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Database: UniProt/TrEMBL
Entry: A0A0P0RJ92_9BURK
LinkDB: A0A0P0RJ92_9BURK
Original site: A0A0P0RJ92_9BURK 
ID   A0A0P0RJ92_9BURK        Unreviewed;       569 AA.
AC   A0A0P0RJ92;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   ORFNames=K788_0000151 {ECO:0000313|EMBL:ALL68839.1};
OS   Paraburkholderia caribensis MBA4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1323664 {ECO:0000313|EMBL:ALL68839.1, ECO:0000313|Proteomes:UP000019146};
RN   [1] {ECO:0000313|EMBL:ALL68839.1, ECO:0000313|Proteomes:UP000019146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBA4 {ECO:0000313|EMBL:ALL68839.1,
RC   ECO:0000313|Proteomes:UP000019146};
RX   PubMed=24558235;
RA   Pan Y., Kong K.F., Tsang J.S.;
RT   "Draft Genome Sequence of the Haloacid-Degrading Burkholderia caribensis
RT   Strain MBA4.";
RL   Genome Announc. 2:e00047-e00014(2014).
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC       mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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DR   EMBL; CP012747; ALL68839.1; -; Genomic_DNA.
DR   RefSeq; WP_035997383.1; NZ_CP012747.1.
DR   AlphaFoldDB; A0A0P0RJ92; -.
DR   GeneID; 69972494; -.
DR   KEGG; bcai:K788_0000151; -.
DR   Proteomes; UP000019146; 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:ALL68839.1};
KW   Pyruvate {ECO:0000313|EMBL:ALL68839.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          308..417
FT                   /note="MobA-like NTP transferase"
FT                   /evidence="ECO:0000259|Pfam:PF12804"
SQ   SEQUENCE   569 AA;  62175 MW;  0819BF985A5D37C6 CRC64;
     MNAREPSFVS TLSRSARLRQ MLTSNELEFL MEAHNGISAR IAREAGFKGI WGSGLAISAQ
     YGVRDNNEAS WTQVVDTLEF MADASDLPIL LDGDTGYGNF NNVRRLVRKL EQRGIAGVCI
     EDKVFPKTNS FIKGEAQPLA DIDEFCGKIK AGKDSQTDEH FSIVARVEAL IAGWGMDEAL
     KRAEAYRQAG ADAILIHSKL SRPDEILEFA REWAGRGPLV IVPTKYYSTP TEVFRKAGIS
     TVIWANHQIR AATSAMQAVV KEIYESQTLV NVEDRIATVN EIFRLQDADE YSVAEERYLS
     SSRVASSAVV LAASRGKGLE AVTTDRPKVM LPIAGKPLLR WLVDAFKKQG VNDITVVGGY
     RADAIDTAGI KLVVNERHEQ TGELASLACA VDGLQNDAVI SYGDLLFRSY IVRDLVDSEA
     LFSVVVDSTT VAEAGATNQS VRDFAWCSAA DDRGLFGNKV LLRRVANNEA DVKGEVPNGR
     WIGLLNVRGA GRERLQAVMN TLRARPDFDS LDMPALLNAL IEAGEEIEVQ YVHGHWRGVN
     DLEDFRRAGD FAHEATPLAK GDAAGGAAQ
//
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