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Database: UniProt
Entry: I1C040_RHIO9
LinkDB: I1C040_RHIO9
Original site: I1C040_RHIO9 
ID   I1C040_RHIO9            Unreviewed;       660 AA.
AC   I1C040;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE            EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN   ORFNames=RO3G_06525 {ECO:0000313|EMBL:EIE81820.1};
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE81820.1, ECO:0000313|Proteomes:UP000009138};
RN   [1] {ECO:0000313|EMBL:EIE81820.1, ECO:0000313|Proteomes:UP000009138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC   {ECO:0000313|Proteomes:UP000009138};
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(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         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; CH476735; EIE81820.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1C040; -.
DR   STRING; 246409.I1C040; -.
DR   VEuPathDB; FungiDB:RO3G_06525; -.
DR   eggNOG; KOG1175; Eukaryota.
DR   InParanoid; I1C040; -.
DR   OMA; AIKASWP; -.
DR   OrthoDB; 144557at2759; -.
DR   Proteomes; UP000009138; 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:UP000009138}.
FT   DOMAIN          34..90
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          92..480
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          541..619
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   660 AA;  73860 MW;  D0A9BF2912A1D35D CRC64;
     MTMTEEEVIT HPVPSRLLDS SKYPVPHINS LDKYKSMWKE SVEDPEKFFG NFAREMLSWS
     KPFQTVRHGS FDQSDIAWFL EGELNAAYNC VDRHAMKNPE KIAIIHEGDE PDQVRNITYG
     ELFRLVCQMA NTLKNLGLRK GDNVAIYMPM IPEALVAALA CARIGAVHSV VFAGFSAESL
     RDRVVDCAAR VIITSDEGRR GGKNIATKRI VDDALRSHQT HVEHVIVYRR TGSPIDWVED
     RDLWWHEEMA KARAFCPPEP MNSEDPLFLL YTSGSTGTPK GILHTTGGYL LGAAMTVKYI
     FDYHENDIFA CMADIGWITG HTYVTYGPLT LGGTTVLFES TPTYPDPSRF WRLVEKHKVT
     QFYTAPTAIR ALRRLGDEWV DKCDLSSLRV IGSVGEPINP EAWEWYYRKV GRSQCAVVDT
     YWQTETGSIV VAPLPGAVPT KPGSATFPFF GINPIILDPT TGKVLEGNDV TGVLAISQPW
     PSMARTVYNN HSRFLDTYLN PYKGYYFTGD GATRDKDGYI WIRGRVDDVI NVSGHRLSTA
     EIESALILHH SVAEAAVVGG HDDLTGQCIH AFALLKPNIE DSEGFEKELV LQVRKVIGPF
     ATPKRIYVVS DLPKTRSGKI MRRILRKIVN GEQDSLGDTS TLADPSVVDQ LIKHVHNKKK
//
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