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Database: UniProt
Entry: A0A158NKC7_ATTCE
LinkDB: A0A158NKC7_ATTCE
Original site: A0A158NKC7_ATTCE 
ID   A0A158NKC7_ATTCE        Unreviewed;       685 AA.
AC   A0A158NKC7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Acyl-CoA synthetase short-chain family member 3, mitochondrial {ECO:0000256|ARBA:ARBA00040004};
DE            EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
DE   AltName: Full=Acetate--CoA ligase 3 {ECO:0000256|ARBA:ARBA00042755};
GN   Name=105621125 {ECO:0000313|EnsemblMetazoa:XP_012057985.1};
OS   Atta cephalotes (Leafcutter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012057985.1, ECO:0000313|Proteomes:UP000005205};
RN   [1] {ECO:0000313|Proteomes:UP000005205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA   Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA   Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA   Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA   Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA   Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA   Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA   Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA   Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA   Weinstock G.M., Gerardo N.M., Currie C.R.;
RT   "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT   insights into its obligate symbiotic lifestyle.";
RL   PLoS Genet. 7:e1002007-e1002007(2011).
RN   [2] {ECO:0000313|EnsemblMetazoa:XP_012057985.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (APR-2016) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate;
CC         Xref=Rhea:RHEA:46172, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00036650};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC         Evidence={ECO:0000256|ARBA:ARBA00036650};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; ADTU01018779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADTU01018780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012057985.1; XM_012202595.1.
DR   AlphaFoldDB; A0A158NKC7; -.
DR   STRING; 12957.A0A158NKC7; -.
DR   EnsemblMetazoa; XM_012202595.1; XP_012057985.1; LOC105621125.
DR   GeneID; 105621125; -.
DR   KEGG; acep:105621125; -.
DR   eggNOG; KOG1175; Eukaryota.
DR   InParanoid; A0A158NKC7; -.
DR   OrthoDB; 144557at2759; -.
DR   Proteomes; UP000005205; Unassembled WGS sequence.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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   PANTHER; PTHR43347; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43347:SF3; ACYL-COA SYNTHETASE SHORT-CHAIN FAMILY MEMBER 3, MITOCHONDRIAL; 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   Reference proteome {ECO:0000313|Proteomes:UP000005205}.
FT   DOMAIN          52..106
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          113..495
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          560..638
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   685 AA;  76721 MW;  C6EC566E93E11486 CRC64;
     MLHRMKPDFL DAESESSRKT CLESCIVRPR ISRKGDSNDY IMNPHCNDCP TYEEAYRKSL
     ESPEEFWGEI AGCLDWNKPW HKVLDNSNEP FTKWFIGGEL NACYNAVDRH VHAGYGEKTA
     LIHDSPQTSS IRKVTYNELL EKTSVLAGAL ADLGIRKGDR VIIYMPLIPE TIIAILATAR
     LGAIHSVVFG GFAANELASR IDHAKSKVII AASCGLEPSK VIKYTTMLNN ALDMIIVPKP
     KCIVFQRRNV WEAPLFESQF DWDDIMKRSK PHPCVMVEAN DPLYILYTSG TTGEPKGILR
     PIGGHLVSLC WSMQTIYGLN KNSIWWVASD MGWVVGHSYI CYGPLVKGAT SIMYEGKPDR
     TPDAGQYFRL IEQHSINGIF CVPTALRVIK RADPETLLGK KYSLKSLKTI FVAGEFCDYE
     TKAWAEKTFK VPILNHWWQS ETGHPITALC LGYGHYANLP KFSTGLPIPG YEIHVLREDG
     SKAPQHELGR IAIKLPLPPG FMLTLYQASE RFKQVYFSTF PGYYDTMDAG YIDEFGYVYV
     TARDDDIINV AGHRISTSAL EDIILGHANV VDAAVIGVPD HMKGEVPLCL YVRREDATSN
     EEEINQELIA RVRKMLGPIA SFRTVAAITA LPRTRSGKII RKAIATLARS KQVKISSTIE
     DPTVFREIKK VLQKLGYAKL APDPQ
//
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