Y5428_STRAW
ID Y5428_STRAW Reviewed; 409 AA.
AC Q82CC3;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Uncharacterized N-acetyltransferase SAV_5428 {ECO:0000255|HAMAP-Rule:MF_01812};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_01812};
GN OrderedLocusNames=SAV_5428;
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; BAC73140.1; -; Genomic_DNA.
DR RefSeq; WP_010986831.1; NZ_JZJK01000066.1.
DR AlphaFoldDB; Q82CC3; -.
DR SMR; Q82CC3; -.
DR STRING; 227882.SAV_5428; -.
DR PRIDE; Q82CC3; -.
DR EnsemblBacteria; BAC73140; BAC73140; SAVERM_5428.
DR KEGG; sma:SAVERM_5428; -.
DR eggNOG; COG4552; Bacteria.
DR HOGENOM; CLU_050659_0_0_11; -.
DR OMA; WNEGRWR; -.
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..409
FT /note="Uncharacterized N-acetyltransferase SAV_5428"
FT /id="PRO_0000220264"
FT DOMAIN 3..162
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT ACT_SITE 409
FT /note="Proton acceptor; via carboxylate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT BINDING 82..84
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT BINDING 90..95
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT BINDING 118..119
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
SQ SEQUENCE 409 AA; 44816 MW; 1BD492984F05D8A9 CRC64;
MTTDVRVLRQ DDWNLWYDTL IRAFGGVAEA SEERELWQTL TECDRSIGVW DGDACVGTAG
AFSFRVTVPG GASVPAAGIT MVSVAATHRR RGVLTAMMRR QLDDIRSWGE PLAVLTASEP
AIYGRFGYGI GTHQLTADVD TSRVRLSVPP GTDDVRLRYA VPADVLDVCE AVYARLVPGR
PGMPARRPGW DRLMVLDPES RRDGASPLQC VVAERDGETV GYTRFRVKPD WEPSGPKGTV
VLQDLEALDP AAHAALWRFL FDIDLTSHLN ARNRPLDEAW LHLVSDIRRC NLRKRDSLHV
RLVDVGAALE ARTYQAPVDV VFEVEDAFCP WNEGRWRLTG DGKGATCVRT RDSVDLALSV
RDLGAAYLGG VSLVSLGAAG RVRELRPGAL TEATSAFSSA IAPWLPHGF