ID MSHD_NOCSJ Reviewed; 295 AA. AC A1SPL0; DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 22-FEB-2012, entry version 35. DE RecName: Full=Mycothiol acetyltransferase; DE Short=MSH acetyltransferase; DE EC=2.3.1.189; DE AltName: Full=Mycothiol synthase; GN Name=mshD; OrderedLocusNames=Noca_4248; OS Nocardioides sp. (strain BAA-499 / JS614). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Nocardioidaceae; Nocardioides. OX NCBI_TaxID=196162; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAA-499 / JS614; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Mattes T., Gossett J., Richardson P.; RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of acetyl from acetyl-CoA to CC desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol (By CC similarity). CC -!- CATALYTIC ACTIVITY: Desacetylmycothiol + acetyl-CoA = mycothiol + CC coenzyme-A. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SIMILARITY: Belongs to the acetyltransferase family. MshD CC subfamily. CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000509; ABL83745.1; -; Genomic_DNA. DR RefSeq; YP_925432.1; NC_008699.1. DR ProteinModelPortal; A1SPL0; -. DR STRING; A1SPL0; -. DR GeneID; 4596762; -. DR GenomeReviews; CP000509_GR; Noca_4248. DR KEGG; nca:Noca_4248; -. DR PATRIC; 22750627; VBINocSp122728_4544. DR eggNOG; COG0456; -. DR HOGENOM; HBG292446; -. DR KO; K15520; -. DR OMA; TILHEST; -. DR BioCyc; NSP35761:NOCA_4248-MONOMER; -. DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro. DR HAMAP; MF_01698; MshD; 1; -. DR InterPro; IPR000182; AcTrfase_GCN5-related_dom. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR017813; Mycothiol_AcTrfase. DR Gene3D; G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 2. DR PANTHER; PTHR23091:SF29; PTHR23091:SF29; 1. DR Pfam; PF00583; Acetyltransf_1; 1. DR PIRSF; PIRSF021524; MSH_acetyltransferase; 1. DR SUPFAM; SSF55729; Acyl_CoA_acyltransferase; 1. DR TIGRFAMs; TIGR03448; Mycothiol_MshD; 1. DR PROSITE; PS51186; GNAT; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Repeat; Transferase. FT CHAIN 1 295 Mycothiol acetyltransferase. FT /FTId=PRO_0000400286. FT DOMAIN 137 295 N-acetyltransferase. FT REGION 62 64 Acetyl-CoA binding 1 (By similarity). FT REGION 231 233 Acetyl-CoA binding 2 (By similarity). FT REGION 238 244 Acetyl-CoA binding 2 (By similarity). FT BINDING 30 30 Desacetylmycothiol; via amide nitrogen FT (By similarity). FT BINDING 165 165 Desacetylmycothiol (By similarity). FT BINDING 209 209 Desacetylmycothiol (By similarity). FT BINDING 227 227 Desacetylmycothiol (By similarity). FT BINDING 265 265 Desacetylmycothiol; via carbonyl oxygen FT (By similarity). SQ SEQUENCE 295 AA; 30832 MW; 66A164AED8AB7224 CRC64; MDDHAADLLA AVAEVARAAE AADGAAPLDE ATWLALRHHP ERVRSWVRAG GFALVIGADL SLVVHPQARG RGLGAGLLSS ALAGLSAGMP LEAWSHGDHP AAAALARSHG FERARELWVM RRQMASALPQ LRAPDGVTVR AFRADSGDAE EVLRVNAAAF AHHPEQGSMD ATNLAERMAE PWFDPDGLLL ATSAAADGGE QVLGFHWTKV HPGDAGAGAG PGVEVGEVYV VGIDPAAQGR GLGKVLTLAG LHHLAGRGVP EVLLYVESDN RPAIAVYAGL GFTHADDDTH VQYRR //