ACSA_NEUCR
ID ACSA_NEUCR Reviewed; 667 AA.
AC P16929; Q7RVJ2; Q8X016;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Acetyl-coenzyme A synthetase;
DE EC=6.2.1.1;
DE AltName: Full=Acetate--CoA ligase;
DE AltName: Full=Acyl-activating enzyme;
GN Name=acu-5; ORFNames=B23D6.070, NCU06836;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-667.
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=1972535; DOI=10.1111/j.1365-2958.1990.tb00611.x;
RA Connerton I.F., Fincham J.R.S., Sandeman R.A., Hynes M.J.;
RT "Comparison and cross-species expression of the acetyl-CoA synthetase genes
RT of the Ascomycete fungi, Aspergillus nidulans and Neurospora crassa.";
RL Mol. Microbiol. 4:451-460(1990).
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 -!- INDUCTION: By acetate.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA34857.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA34857.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL669993; CAD21159.1; -; Genomic_DNA.
DR EMBL; CM002237; EAA34441.2; -; Genomic_DNA.
DR EMBL; X16989; CAA34857.1; ALT_SEQ; Genomic_DNA.
DR PIR; S09244; SYNCAA.
DR RefSeq; XP_963677.2; XM_958584.3.
DR AlphaFoldDB; P16929; -.
DR SMR; P16929; -.
DR STRING; 5141.EFNCRP00000006825; -.
DR PRIDE; P16929; -.
DR EnsemblFungi; EAA34441; EAA34441; NCU06836.
DR GeneID; 3879801; -.
DR KEGG; ncr:NCU06836; -.
DR VEuPathDB; FungiDB:NCU06836; -.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; P16929; -.
DR OMA; DHWWHDL; -.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
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 2: Evidence at transcript level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..667
FT /note="Acetyl-coenzyme A synthetase"
FT /id="PRO_0000208416"
FT BINDING 209..212
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 402..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 426..431
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 532
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 601
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT CONFLICT 102..104
FT /note="RHA -> KR (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
FT CONFLICT 121..123
FT /note="GQG -> VR (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
FT CONFLICT 140..147
FT /note="HVLTNLGV -> MSSPTWVI (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
FT CONFLICT 241..242
FT /note="AD -> PI (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
FT CONFLICT 300..301
FT /note="GA -> R (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
FT CONFLICT 329..330
FT /note="HT -> PH (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="Y -> S (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
FT CONFLICT 351..357
FT /note="AYPNFSR -> PTNSP (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="Y -> S (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="I -> S (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
FT CONFLICT 420..421
FT /note="GR -> AA (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="H -> R (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
FT CONFLICT 535..536
FT /note="DV -> R (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
FT CONFLICT 596..597
FT /note="FV -> SPS (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="R -> L (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
FT CONFLICT 665..667
FT /note="QRQ -> HQ (in Ref. 3; CAA34857)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 667 AA; 73766 MW; 88E360BB2F135495 CRC64;
MSGSTVPAGA VVPEAHTIET FQPPREMLQN HPSKPHLANF EEYQKLYKQS ITEPNVFWAE
RARELLSWSK DFQTVHSGSL ANGDNAWFVE GELNASYNCV DRHAHKDPNR VAIIYEADEP
GQGRNVTYGE LLREVSKLAH VLTNLGVRKG DTVAIYLPMI PEAIVAMLAC TRIGAIHSVV
FAGFSSDSLR DRVVDAQSKV VITTDEGKRG GKLIGTKKIV DEALQQCPDV RNVLVYKRTG
ADISMTPGRD LWWHEEVEKY PAYYTPVAMA SEDPLFLLYT SGSTGKPKGV AHSTGGYLLG
AAMTGKYVFD IHDGDRYFCG GDVGWITGHT YVLYAPLLLG VSTVVFEGTP AYPNFSRYWD
IIEEHKVTQF YVAPTALRLL KRAGDHHVRN EMKHLRVLGS VGEPIAAEVW KWYYDVVGKG
RAQICDTYWQ TETGSNVITP LAGVTPTKPG SASFPFFGIE PALVDPVTGE EIHGNDVEGV
LAFKQPWPSM ARTVWGAHKR YMETYLHVYK GYYFTGDGAA RDHEGFYWIR GRVDDVVNVS
GHRLSTAEIE AALIEHHSIA EAAVVGVADE LTGQAVNAFV AVKEGTQIND ALRKEFVLQV
RRSIGPFAAP KAIYIVPDLP KTRSGKIMRR ILRKIVAGEE DQLGDITTLS DPSVVAKIID
VVHAQRQ
