ID   DAPC_MYCTO              Reviewed;         397 AA.
AC   P9WPZ4; L0T542; O53870; Q7D954;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Probable N-succinyldiaminopimelate aminotransferase DapC;
DE   AltName: Full=DAP-AT;
DE            EC=2.6.1.17;
GN   Name=dapC; OrderedLocusNames=MT0881;
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: Involved in the lysine biosynthetic pathways. It catalyzes
CC       the transfer of an amino group from L-glutamate to N-succinyl-2-l-
CC       amino-6-oxoheptanedioate (N-succinyl-2-l-amino-6-ketopimelate) in a
CC       PLP-dependent reaction, yielding as products N-succinyl-l-2,6-
CC       diaminoheptanedioate (N-succinyl-diaminopimelate) and 2-oxoglutarate
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate =
CC         (S)-2-succinylamino-6-oxoheptanedioate + L-glutamate;
CC         Xref=Rhea:RHEA:11960, ChEBI:CHEBI:15685, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58087; EC=2.6.1.17;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC       (succinylase route): step 2/3.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45122.1; -; Genomic_DNA.
DR   PIR; B70815; B70815.
DR   RefSeq; WP_003404420.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPZ4; -.
DR   SMR; P9WPZ4; -.
DR   EnsemblBacteria; AAK45122; AAK45122; MT0881.
DR   GeneID; 45424824; -.
DR   KEGG; mtc:MT0881; -.
DR   PATRIC; fig|83331.31.peg.946; -.
DR   HOGENOM; CLU_017584_4_0_11; -.
DR   UniPathway; UPA00034; UER00020.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009016; F:succinyldiaminopimelate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aminotransferase; Cytoplasm; Lysine biosynthesis;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..397
FT                   /note="Probable N-succinyldiaminopimelate aminotransferase
FT                   DapC"
FT                   /id="PRO_0000426865"
FT   BINDING         109..110
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         218..222
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         232
FT                   /note="N6-(pyridoxal phosphate)lysine"
SQ   SEQUENCE   397 AA;  42209 MW;  2667A0F603D1C4F5 CRC64;
     MTVSRLRPYA TTVFAEMSAL ATRIGAVNLG QGFPDEDGPP KMLQAAQDAI AGGVNQYPPG
     PGSAPLRRAI AAQRRRHFGV DYDPETEVLV TVGATEAIAA AVLGLVEPGS EVLLIEPFYD
     SYSPVVAMAG AHRVTVPLVP DGRGFALDAD ALRRAVTPRT RALIINSPHN PTGAVLSATE
     LAAIAEIAVA ANLVVITDEV YEHLVFDHAR HLPLAGFDGM AERTITISSA AKMFNCTGWK
     IGWACGPAEL IAGVRAAKQY LSYVGGAPFQ PAVALALDTE DAWVAALRNS LRARRDRLAA
     GLTEIGFAVH DSYGTYFLCA DPRPLGYDDS TEFCAALPEK VGVAAIPMSA FCDPAAGQAS
     QQADVWNHLV RFTFCKRDDT LDEAIRRLSV LAERPAT