(data stored in SCRATCH zone)

SWISSPROT: Q5LWR6_RUEPO

ID   Q5LWR6_RUEPO            Unreviewed;       394 AA.
AC   Q5LWR6;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 102.
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   ECO:0000313|EMBL:AAV93446.1};
GN   OrderedLocusNames=SPO0116 {ECO:0000313|EMBL:AAV93446.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93446.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93446.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93446.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00020}.
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DR   EMBL; CP000031; AAV93446.1; -; Genomic_DNA.
DR   RefSeq; WP_011045889.1; NC_003911.12.
DR   STRING; 246200.SPO0116; -.
DR   EnsemblBacteria; AAV93446; AAV93446; SPO0116.
DR   KEGG; sil:SPO0116; -.
DR   eggNOG; ENOG4105C6H; Bacteria.
DR   eggNOG; COG0282; LUCA.
DR   HOGENOM; HOG000288399; -.
DR   KO; K00925; -.
DR   OMA; CHLGGSS; -.
DR   OrthoDB; 537106at2; -.
DR   BioCyc; RPOM246200:G1G48-117-MONOMER; -.
DR   UniPathway; UPA00340; UER00458.
DR   Proteomes; UP000001023; Chromosome.
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; Q5LWR6.
DR   SWISS-2DPAGE; Q5LWR6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00130545};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
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:AAV93446.1};
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:UP000001023};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|RuleBase:RU003835, ECO:0000256|SAAS:SAAS00130632,
KW   ECO:0000313|EMBL:AAV93446.1}.
FT   NP_BIND     208    212       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   NP_BIND     328    332       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   ACT_SITE    150    150       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      93     93       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   SITE        181    181       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   SITE        241    241       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
SQ   SEQUENCE   394 AA;  42142 MW;  50FB9882C3AAC6A9 CRC64;
     MTDVVLVLNA GSSSIKFAVY PSGTNTVPLI RGKVAGVGRD PVFSAVRADG TAIDMVMPKN
     IDAAADHEAL ISLLLDWLAE HRADRRLVAV GHRVVHGGRD FLKPVIVDDS VLSQLEQLIP
     LAPLHQPHNL AAIRAISRLQ PTVPQVACFD TSFHQTQDRL AQLFALPRDL SDEGIIRYGF
     HGLSYEYIAG ILPDHLGERA EGRVIVAHLG NGASMCAMKN RQSVATSMGF TALDGLMMGR
     RCGALDAGVV LYLMQSKGLN ATEIETLLYR RCGLLGVSGI SNNMRELERS DDPKAREAIE
     LFCFRAASVL GGLVTALGGL DAIVFTAGIG ENSALVRKLI CDRLACFGVD LDPNSNEGNS
     PRIGSVQSSI DVLVLPTDEE IVISNATNET VALG
//

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