(data stored in SCRATCH zone)

SWISSPROT: C5BHF8_EDWI9

ID   C5BHF8_EDWI9            Unreviewed;       652 AA.
AC   C5BHF8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
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:0000256|HAMAP-Rule:MF_01123};
GN   OrderedLocusNames=NT01EI_0193 {ECO:0000313|EMBL:ACR67436.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67436.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA
CC       (AcCoA), an essential intermediate at the junction of anabolic and
CC       catabolic pathways. Acs undergoes a two-step reaction. In the
CC       first half reaction, Acs combines acetate with ATP to form acetyl-
CC       adenylate (AcAMP) intermediate. In the second half reaction, it
CC       can then transfer the acetyl group from AcAMP to the sulfhydryl
CC       group of CoA, forming the product AcCoA. {ECO:0000256|HAMAP-
CC       Rule:MF_01123}.
CC   -!- FUNCTION: Enables the cell to use acetate during aerobic growth to
CC       generate energy via the TCA cycle, and biosynthetic compounds via
CC       the glyoxylate shunt. Acetylates CheY, the response regulator
CC       involved in flagellar movement and chemotaxis. {ECO:0000256|HAMAP-
CC       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, ECO:0000256|SAAS:SAAS00711884};
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}.
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DR   EMBL; CP001600; ACR67436.1; -; Genomic_DNA.
DR   RefSeq; WP_015869647.1; NC_012779.2.
DR   ProteinModelPortal; C5BHF8; -.
DR   STRING; 634503.NT01EI_0193; -.
DR   EnsemblBacteria; ACR67436; ACR67436; NT01EI_0193.
DR   GeneID; 7958781; -.
DR   KEGG; eic:NT01EI_0193; -.
DR   PATRIC; fig|634503.3.peg.171; -.
DR   eggNOG; ENOG4108IQF; Bacteria.
DR   eggNOG; COG0365; LUCA.
DR   HOGENOM; HOG000229981; -.
DR   KO; K01895; -.
DR   OMA; DHWWHDL; -.
DR   OrthoDB; POG091H059D; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-HAMAP.
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:UniProtKB-HAMAP.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-HAMAP.
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;
DR   PRODOM; C5BHF8.
DR   SWISS-2DPAGE; C5BHF8.
KW   Acetylation {ECO:0000256|HAMAP-Rule:MF_01123};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01123, ECO:0000313|EMBL:ACR67436.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01123,
KW   ECO:0000256|SAAS:SAAS00711869};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01123,
KW   ECO:0000256|SAAS:SAAS00711886};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN       24     81       ACAS_N. {ECO:0000259|Pfam:PF16177}.
FT   DOMAIN       83    522       AMP-binding. {ECO:0000259|Pfam:PF00501}.
FT   DOMAIN      531    609       AMP-binding_C. {ECO:0000259|Pfam:
FT                                PF13193}.
FT   NP_BIND     387    389       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   NP_BIND     411    416       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   REGION      191    194       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01123}.
FT   METAL       537    537       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   METAL       539    539       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   METAL       542    542       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     311    311       Coenzyme A. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
FT   BINDING     335    335       Coenzyme A. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
FT   BINDING     500    500       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     515    515       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     523    523       Coenzyme A; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     526    526       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
FT   BINDING     584    584       Coenzyme A. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
FT   MOD_RES     609    609       N6-acetyllysine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01123}.
SQ   SEQUENCE   652 AA;  72182 MW;  9F0CECF132055EE4 CRC64;
     MSQIHTYPIP ADIAQHAFIN AEMYREMYQA SVEAPEAFWA EQGQIISWIT PYSRVKNTSF
     DPGHINIRWF DDGTLNLAAN CLDRHLAERG EQTAIIWEGD DPQESRRVTY RQLHSEVCRF
     ANVLKSLQVE KGDVVAIYMP MVVEAAVAML ACARIGAIHS VIFGGFSPEA VAGRIIDSGA
     KLVITADEGI RAGRTIPLKR NVDEALQHPQ VNSVRHVVVF RRTGGAGEWD SDRDRWWHEL
     MALADEYCPP VEMNSEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPGDI
     YWCTADVGWV TGHSYLLYGP LANGAITLMF EGVPNYPGIN RLSQIVDKHQ VNILYTAPTA
     IRALMAEGKR AIADTHRTSL RIMGSVGEPI NPEAWEWYYH TIGNSHCPIM DTWWQTETGG
     FMITPLPGAT VLKAGSATRP FFGVQPALVD NSGEILEGAS EGNLVILDSW PGQARTLFGA
     HERFEQTYFS TFKGMYFSGD GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP
     KIAEAAVVGI PHSIKGQAIY AYITLNVGEE PSPALYAEVR DWVRKEIGPI ATPDILHWTD
     ALPKTRSGKI MRRILRKIAS GDISNLGDTS TLADPAVVDK LLEEKQSMKV PS
//

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