DAPA_CORGL
ID DAPA_CORGL Reviewed; 301 AA.
AC P19808; P40109;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000255|HAMAP-Rule:MF_00418};
DE Short=HTPA synthase {ECO:0000255|HAMAP-Rule:MF_00418};
DE EC=4.3.3.7 {ECO:0000255|HAMAP-Rule:MF_00418};
GN Name=dapA {ECO:0000255|HAMAP-Rule:MF_00418};
GN OrderedLocusNames=Cgl1971, cg2161;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=2129555; DOI=10.1093/nar/18.21.6421;
RA Bonnassie S., Oreglia J., Sicard A.M.;
RT "Nucleotide sequence of the dapA gene from Corynebacterium glutamicum.";
RL Nucleic Acids Res. 18:6421-6421(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RX PubMed=8478336; DOI=10.1128/jb.175.9.2743-2749.1993;
RA Pisabarro A., Malumbres M., Mateos L.M., Oguiza J.A., Martin J.F.;
RT "A cluster of three genes (dapA, orf2, and dapB) of Brevibacterium
RT lactofermentum encodes dihydrodipicolinate synthase, dihydrodipicolinate
RT reductase, and a third polypeptide of unknown function.";
RL J. Bacteriol. 175:2743-2749(1993).
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=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 [4]
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).
CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde
CC [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
CC {ECO:0000255|HAMAP-Rule:MF_00418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-
CC 2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00418};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_00418}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00418}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00418}.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000255|HAMAP-
CC Rule:MF_00418}.
CC -!- CAUTION: Was originally thought to be a dihydrodipicolinate synthase
CC (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde
CC [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was
CC shown in E.coli that the product of the enzymatic reaction is not
CC dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-
CC dipicolinic acid (HTPA), and that the consecutive dehydration reaction
CC leading to DHDP is not spontaneous but catalyzed by DapB.
CC {ECO:0000305}.
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DR EMBL; X53993; CAA37940.1; -; Genomic_DNA.
DR EMBL; Z21502; CAA79714.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99364.1; -; Genomic_DNA.
DR EMBL; BX927153; CAF20312.1; -; Genomic_DNA.
DR PIR; C40626; C40626.
DR RefSeq; NP_601177.1; NC_003450.3.
DR RefSeq; WP_011014792.1; NC_006958.1.
DR PDB; 3CPR; X-ray; 2.20 A; A/B=2-301.
DR PDBsum; 3CPR; -.
DR AlphaFoldDB; P19808; -.
DR SMR; P19808; -.
DR STRING; 196627.cg2161; -.
DR World-2DPAGE; 0001:P19808; -.
DR KEGG; cgb:cg2161; -.
DR KEGG; cgl:Cgl1971; -.
DR PATRIC; fig|196627.13.peg.1908; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_7_1_11; -.
DR OMA; GMDACVP; -.
DR BioCyc; MetaCyc:MON-6444; -.
DR BRENDA; 4.3.3.7; 960.
DR UniPathway; UPA00034; UER00017.
DR EvolutionaryTrace; P19808; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR CDD; cd00950; DHDPS; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00418; DapA; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005263; DapA.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR InterPro; IPR020624; Schiff_base-form_aldolases_CS.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR TIGRFAMs; TIGR00674; dapA; 1.
DR PROSITE; PS00665; DHDPS_1; 1.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm;
KW Diaminopimelate biosynthesis; Lyase; Lysine biosynthesis;
KW Reference proteome; Schiff base.
FT CHAIN 1..301
FT /note="4-hydroxy-tetrahydrodipicolinate synthase"
FT /id="PRO_0000103109"
FT ACT_SITE 145
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT ACT_SITE 173
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT BINDING 57
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT BINDING 213
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT SITE 56
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT SITE 119
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT CONFLICT 266
FT /note="L -> S (in Ref. 1; CAA37940)"
FT /evidence="ECO:0000305"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:3CPR"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:3CPR"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:3CPR"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:3CPR"
FT TURN 56..62
FT /evidence="ECO:0007829|PDB:3CPR"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:3CPR"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:3CPR"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:3CPR"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:3CPR"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:3CPR"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:3CPR"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:3CPR"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:3CPR"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:3CPR"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:3CPR"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:3CPR"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:3CPR"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3CPR"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:3CPR"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:3CPR"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3CPR"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:3CPR"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:3CPR"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:3CPR"
FT HELIX 258..268
FT /evidence="ECO:0007829|PDB:3CPR"
FT HELIX 285..297
FT /evidence="ECO:0007829|PDB:3CPR"
SQ SEQUENCE 301 AA; 31262 MW; 6B803A4E829393B3 CRC64;
MSTGLTAKTG VEHFGTVGVA MVTPFTESGD IDIAAGREVA AYLVDKGLDS LVLAGTTGES
PTTTAAEKLE LLKAVREEVG DRAKLIAGVG TNNTRTSVEL AEAAASAGAD GLLVVTPYYS
KPSQEGLLAH FGAIAAATEV PICLYDIPGR SGIPIESDTM RRLSELPTIL AVKDAKGDLV
AATSLIKETG LAWYSGDDPL NLVWLALGGS GFISVIGHAA PTALRELYTS FEEGDLVRAR
EINAKLSPLV AAQGRLGGVS LAKAALRLQG INVGDPRLPI MAPNEQELEA LREDMKKAGV
L
