(data stored in ACNUC7421 zone)

SWISSPROT: DAPF_PSEHT

ID   DAPF_PSEHT              Reviewed;         276 AA.
AC   Q3IEW3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 77.
DE   RecName: Full=Diaminopimelate epimerase {ECO:0000255|HAMAP-Rule:MF_00197};
DE            Short=DAP epimerase {ECO:0000255|HAMAP-Rule:MF_00197};
DE            EC=5.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00197};
DE   AltName: Full=PLP-independent amino acid racemase {ECO:0000255|HAMAP-Rule:MF_00197};
GN   Name=dapF {ECO:0000255|HAMAP-Rule:MF_00197};
GN   OrderedLocusNames=PSHAa0092;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6-
CC       diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-
CC       DAP), a precursor of L-lysine and an essential component of the
CC       bacterial peptidoglycan. {ECO:0000255|HAMAP-Rule:MF_00197}.
CC   -!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate = meso-
CC       diaminoheptanedioate. {ECO:0000255|HAMAP-Rule:MF_00197}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step
CC       1/1. {ECO:0000255|HAMAP-Rule:MF_00197}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00197}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00197}.
CC   -!- SIMILARITY: Belongs to the diaminopimelate epimerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00197}.
DR   EMBL; CR954246; CAI85201.1; -; Genomic_DNA.
DR   RefSeq; WP_011326819.1; NC_007481.1.
DR   ProteinModelPortal; Q3IEW3; -.
DR   SMR; Q3IEW3; -.
DR   STRING; 326442.PSHAa0092; -.
DR   EnsemblBacteria; CAI85201; CAI85201; PSHAa0092.
DR   KEGG; pha:PSHAa0092; -.
DR   PATRIC; fig|326442.8.peg.91; -.
DR   eggNOG; ENOG4105E4Z; Bacteria.
DR   eggNOG; COG0253; LUCA.
DR   HOGENOM; HOG000220466; -.
DR   KO; K01778; -.
DR   OMA; MCGNGGR; -.
DR   OrthoDB; POG091H01QC; -.
DR   UniPathway; UPA00034; UER00025.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00197; DAP_epimerase; 1.
DR   InterPro; IPR018510; DAP_epimerase_AS.
DR   InterPro; IPR001653; DAP_epimerase_DapF.
DR   PANTHER; PTHR31689; PTHR31689; 1.
DR   Pfam; PF01678; DAP_epimerase; 2.
DR   TIGRFAMs; TIGR00652; DapF; 1.
DR   PROSITE; PS01326; DAP_EPIMERASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IEW3.
DR   SWISS-2DPAGE; Q3IEW3.
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Isomerase;
KW   Lysine biosynthesis; Reference proteome.
FT   CHAIN         1    276       Diaminopimelate epimerase.
FT                                /FTId=PRO_1000011933.
FT   REGION       76     77       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      210    211       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   REGION      220    221       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   ACT_SITE     75     75       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   ACT_SITE    219    219       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING      13     13       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING      46     46       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING      66     66       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING     159    159       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   BINDING     192    192       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   SITE        161    161       Could be important to modulate the pK
FT                                values of the two catalytic cysteine
FT                                residues. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   SITE        210    210       Could be important to modulate the pK
FT                                values of the two catalytic cysteine
FT                                residues. {ECO:0000255|HAMAP-
FT                                Rule:MF_00197}.
FT   SITE        270    270       Important for dimerization.
FT                                {ECO:0000255|HAMAP-Rule:MF_00197}.
SQ   SEQUENCE   276 AA;  30718 MW;  7E052181A8C9E943 CRC64;
     MLVNFSKMHG LGNDFVVIDN ITQNVFLSRD QIIKLADRHF GIGFDQLLMV EAPYSPDLDF
     HYRIFNADGT EVEQCGNGAR CFARFVRMKG LTNKHKITVS TKSGNLTLYI EKDGQVTVNM
     GHPNFEPSKI PLKATKRELT YIIRTEEHTV FSGAVSMGNP HCVLEVDDIT TAQVDILGPL
     LENHERFPQR ANIGFMQVIS KEHIKLRVWE RGVNETLACG TGACAAMVIG FIQNKLISTV
     QVDLPGGSLQ IRWNGEGHPV RMTGPAEHVF DGQVAL
//

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