FADA4_MYCTU
ID FADA4_MYCTU Reviewed; 393 AA.
AC P9WG69; L0T6A9; P66926; Q10629;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Probable acetyl-CoA acetyltransferase;
DE EC=2.3.1.9;
DE AltName: Full=Acetoacetyl-CoA thiolase;
DE Contains:
DE RecName: Full=Probable acetyl-CoA acetyltransferase, propeptide removed;
GN Name=fadA4; OrderedLocusNames=Rv1323; ORFNames=MTCY130.08;
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 PROTEIN SEQUENCE OF 2-11, PROTEIN SEQUENCE OF 3-11, AND SEQUENCE REVISION
RP TO N-TERMINUS.
RC STRAIN=H37Rv;
RX PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT annotated encoding genes.";
RL Genomics 114:292-304(2022).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10020};
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
CC -!- CAUTION: The revised start codon for this protein is ATA.
CC {ECO:0000269|PubMed:34915127}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP44081.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR EMBL; AL123456; CCP44081.1; ALT_INIT; Genomic_DNA.
DR PIR; G70769; G70769.
DR RefSeq; NP_215839.1; NC_000962.3.
DR RefSeq; WP_003898824.1; NC_018143.2.
DR AlphaFoldDB; P9WG69; -.
DR SMR; P9WG69; -.
DR STRING; 83332.Rv1323; -.
DR PaxDb; P9WG69; -.
DR DNASU; 886904; -.
DR GeneID; 886904; -.
DR KEGG; mtu:Rv1323; -.
DR PATRIC; fig|83332.111.peg.1478; -.
DR TubercuList; Rv1323; -.
DR eggNOG; COG0183; Bacteria.
DR OMA; ICPSIAI; -.
DR PhylomeDB; P9WG69; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; 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 GO; GO:0052572; P:response to host immune response; IEP:MTBBASE.
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 Acyltransferase; Direct protein sequencing; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:34915127"
FT CHAIN 2..393
FT /note="Probable acetyl-CoA acetyltransferase"
FT /id="PRO_0000206458"
FT PROPEP 2
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:34915127"
FT /id="PRO_0000455386"
FT CHAIN 3..393
FT /note="Probable acetyl-CoA acetyltransferase, propeptide
FT removed"
FT /id="PRO_0000455387"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ SEQUENCE 393 AA; 40469 MW; 891C4EADC74B1418 CRC64;
MTTSVIVAGA RTPIGKLMGS LKDFSASELG AIAIKGALEK ANVPASLVEY VIMGQVLTAG
AGQMPARQAA VAAGIGWDVP ALTINKMCLS GIDAIALADQ LIRAREFDVV VAGGQESMTK
APHLLMNSRS GYKYGDVTVL DHMAYDGLHD VFTDQPMGAL TEQRNDVDMF TRSEQDEYAA
ASHQKAAAAW KDGVFADEVI PVNIPQRTGD PLQFTEDEGI RANTTAAALA GLKPAFRGDG
TITAGSASQI SDGAAAVVVM NQEKAQELGL TWLAEIGAHG VVAGPDSTLQ SQPANAINKA
LDREGISVDQ LDVVEINEAF AAVALASIRE LGLNPQIVNV NGGAIAVGHP LGMSGTRITL
HAALQLARRG SGVGVAALCG AGGQGDALIL RAG
