ID   F0QAJ3_PARA1            Unreviewed;       316 AA.
AC   F0QAJ3;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   OrderedLocusNames=Acav_2122 {ECO:0000313|EMBL:ADX46034.1};
OS   Paracidovorax avenae (strain ATCC 19860 / DSM 7227 / CCUG 15838 / JCM 20985
OS   / LMG 2117 / NCPPB 1011) (Acidovorax avenae).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=643561 {ECO:0000313|EMBL:ADX46034.1, ECO:0000313|Proteomes:UP000002482};
RN   [1] {ECO:0000313|Proteomes:UP000002482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19860 / DSM 7227 / CCUG 15838 / JCM 20985 / LMG 2117 /
RC   NCPPB 1011 {ECO:0000313|Proteomes:UP000002482};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Gordon S., Woyke T.;
RT   "Complete sequence of Acidovorax avenae subsp. avenae ATCC 19860.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC       mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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DR   EMBL; CP002521; ADX46034.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0QAJ3; -.
DR   KEGG; aaa:Acav_2122; -.
DR   HOGENOM; CLU_027389_0_0_4; -.
DR   OrthoDB; 9771433at2; -.
DR   Proteomes; UP000002482; Chromosome.
DR   GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR012698; PEnolPyrv_PMutase_core.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   NCBIfam; TIGR02320; PEP_mutase; 1.
DR   PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42905:SF7; PHOSPHOENOLPYRUVATE PHOSPHOMUTASE-RELATED; 1.
DR   Pfam; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ADX46034.1};
KW   Pyruvate {ECO:0000313|EMBL:ADX46034.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002482}.
SQ   SEQUENCE   316 AA;  34939 MW;  603F5374BE1F03ED CRC64;
     MTLTIERNAL QRRDEVLASK LRALISGPQT GFLMEAHNGL SARIVAEAGF KGIWASGLSI
     SASLGVRDAN EASWTQTLEV VEFMTDSTDL PVLLDGDTGY GNFNSVRRLV RKLCQRNVAG
     VCLEDKIFPK TNSFIGESQE LADPDEFAGK IKAAKDSQLN DAFCIVARVE ALIAGRGLTE
     ALKRAEKYHA AGADAILIHS KKSDAAEILQ FAEHWQDRGP LIIVPTMYYA VPTERFIDAK
     IAAIIWANHN LRASVASMRR VCETIYRERS LKDIENDLPR VKEIFDLVEQ DELTQAEHRY
     LPRGNALDPV STGALQ
//