ID A0A0Q9LLP8_9MICC Unreviewed; 943 AA.
AC A0A0Q9LLP8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Pyruvate kinase {ECO:0000313|EMBL:KRE53205.1};
GN ORFNames=ASG92_06600 {ECO:0000313|EMBL:KRE53205.1};
OS Arthrobacter sp. Soil736.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736395 {ECO:0000313|EMBL:KRE53205.1, ECO:0000313|Proteomes:UP000051775};
RN [1] {ECO:0000313|Proteomes:UP000051775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil736 {ECO:0000313|Proteomes:UP000051775};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE53205.1, ECO:0000313|Proteomes:UP000051775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil736 {ECO:0000313|EMBL:KRE53205.1,
RC ECO:0000313|Proteomes:UP000051775};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRE53205.1}.
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DR EMBL; LMSB01000034; KRE53205.1; -; Genomic_DNA.
DR RefSeq; WP_056631322.1; NZ_LMSB01000034.1.
DR AlphaFoldDB; A0A0Q9LLP8; -.
DR STRING; 1736395.ASG92_06600; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000051775; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Kinase {ECO:0000313|EMBL:KRE53205.1};
KW Pyruvate {ECO:0000313|EMBL:KRE53205.1};
KW Transferase {ECO:0000313|EMBL:KRE53205.1}.
FT DOMAIN 26..349
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 851..922
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT REGION 79..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 943 AA; 99586 MW; 6281C6885DA20BEC CRC64;
MSPPESGTPD RLVLELGQLG SEPLTLVGGK ALNLGRLADA GFPVPAGFCL TTAAYRMAVP
PELDALAARL DGLAAGAAHT GEVPATGGPD GNEPAQREGA LREDAQREIA MRARELVGTS
PVPPEVEAAV RRAYAAMGDV STPAGSAPAG SEPAGSPPAV AVRSSATAED LPFASFAGQQ
DSFLNIVGAD AVMQAVRRCW ASLWTDRAVA YRSANGIRHS DVGLAVVVQH VVDATTAGVL
FSANPVTGTR GETVIDASAG PGEAVVSGAV TPDHFVVETA TGRIRQSSPR PVDAGTGDGG
SPGLTDAQLR ELTSLGLSAQ ELFGEPQDVE WVIDAEGTIW LTQSRPITTL YPLPDPSSAK
PFGLESAPDG ETRVYLCGTL LQGLTRPLTP MGLSVMGMMG NRSSPWAYVS PGLRMYADLT
PFVRTAYGRR MLLKWLPLAD GRSASVLPAL LDDPRFGLTK GQPRPSKARA SEARRRDGTA
GLAMVVWLVP ALIRAVLRPK AELHRALRFG KRLEADLALP EPATAFRRLD HAQHAPARTV
DDLVRATLPA PAAGYAMLGL ARWLLRGVAE PRELEAVLRG LPHNVTTEMD LELWRLAVSV
RDDAASREAF LGRRPDELAV SYAAGELPPV AQAGLRRFLE RYGHRAVAEI DLGMPRWSEK
PDHILGMISN YLKVENPELA PDRQFARAAD HAEARIRSLV ARAGAVSRWR GRLVALCLRR
TRQLAGLREL PKFYVVTVFG EVHRQLAAIG AELARAGTIV AADDVFFLTF DEARVGLRGG
ELKGMVAERR RIYDAELRRR HIPRLLLSDG TDVEAAVAGA AAASSLVGTP ASAGKAAGRV
RVILDPVGAH LEPGEILVAP STDPGWTPLF MTAGALVMEM GGVISHGAVV AREYGIPAVV
GVPHATTRLR TGQTVVVDGA AGTITEVETA TDVGTVTGVG TVT
//
