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Database: UniProt
Entry: A0A285QMC0_9ACTN
LinkDB: A0A285QMC0_9ACTN
Original site: A0A285QMC0_9ACTN 
ID   A0A285QMC0_9ACTN        Unreviewed;       405 AA.
AC   A0A285QMC0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=PEP-utilising enzyme, mobile domain {ECO:0000313|EMBL:SOB83100.1};
GN   ORFNames=SAMN06272789_3298 {ECO:0000313|EMBL:SOB83100.1};
OS   Streptomyces sp. 1331.2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1938835 {ECO:0000313|EMBL:SOB83100.1, ECO:0000313|Proteomes:UP000219030};
RN   [1] {ECO:0000313|Proteomes:UP000219030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1331.2 {ECO:0000313|Proteomes:UP000219030};
RA   Varghese N., Submissions S.;
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837}.
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DR   EMBL; OBMJ01000001; SOB83100.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285QMC0; -.
DR   Proteomes; UP000219030; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR000121; PEP_util_C.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR   PANTHER; PTHR46244:SF3; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219030};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          30..98
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          196..372
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
SQ   SEQUENCE   405 AA;  42836 MW;  2F1D2625C1C16C37 CRC64;
     MNGRRIQGSL LTGGNRTTLR ATCNRTRHPQ AGSILIAPNL EAGLYDAIVA ASAVVCGEGG
     QTGHMQSLCR GRGIPVLLVD EADLAALDGE VTLDLENGSI LLGPDPAAGP VPPPGPVTPT
     VQDLGAACAV IADFQDIRTV NSCGPNAMCV DSFFIREEFL CLAAGLSPLD ALDGGPEETA
     RYGRAIAERL CAFVEELLPG QRLVLRLLDL RSDHAASVTE QAPVAVEPNP ELGLHGARWL
     LGSAAYRDAL HIMLGELRSR LGDQAQRIHL SVPFLNDADE YAQLRSHLEL PSDVSLSAFI
     ETPAAVHATP QICAAGASEL FVGVKDLVQF YLAADRGNHL VADSYQTRHP AVLDGVHRVV
     EAARAAGTPV RVFSLGADLT HYLARLATPD GYMMCTAELA QVLQS
//
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