ID J2JRC7_9ACTN Unreviewed; 864 AA.
AC J2JRC7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Phosphoenolpyruvate synthase {ECO:0000313|EMBL:EJJ02620.1};
GN ORFNames=SU9_33023 {ECO:0000313|EMBL:EJJ02620.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ02620.1};
RN [1] {ECO:0000313|EMBL:EJJ02620.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ02620.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
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:EJJ02620.1}.
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DR EMBL; AJGV01000214; EJJ02620.1; -; Genomic_DNA.
DR AlphaFoldDB; J2JRC7; -.
DR STRING; 1160718.SU9_33023; -.
DR PATRIC; fig|1160718.3.peg.6677; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_005950_0_0_11; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43615; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43615:SF1; PHOSPHOENOLPYRUVATE SYNTHASE-RELATED; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:EJJ02620.1}.
FT DOMAIN 17..315
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 787..858
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 864 AA; 94880 MW; 4E482DDBD2343D4E CRC64;
MEQYVWDLQG VDEGQVAVVG GKGAHLGGLS RIDGIRVPGG FCVTTEAFRR IMAEAPSIDD
RLDRLSRLKP DDREAIRTLS AEIRRTIEGI AIPGDLAAAI TRALSQLGEQ AAYAVRSSAT
AEDLPTASFA GQQDTYLNVV GRTAILQHVS RCWASLFTER AVTYRQRNGI DHRTVHMAVL
VQQMVFPDVA GILFTADPVT GNRKVATVDA GFGLGETLVS GLVNPDVFKV RDGEVVAKAI
AAKQRAVHAL PAGGTQEVAI DRQRQERPAL TDAQVVRLVQ LGRRIEAHFG RPQDIEWCLV
DDDFQIVQSR PITTLFPIPE TDDQDNHVYV SVGHQQMMTD PMKPLGLSMW QLTAMVPMHE
AGGRLFVDVT RRLASPASRA GLLDLIGRGD PLVRDALETV LDRDDFVPSL PDAGSGAPPA
GGAPAPIETD PAIVTELIER SRASIAALER DIRTKTGPAL FDFLLEAFEE HKRVLSDPLN
LQAIMAGMEA TWWLNDKLQE WLGEKNAADT LTLSAPDNVT SEMGLALLDV ADVIRPQSEV
VAFLQGVEDE GFLDELAKLA GGTEARDAIE AYLDRYGMRC VGEIDITRPR WRERPSTLVP
VLLDNVRIFE PGAAERRFEQ GRQKAQKKEQ DVLARLRALP DGDQKADEAK RMIDRVRTFI
GYREYPKYDI VSRSFLYKQA LLAEAERLVQ ANVLPEKEDI FYLTFQELHD VVRSHQVDDQ
LIQRRKDAFR SYHALTPPRV LTSDGEAVTG AYRRDDVPAG ALIGLPVSAG TIEGRARVIL
DMAEADLEAG DILVTTFTDP SWSPLFVGIA GLVTEVGGLM THGAVIAREY GLPAVVGVEQ
ATRLIRDGQR IRVHGTDGYV EILP
//
