ACSA_SCHPO
ID ACSA_SCHPO Reviewed; 662 AA.
AC P78773;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable acetyl-coenzyme A synthetase;
DE EC=6.2.1.1;
DE AltName: Full=Acetate--CoA ligase;
DE AltName: Full=Acyl-activating enzyme;
GN ORFNames=SPCC191.02c, SPCC417.14c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-662.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-596, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAA22660.1; -; Genomic_DNA.
DR EMBL; D89121; BAA13783.1; -; mRNA.
DR PIR; T41215; T41215.
DR RefSeq; NP_588291.2; NM_001023281.2.
DR AlphaFoldDB; P78773; -.
DR SMR; P78773; -.
DR STRING; 4896.SPCC191.02c.1; -.
DR iPTMnet; P78773; -.
DR MaxQB; P78773; -.
DR PaxDb; P78773; -.
DR PRIDE; P78773; -.
DR EnsemblFungi; SPCC191.02c.1; SPCC191.02c.1:pep; SPCC191.02c.
DR GeneID; 2539546; -.
DR KEGG; spo:SPCC191.02c; -.
DR PomBase; SPCC191.02c; -.
DR VEuPathDB; FungiDB:SPCC191.02c; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; P78773; -.
DR OMA; SPDIWEW; -.
DR PhylomeDB; P78773; -.
DR Reactome; R-SPO-71384; Ethanol oxidation.
DR PRO; PR:P78773; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003987; F:acetate-CoA ligase activity; ISO:PomBase.
DR GO; GO:0016208; F:AMP binding; ISM:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 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.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..662
FT /note="Probable acetyl-coenzyme A synthetase"
FT /id="PRO_0000208419"
FT BINDING 201..204
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 395..397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 419..424
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 525
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 533
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 536
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 594
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT MOD_RES 596
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 662 AA; 73036 MW; 02FD119ABB622583 CRC64;
MTKNPVDHTL IIEPPVRLHG DPTVPKPNIA SLDEYKRMYE ESINDPSTFW GNMARDMMTW
DKQFSTVVQG SIDKADSAWF ADGAISPCYN LVDRHAIARP DAVALIYEAD EPNQGRYITY
RELLASVSQC AGALQSMGVG MGDRVAIYMP MIPETIIAML AIVRLGAIHS VIFAGFSAES
VADRVNDSEC KVIITADESH RGGKRIPLKG VVNKALTECP TIKKVLVFQR SAEPTASMVE
GRDVWWHDII PKFPRYCPPA VVNPEHPLFL LYTSGSTGKP KGVVHCTGGY LLGAAATCKY
VFDLHPTDRM GCAGDVGWIT GHTYIVYGPL MLGAATLVFE STPAYPDYSR YWSVVERHRL
TQWYIAPTAI RLLQRAGNEF VKHDRSSLRV LGSVGEPIAP ESFMWYYEVV GEKRCAVADT
YWQTETGSHI VTSLGPVTPM KPGSATLPFF GIDAVIIDPL TGKIIEGNDV EGVLAIRSPW
PSAARTVWRG HDRYIDTYLK PYPGFYFTGD GATRDKDGYI WIRGRVDDVV NISGHRLSTA
EIEAALLSHD AVAESAVVGV HDELTGQAVN AFILLKPGYE ATVELEKELI MAVRSTIGPF
ASPRKLIFSD LPKTRSGKIM RRILRKILAG EVDQIGDLST LADPKVVEHI IHAVHYAHQK
KP
