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Database: UniProt
Entry: A0A0M2HSE3_9MICO
LinkDB: A0A0M2HSE3_9MICO
Original site: A0A0M2HSE3_9MICO 
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}.
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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
//
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