GenomeNet

Database: UniProt/TrEMBL
Entry: G0TNZ1_MYCCP
LinkDB: G0TNZ1_MYCCP
Original site: G0TNZ1_MYCCP 
ID   G0TNZ1_MYCCP            Unreviewed;       385 AA.
AC   G0TNZ1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   26-NOV-2014, entry version 23.
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:CCC42747.1};
GN   OrderedLocusNames=MCAN_04071 {ECO:0000313|EMBL:CCC42747.1};
OS   Mycobacterium canettii (strain CIPT 140010059).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=1048245 {ECO:0000313|EMBL:CCC42747.1, ECO:0000313|Proteomes:UP000008896};
RN   [1] {ECO:0000313|EMBL:CCC42747.1, ECO:0000313|Proteomes:UP000008896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIPT 140010059 {ECO:0000313|EMBL:CCC42747.1,
RC   ECO:0000313|Proteomes:UP000008896};
RX   PubMed=22389744; DOI=10.1371/journal.pntd.0001552;
RA   Bentley S.D., Comas I., Bryant J.M., Walker D., Smith N.H.,
RA   Harris S.R., Thurston S., Gagneux S., Wood J., Antonio M., Quail M.A.,
RA   Gehre F., Adegbola R.A., Parkhill J., de Jong B.C.;
RT   "The genome of Mycobacterium africanum West African 2 reveals a
RT   lineage-specific locus and genome erosion common to the M.
RT   tuberculosis complex.";
RL   PLoS Negl. Trop. Dis. 6:E1552-E1552(2012).
RN   [2] {ECO:0000313|EMBL:CCC42747.1, ECO:0000313|Proteomes:UP000008896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIPT 140010059 {ECO:0000313|EMBL:CCC42747.1,
RC   ECO:0000313|Proteomes:UP000008896};
RX   PubMed=23291586; DOI=10.1038/ng.2517;
RA   Supply P., Marceau M., Mangenot S., Roche D., Rouanet C., Khanna V.,
RA   Majlessi L., Criscuolo A., Tap J., Pawlik A., Fiette L., Orgeur M.,
RA   Fabre M., Parmentier C., Frigui W., Simeone R., Boritsch E.C.,
RA   Debrie A.S., Willery E., Walker D., Quail M.A., Ma L., Bouchier C.,
RA   Salvignol G., Sayes F., Cascioferro A., Seemann T., Barbe V.,
RA   Locht C., Gutierrez M.C., Leclerc C., Bentley S.D., Stinear T.P.,
RA   Brisse S., Medigue C., Parkhill J., Cruveiller S., Brosch R.;
RT   "Genomic analysis of smooth tubercle bacilli provides insights into
RT   ancestry and pathoadaptation of Mycobacterium tuberculosis.";
RL   Nat. Genet. 45:172-179(2013).
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       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:SAAS00130554}.
CC   -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00020, ECO:0000256|RuleBase:RU003835}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; HE572590; CCC42747.1; -; Genomic_DNA.
DR   RefSeq; YP_004743886.1; NC_015848.1.
DR   ProteinModelPortal; G0TNZ1; -.
DR   SMR; G0TNZ1; 5-382.
DR   EnsemblBacteria; CCC42747; CCC42747; MCAN_04071.
DR   GeneID; 10986903; -.
DR   KEGG; mce:MCAN_04071; -.
DR   KO; K00925; -.
DR   OMA; KYVTQRA; -.
DR   BioCyc; MCAN1048245:GJCJ-411-MONOMER; -.
DR   UniPathway; UPA00340; UER00458.
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/Proprionate_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.
DR   PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00091196};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008896};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00130644};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|RuleBase:RU003835};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00091199};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00091203};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00091197};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|RuleBase:RU003835}.
FT   NP_BIND     192    196       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   NP_BIND     266    268       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   NP_BIND     314    318       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   ACT_SITE    132    132       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   METAL         9      9       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   METAL       368    368       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   BINDING      16     16       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   BINDING      75     75       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   SITE        164    164       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   SITE        225    225       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
SQ   SEQUENCE   385 AA;  41318 MW;  AE1F50C1665B4A4C CRC64;
     MSSTVLVINS GSSSLKFQLV EPVAGMSRAA GIVERIGERS SPVADHAQAL HRAFKMLAED
     GIDLQTCGLV AVGHRVVHGG TEFHQPTLLD DTVIGKLEEL SALAPLHNPP AVLGIKVARR
     LLANVAHVAV FDTAFFHDLP PAAATYAIDR DVADRWHIRR YGFHGTSHQY VSERAAAFLG
     RPLDGLNQIV LHLGNGASAS AIARGRPVET SMGLTPLEGL VMGTRSGDLD PGVISYLWRT
     ARMGVEDIES MLNHRSGMLG LAGERDFRRL RLVIETGDRS AQLAYEVFIH RLRKYLGAYL
     AVLGHTDVVS FTAGIGENDA AVRRDALAGL QGLGIALDQD RNLGPGHGAR RISSDDSPIA
     VLVVPTNEEL AIARDCLRVL GGRRA
//
DBGET integrated database retrieval system