ACKA_CRYNB
ID ACKA_CRYNB Reviewed; 430 AA.
AC P0CL99; Q55HG8; Q5K706;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 47.
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 OrderedLocusNames=CNBN1520;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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}.
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DR EMBL; AAEY01000066; EAL17325.1; -; Genomic_DNA.
DR RefSeq; XP_771972.1; XM_766879.1.
DR AlphaFoldDB; P0CL99; -.
DR SMR; P0CL99; -.
DR PRIDE; P0CL99; -.
DR EnsemblFungi; AAW47117; AAW47117; CNN01560.
DR EnsemblFungi; EAL17325; EAL17325; CNBN1520.
DR GeneID; 4939763; -.
DR KEGG; cnb:CNBN1520; -.
DR VEuPathDB; FungiDB:CNBN1520; -.
DR HOGENOM; CLU_020352_1_0_1; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000001435; Chromosome 14.
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; 1.
DR PIRSF; PIRSF000722; Acetate_prop_kin; 1.
DR PRINTS; PR00471; ACETATEKNASE.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00016; ackA; 1.
DR PROSITE; PS01075; ACETATE_KINASE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..430
FT /note="Probable acetate kinase"
FT /id="PRO_0000410000"
FT ACT_SITE 159
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03131"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03131"
FT BINDING 19
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 220..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03131"
FT BINDING 416
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03131"
FT SITE 192
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03131"
FT SITE 253
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03131"
SQ SEQUENCE 430 AA; 46972 MW; 21519B732FAB7114 CRC64;
MPDKTEYLLA INCGSSSIKG KLFAIPSFEL LANLAVTNIS SADERVKIRI TWEEGKGKNS
EEEADYGDKI RYASLVPILL DHLTNSTHVE KEEIKYVCHR VVHGGTHDRG IRVVKGHEEG
LIEMDKLSEF APLHNHRAVL AVKSCLDALP HHTSLLLFDT IFHQTIAPEV YTYALPPSDN
ELSMPLRKYG FHGLSYASIV RSLAEHLKKP SDQVNVVVAH LGSGSSSCCI KNGKSVDTSM
GLTPLEGLLG GTRSGTIDPT AIFHHTKDAA SDANVGDFTV SKAEIILNKN SGLKALAGTT
NFGHIIQNLD PSKCSKEDHE KAKLTYAVFL DRLLNFVAQY LFKLLSEVPI ESIDGLVFSG
GIGEKGAELR RDVLKKLAWL GAEVDEEANN SNSGGTVKCI TKEGSKLKGW VVETDEEGWM
ATMAKEEFGF
