(data stored in SCRATCH zone)

SWISSPROT: B2UIL1_RALPJ

ID   B2UIL1_RALPJ            Unreviewed;       393 AA.
AC   B2UIL1;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 88.
DE   RecName: Full=Acetate kinase {ECO:0000256|HAMAP-Rule:MF_00020};
DE            EC=2.7.2.1 {ECO:0000256|HAMAP-Rule:MF_00020};
DE   AltName: Full=Acetokinase {ECO:0000256|HAMAP-Rule:MF_00020};
GN   Name=ackA {ECO:0000256|HAMAP-Rule:MF_00020};
GN   OrderedLocusNames=Rpic_4317 {ECO:0000313|EMBL:ACD29412.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29412.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate
CC       and ATP. Can also catalyze the reverse reaction.
CC       {ECO:0000256|HAMAP-Rule:MF_00020}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP = acetyl phosphate + ADP;
CC         Xref=Rhea:RHEA:11352, ChEBI:CHEBI:22191, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.2.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00020};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00020};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00020};
CC       Note=Mg(2+). Can also accept Mn(2+). {ECO:0000256|HAMAP-
CC       Rule:MF_00020};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA
CC       biosynthesis; acetyl-CoA from acetate: step 1/2.
CC       {ECO:0000256|HAMAP-Rule:MF_00020}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00020}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020,
CC       ECO:0000256|SAAS:SAAS00011667}.
CC   -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00020, ECO:0000256|RuleBase:RU003835,
CC       ECO:0000256|SAAS:SAAS00688878}.
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DR   EMBL; CP001069; ACD29412.1; -; Genomic_DNA.
DR   RefSeq; WP_012430337.1; NC_010678.1.
DR   STRING; 402626.Rpic_4317; -.
DR   EnsemblBacteria; ACD29412; ACD29412; Rpic_4317.
DR   GeneID; 6285881; -.
DR   KEGG; rpi:Rpic_4317; -.
DR   PATRIC; fig|402626.5.peg.578; -.
DR   eggNOG; ENOG4105C6H; Bacteria.
DR   eggNOG; COG0282; LUCA.
DR   HOGENOM; HOG000288399; -.
DR   KO; K00925; -.
DR   OMA; PLPWRYY; -.
DR   OrthoDB; 537106at2; -.
DR   UniPathway; UPA00340; UER00458.
DR   Proteomes; UP000002566; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   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   PANTHER; PTHR21060; PTHR21060; 1.
DR   Pfam; PF00871; Acetate_kinase; 1.
DR   PIRSF; PIRSF000722; Acetate_prop_kin; 1.
DR   PRINTS; PR00471; ACETATEKNASE.
DR   TIGRFAMs; TIGR00016; ackA; 1.
DR   PROSITE; PS01075; ACETATE_KINASE_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2UIL1.
DR   SWISS-2DPAGE; B2UIL1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00130545};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00011637};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|RuleBase:RU003835, ECO:0000256|SAAS:SAAS00130569,
KW   ECO:0000313|EMBL:ACD29412.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00011608};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00011656};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00130625};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|RuleBase:RU003835, ECO:0000256|SAAS:SAAS00130632,
KW   ECO:0000313|EMBL:ACD29412.1}.
FT   NP_BIND     206    210       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   NP_BIND     281    283       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   NP_BIND     328    332       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   ACT_SITE    148    148       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   METAL         9      9       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   METAL       379    379       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   BINDING      16     16       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   BINDING      91     91       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   SITE        179    179       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   SITE        239    239       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
SQ   SEQUENCE   393 AA;  42234 MW;  571995E9E39827F6 CRC64;
     MNDCIVVLNC GSSSIKFALF DATLDPLPRA PMWNGKVEGI GTEHPTATEA GAPTQALELD
     GVQPYHAALM HIRQRVEQRL EGRRLKAVAH RVVHGGAKYF APVRVSAEVL SDLRSYIPLA
     PLHQPFALEA IEALLSGLPD VPQVACFDTA FHNTLPQVET MLPLPYSAWE RGLRRYGFHG
     LSYEYMSMAL PERHGDIARG RTIVAHLGSG ASLCAMHGLK SVATTMGFSA LEGLMMGTRC
     GSLDPGAVLY MMETEHLSPA QVGHVLYHES GLLGVSGLSS DPRDLIPREA DNPRAQAALA
     LYVRRIVREI GALVAVLGGL DLLVFTAGIG EHNAVLRERV VGGLGYLGAN LDGEANQAHA
     AIISSSASRI RVAVEPTNEE WVAARHAVQC NLQ
//

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