(data stored in SCRATCH3701 zone)

SWISSPROT: DAPAT_SYNS3

ID   DAPAT_SYNS3             Reviewed;         408 AA.
AC   Q0ID68;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   11-DEC-2019, entry version 86.
DE   RecName: Full=LL-diaminopimelate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01642};
DE            Short=DAP-AT {ECO:0000255|HAMAP-Rule:MF_01642};
DE            Short=DAP-aminotransferase {ECO:0000255|HAMAP-Rule:MF_01642};
DE            Short=LL-DAP-aminotransferase {ECO:0000255|HAMAP-Rule:MF_01642};
DE            EC=2.6.1.83 {ECO:0000255|HAMAP-Rule:MF_01642};
GN   Name=dapL {ECO:0000255|HAMAP-Rule:MF_01642}; Synonyms=aspB;
GN   OrderedLocusNames=sync_0372;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311;
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA   Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA   Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA   Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT   coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
CC   -!- FUNCTION: Involved in the synthesis of meso-diaminopimelate (m-DAP or
CC       DL-DAP), required for both lysine and peptidoglycan biosynthesis.
CC       Catalyzes the direct conversion of tetrahydrodipicolinate to LL-
CC       diaminopimelate. {ECO:0000255|HAMAP-Rule:MF_01642}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + LL-2,6-diaminoheptanedioate = (S)-2,3,4,5-
CC         tetrahydrodipicolinate + H(+) + H2O + L-glutamate;
CC         Xref=Rhea:RHEA:23988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:16845, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57609; EC=2.6.1.83; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01642};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01642};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC       (aminotransferase route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01642}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01642}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. LL-diaminopimelate aminotransferase subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01642}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABI45974.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000435; ABI45974.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041426857.1; NC_008319.1.
DR   SMR; Q0ID68; -.
DR   STRING; 64471.sync_0372; -.
DR   EnsemblBacteria; ABI45974; ABI45974; sync_0372.
DR   KEGG; syg:sync_0372; -.
DR   eggNOG; ENOG4107QSS; Bacteria.
DR   eggNOG; COG0436; LUCA.
DR   HOGENOM; HOG000223061; -.
DR   KO; K10206; -.
DR   OrthoDB; 417859at2; -.
DR   BioCyc; SSP64471:G1G72-361-MONOMER; -.
DR   UniPathway; UPA00034; UER00466.
DR   Proteomes; UP000001961; Chromosome.
DR   GO; GO:0010285; F:L,L-diaminopimelate aminotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0033362; P:lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01642; DapL_aminotrans_1; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR019942; DapL/ALD1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR43144; PTHR43144; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03542; DAPAT_plant; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q0ID68.
DR   SWISS-2DPAGE; Q0ID68.
KW   Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..408
FT                   /note="LL-diaminopimelate aminotransferase"
FT                   /id="PRO_0000312545"
FT   REGION          108..109
FT                   /note="Pyridoxal phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   REGION          246..248
FT                   /note="Pyridoxal phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         15
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         42
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         72
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         109
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         132
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         132
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         187
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         187
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         218
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         257
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         292
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         292
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   BINDING         388
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
FT   MOD_RES         249
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01642"
SQ   SEQUENCE   408 AA;  44370 MW;  9EE002E4BAB659FE CRC64;
     MVKVNGNYLK LKAGYLFPEI GRRVKAFSSA NPEAQLIRLG IGDVTEPLPQ ACRDAMKSAI
     DEMGTAEGFH GYGPEQGYAW LREAIARDDF QARGCEISAE EIFVSDGSKC DSSNILDILG
     SGNRIAVTDP VYPVYVDSNV MAGRTGESGD DGRYGGLTYL PISADNGFAA QIPSEPVDLI
     YLCYPNNPTG AVATKAQLKK WVDYARANKA LILFDAAYEA FIQDPELPHS IYEIEGARDC
     AIEFRSFSKN AGFTGTRCAL TVVPKGLKGK ADDGSEVELW GLWNRRQSTK FNGVSYIIQR
     GAEAVYSDAG KQEVKALVSF YMENAAIIRR ELSAAGIEVH GGQHAPYVWL KTPSGMDSWS
     FFDHLLQKAN VVGTPGSGFG AAGEGYFRLS AFNSRSNVDE AMARIRNL
//

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