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Database: UniProt
Entry: A0A120E5N4_9BASI
LinkDB: A0A120E5N4_9BASI
Original site: A0A120E5N4_9BASI 
ID   A0A120E5N4_9BASI        Unreviewed;       536 AA.
AC   A0A120E5N4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   22-FEB-2023, entry version 23.
DE   RecName: Full=Acetyl-CoA hydrolase {ECO:0000256|ARBA:ARBA00017958};
DE            EC=3.1.2.1 {ECO:0000256|ARBA:ARBA00011920};
DE   AltName: Full=Acetyl-CoA deacylase {ECO:0000256|ARBA:ARBA00029672};
GN   ORFNames=RHOSPDRAFT_37249 {ECO:0000313|EMBL:KWU41221.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU41221.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU41221.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU41221.1,
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=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=3.1.2.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001831};
CC   -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC       {ECO:0000256|ARBA:ARBA00009632}.
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DR   EMBL; KQ954550; KWU41221.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A120E5N4; -.
DR   STRING; 1305733.A0A120E5N4; -.
DR   OrthoDB; 100792at2759; -.
DR   Proteomes; UP000062823; Unassembled WGS sequence.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR   GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006083; P:acetate metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.750.70; 4-hydroxybutyrate coenzyme like domains; 1.
DR   Gene3D; 3.40.1080.20; Acetyl-CoA hydrolase/transferase C-terminal domain; 1.
DR   Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 1.
DR   InterPro; IPR026888; AcetylCoA_hyd_C.
DR   InterPro; IPR038460; AcetylCoA_hyd_C_sf.
DR   InterPro; IPR046433; ActCoA_hydro.
DR   InterPro; IPR003702; ActCoA_hydro_N.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   PANTHER; PTHR43609; ACETYL-COA HYDROLASE; 1.
DR   PANTHER; PTHR43609:SF1; ACETYL-COA HYDROLASE; 1.
DR   Pfam; PF13336; AcetylCoA_hyd_C; 1.
DR   Pfam; PF02550; AcetylCoA_hydro; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823}.
FT   DOMAIN          22..243
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          346..494
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
SQ   SEQUENCE   536 AA;  59792 MW;  351C175E5B6D94E4 CRC64;
     MLPTRVCRSV QASAALRSRV ARESYLKKVV KPQDLVHQFK DGQYIGWSGF TGVGYPKETP
     LALAEHVEKN NLQGQLRFSL FVGASTGPEV EERWARNKMI ARRSPHQVGK AIAKGINSGE
     IDFADKHLSM FPQDLTYGYY SLKRQGGEDG KMLDWAIVEA TEILPDGSIV PGASVGATPE
     ILQTAEKIII EVNTSLPSFK GLHDITPSHM PPHRQPYLVQ NPSDRIGQVS VPVDPERVVA
     IIETDKPDNT GQNAPETEDS KLIAQHLIQF LEDEVAVGRM PKNLHPLQSG IGNVANSIIA
     GLRDSKFERL QVWTEVLQDS FLPLLNSGKL DFATATSIRF SPEMFKEFYR DWDQYQDKLL
     LRPQQTANSP EIIRRLGVIG MNTPLEVDIY AHANSTNALG SRMLNGIGGS ADFLRNAKLS
     VMHTPSSRPS KTDPTGISCI VPFATHVDQT EHDLDVIVTE QGLADVRGLS PRQRALVIIE
     KCAHPDYRDQ LKEYYDRALH ECLKKGAGHE PHMLRNAFKM HLNFEKNGTM KIDKWD
//
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