ID A0A0Q5PX43_9BURK Unreviewed; 568 AA.
AC A0A0Q5PX43;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN ORFNames=ASG35_01570 {ECO:0000313|EMBL:KQR89951.1};
OS Burkholderia sp. Leaf177.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR89951.1, ECO:0000313|Proteomes:UP000051826};
RN [1] {ECO:0000313|EMBL:KQR89951.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR89951.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR89951.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR89951.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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:KQR89951.1}.
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DR EMBL; LMPF01000001; KQR89951.1; -; Genomic_DNA.
DR RefSeq; WP_056352010.1; NZ_LMPF01000001.1.
DR AlphaFoldDB; A0A0Q5PX43; -.
DR OrthoDB; 9771433at2; -.
DR Proteomes; UP000051826; Unassembled WGS sequence.
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};
KW Pyruvate {ECO:0000313|EMBL:KQR89951.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051826};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 307..432
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
SQ SEQUENCE 568 AA; 61691 MW; 3BFC35DAD437442A CRC64;
MNAPYQLPAA YARSLRLREM LQSNELEFLM EAHNGLSARI VKEAGFKAIW GSGLTISAQF
GVRDNNEASW TQVVDTLEFM ADASDLPILL DGDTGYGNFN NVRRLVKKLE QRGIAGVCIE
DKQFPKTNSF LNGERQPLAE MDEFCGKIKA GKDSQSDPNF SIVARVEALI AGWGMEEALK
RAEAYRQAGA DAILIHSKLS KPDEILTFAR EWAGRGPLVI VPTKYYSTPT DVFRQAGIST
VIWANHLLRG AASTMQAIAK EIHTSQTLVN VEDRVASVNE IFRLQDAEEY STAESVYLSS
ASASRNAVVL AASRGAGLEA VTADKPKVML PIAGKPLLRR LVEAFKKEGI NDITVVGGYR
ADAIDTSGIR LVVNDKHEQT GELASLACAA KSFTADTVIS YGDLLFRSYI LRDLVESDSD
FCVVVDSSQT PQAGVTSTDF AYCSTADDRA LFGQKVWLES VTSSAGPADV ASKTPQGRWM
GLLNVRGAGR ERLVAKLEQL QQRDDFARLD MAALLNALIE AGERIEVQYV HGHWRGVNDL
DELRQAGDFA HGQAPYGSNG SAGAEAGA
//
