ID A0A0C1U563_9CLOT Unreviewed; 432 AA.
AC A0A0C1U563;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:KIE46853.1};
GN ORFNames=U732_1481 {ECO:0000313|EMBL:KIE46853.1};
OS Clostridium argentinense CDC 2741.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE46853.1, ECO:0000313|Proteomes:UP000031366};
RN [1] {ECO:0000313|EMBL:KIE46853.1, ECO:0000313|Proteomes:UP000031366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE46853.1,
RC ECO:0000313|Proteomes:UP000031366};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
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:KIE46853.1}.
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DR EMBL; AYSO01000015; KIE46853.1; -; Genomic_DNA.
DR RefSeq; WP_039632505.1; NZ_AYSO01000015.1.
DR AlphaFoldDB; A0A0C1U563; -.
DR STRING; 29341.RSJ17_12820; -.
DR OrthoDB; 9802794at2; -.
DR Proteomes; UP000031366; Unassembled WGS sequence.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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, ECO:0000313|EMBL:KIE46853.1};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Pyruvate {ECO:0000313|EMBL:KIE46853.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031366};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..99
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 432 AA; 48567 MW; 45F88D9C50C5C694 CRC64;
MKEVYLAISA DIIHNGHINI IKKASELGEV IVGVLTDEVI ASYKRFPILN YEQRKNIVEN
IKGVKCVIPQ KTLDYTENLL LLKPHYVVHG DDWENGVQSS IRKKVIEVLK HWNGELVEFK
YTSGVSITQI DNILNEIGTT PQVRMARLRR LLKMKPLVRV LEAHSGLTGL IAEKTKLEYD
GKTKEFDAMW ISSLCDSTSK GKPDIELVDF TSRLNTINEI LEVTTKPVIL DGDTGGQVEH
FVYTVKSLER LGVSAIIIED KIGLKKNSLF GTEVKQEQDS IENFSNKILL GKNAQVTKEF
MIIARIESLI LGKGLEDAIT RAKAYIDAGA DGIMIHSKEK TAKEIFEFCD LYNRLEARVP
LIVVPTSYCY ITEEELQEKG VNVVIYANHL IRSAYPAMMN TAKSILENGR AYECNENCMS
IKEILNLIPG GH
//
