ID C0QDT4_DESAH Unreviewed; 733 AA.
AC C0QDT4;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=PpsA8 {ECO:0000313|EMBL:ACN17355.1};
DE EC=2.7.9.2 {ECO:0000313|EMBL:ACN17355.1};
GN Name=ppsA8 {ECO:0000313|EMBL:ACN17355.1};
GN OrderedLocusNames=HRM2_42990 {ECO:0000313|EMBL:ACN17355.1};
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN17355.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN17355.1, ECO:0000313|Proteomes:UP000000442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC {ECO:0000313|Proteomes:UP000000442};
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
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DR EMBL; CP001087; ACN17355.1; -; Genomic_DNA.
DR RefSeq; WP_015906087.1; NC_012108.1.
DR AlphaFoldDB; C0QDT4; -.
DR STRING; 177437.HRM2_42990; -.
DR KEGG; dat:HRM2_42990; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_005950_0_0_7; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000000442; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:UniProtKB-EC.
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 Reference proteome {ECO:0000313|Proteomes:UP000000442};
KW Transferase {ECO:0000313|EMBL:ACN17355.1}.
FT DOMAIN 16..314
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 652..723
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT REGION 594..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 81923 MW; 084FDED326BC9F9C CRC64;
MKPLLSIKEF MAAGISQVGG KALCLAKIHE QGVTVPRTFC IPCRVYEDYL AHTRLKDRIL
FEINRKPLEK MRWEEIWDIS LRVRNLFLTT PIPQDIRADL GQLILLHCGD TPVAVRSSAP
GEDDKASSFA GIHASFLNIM GTEHIIKHVQ LVWASLYSDA ALLYRKELGL DIHRSQMAVV
IQALVASDRS GIFFGMNPAN SAESVIESVY GLNQALVDGD IEPDRWVLNR SSGRILSHVE
PIRNRLAVPA AQGVDFADLS EKMSQQPPLN DGEVHRVWET GKTLETLFGK PQDMEWTFSK
NQLVVLQARP ITSGGLEGTD DKRSWYLSLH RSHENLKALY EKINTCLIPE MIRAAHEMGQ
LNFQELSVGQ LTREIKRRQE CYDHWVKVYW ADFIPFAHGI RLFGQVYNDA VRPDDPYEFM
KLLEKTSLKS IERNRLLEQM AHLIQRDDGL ASKLSAGLEL EKDHPFMALL AEFISEFGDL
ACHTTGSGEC HQGSFALVRL ILEFARMPSL PEKKTTGPDI QTLKAAYLDR FEPEKKRFAQ
EVLELGRESF RLRDDDNLHL GKIEACLFDA VREGQARLAE PDLDLGDRKL LTSVSALSSP
PGPRQECGNK QTEPDSSSLW LKARQVVGHP AGPGIAKGRA RVILNPEDLL DFKQGEVLVC
KGVDPNMTFV VPLSAAVVEE RGGMLIHGAI IAREYGLPCV TGAPDITRLV RTGDRVTVDG
YLGIVTCETG DLD
//