ID   A0A120E8Q5_9BASI        Unreviewed;       667 AA.
AC   A0A120E8Q5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE            EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN   ORFNames=RHOSPDRAFT_15787 {ECO:0000313|EMBL:KWU46025.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU46025.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU46025.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU46025.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000256|RuleBase:RU361147};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432, ECO:0000256|RuleBase:RU361147}.
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DR   EMBL; KQ954469; KWU46025.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A120E8Q5; -.
DR   STRING; 1305733.A0A120E8Q5; -.
DR   OrthoDB; 144557at2759; -.
DR   Proteomes; UP000062823; 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-UniRule.
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   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   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361147};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU361147};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361147};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823}.
FT   DOMAIN          32..88
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          90..477
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          538..620
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   667 AA;  73863 MW;  D0322EB0B113B964 CRC64;
     MAEHDYRSAP THPVSKRNDG SGHKPHANEE SYAAMYRESI DKPNEFWDRM AKEHIYWHRP
     YSTVQAGSFE AGDVQWFPEG GLNVSYNCVD RWAYKTPNKT AIIWEADEPG QHVELTYEQL
     FQEVCKTANI LKSYGVKKGD TVAIYLPMVP EAAIAFLACA RLGAIHSVVF AGFSADSLRD
     RVVDAKSRVV ITTDEGKRGG KTIATKSIVD AALADCPLVE HVLVLKRTGG NVKWVEGRDH
     WWHEEKLSVQ PYCPVEIVSS EDPLFILYTS GSTGKPKGVV HSTAGYLLGA LMTLKYVFDV
     HPEDRYACMA DVGWITGHTY IVYGPLANGV TTTVFESTPV YPTPSRFWEV VAKHKLTQFY
     TAPTAIRLLR RLGEEHTKGH DLSTLRTIGS VGEPINPEAW EWYWEHVGKK ECAVVDTYWQ
     TETGSIIITP LPGATKTKPG SATLPFFGID PVLLDASTGE EIKGNEVEGV LCVRKPWPSI
     ARTVYGDHKR FLDTYMNPYP GYYFTGDGAG RDHDGYIWIR GRVDDVINVS GHRLSTAEIE
     SAMIQHNGVA ETAVVGVPDE LTGQAVIAYV TLKPDFKFDD ADEAPLLKEL VLQVRKTIGP
     FAAPKRIVLV SDLPKTRSGK IMRRILRKIS AGEGDQLGDL STLADPSVVD QIKEKFEAAP
     APPTTGK
//