ID U9TGL1_RHIID Unreviewed; 441 AA.
AC U9TGL1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=GLOIN_2v1472812 {ECO:0000313|EMBL:POG78950.1};
OS Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=747089 {ECO:0000313|EMBL:POG78950.1, ECO:0000313|Proteomes:UP000018888};
RN [1] {ECO:0000313|EMBL:POG78950.1, ECO:0000313|Proteomes:UP000018888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194
RC {ECO:0000313|Proteomes:UP000018888};
RX PubMed=24277808; DOI=10.1073/pnas.1313452110;
RA Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA Charron P., Duensing N., Frei Dit Frey N., Gianinazzi-Pearson V.,
RA Gilbert L.B., Handa Y., Herr J.R., Hijri M., Koul R., Kawaguchi M.,
RA Krajinski F., Lammers P.J., Masclaux F.G., Murat C., Morin E.,
RA Ndikumana S., Pagni M., Petitpierre D., Requena N., Rosikiewicz P.,
RA Riley R., Saito K., San Clemente H., Shapiro H., van Tuinen D., Becard G.,
RA Bonfante P., Paszkowski U., Shachar-Hill Y.Y., Tuskan G.A., Young P.W.,
RA Sanders I.R., Henrissat B., Rensing S.A., Grigoriev I.V., Corradi N.,
RA Roux C., Martin F.;
RT "Genome of an arbuscular mycorrhizal fungus provides insight into the
RT oldest plant symbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20117-20122(2013).
RN [2] {ECO:0000313|EMBL:POG78950.1, ECO:0000313|Proteomes:UP000018888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194
RC {ECO:0000313|Proteomes:UP000018888};
RX PubMed=29355972;
RA Chen E.C.H., Morin E., Beaudet D., Noel J., Yildirir G., Ndikumana S.,
RA Charron P., St-Onge C., Giorgi J., Kruger M., Marton T., Ropars J.,
RA Grigoriev I.V., Hainaut M., Henrissat B., Roux C., Martin F., Corradi N.;
RT "High intraspecific genome diversity in the model arbuscular mycorrhizal
RT symbiont Rhizophagus irregularis.";
RL New Phytol. 0:0-0(2018).
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:POG78950.1}.
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DR EMBL; AUPC02000029; POG78950.1; -; Genomic_DNA.
DR AlphaFoldDB; U9TGL1; -.
DR STRING; 747089.U9TGL1; -.
DR VEuPathDB; FungiDB:GLOIN_2v1472812; -.
DR eggNOG; ENOG502QSJJ; Eukaryota.
DR HOGENOM; CLU_020352_1_0_1; -.
DR OrthoDB; 21304at2759; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000018888; 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|HAMAP-Rule:MF_03131};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_03131, ECO:0000313|EMBL:POG78950.1};
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:UP000018888};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03131}.
FT ACT_SITE 158
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT BINDING 17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT BINDING 220..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT BINDING 367..371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT BINDING 429
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT SITE 190
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT SITE 253
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
SQ SEQUENCE 441 AA; 48819 MW; 04530E9855573903 CRC64;
MTKINILAIN AGSSSLKYKL FLFDKSKDEI NLVSKGSITE ITSPTSSQFT AKIISSNTKI
SKSLNIQTHE KAFSHILSYL LDTIINSKEQ IKYIVHRIVH GTTESQPIIL KSDSSPSKEL
SKLDSLSELA PLHNHSSVLI LKSCLKELSN SINYAFFDTL FHQSIKPHIY TYALPYDEAK
QKRIRKYGFH GLSYSYVSKV AAKHMGIDLN DDNSKFICLH LGSGASMCAI RGGKSVDTTM
GLTPLEGLPG GTRSGLIDPC AIFHFSSKAR KGDESHHPVD KQFHLTEAES ILNHNSGFKG
LCGTSDFSEI VKQIQDTTNG SENSNSSINK ERAKLTFDIF INRIVNYIGS YFVTLEGNVS
ALIFTGGIGE NNKELREAVA EKIKCLGFKS VDKERNKSVE ELFKSGKDVV DISSGSTENF
RLLVIETDEE KEMVNQLISK I
//
