ID F0M1Y0_PSEPM Unreviewed; 782 AA.
AC F0M1Y0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Phosphoenolpyruvate synthase/pyruvate phosphate dikinase {ECO:0000313|EMBL:ADX73132.1};
GN OrderedLocusNames=Asphe3_19770 {ECO:0000313|EMBL:ADX73132.1};
OS Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG
OS 23796 / Sphe3) (Arthrobacter phenanthrenivorans).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=930171 {ECO:0000313|EMBL:ADX73132.1, ECO:0000313|Proteomes:UP000008639};
RN [1] {ECO:0000313|EMBL:ADX73132.1, ECO:0000313|Proteomes:UP000008639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18606 / JCM 16027 / LMG 23796 / Sphe3
RC {ECO:0000313|Proteomes:UP000008639};
RX PubMed=21677849; DOI=10.4056/sigs.1393494;
RA Kallimanis A., Labutti K.M., Lapidus A., Clum A., Lykidis A.,
RA Mavromatis K., Pagani I., Liolios K., Ivanova N., Goodwin L., Pitluck S.,
RA Chen A., Palaniappan K., Markowitz V., Bristow J., Velentzas A.D.,
RA Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT "Complete genome sequence of Arthrobacter phenanthrenivorans type strain
RT (Sphe3).";
RL Stand. Genomic Sci. 4:123-130(2011).
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DR EMBL; CP002379; ADX73132.1; -; Genomic_DNA.
DR RefSeq; WP_013601059.1; NC_015145.1.
DR AlphaFoldDB; F0M1Y0; -.
DR STRING; 930171.Asphe3_19770; -.
DR KEGG; apn:Asphe3_19770; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_005950_0_0_11; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000008639; Chromosome.
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; 2.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
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; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ADX73132.1};
KW Pyruvate {ECO:0000313|EMBL:ADX73132.1};
KW Transferase {ECO:0000313|EMBL:ADX73132.1}.
FT DOMAIN 68..219
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 229..281
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 704..775
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT REGION 137..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 83114 MW; C582880D6DE8E749 CRC64;
MGNGADNGGQ RAFGDGLFSP LGGPVPLTRL QAGGKAATLS ELKQAGFPVP PGFVVTRQDL
QARAAGAVSS WEDRLRASAR ACGPGPYAVR SSAAAEDLPG ASYAGMYESY LRVAEGELAA
TVLRCFESAN ASRVRAYQDS LPRPENGAGA GPGPGLGGGH DAAQMAVLVQ QMVDPAAAGV
AFTAHPLTGA RDEGVVSAVR GLGGNLVEGS EDGEEWLVRE GRAVRRHGGA AALSNESATA
VAAMARAVAS HFGCPQDVEW AVDPSGQIMI LQARPMTALP EPVVWKAPGK GAWLRNFRLG
EWLPEPVTPL FMDWIIPLID AGYNDAVYRS AGIRIPMGYA TVNGWYYVAP PTPRALPHLL
FGGQPRSLPY FFNSVLRPMI DPAGADRAVL RDLEHEWRVI GLPAYLALAH RDLSPSATFA
SLVATVEEIG EAAGRYLWFF SATGGAAWKM ERVLAKFWRR HLAPSFTKRP AQGRVPEQAL
QGGSGYQVLL GGLLPRPPAP VPHAVYSLDW YHRTAGEEGP EAGGAGTTAH PGSAAPAAER
RRSAEAACRD ILRGTRRLRR FDELLAVAQH YALLREEQAR DFTAGWPLLR RCARRIGRQL
RDAGIITSED DVFFLSRQDL RLDAPPQQER VAIRREKWSR QRKLAAPLVL GGVPLIGNTF
DRIAHSARST AALPRGALVG HPASPGRARG RVRVVRGPED FPGFRPGEVL VAGATAPAWT
PLFAGAAAVV TDSGNLAAHA SLVAREYGIP AVVGTGNATQ VLHTGQLVTV DGNAGTVEQH
ED
//