ID A0A087MG87_9GAMM Unreviewed; 432 AA.
AC A0A087MG87;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN ORFNames=N788_06350 {ECO:0000313|EMBL:KFL35890.1};
OS Arenimonas donghaensis DSM 18148 = HO3-R19.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Arenimonas.
OX NCBI_TaxID=1121014 {ECO:0000313|EMBL:KFL35890.1, ECO:0000313|Proteomes:UP000029085};
RN [1] {ECO:0000313|Proteomes:UP000029085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO3-R19 {ECO:0000313|Proteomes:UP000029085};
RA Chen F., Wang G.;
RT "Genome sequencing of Arenimonas donghaensis.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KFL35890.1, ECO:0000313|Proteomes:UP000029085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO3-R19 {ECO:0000313|EMBL:KFL35890.1,
RC ECO:0000313|Proteomes:UP000029085};
RX PubMed=26380644; DOI=10.1186/s40793-015-0055-4;
RA Chen F., Wang H., Cao Y., Li X., Wang G.;
RT "High quality draft genomic sequence of Arenimonas donghaensis DSM
RT 18148(T).";
RL Stand. Genomic Sci. 10:59-59(2015).
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:KFL35890.1}.
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DR EMBL; AVCJ01000043; KFL35890.1; -; Genomic_DNA.
DR RefSeq; WP_034225084.1; NZ_AVCJ01000043.1.
DR AlphaFoldDB; A0A087MG87; -.
DR STRING; 1121014.N788_06350; -.
DR PATRIC; fig|1121014.3.peg.2175; -.
DR OrthoDB; 9802794at2; -.
DR Proteomes; UP000029085; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016833; F:oxo-acid-lyase activity; IEA:UniProt.
DR GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd02170; cytidylyltransferase; 1.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR004821; Cyt_trans-like.
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 InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR NCBIfam; TIGR02320; PEP_mutase; 1.
DR PANTHER; PTHR43793; FAD SYNTHASE; 1.
DR PANTHER; PTHR43793:SF1; FAD SYNTHASE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Pyruvate {ECO:0000313|EMBL:KFL35890.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029085};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..130
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 432 AA; 48016 MW; 7290B5D159BBAD1B CRC64;
MKTVYVGMSA DLVHPGHLNI LNEASKHGEV IVGLLTDEAI ASYKRVPLME FDQRRQVIEN
LKPVSRVVPQ STLDYVPNLE MLRPDFVVHG DDWRTGVQQQ TRQRVIDKLA EWGGKLIEVP
YTKDISSTAL HAAIKEIGTT PSIRLKSLKR MLAVKPVLRF IDIHNALSAL IIENTSIETP
NGRREFDGMW GSSLTDSTSK GKPDIEAVDI SARITTINET LEVTTKPIIF DADTGGQTEH
FVYTVKTLER LGVSAAIIED KTGLKKNSLF GTDVPQTQES IENFCNKIRA GKKAQATNDF
MIIARIESLI LDKGMEDAVE RASAYLEAGA DGIMIHSRRK TPDEIFEFCR RYRDIPNRKT
LVAVPSSYNT VTEDELAAEG VNIVIYANQL LRSAYPAMLD TAKSILTHGR SAECDARMLP
IKDILDLIPG TK
//
