC64;
MTRMRAVDAI VQILVKEGAT EAFGLPGAAI NPLYSAMRRH GGIRHTLARH VEGASHMADG
YSRTGDGRIG ICIGTSGPAG TDMITGLYAA IADSIPMLCI TGQAPVAKLD KEDFQAVDIA
SIAKPVTKFA KTVLEAGQIP GAFQTAFQIM RSGRPGPALL DLPFDVQMTE IEFDIDTYEP
LPVAKPAATR AQADKVLDML IGAKHPAIIA GGGIVNSGAS AKLVELAETL GVPVFPTLMG
WGAIGDDHPL AGGLVGIQTS QRYGNASFLE SDFVLGIGNR WANRHTGGLD TYRKGRTFVH
VDIEPTQIGR VFAPDYSVVS DAGAFIDQLL EAARGRVAEL PDYNGWAEEC RGRKARLQRK
TNFDNVPMKP HRVYQEMLSA FGHDTTYVTT IGLSQIAGAQ LLHVYGPRQW INAGQAGPLG
WTLPAALGVV RGKPEEKVVA LSGDYDFQFM IEELAVGAQH KLPYIHVVVN NSYLGLIRQS
QRPFEMDYEV SLAFDNINTP FDENSVATGY GVDHVKVAEG LGCKAIRVER PEDLAAGFAE
AERLREEFQV PVVVEVILER VTNIAMGADL DTMNEFEDLA TTAADAPEAV YALLD
//