Y3976_STRGG
ID Y3976_STRGG Reviewed; 416 AA.
AC B1VS51;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Uncharacterized N-acetyltransferase SGR_3976 {ECO:0000255|HAMAP-Rule:MF_01812};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_01812};
GN OrderedLocusNames=SGR_3976;
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=455632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350;
RX PubMed=18375553; DOI=10.1128/jb.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG20805.1; -; Genomic_DNA.
DR RefSeq; WP_012380280.1; NC_010572.1.
DR AlphaFoldDB; B1VS51; -.
DR SMR; B1VS51; -.
DR STRING; 455632.SGR_3976; -.
DR EnsemblBacteria; BAG20805; BAG20805; SGR_3976.
DR GeneID; 6209377; -.
DR KEGG; sgr:SGR_3976; -.
DR eggNOG; COG4552; Bacteria.
DR HOGENOM; CLU_050659_0_0_11; -.
DR OMA; RRPWCPD; -.
DR OrthoDB; 1497065at2; -.
DR Proteomes; UP000001685; 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; Transferase.
FT CHAIN 1..416
FT /note="Uncharacterized N-acetyltransferase SGR_3976"
FT /id="PRO_1000187721"
FT DOMAIN 3..150
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT ACT_SITE 124
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT ACT_SITE 416
FT /note="Proton acceptor; via carboxylate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT BINDING 83..85
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT BINDING 91..96
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
SQ SEQUENCE 416 AA; 44975 MW; 11F0CA64704A2A61 CRC64;
MSLDVRTITP SESAEWMRAV STGFLTAGTP SEELVADRFA GADLSRTQGA FEAGRCVATF
RSFAQELTVV GGATVAADAI SGVTVTPTHR RRGLLSRMMA TDLAAAKERG EPVASLIAAE
YPIYGRYGFG PAAWTSVWEV SVYRAGLDAR RSGQPADGGR IEMVDGADVR KLGPEVHGAL
AARQPGVVTR DERWWRQRTG AAPSSAHEKW TEPFYVVHRA ADGTVDGLMT YGTDDTWGDA
KQPLNTASVR DMIALNPAAE RALWHYLCSI DWITTIRSGY RAPDDLLPLL LPDPRAARMI
TNADWLWLRM LDVPRALEAR TYGTEASLVL EVRDDAGLAG GRFLLDASTG GARCVSTTRS
ADLVLGVAEL ATLYLGDESV RRLVDLGRAE ESRAGAATTA DAVFRTGRRP WCPDVF