ID   A0A384HPK0_9ACTN        Unreviewed;       540 AA.
AC   A0A384HPK0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Phosphoenolpyruvate phosphomutase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DNK56_29020 {ECO:0000313|EMBL:PZT77252.1};
OS   Streptomyces sp. AC1-42W.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2218666 {ECO:0000313|EMBL:PZT77252.1, ECO:0000313|Proteomes:UP000249154};
RN   [1] {ECO:0000313|EMBL:PZT77252.1, ECO:0000313|Proteomes:UP000249154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AC1-42W {ECO:0000313|EMBL:PZT77252.1,
RC   ECO:0000313|Proteomes:UP000249154};
RA   De Leon M.P., Montecillo A.D., Siringan M.A.T., Kim S.-G., Rosana A.R.R.;
RT   "Near complete genome sequences of Streptomyces sp. strains AC1-42W
RT   isolated from bat guano of Cabalyorisa Cave, Pangasinan, Philippines.";
RL   Submitted (JUN-2018) 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:PZT77252.1}.
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DR   EMBL; QKWY01000002; PZT77252.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A384HPK0; -.
DR   Proteomes; UP000249154; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42905:SF7; PHOSPHOENOLPYRUVATE PHOSPHOMUTASE-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000249154}.
SQ   SEQUENCE   540 AA;  56655 MW;  CFFC956C9D4660B4 CRC64;
     MRAENIPART PGHRLGGAAQ LRALFERPGP ARIVGAHNAL GARLAERAGF DGVWSSGLEV
     SASHALPDAD ILTMTELLEV ARSMAAAVAV PVVADCDAGY GNANNVMHMI RRYEAVGVAA
     VSIEDKRFPK MNSFIPGRQE LAPVTEFAGK IAAAKSAQSG PDLMVIARIE ALVAGWGLDE
     ALRRAEAYAE AGADAVLIHA KGESAEPVLE FLAQWQQRLP VVVVPTTYHT ITAEELSEAG
     AKLVIYANHG LRASITAVSE TFEAILRDGR TSGIETRIAP LATVFDLQGM AALQQAEERF
     LSRAGRRLRA VLTTGSDLPG GSDVDGRSIT ELQCGSLRRA GIDNITVVTS RDGTAGHPAG
     VTVVHTPGLE APAIAEVVLS AAPDFHGHTL VAAPDLLFDP EPLLQLVAEE RDIAVLIDVS
     AASGDPGDSR TSVTTAAGAV QGRRLKGTRG NSVTGFGSGP RDGEFTGIAA FSDKGWAALR
     EAAEKRLAEA GEEPGLAVLL SDLIDAGWTV DAVEIASGWA ELRNQEDVRR AELLLTGQTR
//