ID D5C1X2_NITHN Unreviewed; 723 AA.
AC D5C1X2;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Pyruvate phosphate dikinase PEP/pyruvate-binding protein {ECO:0000313|EMBL:ADE16560.1};
GN OrderedLocusNames=Nhal_3536 {ECO:0000313|EMBL:ADE16560.1};
OS Nitrosococcus halophilus (strain Nc4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE16560.1, ECO:0000313|Proteomes:UP000001844};
RN [1] {ECO:0000313|Proteomes:UP000001844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844};
RG US DOE Joint Genome Institute;
RA Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., Ward B.B.,
RA Klotz M.G.;
RT "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt-adapted,
RT aerobic obligate ammonia-oxidizing sulfur purple bacterium.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001798; ADE16560.1; -; Genomic_DNA.
DR RefSeq; WP_013034409.1; NC_013960.1.
DR AlphaFoldDB; D5C1X2; -.
DR STRING; 472759.Nhal_3536; -.
DR KEGG; nhl:Nhal_3536; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_005950_0_0_6; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000001844; Chromosome.
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:ADE16560.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001844}.
FT DOMAIN 17..322
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 647..718
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 723 AA; 81280 MW; 3D7ECD1600D8AC63 CRC64;
MKAVIPLSAA HDSLSPHIGG KATALAHLFK NGFPVPDAIF ISTQLYHAFL DQGGVRERIA
MELNRKNLNE MRWEEIWDTA LRIRHIFLTT PFPDPLRQAL ANSIEAYFGH KAVVVRSSGA
GEDSPATSFA GLHESYVNLQ GTDSILEHIR LVWASLWSDR ALLYRRELGL DIASSAMAVV
VQEIVAGECS GVIFSQNPND SSQSVIEAVH GLNQGLVDGT VAPDRWLLER SSGRLIQHLS
VPRKHYLVPS ATGVHLTPLP PPKTRSPPLN EARVQQVFAL AQQAEAVFGV PQDVEWTFRG
DHLYLLQSRP ITKLAQDASE DKRPWYLSLH RSFENLEALR FNIEQQWLPA MDEEAARLAE
ENLAPLSNGD LAQAISHRNQ IYEKWRSVYW EEFIPFAHAI RLFGQFYNDT IQPENPDEFY
KLLKTTDMLS LKRNQMLTQM ADYIRSQPQL ATALQQGNDY PVDQVLLTKV DDFLREFSGL
SWKDSPCFPN REAVLRVLSK MLPNPSKGEN QKIDNTTQLT EWFLSHYEGE QRIFAGKLLA
LARASYRLRD DDNIFLGKIE AQVIRALEEG RRRLKERIPF DPQRLTSNDL VRMLREPDFI
PKKRRSKKKT IFSSPLKARQ IIGQPASAGV AFGKARVLKK TADLFQFEAG EILICEAIDP
NMTFIVPLAA GIVECRGGML IHGAIIAREY GIPCVTGIGK ATSRIHTGDR VTVDGYLGIV
TLG
//
