GENTAUR Molecular Products.

 A0A157U0Q1_ENTCL        Unreviewed;       645 AA.
 A0A157U0Q1;
 08-JUN-2016, integrated into UniProtKB/TrEMBL.
 08-JUN-2016, sequence version 1.
 27-SEP-2017, entry version 8.
 RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|HAMAP-Rule:MF_01123};
          Short=AcCoA synthetase {ECO:0000256|HAMAP-Rule:MF_01123};
          Short=Acs {ECO:0000256|HAMAP-Rule:MF_01123};
          EC=6.2.1.1 {ECO:0000256|HAMAP-Rule:MF_01123};
 AltName: Full=Acetate--CoA ligase {ECO:0000256|HAMAP-Rule:MF_01123};
 AltName: Full=Acyl-activating enzyme {ECO:0000256|HAMAP-Rule:MF_01123};
 Name=acsA_1 {ECO:0000313|EMBL:SAI99703.1};
 Synonyms=acs {ECO:0000256|HAMAP-Rule:MF_01123};
 ORFNames=SAMEA2273162_00840 {ECO:0000313|EMBL:SAI99703.1};
 Enterobacter cloacae.
 Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
 Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
 NCBI_TaxID=550 {ECO:0000313|EMBL:SAI99703.1};
 [1] {ECO:0000313|EMBL:SAI99703.1}
 NUCLEOTIDE SEQUENCE.
 STRAIN=E403 {ECO:0000313|EMBL:SAI99703.1};
 Pathogen Informatics;
 Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
 -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA
     (AcCoA), an essential intermediate at the junction of anabolic and
     catabolic pathways. Acs undergoes a two-step reaction. In the
     first half reaction, Acs combines acetate with ATP to form acetyl-
     adenylate (AcAMP) intermediate. In the second half reaction, it
     can then transfer the acetyl group from AcAMP to the sulfhydryl
     group of CoA, forming the product AcCoA. {ECO:0000256|HAMAP-
     Rule:MF_01123}.
 -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA
     (AcCoA), an essential intermediate at the junction of anabolic and
     catabolic pathways. AcsA undergoes a two-step reaction. In the
     first half reaction, AcsA combines acetate with ATP to form
     acetyl-adenylate (AcAMP) intermediate. In the second half
     reaction, it can then transfer the acetyl group from AcAMP to the
     sulfhydryl group of CoA, forming the product AcCoA.
     {ECO:0000256|SAAS:SAAS00711888}.
 -!- FUNCTION: Enables the cell to use acetate during aerobic growth to
     generate energy via the TCA cycle, and biosynthetic compounds via
     the glyoxylate shunt. Acetylates CheY, the response regulator
     involved in flagellar movement and chemotaxis. {ECO:0000256|HAMAP-
     Rule:MF_01123}.
 -!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
     acetyl-CoA. {ECO:0000256|HAMAP-Rule:MF_01123}.
 -!- COFACTOR:
     Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
       Evidence={ECO:0000256|HAMAP-Rule:MF_01123,
       ECO:0000256|SAAS:SAAS00711884};
 -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
     activates the enzyme. {ECO:0000256|HAMAP-Rule:MF_01123}.
 -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
     family. {ECO:0000256|HAMAP-Rule:MF_01123}.
 -!- CAUTION: Lacks conserved residue(s) required for the propagation
     of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01123}.
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 EMBL; FKIY01000005; SAI99703.1; -; Genomic_DNA.
 ProteinModelPortal; A0A157U0Q1; -.
 GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-UniRule.
 GO; GO:0016208; F:AMP binding; IEA:InterPro.
 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:UniProtKB-UniRule.
 GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
 CDD; cd05966; ACS; 1.
 HAMAP; MF_01123; Ac_CoA_synth; 1.
 InterPro; IPR011904; Ac_CoA_lig.
 InterPro; IPR032387; ACAS_N.
 InterPro; IPR025110; AMP-bd_C.
 InterPro; IPR020845; AMP-binding_CS.
 InterPro; IPR000873; AMP-dep_Synth/Lig.
 Pfam; PF16177; ACAS_N; 1.
 Pfam; PF00501; AMP-binding; 1.
 Pfam; PF13193; AMP-binding_C; 1.
 TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
 PROSITE; PS00455; AMP_BINDING; 1.
 3: Inferred from homology;
 Acetylation {ECO:0000256|HAMAP-Rule:MF_01123};
 ATP-binding {ECO:0000256|HAMAP-Rule:MF_01123};
 Ligase {ECO:0000256|HAMAP-Rule:MF_01123, ECO:0000313|EMBL:SAI99703.1};
 Magnesium {ECO:0000256|HAMAP-Rule:MF_01123,
 ECO:0000256|SAAS:SAAS00711869};
 Metal-binding {ECO:0000256|HAMAP-Rule:MF_01123,
 ECO:0000256|SAAS:SAAS00711886};
 Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01123}.
 DOMAIN       24     80       ACAS_N. {ECO:0000259|Pfam:PF16177}.
 DOMAIN       82    519       AMP-binding. {ECO:0000259|Pfam:PF00501}.
 DOMAIN      528    606       AMP-binding_C.
                              {ECO:0000259|Pfam:PF13193}.
 NP_BIND     384    386       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
 NP_BIND     408    413       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
 REGION      190    193       Coenzyme A binding. {ECO:0000256|HAMAP-
                              Rule:MF_01123}.
 METAL       534    534       Magnesium; via carbonyl oxygen.
                              {ECO:0000256|HAMAP-Rule:MF_01123}.
 METAL       536    536       Magnesium; via carbonyl oxygen.
                              {ECO:0000256|HAMAP-Rule:MF_01123}.
 METAL       539    539       Magnesium; via carbonyl oxygen.
                              {ECO:0000256|HAMAP-Rule:MF_01123}.
 BINDING     308    308       Coenzyme A. {ECO:0000256|HAMAP-
                              Rule:MF_01123}.
 BINDING     332    332       Coenzyme A. {ECO:0000256|HAMAP-
                              Rule:MF_01123}.
 BINDING     497    497       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
 BINDING     512    512       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
 BINDING     520    520       Coenzyme A; via carbonyl oxygen.
                              {ECO:0000256|HAMAP-Rule:MF_01123}.
 BINDING     523    523       ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
 MOD_RES     606    606       N6-acetyllysine. {ECO:0000256|HAMAP-
                              Rule:MF_01123}.
 SEQUENCE   645 AA;  71640 MW;  D3F63891F880B1EA CRC64;
 MFEISVHPVP DAVRQRAYLN DDDYQRLYRQ SVENPDEFWS EQAKAFLDWF KPWHSVHHGD
 LRKGQATWFK GGQLNVAYNC IDRHLERRGE QIAIVWEGDN PSESAHITYR KLHHNVCRLA
 NVLKSRGVEK GDRVCIYMPM IPEAAYAMLA CARIGAVHSV VFGGFSPDSL RDRILDADCR
 TVITADEGVR GGKYIPLKQN VEKALKDCPD VSTVVVVERT QGDIPWVEGR DIWYHEALHA
 ASADCPAEAM DAEDPLFILY TSGSTGKPKG VLHTTGGYLL GAAMTHKYVF DYHDGDVYWC
 TADVGWVTGH SYIVYGPLAN GATTLMFEGV PNYPDASRFW QVIDKHQVNI FYTAPTAIRA
 LMREGDAPVR QTSRSSLRLL GSVGEPINPE AWEWYYQVVG EKRCPIVDTW WQTETGSILI
 TPLPGATALK PGSATRPFFG VQPVLLDEKG KEIDGAGSGV LAIKASWPSQ IRSVYGDHQR
 MIDTYFKPYP GYYFSGDGAR RDEDGYYWIT GRVDDVINVS GHRIGTAEVE SALVLHDAVA
 EAAVVGCPHD VKGQAIYAFV TLMAGSQPSE ALQQELLALV GKEIGSFAKP DHLQWAPSLP
 KTRSGKIMRR ILRKIACNEL DSLGDTSTLA DPGVVQGLID NRLNR

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