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Database: UniProt
Entry: A0A0F0HS86_9PSEU
LinkDB: A0A0F0HS86_9PSEU
Original site: A0A0F0HS86_9PSEU 
ID   A0A0F0HS86_9PSEU        Unreviewed;       407 AA.
AC   A0A0F0HS86;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=PEP-utilizing protein {ECO:0000313|EMBL:KJK58389.1};
GN   ORFNames=UK12_10760 {ECO:0000313|EMBL:KJK58389.1};
OS   Saccharothrix sp. ST-888.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK58389.1, ECO:0000313|Proteomes:UP000033409};
RN   [1] {ECO:0000313|EMBL:KJK58389.1, ECO:0000313|Proteomes:UP000033409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST-888 {ECO:0000313|EMBL:KJK58389.1,
RC   ECO:0000313|Proteomes:UP000033409};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) 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}.
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:KJK58389.1}.
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DR   EMBL; JYJF01000022; KJK58389.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0HS86; -.
DR   PATRIC; fig|1427391.3.peg.3097; -.
DR   OrthoDB; 3653914at2; -.
DR   Proteomes; UP000033409; 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:UP000033409};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          32..77
FT                   /note="PEP-utilising enzyme mobile"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          197..371
FT                   /note="PEP-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
SQ   SEQUENCE   407 AA;  42699 MW;  A111D04610225CA1 CRC64;
     MNGRRIQGFL LTGGTQSVLR GICNRTRSPL GGSILVAPSL EASLYEAIVA ARAVVCSSGG
     LTGHMQSICR GRGIPVLRVD QADLADLVGE VTLHLESQSI VIGSDPSAGA PGSGAGSSSL
     DDLGSACAVI ADLQDIHTIN SCGPKAERVD SFFIREEFLC LAAGLRPLDC LDGGPAAIAA
     YGRAVADRLC TFVEALLPGQ RLVLRLLDLR SDHAAGVTEL APVAVEPNPE LGLHGARWLL
     GSTAYRDALH AVLKSLRSRL GDAAGRVHLS VPFLNDAEEF VQLRAHLEVP VEVPVSAFIE
     TPAAVHAAAA ICAAGASELF VGTKDLVQFY LAADRSNHLV ADSYRTRHPA VLDGVRRVVE
     SARAAGTPVR VFALGADLAH YLEGLPTPDG YMMCTAELRQ VVLQSQT
//
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