ACSA_EMENI
ID ACSA_EMENI Reviewed; 670 AA.
AC P16928; C8VFX2; Q5B1F4;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
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=facA; Synonyms=acuA; ORFNames=AN5626;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=D1;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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}.
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DR EMBL; X16990; CAA34858.1; -; Genomic_DNA.
DR EMBL; AACD01000098; EAA62719.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF81525.1; -; Genomic_DNA.
DR PIR; S09245; SYASAA.
DR RefSeq; XP_663230.1; XM_658138.1.
DR AlphaFoldDB; P16928; -.
DR SMR; P16928; -.
DR STRING; 162425.CADANIAP00003444; -.
DR PRIDE; P16928; -.
DR EnsemblFungi; CBF81525; CBF81525; ANIA_05626.
DR EnsemblFungi; EAA62719; EAA62719; AN5626.2.
DR GeneID; 2871910; -.
DR KEGG; ani:AN5626.2; -.
DR VEuPathDB; FungiDB:AN5626; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; P16928; -.
DR OMA; DHWWHDL; -.
DR OrthoDB; 288915at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:AspGD.
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:0045733; P:acetate catabolic process; IMP:AspGD.
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 GO; GO:0015976; P:carbon utilization; IMP:AspGD.
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..670
FT /note="Acetyl-coenzyme A synthetase"
FT /id="PRO_0000208413"
FT BINDING 211..214
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 404..406
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 428..433
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 603
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT CONFLICT 343
FT /note="C -> V (in Ref. 1; CAA34858)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="N -> Q (in Ref. 1; CAA34858)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="D -> S (in Ref. 1; CAA34858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 670 AA; 74280 MW; 69CB00F68E5ED15A CRC64;
MSDGPIAPPK PAVVAEAHEV DTFHVPKAFF DKHPSGPHLK NLDEYKKLYE ESIRSPDVFW
ARKARELLTF DKDFQTTRIG SLENGDVAWF PEGRLNASFN CVDRHAIKNP NKVAIIYEAD
EPNEGRTITY GELLREVSRV AWVLKQRGVK KGDTVAIYLP MIPEAIIAFL ACSRIGAVHS
VVFAGFSSDS LRDRVLDAGS KVVITTDEGK RGGKVIGTKR IVDEGLKQCP DVSTVLVYKR
TGAEVPWTEG RDIWWHEEVE KYPAYIAPDS VNSEDPLFLL YTSGSTGKPK GVMHTTAGYL
LGAAMTGKYV FDIHDDDRYF CGGDVGWITG HTYVVYAPLL LGCSTVVFES TPAYPDFSRY
WDVIEKHKVT QFYVAPTALR LLKRAGDHHI HHKMEHLRVL GSVGEPIAAE VWKWYFEKVG
KEEAHICDTY WQTETGSNVI TPLAGVTPTK PGSASLPFFG IEPAIIDPVS GEEISGNDVE
GVLAFKQPWP SMARTVWGAH KRYMDTYLNV YKGYYFTGDG AGRDHEGYYW IRGRVDDVVN
VSGHRLSTAE IEAALIEHPM VAEAAVVGIA DELTGQAVNA FVSLKEGNET NDQVRKDLIL
QVRKSIGPFA APKAVFVVDD LPKTRSGKIM RRILRKILSG EEDSLGDIST LSDPSVVERI
IATVHASRGK
