Y0859_MYCTU
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 03-AUG-2022, entry version 136.
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; Actinobacteria; Corynebacteriales; 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.m111.011627;
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}.
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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; O53871; -.
DR DNASU; 885774; -.
DR GeneID; 885774; -.
DR KEGG; mtu:Rv0859; -.
DR TubercuList; Rv0859; -.
DR eggNOG; COG0183; Bacteria.
DR InParanoid; O53871; -.
DR OMA; GIWEINE; -.
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:0003985; F:acetyl-CoA C-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
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 Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
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
