ID Y0859_MYCTU Reviewed; 403 AA. AC O53871; L0T7Y0; DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 143. DE RecName: Full=Putative acyltransferase Rv0859; DE EC=2.3.1.-; GN Name=fadA; OrderedLocusNames=Rv0859; OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=83332; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., RA Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the complete RT genome sequence."; RL Nature 393:537-544(1998). RN [2] RP PUPYLATION AT LYS-189, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=20066036; DOI=10.1371/journal.pone.0008589; RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E., RA Gygi S.P., Darwin K.H.; RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium RT tuberculosis."; RL PLoS ONE 5:E8589-E8589(2010). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=21969609; DOI=10.1074/mcp.m111.011445; RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K., RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R., RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M., RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution RT mass spectrometry."; RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011). CC -!- PTM: Pupylated at Lys-189 by the prokaryotic ubiquitin-like protein CC Pup, which probably leads to its degradation by the proteasome. CC {ECO:0000269|PubMed:20066036}. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family. CC {ECO:0000305}. 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; AL123456; CCP43607.1; -; Genomic_DNA. DR PIR; C70815; C70815. DR RefSeq; NP_215374.1; NC_000962.3. DR RefSeq; WP_009934956.1; NZ_NVQJ01000040.1. DR PDB; 4B3H; X-ray; 2.30 A; C/D=1-403. DR PDB; 4B3I; X-ray; 2.63 A; C/D=1-403. DR PDB; 4B3J; X-ray; 2.50 A; C/D=1-403. DR PDB; 7O1G; X-ray; 3.03 A; D=1-403. DR PDB; 7O1I; X-ray; 2.30 A; D=1-403. DR PDB; 7O1J; X-ray; 2.36 A; D=1-403. DR PDB; 7O1K; X-ray; 2.86 A; C/D=1-403. DR PDB; 7O1L; X-ray; 2.38 A; D=1-403. DR PDB; 7O1M; X-ray; 2.89 A; D=1-403. DR PDB; 7O4Q; X-ray; 2.10 A; C=1-403. DR PDB; 7O4R; X-ray; 2.79 A; C/D=1-403. DR PDB; 7O4S; X-ray; 2.79 A; C/D=1-403. DR PDB; 7O4T; X-ray; 2.10 A; C/D=1-403. DR PDB; 7O4V; X-ray; 2.42 A; C/D=1-403. DR PDBsum; 4B3H; -. DR PDBsum; 4B3I; -. DR PDBsum; 4B3J; -. DR PDBsum; 7O1G; -. DR PDBsum; 7O1I; -. DR PDBsum; 7O1J; -. DR PDBsum; 7O1K; -. DR PDBsum; 7O1L; -. DR PDBsum; 7O1M; -. DR PDBsum; 7O4Q; -. DR PDBsum; 7O4R; -. DR PDBsum; 7O4S; -. DR PDBsum; 7O4T; -. DR PDBsum; 7O4V; -. DR AlphaFoldDB; O53871; -. DR SMR; O53871; -. DR STRING; 83332.Rv0859; -. DR PaxDb; 83332-Rv0859; -. DR DNASU; 885774; -. DR GeneID; 885774; -. DR KEGG; mtu:Rv0859; -. DR TubercuList; Rv0859; -. DR eggNOG; COG0183; Bacteria. DR InParanoid; O53871; -. DR OrthoDB; 9764638at2; -. DR PhylomeDB; O53871; -. DR Proteomes; UP000001584; Chromosome. DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE. DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE. DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro. DR CDD; cd00751; thiolase; 1. DR Gene3D; 3.40.47.10; -; 2. DR InterPro; IPR002155; Thiolase. DR InterPro; IPR016039; Thiolase-like. DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS. DR InterPro; IPR020610; Thiolase_AS. DR InterPro; IPR020617; Thiolase_C. DR InterPro; IPR020613; Thiolase_CS. DR InterPro; IPR020616; Thiolase_N. DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1. DR PANTHER; PTHR43365; BLR7806 PROTEIN; 1. DR PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 1. DR Pfam; PF02803; Thiolase_C; 1. DR Pfam; PF00108; Thiolase_N; 1. DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1. DR SUPFAM; SSF53901; Thiolase-like; 2. DR PROSITE; PS00098; THIOLASE_1; 1. DR PROSITE; PS00737; THIOLASE_2; 1. DR PROSITE; PS00099; THIOLASE_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Isopeptide bond; Reference proteome; KW Transferase; Ubl conjugation. FT CHAIN 1..403 FT /note="Putative acyltransferase Rv0859" FT /id="PRO_0000395883" FT ACT_SITE 92 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000250" FT ACT_SITE 359 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020" FT ACT_SITE 389 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020" FT CROSSLNK 189 FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain FT with Q-Cter in protein Pup)" FT /evidence="ECO:0000269|PubMed:20066036" FT STRAND 6..12 FT /evidence="ECO:0007829|PDB:7O4Q" FT STRAND 16..20 FT /evidence="ECO:0007829|PDB:7O4Q" FT TURN 22..25 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 28..42 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:7O4Q" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:7O4Q" FT TURN 66..68 FT /evidence="ECO:0007829|PDB:7O4T" FT HELIX 69..76 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:7O4T" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 91..93 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 94..107 FT /evidence="ECO:0007829|PDB:7O4Q" FT STRAND 112..121 FT /evidence="ECO:0007829|PDB:7O4Q" FT TURN 122..124 FT /evidence="ECO:0007829|PDB:7O4Q" FT TURN 127..130 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 133..136 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 138..144 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 149..160 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 164..183 FT /evidence="ECO:0007829|PDB:7O4Q" FT TURN 184..190 FT /evidence="ECO:0007829|PDB:7O4Q" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 215..219 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:4B3I" FT HELIX 227..230 FT /evidence="ECO:0007829|PDB:7O4Q" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 234..241 FT /evidence="ECO:0007829|PDB:7O4Q" FT STRAND 254..257 FT /evidence="ECO:0007829|PDB:7O4T" FT STRAND 261..270 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 272..277 FT /evidence="ECO:0007829|PDB:7O4Q" FT STRAND 284..293 FT /evidence="ECO:0007829|PDB:7O4Q" FT TURN 296..298 FT /evidence="ECO:0007829|PDB:7O4Q" FT TURN 300..302 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 303..314 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 318..320 FT /evidence="ECO:0007829|PDB:7O4Q" FT STRAND 322..326 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 331..341 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 345..347 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 354..357 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 361..379 FT /evidence="ECO:0007829|PDB:7O4Q" FT STRAND 383..389 FT /evidence="ECO:0007829|PDB:7O4Q" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:7O4Q" FT STRAND 394..402 FT /evidence="ECO:0007829|PDB:7O4Q" SQ SEQUENCE 403 AA; 42414 MW; 840EABC43EB7FE94 CRC64; MSEEAFIYEA IRTPRGKQKN GSLHEVKPLS LVVGLIDELR KRHPDLDENL ISDVILGCVS PVGDQGGDIA RAAVLASGMP VTSGGVQLNR FCASGLEAVN TAAQKVRSGW DDLVLAGGVE SMSRVPMGSD GGAMGLDPAT NYDVMFVPQS IGADLIATIE GFSREDVDAY ALRSQQKAAE AWSGGYFAKS VVPVRDQNGL LILDHDEHMR PDTTKEGLAK LKPAFEGLAA LGGFDDVALQ KYHWVEKINH VHTGGNSSGI VDGAALVMIG SAAAGKLQGL TPRARIVATA TSGADPVIML TGPTPATRKV LDRAGLTVDD IDLFELNEAF ASVVLKFQKD LNIPDEKLNV NGGAIAMGHP LGATGAMILG TMVDELERRN ARRALITLCI GGGMGVATII ERV //