Y2625_STRCO
ID Y2625_STRCO Reviewed; 413 AA.
AC Q9F309;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Uncharacterized N-acetyltransferase SCO2625 {ECO:0000255|HAMAP-Rule:MF_01812};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_01812};
GN OrderedLocusNames=SCO2625; ORFNames=SCC80.10;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; AL939113; CAC10001.1; -; Genomic_DNA.
DR RefSeq; NP_626861.1; NC_003888.3.
DR RefSeq; WP_011028461.1; NZ_VNID01000001.1.
DR AlphaFoldDB; Q9F309; -.
DR SMR; Q9F309; -.
DR STRING; 100226.SCO2625; -.
DR GeneID; 1098059; -.
DR KEGG; sco:SCO2625; -.
DR PATRIC; fig|100226.15.peg.2671; -.
DR eggNOG; COG4552; Bacteria.
DR HOGENOM; CLU_050659_0_0_11; -.
DR InParanoid; Q9F309; -.
DR OMA; WNEGRWR; -.
DR PhylomeDB; Q9F309; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0034069; F:aminoglycoside N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0030649; P:aminoglycoside antibiotic catabolic process; IBA:GO_Central.
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..413
FT /note="Uncharacterized N-acetyltransferase SCO2625"
FT /id="PRO_0000220266"
FT DOMAIN 3..155
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT ACT_SITE 127
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT ACT_SITE 413
FT /note="Proton acceptor; via carboxylate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT BINDING 86..88
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT BINDING 94..99
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT BINDING 122..123
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
SQ SEQUENCE 413 AA; 44719 MW; 29869DA00AD7AB0A CRC64;
MTMEPRVLRR EEWDSWYGSL IRAFGGVPEP AEELELFREL TRVDRSIGVW ERDGEAEACV
GTTGSFDFRM TVPGGAQVRA AGVTMVSVAA THRRRGVLTS MMRRQLDDVR AWGEPLAVLT
ASEPAIYGRF GYGAATFSLS AEIDTSRVRL SVPAGTDDVR LRYAAPADVL DACEAVYARL
VPGRPGMLAR RPGWERLALL DPESGRDGAS PLQCVVARRG GEVTGFARFR VRPAWGPEGA
GGTVVLDDLA GLDPATEAAL WRFLYDVDLT SRLAVRGRPV DEAWQYQVSD IRRCRPESRD
ALYVRLVDVG AALAARTYQA PVDVVFEVED AFCPWNAGRW RLSGDAKGAS CERTSDGADL
ALSVRELGAA YLGGVRLSSL GAAGRVREVR AGALAEASVG FGSDVAPWLP HGF