ID A0A2H3J3K5_WOLCO Unreviewed; 661 AA.
AC A0A2H3J3K5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN ORFNames=WOLCODRAFT_28777 {ECO:0000313|EMBL:PCH36830.1};
OS Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phaeolaceae; Wolfiporia.
OX NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH36830.1, ECO:0000313|Proteomes:UP000218811};
RN [1] {ECO:0000313|EMBL:PCH36830.1, ECO:0000313|Proteomes:UP000218811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-104 {ECO:0000313|EMBL:PCH36830.1,
RC ECO:0000313|Proteomes:UP000218811};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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 Evidence={ECO:0000256|RuleBase:RU361147};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432, ECO:0000256|RuleBase:RU361147}.
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DR EMBL; KB467898; PCH36830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3J3K5; -.
DR STRING; 742152.A0A2H3J3K5; -.
DR OMA; INVSYNC; -.
DR OrthoDB; 144557at2759; -.
DR Proteomes; UP000218811; Unassembled WGS sequence.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR CDD; cd05966; ACS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF14; ACETYL-COENZYME A SYNTHETASE 1; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361147};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU361147};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361147};
KW Reference proteome {ECO:0000313|Proteomes:UP000218811}.
FT DOMAIN 33..90
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 92..479
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 540..622
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 72528 MW; D8488DF4D8819923 CRC64;
MSDSAEPVPT HPIAPRLANG DKTPHVGPHI DAYRSLHAQT LGHESDKWWA KMARETISWD
RPFHTVRAGG FETGDIVWFP EGGLNASYNC VDRWAFKHPD KTAIIYEGDE PGEGCEITYA
QLLREVCSVA NVLKSLGVKR GDTVSIYLPM TWHAIAAFLA CARIGAVHSV VFAGFSAESL
RDRVRDCGSR VLITSDEGRR GGKAIATKAI ADAAVRECPE VEHLLVLRRT GNEVPWTEGR
DHWWHEEVEK VPNYCPPEVM SSEDPLFILY TSGSTGKPKG VVHTTAGYLL CAAMTVKYVF
DVHPDDRFAC MADVGWITGH TYIVYGPLMN GVATTVFEST PVYPTPARYW QTVDKHQLTQ
FYSAPTAIRL LRRLGAHHVA PHDLSSLRVL GSVGEPINPE AWHWYNEHVG RGQCAIVDTF
WQTETGSIVV TPFPGAIETK PGAATVPFFG IEPAILDPVT GEEISGTNVE GVLVIKTPWP
SIARTVYGDH KRYLETYMKP YPGVFYTGDG AARDEHGYIW IKGRVDDVIN VSGHRLSTAE
IESALITHAG VAETAVVGTA DELTGQAVYA FVTLKPEFTF DPNDEAALTK ELTLQVRKVI
GPFAAPKRVY LVPDLPKTRS GKIMRRIMRK LVAGEADQLG DLSTLADPSV VDVIKAKVAA
A
//
