Y802_MYCTU
ID Y802_MYCTU Reviewed; 218 AA.
AC P9WQG7; 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 35.
DE RecName: Full=Putative succinyl-CoA transferase Rv0802c;
DE EC=2.8.3.-;
GN OrderedLocusNames=Rv0802c;
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 IDENTIFICATION.
RX PubMed=16400876; DOI=10.1556/amicr.52.2005.3-4.8;
RA Kovacs L., Csanadi A., Kiss E., Miczak A.;
RT "Rv0802c acetyltransferase from Mycobacterium tuberculosis H37Rv.";
RL Acta Microbiol. Immunol. Hung. 52:363-371(2005).
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP SUBUNIT, AND PUTATIVE FUNCTION.
RX PubMed=18997321; DOI=10.1107/s1744309108031679;
RA Vetting M.W., Errey J.C., Blanchard J.S.;
RT "Rv0802c from Mycobacterium tuberculosis: the first structure of a
RT succinyltransferase with the GNAT fold.";
RL Acta Crystallogr. F 64:978-985(2008).
CC -!- FUNCTION: May function as a succinyl-CoA transferase.
CC {ECO:0000305|PubMed:18997321}.
CC -!- SUBUNIT: Dimer of dimers. {ECO:0000269|PubMed:18997321}.
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; CCP43550.1; -; Genomic_DNA.
DR PIR; C70536; C70536.
DR RefSeq; NP_215317.1; NC_000962.3.
DR RefSeq; WP_003404111.1; NZ_NVQJ01000064.1.
DR PDB; 2VZY; X-ray; 2.00 A; A/B/C/D=1-218.
DR PDB; 2VZZ; X-ray; 2.30 A; A/B/C/D=1-218.
DR PDBsum; 2VZY; -.
DR PDBsum; 2VZZ; -.
DR AlphaFoldDB; P9WQG7; -.
DR SMR; P9WQG7; -.
DR STRING; 83332.Rv0802c; -.
DR PaxDb; P9WQG7; -.
DR PRIDE; P9WQG7; -.
DR DNASU; 885332; -.
DR GeneID; 885332; -.
DR KEGG; mtu:Rv0802c; -.
DR TubercuList; Rv0802c; -.
DR eggNOG; COG1670; Bacteria.
DR OMA; WEAHRTV; -.
DR PhylomeDB; P9WQG7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0008999; F:ribosomal protein S5-alanine N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0017198; P:N-terminal peptidyl-serine acetylation; IBA:GO_Central.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..218
FT /note="Putative succinyl-CoA transferase Rv0802c"
FT /id="PRO_0000414586"
FT DOMAIN 32..188
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:18997321"
FT BINDING 109..113
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:18997321"
FT BINDING 119..124
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:18997321"
FT BINDING 145..151
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:18997321"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:18997321"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:2VZY"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2VZY"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:2VZY"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:2VZY"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:2VZZ"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2VZZ"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:2VZZ"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:2VZY"
FT STRAND 77..86
FT /evidence="ECO:0007829|PDB:2VZY"
FT STRAND 89..100
FT /evidence="ECO:0007829|PDB:2VZY"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:2VZY"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:2VZY"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2VZY"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2VZZ"
FT HELIX 122..136
FT /evidence="ECO:0007829|PDB:2VZY"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:2VZY"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:2VZY"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:2VZY"
FT STRAND 176..186
FT /evidence="ECO:0007829|PDB:2VZY"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:2VZY"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:2VZY"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:2VZY"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:2VZY"
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
