ID DAPE_CORGL Reviewed; 369 AA.
AC Q59284; Q46066;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=Succinyl-diaminopimelate desuccinylase;
DE Short=SDAP desuccinylase;
DE EC=3.5.1.18;
GN Name=dapE; OrderedLocusNames=Cgl1109, cg1260;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=7881553; DOI=10.1099/13500872-140-12-3349;
RA Wehrmann A., Eggeling L., Sahm H.;
RT "Analysis of different DNA fragments of Corynebacterium glutamicum
RT complementing dapE of Escherichia coli.";
RL Microbiology 140:3349-3356(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=7592354; DOI=10.1128/jb.177.20.5991-5993.1995;
RA Wehrmann A., Morakkabati S., Kraemer R., Sahm H., Eggeling L.;
RT "Functional analysis of sequences adjacent to dapE of Corynebacterium
RT glutamicum reveals the presence of aroP, which encodes the aromatic amino
RT acid transporter.";
RL J. Bacteriol. 177:5991-5993(1995).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-
CC 2,6-diaminoheptanedioate + succinate; Xref=Rhea:RHEA:22608,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30031, ChEBI:CHEBI:57609,
CC ChEBI:CHEBI:58087; EC=3.5.1.18;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit.;
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC (succinylase route): step 3/3.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; X81379; CAA57141.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98502.1; -; Genomic_DNA.
DR EMBL; BX927151; CAF19815.1; -; Genomic_DNA.
DR EMBL; X85965; CAA59951.1; -; Genomic_DNA.
DR PIR; S60063; S60063.
DR RefSeq; NP_600337.1; NC_003450.3.
DR RefSeq; WP_011014127.1; NC_006958.1.
DR PDB; 3TX8; X-ray; 2.97 A; A=5-369.
DR PDBsum; 3TX8; -.
DR AlphaFoldDB; Q59284; -.
DR SMR; Q59284; -.
DR STRING; 196627.cg1260; -.
DR KEGG; cgb:cg1260; -.
DR KEGG; cgl:Cgl1109; -.
DR PATRIC; fig|196627.13.peg.1088; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_1_0_11; -.
DR OrthoDB; 7055905at2; -.
DR BioCyc; CORYNE:G18NG-10681-MONOMER; -.
DR BRENDA; 3.5.1.18; 960.
DR UniPathway; UPA00034; UER00021.
DR EvolutionaryTrace; Q59284; -.
DR Proteomes; UP000000582; Chromosome.
DR Proteomes; UP000001009; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-EC.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR CDD; cd05647; M20_DapE_actinobac; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR010174; Succinyl-DAP_deSuclase_DapE.
DR NCBIfam; TIGR01900; dapE-gram_pos; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cobalt;
KW Diaminopimelate biosynthesis; Hydrolase; Lysine biosynthesis;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..369
FT /note="Succinyl-diaminopimelate desuccinylase"
FT /id="PRO_0000185260"
FT ACT_SITE 79
FT /evidence="ECO:0000250"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:3TX8"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:3TX8"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:3TX8"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:3TX8"
FT HELIX 105..118
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:3TX8"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:3TX8"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 177..186
FT /evidence="ECO:0007829|PDB:3TX8"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3TX8"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:3TX8"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 230..238
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 247..257
FT /evidence="ECO:0007829|PDB:3TX8"
FT HELIX 263..273
FT /evidence="ECO:0007829|PDB:3TX8"
FT TURN 274..278
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:3TX8"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:3TX8"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:3TX8"
FT HELIX 323..327
FT /evidence="ECO:0007829|PDB:3TX8"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:3TX8"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:3TX8"
FT HELIX 353..368
FT /evidence="ECO:0007829|PDB:3TX8"
SQ SEQUENCE 369 AA; 39974 MW; A3A7BAEC4B36AE41 CRC64;
MNSELKPGLD LLGDPIVLTQ RLVDIPSPSG QEKQIADEIE DALRNLNLPG VEVFRFNNNV
LARTNRGLAS RVMLAGHIDT VPIADNLPSR VEDGIMYGCG TVDMKSGLAV YLHTFATLAT
STELKHDLTL IAYECEEVAD HLNGLGHIRD EHPEWLAADL ALLGEPTGGW IEAGCQGNLR
IKVTAHGVRA HSARSWLGDN AMHKLSPIIS KVAAYKAAEV NIDGLTYREG LNIVFCESGV
ANNVIPDLAW MNLNFRFAPN RDLNEAIEHV VETLELDGQD GIEWAVEDGA GGALPGLGQQ
VTSGLIDAVG REKIRAKFGW TDVSRFSAMG IPALNFGAGD PSFAHKRDEQ CPVEQITDVA
AILKQYLSE
//
