ID A0A1I9YMH8_9BURK Unreviewed; 581 AA.
AC A0A1I9YMH8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN Name=aepX {ECO:0000313|EMBL:APA87511.1};
GN ORFNames=BJG93_18660 {ECO:0000313|EMBL:APA87511.1};
OS Paraburkholderia sprentiae WSM5005.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=754502 {ECO:0000313|EMBL:APA87511.1, ECO:0000313|Proteomes:UP000179860};
RN [1] {ECO:0000313|EMBL:APA87511.1, ECO:0000313|Proteomes:UP000179860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM5005 {ECO:0000313|EMBL:APA87511.1,
RC ECO:0000313|Proteomes:UP000179860};
RA De Meyer S., Wang P., Terpolilli J.;
RT "The Complete Genome of Burkholderia sprentiae wsm5005.";
RL Submitted (SEP-2016) 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; CP017562; APA87511.1; -; Genomic_DNA.
DR RefSeq; WP_027194158.1; NZ_KI421529.1.
DR AlphaFoldDB; A0A1I9YMH8; -.
DR STRING; 754502.BJG93_18660; -.
DR KEGG; pspw:BJG93_18660; -.
DR OrthoDB; 9771433at2; -.
DR Proteomes; UP000179860; Chromosome 2.
DR GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd00377; ICL_PEPM; 1.
DR CDD; cd02523; PC_cytidylyltransferase; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
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; PF12804; NTP_transf_3; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:APA87511.1};
KW Pyruvate {ECO:0000313|EMBL:APA87511.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 307..422
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
SQ SEQUENCE 581 AA; 62878 MW; A34C5C5BC883703A CRC64;
MNAREPAFVS QSRSARLRQM LVSSELEFMM EAHNGLSARI VREAGFKAIW GSGLAISAQF
GVRDNNEASW TQVVDTLEFM ADASDLPILL DGDTGYGNFN NVRRLVRKLE QRGIAGVCIE
DKQFPKTNSF INGEAQPLAD IDEFCGKIKA GKDSQNDEHF SIVARVEALI AGWGMDEALR
RAEAYAQAGA DAILIHSKLS RPDEILEFAR EWAGRAPLVI VPTKYYSTPT EVFREAGIST
VIWANHLIRA ATSAMQAVAK EIHASETLVN VDDSVATVNE IFRLQDADEY SEAEDRYLSS
GRAAGSAVVL AASRGKGLEA LTGDRPKVML PLAGKPLLRW LVDAFKKQGV NDITVVGGYR
ADAIDTAGIR LVVNEQYAQA GELASLACAL DPGAPPKQSG DTVISYGDLL FRSYILRDLV
ESEAAFSVVV DSSLTDAENA SVRDFAWCSA ADDRGLFGNK IVLRHVASGR EQSSAASAAE
PPHGRWVGLL NVRGAGRERL RAVMRELQTR DDFASLDMPA LLNALIEAGE SIEVQYVHGH
WRGVNDLDDF RRAGDFAHTQ APFATAVGGG STTNDAHGGP Q
//