ID C4M1C3_ENTH1 Unreviewed; 392 AA. AC C4M1C3; A0A175JMN7; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 90. DE RecName: Full=Probable acetate kinase {ECO:0000256|HAMAP-Rule:MF_03131}; DE EC=2.7.2.1 {ECO:0000256|HAMAP-Rule:MF_03131}; DE AltName: Full=Acetokinase {ECO:0000256|HAMAP-Rule:MF_03131}; GN ORFNames=EHI_170010 {ECO:0000313|EMBL:EAL50605.1}; OS Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM). OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae; OC Entamoeba. OX NCBI_TaxID=294381 {ECO:0000313|EMBL:EAL50605.1, ECO:0000313|Proteomes:UP000001926}; RN [1] {ECO:0000313|EMBL:EAL50605.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HM-1:IMSS {ECO:0000313|EMBL:EAL50605.1}; RX PubMed=15729342; DOI=10.1038/nature03291; RA Loftus B.J., Anderson I., Davies R., Alsmark U.C., Samuelson J., Amedeo P., RA Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T., Suh B., Pop M., RA Duchene M., Ackers J., Tannich E., Leippe M., Hofer M., Bruchhaus I., RA Willhoeft U., Bhattacharya A., Chillingworth T., Churcher C.M., Hance Z., RA Harris B., Harris D., Jagels K., Moule S., Mungall K.L., Ormond D., RA Squares R., Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H., RA Price C., Wang Z., Guillen N., Gilchrist C., Stroup S.E., Bhattacharya S., RA Lohia A., Foster P.G., Sicheritz-Ponten T., Weber C., Singh U., RA Mukherjee C., El-Sayed N.M.A., Petri W.A., Clark C.G., Embley T.M., RA Barrell B.G., Fraser C.M., Hall N.; RT "The genome of the protist parasite Entamoeba histolytica."; RL Nature 433:865-868(2005). RN [2] {ECO:0000313|EMBL:EAL50605.1} RP GENOME REANNOTATION. RC STRAIN=HM-1:IMSS {ECO:0000313|EMBL:EAL50605.1}; RA Lorenzi H., Amedeo P., Inman J., Schobel S., Caler E.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0007829|PDB:4H0O} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS). RX PubMed=23159802; DOI=10.1016/j.jsb.2012.11.001; RA Thaker T.M., Tanabe M., Fowler M.L., Preininger A.M., Ingram-Smith C., RA Smith K.S., Iverson T.M.; RT "Crystal structures of acetate kinases from the eukaryotic pathogens RT Entamoeba histolytica and Cryptococcus neoformans."; RL J. Struct. Biol. 181:185-189(2013). CC -!- CATALYTIC ACTIVITY: CC Reaction=acetate + ATP = acetyl phosphate + ADP; Xref=Rhea:RHEA:11352, CC ChEBI:CHEBI:22191, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:456216; EC=2.7.2.1; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03131}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03131}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; CC acetyl-CoA from acetate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_03131}. CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000256|HAMAP- CC Rule:MF_03131}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03131}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DS571207; EAL50605.1; -; Genomic_DNA. DR RefSeq; XP_655990.1; XM_650898.1. DR PDB; 4H0O; X-ray; 2.40 A; A/B=1-392. DR PDBsum; 4H0O; -. DR AlphaFoldDB; C4M1C3; -. DR SMR; C4M1C3; -. DR STRING; 5759.C4M1C3; -. DR EnsemblProtists; GAT95000; GAT95000; CL6EHI_170010. DR EnsemblProtists; rna_EHI_170010-1; rna_EHI_170010-1; EHI_170010. DR GeneID; 3410291; -. DR KEGG; ehi:EHI_170010; -. DR VEuPathDB; AmoebaDB:EHI5A_016990; -. DR VEuPathDB; AmoebaDB:EHI7A_005690; -. DR VEuPathDB; AmoebaDB:EHI8A_003960; -. DR VEuPathDB; AmoebaDB:EHI_170010; -. DR VEuPathDB; AmoebaDB:KM1_017390; -. DR HOGENOM; CLU_020352_0_1_1; -. DR InParanoid; C4M1C3; -. DR OMA; HKYVSQR; -. DR OrthoDB; 21304at2759; -. DR BRENDA; 2.7.2.1; 2080. DR BRENDA; 2.7.2.12; 2080. DR UniPathway; UPA00340; UER00458. DR Proteomes; UP000001926; Partially assembled WGS sequence. DR GO; GO:0008776; F:acetate kinase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006083; P:acetate metabolic process; IBA:GO_Central. DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.420.40; -; 2. DR HAMAP; MF_00020; Acetate_kinase; 1. DR InterPro; IPR004372; Ac/propionate_kinase. DR InterPro; IPR000890; Aliphatic_acid_kin_short-chain. DR InterPro; IPR043129; ATPase_NBD. DR NCBIfam; TIGR00016; ackA; 1. DR PANTHER; PTHR21060; ACETATE KINASE; 1. DR PANTHER; PTHR21060:SF19; ACETATE KINASE; 1. DR Pfam; PF00871; Acetate_kinase; 1. DR PIRSF; PIRSF000722; Acetate_prop_kin; 1. DR PRINTS; PR00471; ACETATEKNASE. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4H0O}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03131}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_03131, ECO:0000313|EMBL:EAL50605.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03131}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03131}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03131}; KW Reference proteome {ECO:0000313|Proteomes:UP000001926}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03131}. FT ACT_SITE 142 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131" FT BINDING 8 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131" FT BINDING 85 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131" FT BINDING 272..274 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131" FT BINDING 378 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131" FT SITE 172 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131" FT SITE 232 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131" SQ SEQUENCE 392 AA; 43247 MW; 55ED2FE3B0836FF1 CRC64; MSNVLIFNVG SSSLTYKVFC SDNIVCSGKS NRVNVTGTEK PFIEHHLNGQ IIKIETPILN HPQAAKLIIQ FLKENHISIA FVGHRFVHGG SYFKKSAVID EVVLKELKEC LPLAPIHNPS SFGVIEISMK ELPTTRQYVA IDTAFHSTIS QAERTYAIPQ PYQSQYLKFG FHGLSYEYVI NSLKNVIDVS HSKIIACHLG TGGSSCCGIV NGKSFDTSMG NSTLAGLVMS TRCGDIDPTI PIDMIQQVGI EKVVDILNKK SGLLGVSELS SDMRDILHEI ETRGPKAKTC QLAFDVYIKQ LAKTIGGLMV EIGGLDLLVF TDQMGLEVWQ VRKAICDKMK FLGIELDDSL NEKSMGKKIE FLTMPSSKVQ VCVAPNDEEL VILQKGKELF QF //