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Database: UniProt
Entry: A0A328VFR4_9CHLR
LinkDB: A0A328VFR4_9CHLR
Original site: A0A328VFR4_9CHLR 
ID   A0A328VFR4_9CHLR        Unreviewed;       300 AA.
AC   A0A328VFR4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=Carboxyvinyl-carboxyphosphonate phosphorylmutase {ECO:0000313|EMBL:RAQ95671.1};
GN   ORFNames=A4R35_09010 {ECO:0000313|EMBL:RAQ95671.1};
OS   Thermogemmatispora tikiterensis.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Thermogemmatisporales;
OC   Thermogemmatisporaceae; Thermogemmatispora.
OX   NCBI_TaxID=1825093 {ECO:0000313|EMBL:RAQ95671.1, ECO:0000313|Proteomes:UP000248706};
RN   [1] {ECO:0000313|EMBL:RAQ95671.1, ECO:0000313|Proteomes:UP000248706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T81 {ECO:0000313|EMBL:RAQ95671.1,
RC   ECO:0000313|Proteomes:UP000248706};
RA   Tomazini A., Lal S., Stott M., Henrissat B., Polikarpov I., Sparling R.,
RA   Levin D.B.;
RT   "Analysis of Carbohydrate Active Enzymes in Thermogemmatispora T81 Reveals
RT   Carbohydrate Degradation Ability.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:RAQ95671.1}.
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DR   EMBL; MCIF01000002; RAQ95671.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A328VFR4; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000248706; Unassembled WGS sequence.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:UniProt.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR42905:SF5; CARBOXYVINYL-CARBOXYPHOSPHONATE PHOSPHORYLMUTASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000248706}.
SQ   SEQUENCE   300 AA;  32777 MW;  C26203898DB91D12 CRC64;
     MRVTTRLRQL LAGPELVVAP GAYDALSARL IAQAGFSVVY MTGFGTSASV LGMPDVGLLT
     MSEMVSRAAA LAAVTGEVPL IADADTGYGN PLNVRRTVRE YERAGVAGLH LEDQVWPKKC
     GHMEGKQVIP MEEMVQKVRA AVEARQDPDF VIIARTDAAA VLGFEEALRR GRAYREAGAD
     VIFIEAPRTM EELRAIVQAF PDVPLLFNWA QSGKTPPLSV NEIRELGFKL VLFPVALLFT
     ATHAMLRLLE GLKRGETPTA FAEQSVSFQQ FTELVGLPFI QELEARYGVR QEATPQPHQS
//
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