Y4024_STRAW
ID Y4024_STRAW Reviewed; 418 AA.
AC Q82G74;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Uncharacterized N-acetyltransferase SAV_4024 {ECO:0000255|HAMAP-Rule:MF_01812};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_01812};
GN OrderedLocusNames=SAV_4024;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_01812}.
CC -!- SIMILARITY: Belongs to the acetyltransferase Eis family.
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DR EMBL; BA000030; BAC71736.1; -; Genomic_DNA.
DR RefSeq; WP_010985453.1; NZ_JZJK01000060.1.
DR AlphaFoldDB; Q82G74; -.
DR SMR; Q82G74; -.
DR STRING; 227882.SAV_4024; -.
DR PRIDE; Q82G74; -.
DR EnsemblBacteria; BAC71736; BAC71736; SAVERM_4024.
DR KEGG; sma:SAVERM_4024; -.
DR eggNOG; COG4552; Bacteria.
DR HOGENOM; CLU_050659_0_0_11; -.
DR OMA; RRPWCPD; -.
DR OrthoDB; 1497065at2; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1050.10; -; 1.
DR HAMAP; MF_01812; Eis; 1.
DR InterPro; IPR041380; Acetyltransf_17.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR025559; Eis_dom.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR022902; NAcTrfase_Eis.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR Pfam; PF17668; Acetyltransf_17; 1.
DR Pfam; PF13530; SCP2_2; 1.
DR SUPFAM; SSF55718; SSF55718; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..418
FT /note="Uncharacterized N-acetyltransferase SAV_4024"
FT /id="PRO_0000220263"
FT DOMAIN 7..158
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT ACT_SITE 128
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT ACT_SITE 418
FT /note="Proton acceptor; via carboxylate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT BINDING 87..89
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT BINDING 95..100
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
SQ SEQUENCE 418 AA; 46001 MW; 724C85A9721C5BEB CRC64;
MSRPDDIDVR PIAEAETADW IRALNTGFLR SPEVSEREVA DRSSYLVPAR TLGAFDNGRC
VATFRSFPQE LTAVGGASVP ADAISNVTVT ATHRRRGLLT RMMAQDLAAA KERGDVVATL
IAAEYPIYGR YGFGAATHST EWTIDVPRTG LDPRWSGPGD GGRIDLVDGE DVRKAGPELH
ERLRRTQPGA VSRDERWWQV HTGVVRLDRS PWTEPFYAVY RSASGEVEGL VSYECDDHWG
DAKQPQNTAK VNWLIATTPA AERALWHYLC SIDWITKVRT GWRAPDDLLP HFLPDPRAAR
VTTHADWLWV RILDVVRALE ARTYDGSGTL VLDVVDRHGL AGGRYRLTVG PDGAVCEPTT
RDAGLTLDVG ELAALWLGDA SAVRLAALGR VREQQEGAAS VADALLRTSG RPWCPDMF