ID   Y802_MYCTO              Reviewed;         218 AA.
AC   P9WQG6; L0T4S8; O06632; Q7D995;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Putative succinyl-CoA transferase MT0822;
DE            EC=2.8.3.-;
GN   OrderedLocusNames=MT0822;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: May function as a succinyl-CoA transferase. {ECO:0000250}.
CC   -!- SUBUNIT: Dimer of dimers. {ECO:0000250}.
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DR   EMBL; AE000516; AAK45064.1; -; Genomic_DNA.
DR   PIR; C70536; C70536.
DR   RefSeq; WP_003404111.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQG6; -.
DR   SMR; P9WQG6; -.
DR   EnsemblBacteria; AAK45064; AAK45064; MT0822.
DR   KEGG; mtc:MT0822; -.
DR   PATRIC; fig|83331.31.peg.884; -.
DR   HOGENOM; CLU_106319_1_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF13302; Acetyltransf_3; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Transferase.
FT   CHAIN           1..218
FT                   /note="Putative succinyl-CoA transferase MT0822"
FT                   /id="PRO_0000426778"
FT   DOMAIN          32..188
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG7"
FT   BINDING         109..113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG7"
FT   BINDING         119..124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG7"
FT   BINDING         145..151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG7"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG7"
SQ   SEQUENCE   218 AA;  24983 MW;  88735487DF5EE59C CRC64;
     MSRHWPLFDL RITTPRLQLQ LPTEELCDQL IDTILEGVHD PDRMPFSVPW TRASREDLPF
     NTLSHLWQQL AGFKRDDWSL PLAVLVDGRA VGVQALSSKD FPITRQVDSG SWLGLRYQGH
     GYGTEMRAAV LYFAFAELEA QVATSRSFVD NPASIAVSRR NGYRDNGLDR VAREGAMAEA
     LLFRLTRDDW QRHRTVEVRV DGFDRCRPLF GPLEPPRY