ACKA_CHAGB
ID ACKA_CHAGB Reviewed; 459 AA.
AC Q2HAJ4;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Probable acetate kinase {ECO:0000255|HAMAP-Rule:MF_03131};
DE EC=2.7.2.1 {ECO:0000255|HAMAP-Rule:MF_03131};
DE AltName: Full=Acetokinase {ECO:0000255|HAMAP-Rule:MF_03131};
GN ORFNames=CHGG_02760;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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:0000255|HAMAP-
CC Rule:MF_03131};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03131};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_03131}.
CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_03131}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAQ90825.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH408030; EAQ90825.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001229276.1; XM_001229275.1.
DR AlphaFoldDB; Q2HAJ4; -.
DR SMR; Q2HAJ4; -.
DR STRING; 38033.XP_001229276.1; -.
DR EnsemblFungi; EAQ90825; EAQ90825; CHGG_02760.
DR GeneID; 4388475; -.
DR eggNOG; ENOG502QSJJ; Eukaryota.
DR HOGENOM; CLU_015938_0_0_1; -.
DR InParanoid; Q2HAJ4; -.
DR OrthoDB; 510084at2759; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000001056; 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 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 PANTHER; PTHR21060; PTHR21060; 1.
DR Pfam; PF00871; Acetate_kinase; 2.
DR PRINTS; PR00471; ACETATEKNASE.
DR SUPFAM; SSF53067; SSF53067; 3.
DR PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..459
FT /note="Probable acetate kinase"
FT /id="PRO_0000402094"
FT REGION 308..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..334
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03131"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03131"
FT BINDING 16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03131"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03131"
FT BINDING 216..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03131"
FT BINDING 299..301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03131"
FT BINDING 441
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03131"
FT SITE 188
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03131"
FT SITE 249
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03131"
SQ SEQUENCE 459 AA; 49007 MW; B941CF7178249EF1 CRC64;
MKTVILSVNA GSSSVKLSAY TAEQGQSPIQ IAEVQVSGLT APPASLKYER GGKTIVKSRE
VDDQVSDQRD AFSLILKTLI EDDDLHDIQT KDDIGIICHR IVHGGDYTKP QLITNGTYHH
LENLNDLAPL HNANSLPIVR LCVQDFPSAR NVACFDSQFH STIPEHIRTY PINQDIARRG
RLRKYGFHGI SYSFITRATA EFLGKDPSDV NIIALHLGSG ASACAIKGGK SWDTSMGLTP
LAGLPGATRS GSVDPSLVFH YASDVGKLSP ASTKDLHISR AEEILNKQAG WKALTGTTDF
RVIAAAATTT SSPTPSPNPN PNPNPDPNPD PNPDPQNQNH RLAFALLVDR ISAFVGAYYV
SLHGRVDALV FAGGIGERSA ALRAAVVEQV GCLGFAADGD EDFDGDGGEG AVVVDVGREA
AGGSDLGGRP RPRVLVCRTD EQFEMARMCA EDAEFWGSG
