ID W9XCJ0_9EURO Unreviewed; 416 AA.
AC W9XCJ0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 13-SEP-2023, entry version 30.
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=A1O5_01349 {ECO:0000313|EMBL:EXJ74656.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ74656.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ74656.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ74656.1,
RC ECO:0000313|Proteomes:UP000019471};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:EXJ74656.1}.
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DR EMBL; AMGX01000002; EXJ74656.1; -; Genomic_DNA.
DR RefSeq; XP_007740158.1; XM_007741968.1.
DR AlphaFoldDB; W9XCJ0; -.
DR STRING; 1182543.W9XCJ0; -.
DR GeneID; 19186085; -.
DR eggNOG; ENOG502QSJJ; Eukaryota.
DR HOGENOM; CLU_020352_1_0_1; -.
DR OrthoDB; 21304at2759; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000019471; 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:UP000019471};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03131}.
FT ACT_SITE 157
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 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT BINDING 217..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT BINDING 402
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT SITE 189
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
FT SITE 250
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03131"
SQ SEQUENCE 416 AA; 45194 MW; 77A1CAB14245772F CRC64;
MANVILSINA GSSSLKTTLF VEEATEGKAR GLRRLGSAEI SSINAPPARL KYLRGPYKDT
RELGDINDHK HAFEHILNAF LADTEIPEVS SKDDIDYTAH RVVQGGSFEE NQFITKKTFD
KINKLSDLAP LHNASAVSLM IACHEHLPNV INVACFDSCF HQTMPDYVKS YAIDQKIAKE
KGLRKYGFHG LSYQYITRAT AKFLGKPESE TNIIALHLGS GASMCAIQNG RSIDTTMGLT
PVSGLPGGSR SGDIDPSLVF HYTSDASALS PNSTKDLHIS TAEEILNKQS GWKALTGTSD
FSKIADPNAP DSYKLAFNIF VDRVVGYVGN YFVKLGGKID ALVFAGGIGE KSPYVRQVVI
DKVSCLGFTI DDDKNKQGAD GNDVVDIGTS DTKRTLVCET DEDVRFSKSF DCKGPC
//
