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
//