ID A0A1V9K1Y6_9ACTN Unreviewed; 865 AA.
AC A0A1V9K1Y6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 28-JUN-2023, entry version 16.
DE SubName: Full=Phosphoenolpyruvate synthase {ECO:0000313|EMBL:OQQ13603.1};
GN ORFNames=B0675_37355 {ECO:0000313|EMBL:OQQ13603.1};
OS Streptomyces sp. M41(2017).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1955065 {ECO:0000313|EMBL:OQQ13603.1, ECO:0000313|Proteomes:UP000192467};
RN [1] {ECO:0000313|EMBL:OQQ13603.1, ECO:0000313|Proteomes:UP000192467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M41 {ECO:0000313|EMBL:OQQ13603.1,
RC ECO:0000313|Proteomes:UP000192467};
RX PubMed=28326787; DOI=10.1021/acs.orglett.7b00545;
RA Wyche T.P., Ruzzini A.C., Beemelmanns C., Kim K.H., Klassen J.L., Cao S.,
RA Poulsen M., Bugni T.S., Currie C.R., Clardy J.;
RT "Linear Peptides Are the Major Products of a Biosynthetic Pathway That
RT Encodes for Cyclic Depsipeptides.";
RL Org. Lett. 19:1772-1775(2017).
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:OQQ13603.1}.
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DR EMBL; MWFK01000003; OQQ13603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9K1Y6; -.
DR STRING; 1955065.B0675_37355; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000192467; Unassembled WGS sequence.
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:OQQ13603.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192467}.
FT DOMAIN 18..316
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 788..859
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 865 AA; 94876 MW; C44FFBDBEED467D2 CRC64;
MTEQYVLDLQ EVDETQVAVV GGKGAHLGEL SRIEGIRVPA GFCVTTEAFR RTVAEASSLD
GQLDRLSRSA PDDREGIRTL SARIRRTIEE ATVPEELAAA ITNALGRHGA QEAYAVRSSA
TAEDLPTASF AGQQDTYLNV MGVTAVLQHV SRCWASLFTE RAVAYRQRNG IDHRTVRMAV
VVQRMVFPHA AGVLFTADPV TGNRKVASVD AGFGLGEALV SGLVNPDVFK VRDGEIVSKV
IAAKQRAVHA LPTGGTREVA VDAQRQEQPA LTDAQAVRLA EVGRRIEAHF GRPQDIEWCL
DDHGFQIVQS RPITTLFPVP ESDDQENHVY VSVGHQQMMT DAMKPLGLSM WQLTAMAPMH
AAGGRLFVDV ARRLASPASR AGLLDLMGKG DPLVRDALET VLAQDGFVPS LPDAGPGGLP
GRGASDPIET DPAVVTELIE RSRTSIAALE HDIRSKTGPA LFDFLLEAFE EHKRVLADPL
SIQVIMAGME ATWWLNDQLQ EWLGEKNAAD TLTLSAPDNI TSEMGLALLD VADVIRRHPD
VVAFLEGVQD DGFLDELAKL TGGAEARDAI EAYLDRYGMR CVGEIDITRP RWRERPSTLV
PVILDNVRLF EPGAAERRFE QGRRKARQKE QDVLARLRAL PDGDRKADET QRMIHRVRTF
VGYREYPKYG IIARYFVYKT ALMEEAERLV QAGVLAEPED SFYLTFQEFH AVARSHRVDH
RLVQRRKDAF RSFERLTPPR VLTSDGEAVN GAYRRDDVPP GALTGLPVSA GTVEGRARVI
LDMAEADLEA GDILVTTFTD PSWSPLFVGI AGLVTEVGGQ MTHGAVIARE YGLPTVVGVD
RATRLIEDGR RIRVHGTDGY VELLS
//
