ACH1_NEUCR
ID ACH1_NEUCR Reviewed; 525 AA.
AC P15937; Q7RV87;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Acetyl-CoA hydrolase;
DE EC=3.1.2.1;
DE AltName: Full=Acetate utilization protein;
DE AltName: Full=Acetyl-CoA deacylase;
DE Short=Acetyl-CoA acylase;
GN Name=acu-8; ORFNames=NCU09770;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2140429; DOI=10.1128/mcb.10.6.2638-2644.1990;
RA Marathe S., Connerton I.F., Fincham J.R.S.;
RT "Duplication-induced mutation of a new Neurospora gene required for acetate
RT utilization: properties of the mutant and predicted amino acid sequence of
RT the protein product.";
RL Mol. Cell. Biol. 10:2638-2644(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
RP FUNCTION.
RX PubMed=1357077; DOI=10.1099/00221287-138-9-1797;
RA Connerton I.F., McCullough W., Fincham J.R.S.;
RT "An acetate-sensitive mutant of Neurospora crassa deficient in acetyl-CoA
RT hydrolase.";
RL J. Gen. Microbiol. 138:1797-1800(1992).
CC -!- FUNCTION: Required for utilization of acetate.
CC {ECO:0000269|PubMed:1357077}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC {ECO:0000305}.
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DR EMBL; M31521; AAA33554.1; -; Genomic_DNA.
DR EMBL; CM002237; EAA29118.1; -; Genomic_DNA.
DR PIR; A36316; A36316.
DR RefSeq; XP_958354.1; XM_953261.3.
DR AlphaFoldDB; P15937; -.
DR SMR; P15937; -.
DR STRING; 5141.EFNCRP00000009588; -.
DR EnsemblFungi; EAA29118; EAA29118; NCU09770.
DR GeneID; 3874501; -.
DR KEGG; ncr:NCU09770; -.
DR VEuPathDB; FungiDB:NCU09770; -.
DR HOGENOM; CLU_019748_3_0_1; -.
DR InParanoid; P15937; -.
DR OMA; DEALSWH; -.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IBA:GO_Central.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0006083; P:acetate metabolic process; IBA:GO_Central.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
DR Gene3D; 3.40.1080.20; -; 1.
DR InterPro; IPR026888; AcetylCoA_hyd_C.
DR InterPro; IPR038460; AcetylCoA_hyd_C_sf.
DR InterPro; IPR003702; ActCoA_hydro.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF13336; AcetylCoA_hyd_C; 1.
DR Pfam; PF02550; AcetylCoA_hydro; 1.
DR SUPFAM; SSF100950; SSF100950; 2.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..525
FT /note="Acetyl-CoA hydrolase"
FT /id="PRO_0000215521"
FT ACT_SITE 305
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:B3EY95"
FT BINDING 280..284
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:B3EY95"
FT BINDING 395
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:B3EY95"
FT BINDING 399
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:B3EY95"
FT CONFLICT 14..16
FT /note="VKR -> QG (in Ref. 1; AAA33554)"
FT /evidence="ECO:0000305"
FT CONFLICT 46..56
FT /note="GVGYPKKVPTM -> ASATPRRSYY (in Ref. 1; AAA33554)"
FT /evidence="ECO:0000305"
FT CONFLICT 65..86
FT /note="GLQGQLKYSLFVGASAGAETEN -> ASRPAQVQPLRRCLRRRRDRE (in
FT Ref. 1; AAA33554)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="A -> AHDR (in Ref. 1; AAA33554)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 58006 MW; E6134462D4A35423 CRC64;
MASPIASAAL RARVKRPSML KKLCNPEDML QHFPNGAYIG WSGFTGVGYP KKVPTMLADH
VEKNGLQGQL KYSLFVGASA GAETENRWAA LDMIARRAPH QVGKNIAKGI NEGRINFFDK
HLSMFPVDLV YGYYTKDRQN KNLDVVCVEA TEIKEDGSIV LGASVGATPE LIQMADKVII
EVNTAIPSFD GLHDITFSDL PPNRKPYLIQ QCRDRIGTTS VPVDPEKVVG IIECTTPDQT
LPNSPADETA TAIAGHLIEF FEHEVAHGRL PKNLLPLQSG IGNIANAVIG GLETSNFKNL
NVWTEVIQDT FLDLFDSGKL DFATATSIRF SPTGFERFYK NWDNYYDKLL LRSQSVSNAP
EIIRRLGVIG MNTPVEVDIY AHANSTNVMG SRMLNGLGGS ADFLRNSKYS IMHTPSTRPS
KTDAHGVSCI VPMCTHVDQT EHDLDVIVTE NGLADVRGLS PRERARVIID KCAHDVYKPI
LKAYFEKAEF ECLRKGMGHE PHLLFNSFDM HKALVEEGSM AKVKF
