ID G4TD17_SERID Unreviewed; 411 AA.
AC G4TD17;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=PIIN_03108 {ECO:0000313|EMBL:CCA69208.1};
OS Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS (Piriformospora indica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Sebacinales; Serendipitaceae; Serendipita.
OX NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA69208.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA69208.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA69208.1,
RC ECO:0000313|Proteomes:UP000007148};
RX PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA Kogel K.H.;
RT "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT the Mutualistic Root Symbiont Piriformospora indica.";
RL PLoS Pathog. 7:e1002290-e1002290(2011).
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;
CC Evidence={ECO:0000256|HAMAP-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 -!- 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:CCA69208.1}.
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DR EMBL; CAFZ01000049; CCA69208.1; -; Genomic_DNA.
DR AlphaFoldDB; G4TD17; -.
DR STRING; 1109443.G4TD17; -.
DR eggNOG; ENOG502QSJJ; Eukaryota.
DR HOGENOM; CLU_020352_1_0_1; -.
DR InParanoid; G4TD17; -.
DR OMA; HKYVSQR; -.
DR OrthoDB; 21304at2759; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000007148; Unassembled WGS sequence.
DR GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006082; P:organic acid metabolic process; IEA:InterPro.
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; IPR023865; Aliphatic_acid_kinase_CS.
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.
DR PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03131};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03131};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03131};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03131};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03131}; Reference proteome {ECO:0000313|Proteomes:UP000007148};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03131}.
FT ACT_SITE 148
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT BINDING 16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT BINDING 208..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT BINDING 391
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT SITE 180
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT SITE 241
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
SQ SEQUENCE 411 AA; 45597 MW; 210DA47D5466EF80 CRC64;
MAGIVLSVNA GSSSLKVSLF APTFEGPKHL ATCTVDAINT DQPSFTSSVK DINDEEKNVR
RVKDHDEALR YILNHLFRTT TSAEDLTHVC HRVVHGGDYQ KRQPINEDSL HHLESLIELA
PLHNKSSTAL IRATLKQLPN ATSIAYFDTT FHRSLPRHIY TLPLDRKLAD QCSLRKYGFH
GISYSFILRN VAEFLQKPES DMNLIIMHLG SGASICCVQN GKSLDTSMGL TPLAGLPGAT
RSGDIDPTTI LHYIRISHAS VDTAEEVLNK QSGWKALTGT TSFGDVAKRS NDETKLAFDL
FVDRILNFVG AYYLKLGGQV DALVFAGGIG EKSAELREAV SNQCQCLGFV FDKDRNQRPE
GKAPVKALCN MERQGGEGDR KKRVLVCETD EQFEMAFQCM QDRDLYEKGD R
//
