ID   A0A1I8NZX8_STOCA        Unreviewed;       670 AA.
AC   A0A1I8NZX8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE            EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN   Name=106094587 {ECO:0000313|EnsemblMetazoa:SCAU003592-PA};
OS   Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Stomoxys.
OX   NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU003592-PA, ECO:0000313|Proteomes:UP000095300};
RN   [1] {ECO:0000313|EnsemblMetazoa:SCAU003592-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU003592-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_013117264.1; XM_013261810.1.
DR   AlphaFoldDB; A0A1I8NZX8; -.
DR   STRING; 35570.A0A1I8NZX8; -.
DR   EnsemblMetazoa; SCAU003592-RA; SCAU003592-PA; SCAU003592.
DR   GeneID; 106094587; -.
DR   KEGG; scac:106094587; -.
DR   VEuPathDB; VectorBase:SCAU003592; -.
DR   OrthoDB; 144557at2759; -.
DR   Proteomes; UP000095300; 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:SF244; ACETYL-COENZYME A SYNTHETASE; 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}.
FT   DOMAIN          26..86
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          98..496
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          552..630
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   670 AA;  76030 MW;  5FF287D58C1F6A88 CRC64;
     MPADKSIYHP NPAISKNAYI SSMEEYKKFY EESLDNPEEF WSRVAKQFHW ETPAEPKKFL
     QYNFDISKGP ISIKWMEGAS TNICYNLLDR NIRNGLGDNI AYYWEGNHPD DYSRGLTYRK
     LLEEVCRFAN VLKDHGVQKG DRVSIYMPMI LELPIAMLAC ARIGAVHSIV FAGFSSDSLA
     ERMVDCQAKI LITADGAWRG EKPLYLKALC DVALEKAEEM GHAVEKCIVV SHLKRVTPCQ
     ENHVEQDIPW TEDRDYWWHE EMEDKEPACY PEWMDAEDPL FMLYTSGSTG KPKGVLHTTA
     GYLLYAATTF KIVFDYKPGD IYWCTADIGW ITGHTYVVYG PLANGASSVI FEGTPFYPDN
     DRYWGVIDKY KVTQFYTAPT AIRALMKFGD SLVTRHKLDH LKVLGSVGEP INPEAWLWYY
     RVIGKERCSI VDTFWQTETG GHVITPLPGC TPMKPGSASF PFFGVKPILL DEAGIEIKGE
     GEGYLVFPQP WPGMMRTLFN NHARYEETYF SKFLGYYCTG DGARRDADGY LWITGRVDDM
     LNVSGHLMST AEVESVLTEH PRVAESAVVA RPHPVKGQCL YCFITPNENE TFDPKMVSEL
     KKLVRERIGP FAMPDVVQHA PGLPKTRSGK IMRRVLRKVA VNDRNVGDTS TLADETIVEQ
     LFANRPVESK
//