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Database: UniProt
Entry: B1X1D7_CYAA5
LinkDB: B1X1D7_CYAA5
Original site: B1X1D7_CYAA5 
ID   B1X1D7_CYAA5            Unreviewed;       665 AA.
AC   B1X1D7;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-SEP-2017, entry version 61.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|HAMAP-Rule:MF_01123};
DE            Short=AcCoA synthetase {ECO:0000256|HAMAP-Rule:MF_01123};
DE            Short=Acs {ECO:0000256|HAMAP-Rule:MF_01123};
DE            EC=6.2.1.1 {ECO:0000256|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acetate--CoA ligase {ECO:0000256|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acyl-activating enzyme {ECO:0000256|HAMAP-Rule:MF_01123};
GN   Name=acs {ECO:0000313|EMBL:ACB51366.1};
GN   Synonyms=acsA {ECO:0000256|HAMAP-Rule:MF_01123};
GN   OrderedLocusNames=cce_2016 {ECO:0000313|EMBL:ACB51366.1};
OS   Cyanothece sp. (strain ATCC 51142).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Cyanothecaceae; Cyanothece.
OX   NCBI_TaxID=43989 {ECO:0000313|EMBL:ACB51366.1, ECO:0000313|Proteomes:UP000001203};
RN   [1] {ECO:0000313|EMBL:ACB51366.1, ECO:0000313|Proteomes:UP000001203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51142 {ECO:0000313|EMBL:ACB51366.1,
RC   ECO:0000313|Proteomes:UP000001203};
RX   PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA   Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA   Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R.,
RA   Ghosh B.K., Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT   "The genome of Cyanothece 51142, a unicellular diazotrophic
RT   cyanobacterium important in the marine nitrogen cycle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
CC   -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA
CC       (AcCoA), an essential intermediate at the junction of anabolic and
CC       catabolic pathways. AcsA undergoes a two-step reaction. In the
CC       first half reaction, AcsA combines acetate with ATP to form
CC       acetyl-adenylate (AcAMP) intermediate. In the second half
CC       reaction, it can then transfer the acetyl group from AcAMP to the
CC       sulfhydryl group of CoA, forming the product AcCoA.
CC       {ECO:0000256|HAMAP-Rule:MF_01123}.
CC   -!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
CC       acetyl-CoA. {ECO:0000256|HAMAP-Rule:MF_01123}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01123};
CC   -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC       activates the enzyme. {ECO:0000256|HAMAP-Rule:MF_01123}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. {ECO:0000256|HAMAP-Rule:MF_01123}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01123}.
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DR   EMBL; CP000806; ACB51366.1; -; Genomic_DNA.
DR   ProteinModelPortal; B1X1D7; -.
DR   STRING; 43989.cce_2016; -.
DR   EnsemblBacteria; ACB51366; ACB51366; cce_2016.
DR   KEGG; cyt:cce_2016; -.
DR   eggNOG; ENOG4108IQF; Bacteria.
DR   eggNOG; COG0365; LUCA.
DR   HOGENOM; HOG000229981; -.
DR   KO; K01895; -.
DR   OMA; DHWWHDL; -.
DR   OrthoDB; POG091H059D; -.
DR   Proteomes; UP000001203; Chromosome circular.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR   CDD; cd05966; ACS; 1.
DR   HAMAP; MF_01123; Ac_CoA_synth; 1.
DR   InterPro; IPR011904; Ac_CoA_lig.
DR   InterPro; IPR032387; ACAS_N.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|HAMAP-Rule:MF_01123};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001203};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001203}.
FT   DOMAIN       44     98       ACAS_N. {ECO:0000259|Pfam:PF16177}.
FT   DOMAIN      107    543       AMP-binding. {ECO:0000259|Pfam:PF00501}.
FT   DOMAIN      552    630       AMP-binding_C. {ECO:0000259|Pfam:
FT                                PF13193}.
FT   NP_BIND     403    405       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   NP_BIND     427    432       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   REGION      208    211       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01123}.
FT   METAL       558    558       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   METAL       560    560       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   METAL       563    563       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     327    327       Coenzyme A. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
FT   BINDING     521    521       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     536    536       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     544    544       Coenzyme A; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     547    547       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   MOD_RES     630    630       N6-acetyllysine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
SQ   SEQUENCE   665 AA;  74494 MW;  2E07EF5E6D773803 CRC64;
     MLRSIVMVAS SEKNNIESVL QEKRVFNPPA DFATNAHIKS LQQYEELYEK AKNDPETFWA
     ELAEQELYWF EKWDQVLDWN PPTAKWFVNG KLNMSYNCLD RHLTTWRRNK AAIIWEGEPG
     DSRTLTYGEL HREVCQFANV LKDMGVQKGD RVGIYMPMVP EAAIAMLACT RIGAPHSVVF
     GGFSAEALRD RLEDAEAKVV ITADGGFRKD KIVPLKIEVD QALENGASSV EKVIVVQRTK
     QDVTMREGRD YWWHDLQKDA SPKCDAEVMD SEDPLFILYT SGSTGKPKGV VHTTGGYNLY
     THMTTKWIFD LKDTDVYWCT ADVGWITGHS YIVYGPLSNG ATSLMYEGVP RPSNPGCFWD
     VVEKYGVNVF YTAPTAIRAF MKMGEELPNA RDLSSLRLLG TVGEPINPEA WMWYHRVIGG
     EKCPIVDTWW QTETGGIMIT PLPGATPTKP GSATRPFPGI IADVVDKDGN PVPNNAGGYL
     VIKHPWPSML RTVYNNPERF QKTYWDPIPE VEGKPVYFAG DSARKDENGY FWIMGRTDDV
     MNVSGHRLGS MELESALVSH PAVAEASVVG VPHEIKGEDI YAFVTLKDNY SPSDELNKEL
     KQHVVTKISA IARPGTIQFA EALPKTRSGK IVRRFLRQIA AGQDIVGDKS TVVDPSVLDQ
     LREKG
//
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