ID B2HIZ6_MYCMM Unreviewed; 280 AA. AC B2HIZ6; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 27-MAR-2024, entry version 82. DE SubName: Full=Arylamine N-acetyltransferase Nat {ECO:0000313|EMBL:ACC43459.1}; GN Name=nat {ECO:0000313|EMBL:ACC43459.1}; GN OrderedLocusNames=MMAR_5055 {ECO:0000313|EMBL:ACC43459.1}; OS Mycobacterium marinum (strain ATCC BAA-535 / M). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium ulcerans group. OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC43459.1, ECO:0000313|Proteomes:UP000001190}; RN [1] {ECO:0000313|EMBL:ACC43459.1, ECO:0000313|Proteomes:UP000001190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190}; RX PubMed=18403782; DOI=10.1101/gr.075069.107; RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A., RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R., RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.; RT "Insights from the complete genome sequence of Mycobacterium marinum on the RT evolution of Mycobacterium tuberculosis."; RL Genome Res. 18:729-741(2008). RN [2] {ECO:0007829|PDB:2VFB, ECO:0007829|PDB:2VFC} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH COENZYME A. RX PubMed=18005984; DOI=10.1016/j.jmb.2007.10.019; RA Fullam E., Westwood I.M., Anderton M.C., Lowe E.D., Sim E., Noble M.E.; RT "Divergence of cofactor recognition across evolution: coenzyme A binding in RT a prokaryotic arylamine N-acetyltransferase."; RL J. Mol. Biol. 375:178-191(2008). RN [3] {ECO:0007829|PDB:3LTW} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS). RX PubMed=21203950; DOI=10.1007/s13238-010-0037-7; RA Abuhammad A.M., Lowe E.D., Fullam E., Noble M., Garman E.F., Sim E.; RT "Probing the architecture of the Mycobacterium marinum arylamine N- RT acetyltransferase active site."; RL Protein Cell 1:384-392(2010). RN [4] {ECO:0007829|PDB:4B55} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS). RX PubMed=23285185; DOI=10.1371/journal.pone.0052790; RA Abuhammad A., Fullam E., Lowe E.D., Staunton D., Kawamura A., RA Westwood I.M., Bhakta S., Garner A.C., Wilson D.L., Seden P.T., RA Davies S.G., Russell A.J., Garman E.F., Sim E.; RT "Piperidinols that show anti-tubercular activity as inhibitors of arylamine RT N-acetyltransferase: an essential enzyme for mycobacterial survival inside RT macrophages."; RL PLoS ONE 7:e52790-e52790(2012). RN [5] {ECO:0007829|PDB:4C5P} RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS). RA Abuhammad A.; RT "Arylamine N-Acetyltransferases from Mycobacteria: Investigations of a RT Potential Target for Anti- Tubercular Therapy."; RL Submitted (SEP-2013) to the PDB data bank. CC -!- SIMILARITY: Belongs to the arylamine N-acetyltransferase family. CC {ECO:0000256|ARBA:ARBA00006547}. 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; CP000854; ACC43459.1; -; Genomic_DNA. DR RefSeq; WP_012396579.1; NC_010612.1. DR PDB; 2VFB; X-ray; 2.00 A; A=1-280. DR PDB; 2VFC; X-ray; 2.70 A; A/B=1-280. DR PDB; 3LTW; X-ray; 2.10 A; A=1-280. DR PDB; 4B55; X-ray; 2.70 A; A=1-280. DR PDB; 4C5P; X-ray; 1.59 A; A=1-280. DR PDBsum; 2VFB; -. DR PDBsum; 2VFC; -. DR PDBsum; 3LTW; -. DR PDBsum; 4B55; -. DR PDBsum; 4C5P; -. DR AlphaFoldDB; B2HIZ6; -. DR SMR; B2HIZ6; -. DR STRING; 216594.MMAR_5055; -. DR KEGG; mmi:MMAR_5055; -. DR eggNOG; COG2162; Bacteria. DR HOGENOM; CLU_049918_1_1_11; -. DR OrthoDB; 7181050at2; -. DR BRENDA; 2.3.1.5; 3506. DR EvolutionaryTrace; B2HIZ6; -. DR Proteomes; UP000001190; Chromosome. DR GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro. DR Gene3D; 3.30.2140.10; Arylamine N-acetyltransferase; 1. DR Gene3D; 2.40.128.150; Cysteine proteinases; 1. DR InterPro; IPR001447; Arylamine_N-AcTrfase. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR PANTHER; PTHR11786:SF0; ARYLAMINE N-ACETYLTRANSFERASE 1-RELATED; 1. DR PANTHER; PTHR11786; N-HYDROXYARYLAMINE O-ACETYLTRANSFERASE; 1. DR Pfam; PF00797; Acetyltransf_2; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2VFB, ECO:0007829|PDB:2VFC}; KW Reference proteome {ECO:0000313|Proteomes:UP000001190}; KW Transferase {ECO:0000313|EMBL:ACC43459.1}. FT BINDING 70 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:2VFC" FT BINDING 97 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:2VFC" FT BINDING 130 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:2VFC" FT BINDING 132 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:2VFC" FT BINDING 152 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:2VFC" FT BINDING 229 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:2VFC" FT BINDING 236 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:2VFC" SQ SEQUENCE 280 AA; 30635 MW; 7A8CBC3B199A1B91 CRC64; MALDLTGYLD RINYRGATDP TLDVLRDLVS AHTGAIAFEN LDPLMGVPVD DLSAEALADK LVDRRRGGYC YEHNGLIGYV LAELGYRVRR LAGRVVWLAP PDAPTPAQTH TVLAVTFPGC QGPYLVDVGF GGMTPTAPLR LETGTVQQTA LEPYRLDDRG DGLVLQAMVR DEWQALYEFS TLTRPQVDLR VGSWFVSTHP TSHFVTGLMA ATVADDARWN LMGRNLAIHR RGGTEKILLE DAAAVVDTLG DRFGINVADV GERGRLEARI DKVCFGAENR //