(data stored in ACNUC7421 zone)

SWISSPROT: B8IB57_METNO

ID   B8IB57_METNO            Unreviewed;       389 AA.
AC   B8IB57;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 73.
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=Mnod_0408 {ECO:0000313|EMBL:ACL55450.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55450.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55450.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) 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: ATP + acetate = ADP + acetyl phosphate.
CC       {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; CP001349; ACL55450.1; -; Genomic_DNA.
DR   RefSeq; WP_015927161.1; NC_011894.1.
DR   ProteinModelPortal; B8IB57; -.
DR   STRING; 460265.Mnod_0408; -.
DR   EnsemblBacteria; ACL55450; ACL55450; Mnod_0408.
DR   KEGG; mno:Mnod_0408; -.
DR   eggNOG; ENOG4105C6H; Bacteria.
DR   eggNOG; COG0282; LUCA.
DR   HOGENOM; HOG000288399; -.
DR   KO; K00925; -.
DR   OMA; TIRERVC; -.
DR   OrthoDB; POG091H02K4; -.
DR   UniPathway; UPA00340; UER00458.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
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; B8IB57.
DR   SWISS-2DPAGE; B8IB57.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00483886};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
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:SAAS00483909,
KW   ECO:0000313|EMBL:ACL55450.1};
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:SAAS00483892};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|RuleBase:RU003835, ECO:0000256|SAAS:SAAS00483925}.
FT   NP_BIND     202    206       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   NP_BIND     277    279       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   NP_BIND     322    326       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   ACT_SITE    144    144       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   METAL         9      9       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   METAL       373    373       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   BINDING      16     16       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   BINDING      87     87       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   SITE        175    175       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   SITE        235    235       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
SQ   SEQUENCE   389 AA;  40125 MW;  4F446BD58550BCD6 CRC64;
     MSDAILAINA GSSSLKFALY AAGSLALLCR GGVSGLGGPV AVEASGPVPL ATGAPPPAGS
     NHATAIAWLL DAVRRMPDLV LRAAGHRVVH GGRDYAAPVL IDGAVLDALE RLVPLAPAHQ
     PHNLAAIRAV AAAWPNLPQV ACFDTAFHRT QPRLAQLFPI PRALTDAGIL RYGFHGLSYQ
     HVAETLPEVA GERAEGRVIV AHLGHGASLC AMRARRSIAS TMGFTALDGL MMGTRSGAVD
     PGLVLHLIRE RGLDPAAVAD LLNNRSGLLG VSELSDDVRV LQESGDPRAA EALDLFAYRA
     VREAGSLMAA LGGLDLIVFT AGIGEHAPRV RAAIAAGLSF AGVELDEERN AAGRGRISRD
     GSPVAVYVVP ANEELPIARA AARLVLGAG
//

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