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Database: UniProt
Entry: A0A1H5XY47_9RHOB
LinkDB: A0A1H5XY47_9RHOB
Original site: A0A1H5XY47_9RHOB 
ID   A0A1H5XY47_9RHOB        Unreviewed;       650 AA.
AC   A0A1H5XY47;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=acsA {ECO:0000256|HAMAP-Rule:MF_01123};
GN   ORFNames=SAMN05421751_11361 {ECO:0000313|EMBL:SEG16631.1};
OS   Jhaorihella thermophila.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Jhaorihella.
OX   NCBI_TaxID=488547 {ECO:0000313|EMBL:SEG16631.1, ECO:0000313|Proteomes:UP000236742};
RN   [1] {ECO:0000313|EMBL:SEG16631.1, ECO:0000313|Proteomes:UP000236742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23413 {ECO:0000313|EMBL:SEG16631.1,
RC   ECO:0000313|Proteomes:UP000236742};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA),
CC       an essential intermediate at the junction of anabolic and catabolic
CC       pathways. AcsA undergoes a two-step reaction. In the first half
CC       reaction, AcsA combines acetate with ATP to form acetyl-adenylate
CC       (AcAMP) intermediate. In the second half reaction, it can then transfer
CC       the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the
CC       product AcCoA. {ECO:0000256|HAMAP-Rule:MF_01123}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:456215; EC=6.2.1.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01123};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-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 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01123}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01123}.
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DR   EMBL; FNVD01000013; SEG16631.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5XY47; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000236742; Unassembled WGS sequence.
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   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR   PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR   PANTHER; PTHR24095:SF14; ACETYL-COENZYME A SYNTHETASE 1; 1.
DR   Pfam; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990, ECO:0000256|HAMAP-
KW   Rule:MF_01123};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01123};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, 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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01123}; Reference proteome {ECO:0000313|Proteomes:UP000236742}.
FT   DOMAIN          26..83
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          86..470
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          533..611
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
FT   BINDING         194..197
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         311
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         387..389
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         411..416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         502
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         517
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         525
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         528
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         539
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         541
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         544
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         586
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   MOD_RES         611
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
SQ   SEQUENCE   650 AA;  71392 MW;  3B22666B92A5F0C2 CRC64;
     MTHSENEVYP PSPEFVAQAH IDGAKYEEMY AASVNDPEAF WGEQGKTLDW IKPYTKVKNT
     TFEYPNVSIK WFEDGVLNVA ANCIDRHLDT RGDQTAIIWE PDDPNAPARH ITYRELHEQV
     SKLGNVLKGL GIAKGDRVVL YMPMIPEAAF AMLACARIGA IHSVVFGGFS PDALASRIED
     CSAKLVITAD EAPRGGRNTP LKANADKAME ICGDVPMLVV SRTGGGPGMK EGRDHSYEAL
     MAEASADCPP EPMGAEDPLF ILYTSGSTGK PKGVLHTSGG YLLYVSLTHK YVFDYHDGDI
     FWCTADVGWV TGHSYIVYGP LANGATTLMF EGVPTYPDAG RFWAVCEKHK VNQFYTAPTA
     IRALMGQGPQ FVDPYDLSSL KVLGTVGEPI NPEAWHWYND HVGKGRCPIV DTWWQTETGG
     HLLTPLPGAI PTKPGSATKP FFGVQPVVLD AQSGEEITTT EAEGVLCMKD SWPGQMRTVF
     GDHERFVKTY FSDYKGYYFS GDGCRRDADG YYWITGRVDD VINVSGHRMG TAEVESALVA
     HPKVSEAAVV GYPHPVKGQG IYCYVTLMAG EEYTDELREE LRQWVRKEIG PIATPDVIQW
     APGLPKTRSG KIMRRILRKI AENDFGNLGD TSTLADPSVV DDLIANRANT
//
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